ENST00000000233.10 ARF5 ENST00000000233.10 ADP ribosylation factor 5 (from RefSeq NM_001662.4) ARF5_HUMAN ENST00000000233.1 ENST00000000233.2 ENST00000000233.3 ENST00000000233.4 ENST00000000233.5 ENST00000000233.6 ENST00000000233.7 ENST00000000233.8 ENST00000000233.9 NM_001662 P26437 P84085 uc003vmb.1 uc003vmb.2 uc003vmb.3 uc003vmb.4 This gene is a member of the human ADP-ribosylation factor (ARF) gene family. These genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6). The members of each class share a common gene organization. [provided by RefSeq, Dec 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC033104.1, SRR3476690.883380.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000000233.10/ ENSP00000000233.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392). Binds ASAP2 (PubMed:10022920). Interacts with NCS1/FREQ at the Golgi complex (PubMed:17555535). Interacts with RAB11FIP3 and RAB11FIP4 (PubMed:17030804). P84085; Q96HD9: ACY3; NbExp=3; IntAct=EBI-4289908, EBI-3916242; P84085; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-4289908, EBI-2340258; Golgi apparatus Cytoplasm, perinuclear region Membrane ; Lipid-anchor Golgi apparatus, trans-Golgi network membrane ; Lipid-anchor Belongs to the small GTPase superfamily. Arf family. nucleotide binding GTPase activity protein binding GTP binding cytoplasm Golgi apparatus plasma membrane intracellular protein transport retrograde vesicle-mediated transport, Golgi to ER protein transport membrane vesicle-mediated transport perinuclear region of cytoplasm extracellular exosome uc003vmb.1 uc003vmb.2 uc003vmb.3 uc003vmb.4 
ENST00000000412.8 M6PR ENST00000000412.8 mannose-6-phosphate receptor, cation dependent, transcript variant 1 (from RefSeq NM_002355.4) A8K528 D3DUV5 ENST00000000412.1 ENST00000000412.2 ENST00000000412.3 ENST00000000412.4 ENST00000000412.5 ENST00000000412.6 ENST00000000412.7 MPR46 MPRD MPRD_HUMAN NM_002355 P20645 uc001qvf.1 uc001qvf.2 uc001qvf.3 uc001qvf.4 uc001qvf.5 This gene encodes a member of the P-type lectin family. P-type lectins play a critical role in lysosome function through the specific transport of mannose-6-phosphate-containing acid hydrolases from the Golgi complex to lysosomes. The encoded protein functions as a homodimer and requires divalent cations for ligand binding. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. A pseudogene of this gene is located on the long arm of chromosome X. [provided by RefSeq, May 2011]. Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. Homodimer. Binds GGA1, GGA2 and GGA3. P20645; P21964-2: COMT; NbExp=3; IntAct=EBI-2907262, EBI-10200977; P20645; Q9UNI6: DUSP12; NbExp=3; IntAct=EBI-2907262, EBI-715161; P20645; Q9NZ52: GGA3; NbExp=2; IntAct=EBI-2907262, EBI-447404; P20645; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-2907262, EBI-6166686; P20645; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-2907262, EBI-12007212; P20645; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-2907262, EBI-10317425; P20645; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-2907262, EBI-8640191; Lysosome membrane; Single-pass type I membrane protein. The extracellular domain is homologous to the repeating units (of approximately 147 AA) of the cation-independent mannose 6-phosphate receptor. This receptor has optimal binding in the presence of divalent cations. transmembrane signaling receptor activity protein binding lysosome lysosomal membrane endosome late endosome Golgi apparatus trans-Golgi network plasma membrane integral component of plasma membrane protein targeting to lysosome receptor-mediated endocytosis lysosomal transport endosome to lysosome transport membrane integral component of membrane protein domain specific binding transport vesicle clathrin-coated vesicle membrane trans-Golgi network membrane secretion of lysosomal enzymes perinuclear region of cytoplasm membrane organization retromer complex binding uc001qvf.1 uc001qvf.2 uc001qvf.3 uc001qvf.4 uc001qvf.5 
ENST00000000442.11 ESRRA ENST00000000442.11 estrogen related receptor alpha, transcript variant 1 (from RefSeq NM_004451.5) ENST00000000442.1 ENST00000000442.10 ENST00000000442.2 ENST00000000442.3 ENST00000000442.4 ENST00000000442.5 ENST00000000442.6 ENST00000000442.7 ENST00000000442.8 ENST00000000442.9 ESRRA NM_004451 NR3B1 Q569H8 Q569H8_HUMAN Q6P3W9 hCG_2016877 uc001nzq.1 uc001nzq.2 uc001nzq.3 uc001nzq.4 The protein encoded by this gene is a nuclear receptor that is most closely related to the estrogen receptor. This protein acts as a site-specific transcription factor and interacts with members of the PGC-1 family of transcription cofactors to regulate the expression of most genes involved in cellular energy production as well as in the process of mitochondrial biogenesis. A processed pseudogene of ESRRA is located on chromosome 13q12.1. [provided by RefSeq, Jun 2019]. Nucleus Belongs to the nuclear hormone receptor family. NR3 subfamily. negative regulation of transcription from RNA polymerase II promoter RNA polymerase II core promoter proximal region sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding fibrillar center DNA binding transcription factor activity, sequence-specific DNA binding steroid hormone receptor activity steroid binding nucleus regulation of transcription, DNA-templated zinc ion binding microtubule cytoskeleton regulation of ossification response to estradiol regulation of cell proliferation steroid hormone mediated signaling pathway sequence-specific DNA binding intercellular bridge regulation of osteoblast differentiation regulation of osteoclast differentiation positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter metal ion binding cartilage development positive regulation of cellular response to insulin stimulus uc001nzq.1 uc001nzq.2 uc001nzq.3 uc001nzq.4 
ENST00000001008.6 FKBP4 ENST00000001008.6 FKBP prolyl isomerase 4 (from RefSeq NM_002014.4) D3DUQ1 ENST00000001008.1 ENST00000001008.2 ENST00000001008.3 ENST00000001008.4 ENST00000001008.5 FKBP4_HUMAN FKBP52 NM_002014 Q02790 Q9UCP1 Q9UCV7 uc001qkz.1 uc001qkz.2 uc001qkz.3 uc001qkz.4 uc001qkz.5 The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory gene expression in B and T lymphocytes. This encoded protein is known to associate with phytanoyl-CoA alpha-hydroxylase. It can also associate with two heat shock proteins (hsp90 and hsp70) and thus may play a role in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. This protein correlates strongly with adeno-associated virus type 2 vectors (AAV) resulting in a significant increase in AAV-mediated transgene expression in human cell lines. Thus this encoded protein is thought to have important implications for the optimal use of AAV vectors in human gene therapy. The human genome contains several non-transcribed pseudogenes similar to this gene. [provided by RefSeq, Sep 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.159743.1, SRR1803615.213037.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000001008.6/ ENSP00000001008.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Inhibited by FK506. Homodimer (By similarity). Interacts with GLMN (PubMed:12604780). Associates with HSP90AA1 and HSP70 in steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl- CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90 complex. Associates with tubulin. Interacts with MAPT/TAU (By similarity). Interacts (via TPR domain) with S100A1, S100A2 and S100A6; the interaction is Ca(2+) dependent. Interaction with S100A1 and S100A2 (but not with S100A6) leads to inhibition of FKBP4-HSP90 interaction. Interacts with dynein; causes partially NR3C1 transport to the nucleus. Q02790; Q9UKV8: AGO2; NbExp=2; IntAct=EBI-1047444, EBI-528269; Q02790; P10275: AR; NbExp=2; IntAct=EBI-1047444, EBI-608057; Q02790; Q16543: CDC37; NbExp=3; IntAct=EBI-1047444, EBI-295634; Q02790; Q92990: GLMN; NbExp=4; IntAct=EBI-1047444, EBI-726150; Q02790; P07900: HSP90AA1; NbExp=8; IntAct=EBI-1047444, EBI-296047; Q02790; P08238: HSP90AB1; NbExp=6; IntAct=EBI-1047444, EBI-352572; Q02790; P04792: HSPB1; NbExp=2; IntAct=EBI-1047444, EBI-352682; Q02790; P10636-8: MAPT; NbExp=7; IntAct=EBI-1047444, EBI-366233; Q02790; P29034: S100A2; NbExp=3; IntAct=EBI-1047444, EBI-752230; Q02790; P06703: S100A6; NbExp=3; IntAct=EBI-1047444, EBI-352877; Q02790; P35467: S100a1; Xeno; NbExp=7; IntAct=EBI-1047444, EBI-6477109; Cytoplasm, cytosol Mitochondrion Nucleus Cytoplasm, cytoskeleton Cell projection, axon Note=Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor (PubMed:21730050). Colocalized with MAPT/TAU in the distal part of the primary cortical neurons (By similarity). Widely expressed. The PPIase activity is mainly due to the first PPIase FKBP-type domain (1-138 AA). The C-terminal region (AA 375-458) is required to prevent tubulin polymerization. The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400. The TPR repeats mediate mitochondrial localization. Phosphorylation by CK2 results in loss of HSP90 binding activity. Name=Protein Spotlight; Note=A mind astray - Issue 118 of June 2010; URL="https://web.expasy.org/spotlight/back_issues/118"; protein peptidyl-prolyl isomerization RNA binding peptidyl-prolyl cis-trans isomerase activity protein binding ATP binding GTP binding FK506 binding nucleus nucleoplasm cytoplasm mitochondrion cytosol cytoskeleton microtubule protein folding steroid hormone receptor complex assembly copper ion transport embryo implantation negative regulation of neuron projection development isomerase activity axon androgen receptor signaling pathway protein binding, bridging prostate gland development heat shock protein binding negative regulation of microtubule polymerization or depolymerization negative regulation of microtubule polymerization protein complex localization copper-dependent protein binding macromolecular complex glucocorticoid receptor binding cell projection neuron projection neuronal cell body axonal growth cone male sex differentiation tau protein binding perinuclear region of cytoplasm reproductive structure development phosphoprotein binding chaperone-mediated protein folding extracellular exosome regulation of cellular response to heat uc001qkz.1 uc001qkz.2 uc001qkz.3 uc001qkz.4 uc001qkz.5 
ENST00000001146.7 CYP26B1 ENST00000001146.7 cytochrome P450 family 26 subfamily B member 1, transcript variant 1 (from RefSeq NM_019885.4) B2R8M7 B7Z2K6 B7Z2P4 B7Z3B8 CP26B_HUMAN CYP26A2 E4W5W7 ENST00000001146.1 ENST00000001146.2 ENST00000001146.3 ENST00000001146.4 ENST00000001146.5 ENST00000001146.6 NM_019885 P450RAI2 Q32MC0 Q53TW1 Q9NP41 Q9NR63 uc002sih.1 uc002sih.2 uc002sih.3 uc002sih.4 This gene encodes a member of the cytochrome P450 superfamily. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The encoded protein is localized to the endoplasmic reticulum, and functions as a critical regulator of all-trans retinoic acid levels by the specific inactivation of all-trans retinoic acid to hydroxylated forms. Mutations in this gene are associated with radiohumeral fusions and other skeletal and craniofacial anomalies, and increased levels of the encoded protein are associated with atherosclerotic lesions. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2013]. A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:10823918, PubMed:22020119). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis- RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (Probable). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (PubMed:10823918). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (PubMed:10823918, PubMed:22020119). Involved in the convertion of atRA to all-trans-4-oxo-RA. Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8- epoxy-DRA, and all-trans-18-hydroxy-DRA (By similarity). Shows preference for the following substrates: atRA > 9-cis-RA > 13-cis-RA (PubMed:10823918, PubMed:22020119). Plays a central role in germ cell development: acts by degrading RAs in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints (PubMed:22019272). Essential for postnatal survival (By similarity). Has also a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo. Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985; Evidence=; Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-18-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55856, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:139258; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55857; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Kinetic parameters: KM=1.01 uM for tazarotenic acid (measured in vitro by the production of tazarotenic acid-sulfoxide) ; KM=0.56 uM for tazarotenic acid (measured in vitro by the production of hydroxytazarotenic acid production) ; Q9NR63; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25928065, EBI-1055254; Endoplasmic reticulum membrane ; Peripheral membrane protein Microsome membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NR63-1; Sequence=Displayed; Name=2; IsoId=Q9NR63-2; Sequence=VSP_042968; Name=3; IsoId=Q9NR63-3; Sequence=VSP_042967; Highly expressed in brain, particularly in the cerebellum and pons. By retinoic acid. Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA) [MIM:614416]: A disease characterized by craniofacial malformations, occipital encephalocele, radiohumeral fusions, oligodactyly, advanced osseous maturation, and calvarial mineralization defects. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the cytochrome P450 family. Sequence=BAH12154.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cyp26b1/"; C-22 sterol desaturase activity cell fate determination establishment of T cell polarity kidney development retinoic acid binding monooxygenase activity iron ion binding cytoplasm endoplasmic reticulum endoplasmic reticulum membrane ergosterol biosynthetic process vitamin metabolic process xenobiotic metabolic process inflammatory response male meiosis spermatogenesis retinoic acid 4-hydroxylase activity proximal/distal pattern formation positive regulation of gene expression membrane sterol metabolic process oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen heme binding embryonic limb morphogenesis organelle membrane response to retinoic acid response to vitamin A retinoic acid catabolic process intracellular membrane-bounded organelle tongue morphogenesis regulation of T cell differentiation metal ion binding retinoic acid receptor signaling pathway regulation of retinoic acid receptor signaling pathway negative regulation of retinoic acid receptor signaling pathway oxidation-reduction process bone morphogenesis establishment of skin barrier cornification cellular response to retinoic acid positive regulation of tongue muscle cell differentiation uc002sih.1 uc002sih.2 uc002sih.3 uc002sih.4 
ENST00000002125.9 NDUFAF7 ENST00000002125.9 NADH:ubiquinone oxidoreductase complex assembly factor 7, transcript variant 14 (from RefSeq NR_146409.3) C2orf56 ENST00000002125.1 ENST00000002125.2 ENST00000002125.3 ENST00000002125.4 ENST00000002125.5 ENST00000002125.6 ENST00000002125.7 ENST00000002125.8 NDUF7_HUMAN NDUFAF7 NR_146409 PRO1853 Q7L592 Q7Z399 Q9P1G3 uc002rqa.1 uc002rqa.2 uc002rqa.3 uc002rqa.4 uc002rqa.5 uc002rqa.6 uc002rqa.7 This gene encodes an assembly factor protein which helps in the assembly and stabilization of Complex I, a large multi-subunit enzyme in the mitochondrial respiratory chain. Complex I is involved in several physiological activities in the cell, including metabolite transport and ATP synthesis. The encoded protein is a methyltransferase which methylates Arg85 of a subunit of Complex I in the early stages of its assembly. A pseudogene related to this gene is located on chromosome 8. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2016]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. ##Evidence-Data-START## Transcript exon combination :: SRR1660805.138693.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta ##RefSeq-Attributes-END## Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) (PubMed:20406883, PubMed:24089531, PubMed:24838397). Acts by mediating symmetric dimethylation of 'Arg-118' of NDUFS2 after it assembles into the complex I, stabilizing the early intermediate complex (PubMed:24089531). Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA- COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320; Evidence=; Interacts with NDUFS2 (PubMed:20406883, PubMed:24089531). Q7L592; Q5S007: LRRK2; NbExp=2; IntAct=EBI-2555519, EBI-5323863; Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q7L592-1; Sequence=Displayed; Name=2; IsoId=Q7L592-2; Sequence=VSP_030606, VSP_030607; Note=Defects in NDUFAF7 may be a cause of susceptibility to pathologic myopia, a genetically heterogeneous disorder characterized by extreme, familial, early-onset vision loss and described as myopia accompanied by severe deformation of the eye besides excessive elongation of the eye. Belongs to the NDUFAF7 family. Stoichiometry of the protein is unclear. According to a report, it forms a homodimer (PubMed:20406883). According to another publication, it is mainly monomeric (PubMed:24838397). Sequence=AAF71091.1; Type=Erroneous initiation; Evidence=; Sequence=AAH12374.2; Type=Erroneous initiation; Evidence=; protein binding extracellular space mitochondrion mitochondrial matrix methyltransferase activity transferase activity enzyme binding peptidyl-arginine methylation, to symmetrical-dimethyl arginine methylation mitochondrial respiratory chain complex I assembly protein-arginine omega-N symmetric methyltransferase activity uc002rqa.1 uc002rqa.2 uc002rqa.3 uc002rqa.4 uc002rqa.5 uc002rqa.6 uc002rqa.7 
ENST00000002165.11 FUCA2 ENST00000002165.11 alpha-L-fucosidase 2 (from RefSeq NM_032020.5) E9PEB6 ENST00000002165.1 ENST00000002165.10 ENST00000002165.2 ENST00000002165.3 ENST00000002165.4 ENST00000002165.5 ENST00000002165.6 ENST00000002165.7 ENST00000002165.8 ENST00000002165.9 FUCO2_HUMAN NM_032020 PSEC0151 Q7Z6V1 Q7Z6Y2 Q8NBK4 Q9BTY2 UNQ227/PRO260 uc003qjm.1 uc003qjm.2 uc003qjm.3 uc003qjm.4 uc003qjm.5 This gene encodes a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. The protein is a member of the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. This enzyme is essential for Helicobacter pylori adhesion to human gastric cancer cells. [provided by RefSeq, Aug 2010]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803617.230531.1, SRR1803615.84845.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2155770 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000002165.11/ ENSP00000002165.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Alpha-L-fucosidase is responsible for hydrolyzing the alpha- 1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose; Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51; Evidence=; Homotetramer. Q9BTY2; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-9050116, EBI-11978177; Q9BTY2; P49639: HOXA1; NbExp=3; IntAct=EBI-9050116, EBI-740785; Q9BTY2; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-9050116, EBI-739863; Q9BTY2; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-9050116, EBI-11958178; Q9BTY2; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-9050116, EBI-11974251; Q9BTY2; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-9050116, EBI-11962058; Q9BTY2; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-9050116, EBI-10245913; Q9BTY2; Q5T753: LCE1E; NbExp=3; IntAct=EBI-9050116, EBI-11955335; Q9BTY2; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-9050116, EBI-10246358; Q9BTY2; P50222: MEOX2; NbExp=4; IntAct=EBI-9050116, EBI-748397; Q9BTY2; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-9050116, EBI-1210753; Q9BTY2; Q13526: PIN1; NbExp=3; IntAct=EBI-9050116, EBI-714158; Q9BTY2; O14787-2: TNPO2; NbExp=3; IntAct=EBI-9050116, EBI-12076664; Q9BTY2; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-9050116, EBI-11957238; Q9BTY2; O96014: WNT11; NbExp=3; IntAct=EBI-9050116, EBI-8058160; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BTY2-1; Sequence=Displayed; Name=2; IsoId=Q9BTY2-2; Sequence=VSP_057004, VSP_057005; Belongs to the glycosyl hydrolase 29 family. alpha-L-fucosidase activity protein binding extracellular region extracellular space lysosome endoplasmic reticulum lumen carbohydrate metabolic process fucose metabolic process metabolic process response to bacterium glycoside catabolic process hydrolase activity hydrolase activity, acting on glycosyl bonds azurophil granule lumen neutrophil degranulation post-translational protein modification cellular protein metabolic process extracellular exosome regulation of entry of bacterium into host cell uc003qjm.1 uc003qjm.2 uc003qjm.3 uc003qjm.4 uc003qjm.5 
ENST00000002501.11 DBNDD1 ENST00000002501.11 dysbindin domain containing 1, transcript variant 1 (from RefSeq NM_001042610.3) B4DQS3 DBND1_HUMAN ENST00000002501.1 ENST00000002501.10 ENST00000002501.2 ENST00000002501.3 ENST00000002501.4 ENST00000002501.5 ENST00000002501.6 ENST00000002501.7 ENST00000002501.8 ENST00000002501.9 NM_001042610 Q69YT2 Q9BW25 Q9H9R9 uc002fqf.1 uc002fqf.2 uc002fqf.3 uc002fqf.4 Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9H9R9-1; Sequence=Displayed; Name=2; IsoId=Q9H9R9-2; Sequence=VSP_026214; Name=3; IsoId=Q9H9R9-3; Sequence=VSP_037541; Belongs to the dysbindin family. cytoplasm uc002fqf.1 uc002fqf.2 uc002fqf.3 uc002fqf.4 
ENST00000002596.6 HS3ST1 ENST00000002596.6 heparan sulfate-glucosamine 3-sulfotransferase 1 (from RefSeq NM_005114.4) 3OST 3OST1 B3KUA6 ENST00000002596.1 ENST00000002596.2 ENST00000002596.3 ENST00000002596.4 ENST00000002596.5 HS3S1_HUMAN NM_005114 O14792 Q6PEY8 uc003gmq.1 uc003gmq.2 uc003gmq.3 uc003gmq.4 uc003gmq.5 Heparan sulfate biosynthetic enzymes are key components in generating a myriad of distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It possesses both heparan sulfate glucosaminyl 3-O-sulfotransferase activity, anticoagulant heparan sulfate conversion activity, and is a rate limiting enzyme for synthesis of anticoagulant heparan. This enzyme is an intraluminal Golgi resident protein. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803615.89832.1, SRR1803615.254596.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000002596.6/ ENSP00000002596.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan (PubMed:9346953, PubMed:8900198, PubMed:9988768). Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) (PubMed:8900198, PubMed:9988768). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site (PubMed:8900198, PubMed:9988768). Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA- COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.23; Evidence=; Golgi apparatus lumen Highly expressed in the brain and kidney and weakly expressed in the heart, lung and placenta. Belongs to the sulfotransferase 1 family. Golgi apparatus Golgi lumen glycosaminoglycan biosynthetic process sulfotransferase activity [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity transferase activity uc003gmq.1 uc003gmq.2 uc003gmq.3 uc003gmq.4 uc003gmq.5 
ENST00000002829.8 SEMA3F ENST00000002829.8 semaphorin 3F, transcript variant 1 (from RefSeq NM_004186.5) C9JQ85 ENST00000002829.1 ENST00000002829.2 ENST00000002829.3 ENST00000002829.4 ENST00000002829.5 ENST00000002829.6 ENST00000002829.7 NM_004186 Q13274 Q13275 Q13372 Q15704 Q6GTR4 SEM3F_HUMAN uc003cyj.1 uc003cyj.2 uc003cyj.3 uc003cyj.4 uc003cyj.5 This gene encodes a member of the semaphorin III family of secreted signaling proteins that are involved in axon guidance during neuronal development. The encoded protein contains an N-terminal Sema domain, an immunoglobulin loop and a C-terminal basic domain. This gene is expressed by the endothelial cells where it was found to act in an autocrine fashion to induce apoptosis, inhibit cell proliferation and survival, and function as an anti-tumorigenic agent. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jan 2016]. May play a role in cell motility and cell adhesion. Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13275-1; Sequence=Displayed; Name=2; IsoId=Q13275-2; Sequence=VSP_053417; Expressed abundantly but differentially in a variety of neural and nonneural tissues. There is high expression in mammary gland, kidney, fetal brain, and lung and lower expression in heart and liver. Detected as early as embryonic day 10. Belongs to the semaphorin family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42254/SEMA3F"; neural crest cell migration extracellular region extracellular space integral component of plasma membrane axon guidance facial nerve structural organization trigeminal nerve structural organization nerve development branchiomotor neuron axon guidance semaphorin receptor binding positive regulation of cell migration ventral trunk neural crest cell migration chemorepellent activity negative regulation of axon extension involved in axon guidance axon extension involved in axon guidance negative chemotaxis sympathetic ganglion development semaphorin-plexin signaling pathway sympathetic neuron projection extension sympathetic neuron projection guidance glutamatergic synapse neural crest cell migration involved in autonomic nervous system development semaphorin-plexin signaling pathway involved in neuron projection guidance semaphorin-plexin signaling pathway involved in axon guidance uc003cyj.1 uc003cyj.2 uc003cyj.3 uc003cyj.4 uc003cyj.5 
ENST00000003084.11 CFTR ENST00000003084.11 CF transmembrane conductance regulator (from RefSeq NM_000492.4) ABCC7 CFTR_HUMAN ENST00000003084.1 ENST00000003084.10 ENST00000003084.2 ENST00000003084.3 ENST00000003084.4 ENST00000003084.5 ENST00000003084.6 ENST00000003084.7 ENST00000003084.8 ENST00000003084.9 NM_000492 P13569 Q20BG8 Q20BH2 Q2I0A1 Q2I102 uc003vjd.1 uc003vjd.2 uc003vjd.3 uc003vjd.4 uc003vjd.5 This gene encodes a member of the ATP-binding cassette (ABC) transporter superfamily. The encoded protein functions as a chloride channel, making it unique among members of this protein family, and controls ion and water secretion and absorption in epithelial tissues. Channel activation is mediated by cycles of regulatory domain phosphorylation, ATP-binding by the nucleotide-binding domains, and ATP hydrolysis. Mutations in this gene cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent. The most frequently occurring mutation in cystic fibrosis, DeltaF508, results in impaired folding and trafficking of the encoded protein. Multiple pseudogenes have been identified in the human genome. [provided by RefSeq, Aug 2017]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M28668.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000003084.11/ ENSP00000003084.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:10792060, PubMed:11524016, PubMed:11707463, PubMed:12519745, PubMed:15010471, PubMed:12588899, PubMed:17036051, PubMed:19398555, PubMed:19621064, PubMed:22178883, PubMed:25330774, PubMed:1712898, PubMed:8910473, PubMed:9804160, PubMed:12529365, PubMed:17182731, PubMed:26846474, PubMed:28087700). Channel activity is coupled to ATP hydrolysis (PubMed:8910473). The ion channel is also permeable to HCO(3)(-); selectivity depends on the extracellular chloride concentration (PubMed:15010471, PubMed:19019741). Exerts its function also by modulating the activity of other ion channels and transporters (PubMed:12403779, PubMed:22178883, PubMed:22121115, PubMed:27941075). Plays an important role in airway fluid homeostasis (PubMed:16645176, PubMed:19621064, PubMed:26823428). Contributes to the regulation of the pH and the ion content of the airway surface fluid layer and thereby plays an important role in defense against pathogens (PubMed:14668433, PubMed:16645176, PubMed:26823428). Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex (PubMed:17434346, PubMed:27941075, PubMed:17182731). Inhibits the activity of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731). Inhibits the activity of the ENaC channel containing subunits SCNN1D, SCNN1B and SCNN1G, but not of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731, PubMed:27941075). May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7 (PubMed:12403779). Can inhibit the chloride channel activity of ANO1 (PubMed:22178883). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (PubMed:19923167, PubMed:27714810). Reaction=ATP + H2O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.; EC=5.6.1.6; Evidence= Monomer; does not require oligomerization for channel activity (PubMed:11524016). May form oligomers in the membrane (PubMed:11524016). Interacts with SLC26A3, SLC26A6 and SHANK2 (By similarity). Interacts with NHERF1 and MYO6 (PubMed:12403779, PubMed:15247260, PubMed:11304524). Interacts (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR internalization and thereby decreases channel activity (PubMed:11707463, PubMed:16331976). Interacts with SLC4A7 through NHERF1 (PubMed:12403779). Found in a complex with MYO5B and RAB11A (PubMed:17462998). Interacts with ANO1 (PubMed:22178883). Interacts with SLC26A8 (PubMed:22121115). Interacts with AHCYL1; the interaction increases CFTR activity (By similarity). Interacts with CSE1L (PubMed:20933420). The core-glycosylated form interacts with GORASP2 (via PDZ GRASP-type 1 domain) in respone to ER stress (PubMed:21884936). Interacts with MARCHF2; the interaction leads to CFTR ubiqtuitination and degradation (PubMed:23818989). P13569; Q6UWZ7: ABRAXAS1; NbExp=3; IntAct=EBI-349854, EBI-1263451; P13569; Q96QU6: ACCS; NbExp=3; IntAct=EBI-349854, EBI-743387; P13569; O14734: ACOT8; NbExp=3; IntAct=EBI-349854, EBI-1237371; P13569; P60709: ACTB; NbExp=6; IntAct=EBI-349854, EBI-353944; P13569; O43865: AHCYL1; NbExp=7; IntAct=EBI-349854, EBI-2371423; P13569; O95154: AKR7A3; NbExp=4; IntAct=EBI-349854, EBI-748869; P13569; P09972: ALDOC; NbExp=8; IntAct=EBI-349854, EBI-2952751; P13569; Q9BT30: ALKBH7; NbExp=4; IntAct=EBI-349854, EBI-2878075; P13569; Q9NP61: ARFGAP3; NbExp=8; IntAct=EBI-349854, EBI-2875816; P13569; P16615-1: ATP2A2; NbExp=6; IntAct=EBI-349854, EBI-11613988; P13569; P51572: BCAP31; NbExp=9; IntAct=EBI-349854, EBI-77683; P13569; A1A5D9: BICDL2; NbExp=3; IntAct=EBI-349854, EBI-10171799; P13569; Q9H7E9: C8orf33; NbExp=5; IntAct=EBI-349854, EBI-715389; P13569; P62158: CALM3; NbExp=18; IntAct=EBI-349854, EBI-397435; P13569; O43852-1: CALU; NbExp=2; IntAct=EBI-349854, EBI-5280679; P13569; P27824: CANX; NbExp=26; IntAct=EBI-349854, EBI-355947; P13569; Q01518: CAP1; NbExp=14; IntAct=EBI-349854, EBI-2808398; P13569; P07384: CAPN1; NbExp=7; IntAct=EBI-349854, EBI-1542113; P13569; P47756: CAPZB; NbExp=23; IntAct=EBI-349854, EBI-353595; P13569; Q9Y3X0: CCDC9; NbExp=4; IntAct=EBI-349854, EBI-2557532; P13569; Q53EZ4: CEP55; NbExp=5; IntAct=EBI-349854, EBI-747776; P13569; Q8NCH0: CHST14; NbExp=3; IntAct=EBI-349854, EBI-21717278; P13569; P51790-2: CLCN3; NbExp=2; IntAct=EBI-349854, EBI-25495635; P13569; O00299: CLIC1; NbExp=15; IntAct=EBI-349854, EBI-347404; P13569; Q13057: COASY; NbExp=7; IntAct=EBI-349854, EBI-745967; P13569; Q9Y678: COPG1; NbExp=21; IntAct=EBI-349854, EBI-1049127; P13569; P29762: CRABP1; NbExp=4; IntAct=EBI-349854, EBI-725950; P13569; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-349854, EBI-6942903; P13569; Q14406: CSHL1; NbExp=3; IntAct=EBI-349854, EBI-21022791; P13569; Q13616: CUL1; NbExp=7; IntAct=EBI-349854, EBI-359390; P13569; Q8N8Q1: CYB561D1; NbExp=3; IntAct=EBI-349854, EBI-12873482; P13569; Q6PI48: DARS2; NbExp=5; IntAct=EBI-349854, EBI-3917045; P13569; Q96HY6: DDRGK1; NbExp=4; IntAct=EBI-349854, EBI-1054024; P13569; Q9NUU7: DDX19A; NbExp=9; IntAct=EBI-349854, EBI-740301; P13569; Q9UHI6: DDX20; NbExp=5; IntAct=EBI-349854, EBI-347658; P13569; Q9BUN8: DERL1; NbExp=8; IntAct=EBI-349854, EBI-398977; P13569; Q7L2E3: DHX30; NbExp=5; IntAct=EBI-349854, EBI-1211456; P13569; Q8TBM8: DNAJB14; NbExp=3; IntAct=EBI-349854, EBI-2689808; P13569; Q96KC8: DNAJC1; NbExp=7; IntAct=EBI-349854, EBI-296550; P13569; Q9Y295: DRG1; NbExp=9; IntAct=EBI-349854, EBI-719554; P13569; P60981: DSTN; NbExp=16; IntAct=EBI-349854, EBI-745191; P13569; O60869: EDF1; NbExp=3; IntAct=EBI-349854, EBI-781301; P13569; P07099: EPHX1; NbExp=5; IntAct=EBI-349854, EBI-6138796; P13569; Q6P6B1: ERICH5; NbExp=4; IntAct=EBI-349854, EBI-11343491; P13569; P13804: ETFA; NbExp=7; IntAct=EBI-349854, EBI-1052886; P13569; Q0VG06: FAAP100; NbExp=4; IntAct=EBI-349854, EBI-2557990; P13569; Q9NYY8: FASTKD2; NbExp=5; IntAct=EBI-349854, EBI-1055752; P13569; Q14314: FGL2; NbExp=6; IntAct=EBI-349854, EBI-21370828; P13569; Q14192: FHL2; NbExp=10; IntAct=EBI-349854, EBI-701903; P13569; O75344: FKBP6; NbExp=4; IntAct=EBI-349854, EBI-744771; P13569; Q9UJY5: GGA1; NbExp=6; IntAct=EBI-349854, EBI-447141; P13569; P62879: GNB2; NbExp=12; IntAct=EBI-349854, EBI-356942; P13569; Q9HD26: GOPC; NbExp=10; IntAct=EBI-349854, EBI-349832; P13569; Q9H8Y8: GORASP2; NbExp=6; IntAct=EBI-349854, EBI-739467; P13569; P07203: GPX1; NbExp=3; IntAct=EBI-349854, EBI-7209024; P13569; P0CG30: GSTT2B; NbExp=4; IntAct=EBI-349854, EBI-13572836; P13569; Q9P035: HACD3; NbExp=15; IntAct=EBI-349854, EBI-359013; P13569; Q9BX68: HINT2; NbExp=3; IntAct=EBI-349854, EBI-8523143; P13569; P19367: HK1; NbExp=5; IntAct=EBI-349854, EBI-713162; P13569; O75330: HMMR; NbExp=7; IntAct=EBI-349854, EBI-2556203; P13569; P10809: HSPD1; NbExp=24; IntAct=EBI-349854, EBI-352528; P13569; O15554: KCNN4; NbExp=5; IntAct=EBI-349854, EBI-2924473; P13569; O94889: KLHL18; NbExp=3; IntAct=EBI-349854, EBI-2510096; P13569; O15131: KPNA5; NbExp=4; IntAct=EBI-349854, EBI-540602; P13569; P05787: KRT8; NbExp=11; IntAct=EBI-349854, EBI-297852; P13569; Q08380: LGALS3BP; NbExp=18; IntAct=EBI-349854, EBI-354956; P13569; Q9HBW0: LPAR2; NbExp=3; IntAct=EBI-349854, EBI-765995; P13569; P33241: LSP1; NbExp=4; IntAct=EBI-349854, EBI-9060697; P13569; Q9HCC0: MCCC2; NbExp=5; IntAct=EBI-349854, EBI-2211296; P13569; P08582: MELTF; NbExp=7; IntAct=EBI-349854, EBI-7172128; P13569; Q92552: MRPS27; NbExp=5; IntAct=EBI-349854, EBI-2211879; P13569; Q96S97: MYADM; NbExp=3; IntAct=EBI-349854, EBI-13301517; P13569; P41227: NAA10; NbExp=5; IntAct=EBI-349854, EBI-747693; P13569; O14745: NHERF1; NbExp=26; IntAct=EBI-349854, EBI-349787; P13569; Q15599: NHERF2; NbExp=28; IntAct=EBI-349854, EBI-1149760; P13569; Q9NZM5: NOP53; NbExp=4; IntAct=EBI-349854, EBI-720156; P13569; Q9BVG4: PBDC1; NbExp=3; IntAct=EBI-349854, EBI-722092; P13569; P08559: PDHA1; NbExp=5; IntAct=EBI-349854, EBI-715747; P13569; P30101: PDIA3; NbExp=12; IntAct=EBI-349854, EBI-979862; P13569; Q5T2W1: PDZK1; NbExp=3; IntAct=EBI-349854, EBI-349819; P13569; O60831: PRAF2; NbExp=4; IntAct=EBI-349854, EBI-2506064; P13569; P55036: PSMD4; NbExp=13; IntAct=EBI-349854, EBI-359318; P13569; O75127: PTCD1; NbExp=3; IntAct=EBI-349854, EBI-2560233; P13569; Q96PK6: RBM14; NbExp=13; IntAct=EBI-349854, EBI-954272; P13569; Q99942: RNF5; NbExp=8; IntAct=EBI-349854, EBI-348482; P13569; Q7Z5V6: SAXO4; NbExp=3; IntAct=EBI-349854, EBI-4311771; P13569; O15126: SCAMP1; NbExp=7; IntAct=EBI-349854, EBI-954338; P13569; P31040: SDHA; NbExp=15; IntAct=EBI-349854, EBI-1057265; P13569; Q9P0V3: SH3BP4; NbExp=4; IntAct=EBI-349854, EBI-1049513; P13569; P29353: SHC1; NbExp=6; IntAct=EBI-349854, EBI-78835; P13569; Q96RN1: SLC26A8; NbExp=2; IntAct=EBI-349854, EBI-1792052; P13569; O00400: SLC33A1; NbExp=6; IntAct=EBI-349854, EBI-11135403; P13569; P63162: SNRPN; NbExp=6; IntAct=EBI-349854, EBI-712493; P13569; Q9UHB9: SRP68; NbExp=7; IntAct=EBI-349854, EBI-1048560; P13569; Q9NSC7: ST6GALNAC1; NbExp=5; IntAct=EBI-349854, EBI-2854712; P13569; O95793: STAU1; NbExp=13; IntAct=EBI-349854, EBI-358174; P13569; Q9P289: STK26; NbExp=6; IntAct=EBI-349854, EBI-618239; P13569; Q92734: TFG; NbExp=7; IntAct=EBI-349854, EBI-357061; P13569; Q96Q45: TMEM237; NbExp=4; IntAct=EBI-349854, EBI-2602465; P13569; Q8WWA1: TMEM40; NbExp=9; IntAct=EBI-349854, EBI-39962964; P13569; O14545: TRAFD1; NbExp=9; IntAct=EBI-349854, EBI-1396921; P13569; P19474: TRIM21; NbExp=24; IntAct=EBI-349854, EBI-81290; P13569; Q13049: TRIM32; NbExp=5; IntAct=EBI-349854, EBI-742790; P13569; Q9C035: TRIM5; NbExp=3; IntAct=EBI-349854, EBI-924214; P13569; Q13432: UNC119; NbExp=4; IntAct=EBI-349854, EBI-711260; P13569; Q14694: USP10; NbExp=7; IntAct=EBI-349854, EBI-2510389; P13569; O94966: USP19; NbExp=6; IntAct=EBI-349854, EBI-2511895; P13569; Q9BXU7: USP26; NbExp=4; IntAct=EBI-349854, EBI-1641713; P13569; Q9P0L0: VAPA; NbExp=13; IntAct=EBI-349854, EBI-1059156; P13569; O95292: VAPB; NbExp=12; IntAct=EBI-349854, EBI-1188298; P13569; P45880: VDAC2; NbExp=10; IntAct=EBI-349854, EBI-354022; P13569; Q9UN37: VPS4A; NbExp=9; IntAct=EBI-349854, EBI-1171942; P13569; Q9UEU0: VTI1B; NbExp=10; IntAct=EBI-349854, EBI-723716; P13569; O00308: WWP2; NbExp=3; IntAct=EBI-349854, EBI-743923; P13569; Q8WTP9: XAGE3; NbExp=4; IntAct=EBI-349854, EBI-6448284; P13569; Q9BYJ9: YTHDF1; NbExp=5; IntAct=EBI-349854, EBI-1051237; P13569; P17026: ZNF22; NbExp=2; IntAct=EBI-349854, EBI-20803387; P13569; P19120: HSPA8; Xeno; NbExp=2; IntAct=EBI-349854, EBI-907802; P13569; Q9QX74: Shank2; Xeno; NbExp=3; IntAct=EBI-349854, EBI-397902; Apical cell membrane ulti-pass membrane protein Early endosome membrane ; Multi-pass membrane protein Cell membrane ulti-pass membrane protein Recycling endosome membrane ; Multi-pass membrane protein Endoplasmic reticulum membrane ; Multi-pass membrane protein Nucleus Note=The channel is internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (PubMed:17462998, PubMed:19398555, PubMed:20008117). In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia (PubMed:22207244). In Sertoli cells, a processed product is detected in the nucleus (By similarity). ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P13569-1; Sequence=Displayed; Name=2; IsoId=P13569-2; Sequence=VSP_022123; Name=3; IsoId=P13569-3; Sequence=VSP_022124, VSP_022125; Expressed in the respiratory airway, including bronchial epithelium, and in the female reproductive tract, including oviduct (at protein level) (PubMed:22207244, PubMed:15716351). Detected in pancreatic intercalated ducts in the exocrine tissue, on epithelial cells in intralobular striated ducts in sublingual salivary glands, on apical membranes of crypt cells throughout the small and large intestine, and on the reabsorptive duct in eccrine sweat glands (PubMed:1284548, PubMed:28130590). Detected on the equatorial segment of the sperm head (at protein level) (PubMed:19923167). Detected in nasal and bronchial superficial epithelium (PubMed:15716351). Expressed by the central cells on the sebaceous glands, dermal adipocytes and, at lower levels, by epithelial cells (PubMed:28130590). Binds and hydrolyzes ATP via the two cytoplasmic ABC transporter nucleotide-binding domains (PubMed:15284228). The two ATP- binding domains interact with each other, forming a head-to-tail dimer (PubMed:17036051). Normal ATPase activity requires interaction between the two domains (PubMed:15284228). The first ABC transporter nucleotide-binding domain has no ATPase activity by itself (By similarity). The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, NHERF1/EBP50 complex. The R region is intrinsically disordered (PubMed:10792060, PubMed:17660831). It mediates channel activation when it is phosphorylated, but not in the absence of phosphorylation (PubMed:10792060). N-glycosylated. Phosphorylated; cAMP treatment promotes phosphorylation and activates the channel (PubMed:12588899, PubMed:17036051, PubMed:8910473). Dephosphorylation decreases the ATPase activity (in vitro) (PubMed:8910473). Phosphorylation at PKA sites activates the channel (PubMed:10792060, PubMed:12519745, PubMed:12588899, PubMed:25330774). Phosphorylation at PKC sites enhances the response to phosphorylation by PKA (PubMed:12588899). Phosphorylated by AMPK; this inhibits channel activity (PubMed:12519745). Ubiquitinated, leading to its degradation in the lysosome (PubMed:19398555, PubMed:23818989). Deubiquitination by USP10 in early endosomes enhances its endocytic recycling to the cell membrane (PubMed:19398555). Ubiquitinated by RNF185 during ER stress (PubMed:24019521). Ubiquitinated by MARCHF2 (PubMed:23818989). Cystic fibrosis (CF) [MIM:219700]: A common generalized disorder of the exocrine glands which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes. It is the most common genetic disease in Caucasians, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. te=The disease is caused by variants affecting the gene represented in this entry. There is some evidence that the functional defect caused by the most common variant Phe-508 DEL can be corrected by the binding to the snake phospholipase A2 crotoxin basic subunit CB. This toxin both disrupts the Phe-508 DEL-cytokeratin 8 complex, allowing for the escape from degradation, and increases the chloride channel current (PubMed:27241308). Congenital bilateral absence of the vas deferens (CBAVD) [MIM:277180]: An autosomal recessive disease characterized by vas deferens aplasia resulting in azoospermia and male infertility. CBAVD may occur in isolation or as a manifestation of cystic fibrosis. te=The disease is caused by variants affecting the gene represented in this entry. [Isoform 2]: Exon 9 splicing depends upon 2 polymorphic tracts within intron 8, a T(n) tract and TG(n) tract, where the number of T and/or TG repeats affect the extent of correct splicing of exon 9. Low numbers of T residues and high numbers of TG repeats give rise to less efficient splicing. Transcripts that lack exon 9 sequences fail to mature. Causes congenital bilateral absence of the vas deferens (CBAVD). [Isoform 3]: Alternative acceptor site favored by mutation in an exonic splicing enhancer (ESE). Causes cystic fibrosis (CF). Belongs to the ABC transporter superfamily. ABCC family. CFTR transporter (TC 3.A.1.202) subfamily. Name=Wikipedia; Note=CFTR entry; URL="https://en.wikipedia.org/wiki/Cystic_fibrosis_transmembrane_conductance_regulator"; Name=ABCMdb; Note=Database for mutations in ABC proteins; URL="http://abcm2.hegelab.org/search"; nucleotide binding chloride channel activity channel-conductance-controlling ATPase activity protein binding ATP binding nucleus cytoplasm lysosomal membrane endosome early endosome endoplasmic reticulum endoplasmic reticulum membrane cytosol plasma membrane integral component of plasma membrane cholesterol biosynthetic process ion transport chloride transport vesicle docking involved in exocytosis cell surface endosome membrane bicarbonate transmembrane transporter activity chloride transmembrane transporter activity bicarbonate transport membrane integral component of membrane apical plasma membrane protein deubiquitination isomerase activity ATPase activity chloride channel regulator activity chloride channel inhibitor activity enzyme binding PDZ domain binding cholesterol transport Golgi-associated vesicle membrane clathrin-coated vesicle membrane early endosome membrane macromolecular complex chloride channel complex response to endoplasmic reticulum stress transepithelial water transport positive regulation of insulin secretion involved in cellular response to glucose stimulus ATPase activity, coupled to transmembrane movement of substances positive regulation of exocytosis sperm capacitation multicellular organismal water homeostasis chaperone binding intracellular pH elevation recycling endosome recycling endosome membrane transmembrane transport membrane hyperpolarization membrane organization cellular response to cAMP positive regulation of cyclic nucleotide-gated ion channel activity chloride transmembrane transport positive regulation of voltage-gated chloride channel activity cellular response to forskolin uc003vjd.1 uc003vjd.2 uc003vjd.3 uc003vjd.4 uc003vjd.5 
ENST00000003100.13 CYP51A1 ENST00000003100.13 cytochrome P450 family 51 subfamily A member 1, transcript variant 1 (from RefSeq NM_000786.4) A0A0C4DFL7 A4D1F8 B2RAI4 B4DJ55 CP51A_HUMAN CYP51 CYP51A1 ENST00000003100.1 ENST00000003100.10 ENST00000003100.11 ENST00000003100.12 ENST00000003100.2 ENST00000003100.3 ENST00000003100.4 ENST00000003100.5 ENST00000003100.6 ENST00000003100.7 ENST00000003100.8 ENST00000003100.9 NM_000786 O00770 O00772 Q16784 Q16850 Q8N1A8 Q99868 uc003ulm.1 uc003ulm.2 uc003ulm.3 uc003ulm.4 uc003ulm.5 uc003ulm.6 This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This endoplasmic reticulum protein participates in the synthesis of cholesterol by catalyzing the removal of the 14alpha-methyl group from lanosterol. Homologous genes are found in all three eukaryotic phyla, fungi, plants, and animals, suggesting that this is one of the oldest cytochrome P450 genes. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009]. Sterol 14alpha-demethylase that plays a critical role in the cholesterol biosynthesis pathway, being cholesterol the major sterol component in mammalian membranes as well as a precursor for bile acid and steroid hormone synthesis (PubMed:8619637, PubMed:9559662, PubMed:20149798). Cytochrome P450 monooxygenase that catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of sterols such as lanosterol (lanosta-8,24-dien-3beta-ol) and 24,25- dihydrolanosterol (DHL) in the form of formate, and converts the sterols to 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol and 4,4- dimethyl-8,14-cholestadien-3beta-ol, respectively, which are intermediates of cholesterol biosynthesis (PubMed:8619637, PubMed:9559662, PubMed:20149798). Can also demethylate substrates not intrinsic to mammals, such as eburicol (24-methylene-24,25- dihydrolanosterol), but at a lower rate than DHL (PubMed:9559662). Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH-- hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence= Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence=; Reaction=24,25-dihydrolanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:45960, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78904; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45961; Evidence=; Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence=; Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH-- hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence=; Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence=; Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32- hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence=; Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence=; Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence=; Reaction=24,25-dihydrolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxy-24,25-dihydrolanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75079, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87057; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75080; Evidence=; Reaction=32-hydroxy-24,25-dihydrolanosterol + O2 + reduced [NADPH-- hemoprotein reductase] = 32-oxo-24,25-dihydrolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75087, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87057, ChEBI:CHEBI:87060; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75088; Evidence=; Reaction=32-oxo-24,25-dihydrolanosterol + O2 + reduced [NADPH-- hemoprotein reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75083, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78904, ChEBI:CHEBI:87060; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75084; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Inhibited by azalanstat. Inhibited by azole antifungal agents ketoconazole, itraconazole and fluconazole. Kinetic parameters: KM=29 uM for lanosterol ; KM=27 uM for 24,25-dihydrolanosterol ; KM=32 uM for eburicol ; KM=32 uM for obtusifoliol ; Vmax=0.18 nmol/min/nmol enzyme towards lanosterol ; Vmax=0.5 nmol/min/nmol enzyme towards 24,25-dihydrolanosterol ; Vmax=0.22 nmol/min/nmol enzyme towards eburicol ; Vmax=0.44 nmol/min/nmol enzyme towards obtusifoliol ; Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. Endoplasmic reticulum membrane ; Single-pass membrane protein Microsome membrane ; Single-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q16850-1; Sequence=Displayed; Name=2; IsoId=Q16850-2; Sequence=VSP_037413; Ubiquitously expressed with highest levels in testis, ovary, adrenal, prostate, liver, kidney and lung. Belongs to the cytochrome P450 family. It is uncertain whether Met-1 or Met-7 is the initiator. Sequence=AAC50951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; monooxygenase activity iron ion binding endoplasmic reticulum endoplasmic reticulum membrane plasma membrane lipid metabolic process steroid biosynthetic process cholesterol biosynthetic process steroid metabolic process cholesterol metabolic process sterol 14-demethylase activity membrane integral component of membrane sterol metabolic process sterol biosynthetic process oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen heme binding organelle membrane cholesterol biosynthetic process via 24,25-dihydrolanosterol negative regulation of protein catabolic process intracellular membrane-bounded organelle regulation of cholesterol biosynthetic process metal ion binding negative regulation of protein secretion oxidation-reduction process demethylation negative regulation of beta-amyloid clearance uc003ulm.1 uc003ulm.2 uc003ulm.3 uc003ulm.4 uc003ulm.5 uc003ulm.6 
ENST00000004103.8 TMEM176A ENST00000004103.8 transmembrane protein 176A (from RefSeq NM_018487.3) D3DX00 ENST00000004103.1 ENST00000004103.2 ENST00000004103.3 ENST00000004103.4 ENST00000004103.5 ENST00000004103.6 ENST00000004103.7 HCA112 NM_018487 Q96HP8 Q9NYC7 T176A_HUMAN uc003whx.1 uc003whx.2 uc003whx.3 Interacts with MCOLN2. Q96HP8; P11912: CD79A; NbExp=3; IntAct=EBI-2800645, EBI-7797864; Q96HP8; Q9HA82: CERS4; NbExp=3; IntAct=EBI-2800645, EBI-2622997; Q96HP8; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-2800645, EBI-712073; Q96HP8; O95279: KCNK5; NbExp=3; IntAct=EBI-2800645, EBI-3934936; Q96HP8; Q99732: LITAF; NbExp=3; IntAct=EBI-2800645, EBI-725647; Q96HP8; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2800645, EBI-373355; Q96HP8; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-2800645, EBI-3923617; Q96HP8; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-2800645, EBI-10192441; Q96HP8; Q9BSN4: SCD5; NbExp=3; IntAct=EBI-2800645, EBI-13385260; Q96HP8; O95470: SGPL1; NbExp=3; IntAct=EBI-2800645, EBI-1046170; Q96HP8; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2800645, EBI-6268651; Q96HP8; Q3YBM2: TMEM176B; NbExp=3; IntAct=EBI-2800645, EBI-2821479; Q96HP8; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2800645, EBI-6447886; Membrane ; Multi-pass membrane protein Belongs to the TMEM176 family. membrane integral component of membrane negative regulation of dendritic cell differentiation uc003whx.1 uc003whx.2 uc003whx.3 
ENST00000004982.6 HSPB6 ENST00000004982.6 heat shock protein family B (small) member 6 (from RefSeq NM_144617.3) ENST00000004982.1 ENST00000004982.2 ENST00000004982.3 ENST00000004982.4 ENST00000004982.5 HEL55 NM_144617 V9HWB6 V9HWB6_HUMAN uc002obn.1 uc002obn.2 uc002obn.3 uc002obn.4 uc002obn.5 This locus encodes a heat shock protein. The encoded protein likely plays a role in smooth muscle relaxation. [provided by RefSeq, Jan 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK056951.1, SRR3476690.1067911.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968189 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000004982.6/ ENSP00000004982.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Nucleus Belongs to the small heat shock protein (HSP20) family. structural constituent of eye lens regulation of muscle contraction negative regulation of cardiac muscle cell apoptotic process protein homodimerization activity uc002obn.1 uc002obn.2 uc002obn.3 uc002obn.4 uc002obn.5 
ENST00000005178.6 PDK4 ENST00000005178.6 pyruvate dehydrogenase kinase 4 (from RefSeq NM_002612.4) ENST00000005178.1 ENST00000005178.2 ENST00000005178.3 ENST00000005178.4 ENST00000005178.5 NM_002612 PDHK4 PDK4_HUMAN Q16654 uc003uoa.1 uc003uoa.2 uc003uoa.3 uc003uoa.4 uc003uoa.5 This gene is a member of the PDK/BCKDK protein kinase family and encodes a mitochondrial protein with a histidine kinase domain. This protein is located in the matrix of the mitrochondria and inhibits the pyruvate dehydrogenase complex by phosphorylating one of its subunits, thereby contributing to the regulation of glucose metabolism. Expression of this gene is regulated by glucocorticoids, retinoic acid and insulin. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660803.60745.1, SRR1660805.157673.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000005178.6/ ENSP00000005178.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism. Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]; Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2; Evidence=; Homodimer. Interacts with the pyruvate dehydrogenase complex subunit DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). Q16654; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-2861674, EBI-742388; Mitochondrion matrix. Ubiquitous; highest levels of expression in heart and skeletal muscle. Up-regulated by prolonged fasting, in glucose-deprived cells and in response to a high-fat diet. Down-regulated by insulin. Up- regulated by PPARD. Belongs to the PDK/BCKDK protein kinase family. nucleotide binding protein kinase activity pyruvate dehydrogenase (acetyl-transferring) kinase activity ATP binding mitochondrion mitochondrial matrix carbohydrate metabolic process glucose metabolic process protein phosphorylation regulation of pH insulin receptor signaling pathway cellular response to starvation regulation of acetyl-CoA biosynthetic process from pyruvate regulation of cellular ketone metabolic process regulation of glucose metabolic process kinase activity phosphorylation transferase activity regulation of fatty acid biosynthetic process glucose homeostasis response to starvation regulation of bone resorption regulation of fatty acid oxidation cellular response to fatty acid reactive oxygen species metabolic process negative regulation of anoikis uc003uoa.1 uc003uoa.2 uc003uoa.3 uc003uoa.4 uc003uoa.5 
ENST00000005180.9 CCL26 ENST00000005180.9 C-C motif chemokine ligand 26, transcript variant 2 (from RefSeq NM_001371938.1) A0N0Q5 CCL26 CCL26_HUMAN ENST00000005180.1 ENST00000005180.2 ENST00000005180.3 ENST00000005180.4 ENST00000005180.5 ENST00000005180.6 ENST00000005180.7 ENST00000005180.8 NM_001371938 Q52LV8 Q9Y258 SCYA26 UNQ216/PRO242 uc064emt.1 uc064emt.2 This gene is one of two Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 7. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity for normal peripheral blood eosinophils and basophils. The product of this gene is one of three related chemokines that specifically activate chemokine receptor CCR3. This chemokine may contribute to the eosinophil accumulation in atopic diseases. [provided by RefSeq, Jul 2008]. Chemoattractant for eosinophils and basophils (PubMed:10415065, PubMed:10488147). Acts as a ligand for C-C chemokine receptor CCR3 which triggers Ca(2+) mobilization in eosinophils (PubMed:10415065, PubMed:10488147, PubMed:11425309). Also acts as a ligand for CX3C chemokine receptor CX3CR1, inducing cell chemotaxis (PubMed:20974991). Monomer. Q9Y258; Q99616: CCL13; NbExp=2; IntAct=EBI-7783416, EBI-725342; Q9Y258; Q92583: CCL17; NbExp=2; IntAct=EBI-7783416, EBI-16640146; Q9Y258; O00585: CCL21; NbExp=2; IntAct=EBI-7783416, EBI-953695; Q9Y258; Q9NRJ3: CCL28; NbExp=2; IntAct=EBI-7783416, EBI-7783254; Q9Y258; P13501: CCL5; NbExp=4; IntAct=EBI-7783416, EBI-2848366; Q9Y258; P02778: CXCL10; NbExp=2; IntAct=EBI-7783416, EBI-7815386; Q9Y258; O14625: CXCL11; NbExp=2; IntAct=EBI-7783416, EBI-2871971; Q9Y258; P48061: CXCL12; NbExp=2; IntAct=EBI-7783416, EBI-3913254; Q9Y258; O95715: CXCL14; NbExp=2; IntAct=EBI-7783416, EBI-2798068; Q9Y258; Q07325: CXCL9; NbExp=2; IntAct=EBI-7783416, EBI-3911467; Q9Y258; P26367: PAX6; NbExp=3; IntAct=EBI-7783416, EBI-747278; Q9Y258; P02776: PF4; NbExp=3; IntAct=EBI-7783416, EBI-2565740; Q9Y258; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-7783416, EBI-10243654; Q9Y258; P47992: XCL1; NbExp=2; IntAct=EBI-7783416, EBI-10209901; Secreted Ubiquitously expressed at low levels in various tissues including heart and ovary. Belongs to the intercrine beta (chemokine CC) family. Name=Wikipedia; Note=CCL26 entry; URL="https://en.wikipedia.org/wiki/CCL26"; positive regulation of endothelial cell proliferation monocyte chemotaxis cytokine activity protein binding extracellular region extracellular space chemotaxis inflammatory response immune response signal transduction G-protein coupled receptor signaling pathway cell-cell signaling chemokine activity T cell chemotaxis positive regulation of cell migration neutrophil chemotaxis positive regulation of actin filament polymerization CCR3 chemokine receptor binding positive regulation of GTPase activity receptor agonist activity CCR chemokine receptor binding lymphocyte chemotaxis positive regulation of chemotaxis chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor uc064emt.1 uc064emt.2 
ENST00000005257.7 RALA ENST00000005257.7 RAS like proto-oncogene A (from RefSeq NM_005402.4) A4D1W3 ENST00000005257.1 ENST00000005257.2 ENST00000005257.3 ENST00000005257.4 ENST00000005257.5 ENST00000005257.6 NM_005402 P11233 RAL RALA_HUMAN uc003thd.1 uc003thd.2 uc003thd.3 uc003thd.4 uc003thd.5 The product of this gene belongs to the small GTPase superfamily, Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors. This gene encodes a low molecular mass ras-like GTP-binding protein that shares about 50% similarity with other ras proteins. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.815446.1, SRR1803612.213239.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000005257.7/ ENSP00000005257.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors (PubMed:18756269, PubMed:19306925, PubMed:20005108, PubMed:21822277, PubMed:30500825). Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. The RALA- exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling (PubMed:20005108). Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage- independent proliferation of transformed cells (PubMed:19306925). During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody (PubMed:18756269). During mitosis, also controls mitochondrial fission by recruiting to the mitochondrion RALBP1, which mediates the phosphorylation and activation of DNM1L by the mitotic kinase cyclin B- CDK1 (PubMed:21822277). Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence=; Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide- exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP). Interacts (via effector domain) with RALBP1; during mitosis, recruits RALBP1 to the mitochondrion where it promotes DNM1L phosphorylation and mitochondrial fission (PubMed:7673236, PubMed:21822277). Interacts with EXOC2/Sec5 and EXOC8/Exo84; binding to EXOC2 and EXOC8 is mutually exclusive (PubMed:14525976, PubMed:18756269, PubMed:15920473). Interacts with Clostridium exoenzyme C3 (PubMed:16177825, PubMed:15809419). Interacts with RALGPS1 (PubMed:10747847). Interacts with LPAR1 and LPAR2. Interacts with GRK2 in response to LPAR1 activation. RALA and GRK2 binding to LPAR1 is mutually exclusive (PubMed:19306925). Interacts with CDC42 (By similarity). P11233; P01112: HRAS; NbExp=2; IntAct=EBI-1036803, EBI-350145; P11233; P30154: PPP2R1B; NbExp=6; IntAct=EBI-1036803, EBI-357094; P11233; Q15311: RALBP1; NbExp=6; IntAct=EBI-1036803, EBI-749285; P11233; O54921: Exoc2; Xeno; NbExp=2; IntAct=EBI-1036803, EBI-1036795; Cell membrane ipid-anchor ; Cytoplasmic side. Cleavage furrow Midbody, Midbody ring Mitochondrion Note=Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles (PubMed:19306925). May colocalize with CNTRL/centriolin at the midbody ring (PubMed:16213214). However, localization at the midbody at late cytokinesis was not confirmed (PubMed:18756269). Relocalizes to the mitochondrion during mitosis where it regulates mitochondrial fission (PubMed:21822277). Activated in an LPA-dependent manner by LPAR1 and in an LPA- independent manner by LPAR2. Phosphorylated. Phosphorylation at Ser-194 by AURKA/Aurora kinase A, during mitosis, induces RALA localization to the mitochondrion where it regulates mitochondrial fission. Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant do not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs). (Microbial infection) Glucosylated at Thr-46 by P.sordellii toxin TcsL from strain 6018 (PubMed:8858106). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form (PubMed:8858106). Not glucosylated by TcsL from strain VPI 9048 (PubMed:8858106). Hiatt-Neu-Cooper neurodevelopmental syndrome (HINCONS) [MIM:619311]: An autosomal dominant neurodevelopmental disorder characterized by global developmental delay, delayed walking or inability to walk, impaired intellectual development, poor or absent speech, axial hypotonia, and facial dysmorphism. Additional variable features may include seizures, autistic or behavioral abnormalities, and brain abnormalities. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the small GTPase superfamily. Ras family. nucleotide binding neural tube closure GTPase activity protein binding GTP binding plasma membrane focal adhesion exocytosis chemotaxis cell cycle signal transduction Ras protein signal transduction cell surface membrane myosin binding regulation of exocytosis GDP binding cytoplasmic vesicle membrane actin cytoskeleton reorganization ubiquitin protein ligase binding Edg-2 lysophosphatidic acid receptor binding cleavage furrow interleukin-12-mediated signaling pathway ATPase binding cell division positive regulation of filopodium assembly membrane raft localization membrane organization extracellular exosome Flemming body endocytic vesicle uc003thd.1 uc003thd.2 uc003thd.3 uc003thd.4 uc003thd.5 
ENST00000005259.9 BCAP29 ENST00000005259.9 B cell receptor associated protein 29, transcript variant 23 (from RefSeq NR_163938.1) BAP29 BAP29_HUMAN ENST00000005259.1 ENST00000005259.2 ENST00000005259.3 ENST00000005259.4 ENST00000005259.5 ENST00000005259.6 ENST00000005259.7 ENST00000005259.8 G5E9L4 NR_163938 O95003 Q9UHQ4 uc003vej.1 uc003vej.2 uc003vej.3 uc003vej.4 May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8- mediated apoptosis (By similarity). Homodimer (PubMed:25327138). Heterodimer with BCAP31. Binds CASP8 (isoform 9) as a complex containing BCAP31, BCAP29, BCL2 and/or BCL2L1. Interacts with VAMP3, VAMP1 and membrane IgD immunoglobulins. May interact with ACTG1 and non-muscle myosin II (By similarity). Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UHQ4-1; Sequence=Displayed; Name=2; IsoId=Q9UHQ4-2; Sequence=VSP_047096; Belongs to the BCAP29/BCAP31 family. osteoblast differentiation endoplasmic reticulum endoplasmic reticulum membrane integral component of plasma membrane intracellular protein transport ER to Golgi vesicle-mediated transport apoptotic process protein transport membrane integral component of membrane vesicle-mediated transport protein localization to endoplasmic reticulum exit site uc003vej.1 uc003vej.2 uc003vej.3 uc003vej.4 
ENST00000005260.9 BAIAP2L1 ENST00000005260.9 BAR/IMD domain containing adaptor protein 2 like 1 (from RefSeq NM_018842.5) A4D268 BI2L1_HUMAN ENST00000005260.1 ENST00000005260.2 ENST00000005260.3 ENST00000005260.4 ENST00000005260.5 ENST00000005260.6 ENST00000005260.7 ENST00000005260.8 IRTKS NM_018842 Q75L21 Q75L22 Q96CV4 Q9H5F5 Q9UHR4 Q9Y2M8 uc003upj.1 uc003upj.2 uc003upj.3 uc003upj.4 uc003upj.5 This gene encodes a member of the IMD (IRSp53/MIM homology domain) family. Members of this family can be subdivided in two groups, the IRSp53-like and MIM-like, based on the presence or absence of the SH3 (Src homology 3) domain. The protein encoded by this gene contains a conserved IMD, also known as F-actin bundling domain, at the N-terminus, and a canonical SH3 domain near the C-terminus, so it belongs to the IRSp53-like group. This protein is the substrate for insulin receptor tyrosine kinase and binds to the small GTPase Rac. It is involved in signal transduction pathways that link deformation of the plasma membrane and remodeling of the actin cytoskeleton. It also promotes actin assembly and membrane protrusions when overexpressed in mammalian cells, and is essential to the formation of a potent actin assembly complex during EHEC (Enterohemorrhagic Escherichia coli) pedestal formation. [provided by RefSeq, Oct 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.72776.1, AF119666.2 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000005260.9/ ENSP00000005260.8 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Interacts with RAC1. Binds to F-actin. Interacts with FASLG. Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Interacts with E.coli intimin receptor Tir. Q9UHR4; O95817: BAG3; NbExp=3; IntAct=EBI-2483278, EBI-747185; Q9UHR4; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-2483278, EBI-9092016; Q9UHR4; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2483278, EBI-3867333; Q9UHR4; Q12929: EPS8; NbExp=4; IntAct=EBI-2483278, EBI-375576; Q9UHR4; O43813: LANCL1; NbExp=3; IntAct=EBI-2483278, EBI-3046631; Q9UHR4; P0DJ88: espF(U); Xeno; NbExp=9; IntAct=EBI-2483278, EBI-10039462; Q9UHR4; Q7DB77: tir; Xeno; NbExp=3; IntAct=EBI-2483278, EBI-6480811; Cytoplasm, cytoskeleton Note=Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites. The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity). Phosphorylated on tyrosine in response to insulin. Sequence=AAD20937.1; Type=Erroneous gene model prediction; Evidence=; Sequence=AAS07549.1; Type=Erroneous initiation; Evidence=; Sequence=BAB15671.1; Type=Erroneous initiation; Evidence=; actin binding protein binding nucleoplasm cytoplasm cytosol cytoskeleton plasma membrane cell-cell adherens junction plasma membrane organization response to bacterium actin cytoskeleton regulation of actin filament polymerization positive regulation of actin filament polymerization regulation of insulin receptor signaling pathway actin filament bundle assembly actin crosslink formation extracellular exosome proline-rich region binding cell-cell adhesion cadherin binding involved in cell-cell adhesion positive regulation of actin cytoskeleton reorganization uc003upj.1 uc003upj.2 uc003upj.3 uc003upj.4 uc003upj.5 
ENST00000005284.4 CACNG3 ENST00000005284.4 calcium voltage-gated channel auxiliary subunit gamma 3 (from RefSeq NM_006539.4) CCG3_HUMAN ENST00000005284.1 ENST00000005284.2 ENST00000005284.3 NM_006539 O60359 uc002dmf.1 uc002dmf.2 uc002dmf.3 uc002dmf.4 uc002dmf.5 The protein encoded by this gene is a type I transmembrane AMPA receptor regulatory protein (TARP). TARPs regulate both trafficking and channel gating of the AMPA receptors. This gene is part of a functionally diverse eight-member protein subfamily of the PMP-22/EMP/MP20 family. This gene is a susceptibility locus for childhood absence epilepsy. [provided by RefSeq, Dec 2010]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. ##Evidence-Data-START## Transcript exon combination :: SRR1803615.263009.1, SRR1803613.49646.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000005284.4/ ENSP00000005284.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Regulates the trafficking to the somatodendritic compartment and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. The L-type calcium channel is composed of five subunits: alpha-1, alpha-2/delta, beta and gamma. Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with AP4M1 and GRIA1; associates GRIA1 with the adaptor protein complex 4 (AP-4) to target GRIA1 to the somatodendritic compartment of neurons. Membrane ; Multi-pass membrane protein Note=Displays a somatodendritic localization and is excluded from axons in neurons. Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily. voltage-gated ion channel activity voltage-gated calcium channel activity calcium channel activity plasma membrane voltage-gated calcium channel complex protein targeting ion transport calcium ion transport protein localization membrane integral component of membrane transmission of nerve impulse PDZ domain binding dendrite endocytic vesicle membrane AMPA glutamate receptor complex regulation of ion transmembrane transport ionotropic glutamate receptor binding somatodendritic compartment excitatory synapse cardiac conduction calcium ion transmembrane transport postsynaptic density membrane neurotransmitter receptor transport, postsynaptic endosome to lysosome postsynaptic neurotransmitter receptor diffusion trapping glutamatergic synapse integral component of postsynaptic density membrane neurotransmitter receptor internalization neurotransmitter receptor localization to postsynaptic specialization membrane regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity uc002dmf.1 uc002dmf.2 uc002dmf.3 uc002dmf.4 uc002dmf.5 
ENST00000005340.10 DVL2 ENST00000005340.10 dishevelled segment polarity protein 2 (from RefSeq NM_004422.3) D3DTN3 DVL2_HUMAN ENST00000005340.1 ENST00000005340.2 ENST00000005340.3 ENST00000005340.4 ENST00000005340.5 ENST00000005340.6 ENST00000005340.7 ENST00000005340.8 ENST00000005340.9 NM_004422 O14641 Q53XM0 uc002gez.1 uc002gez.2 uc002gez.3 This gene encodes a member of the dishevelled (dsh) protein family. The vertebrate dsh proteins have approximately 40% amino acid sequence similarity with Drosophila dsh. This gene encodes a 90-kD protein that undergoes posttranslational phosphorylation to form a 95-kD cytoplasmic protein, which may play a role in the signal transduction pathway mediated by multiple Wnt proteins. The mechanisms of dishevelled function in Wnt signaling are likely to be conserved among metazoans. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC014844.1, SRR1660803.149730.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000005340.10/ ENSP00000005340.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Interacts through its PDZ domain with the C-terminal regions of VANGL1 and VANGL2. Interacts with Rac. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 (By similarity). Can form large oligomers (via DIX domain). Interacts (via DIX domain) with DIXDC1 (via DIX domain). Interacts (via DEP domain) with AP2M1 and the AP-2 complex (By similarity). Interacts with DACT1 and FAM105B/otulin. Interacts with DCDC2. Interacts (when phosphorylated) with FOXK1 and FOXK2; the interaction induces DVL2 nuclear translocation (PubMed:25805136). Interacts with MAPK15 (By similarity). Interacts with PKD1 (via extracellular domain) (PubMed:27214281). Interacts with LMBR1L (By similarity). O14641; P25054: APC; NbExp=2; IntAct=EBI-740850, EBI-727707; O14641; O15169: AXIN1; NbExp=3; IntAct=EBI-740850, EBI-710484; O14641; P28329-3: CHAT; NbExp=3; IntAct=EBI-740850, EBI-25837549; O14641; Q5R2U3: CK1E; NbExp=2; IntAct=EBI-740850, EBI-9106301; O14641; P49674: CSNK1E; NbExp=4; IntAct=EBI-740850, EBI-749343; O14641; Q9NYF0: DACT1; NbExp=6; IntAct=EBI-740850, EBI-3951744; O14641; Q155Q3: DIXDC1; NbExp=2; IntAct=EBI-740850, EBI-1104700; O14641; O14641: DVL2; NbExp=4; IntAct=EBI-740850, EBI-740850; O14641; P22607: FGFR3; NbExp=3; IntAct=EBI-740850, EBI-348399; O14641; P01112: HRAS; NbExp=3; IntAct=EBI-740850, EBI-350145; O14641; Q5S007: LRRK2; NbExp=5; IntAct=EBI-740850, EBI-5323863; O14641; P53350: PLK1; NbExp=2; IntAct=EBI-740850, EBI-476768; O14641; P57078: RIPK4; NbExp=4; IntAct=EBI-740850, EBI-4422308; O14641; Q96CG3: TIFA; NbExp=3; IntAct=EBI-740850, EBI-740711; O14641; Q08117-2: TLE5; NbExp=3; IntAct=EBI-740850, EBI-11741437; O14641; P04637: TP53; NbExp=6; IntAct=EBI-740850, EBI-366083; O14641; Q14134: TRIM29; NbExp=5; IntAct=EBI-740850, EBI-702370; O14641; Q96RL1: UIMC1; NbExp=4; IntAct=EBI-740850, EBI-725300; O14641; Q9GZV5: WWTR1; NbExp=4; IntAct=EBI-740850, EBI-747743; O14641; P49910: ZNF165; NbExp=3; IntAct=EBI-740850, EBI-741694; O14641; Q9Z101: Pard6a; Xeno; NbExp=6; IntAct=EBI-740850, EBI-81732; O14641; A2A5Z6: Smurf2; Xeno; NbExp=8; IntAct=EBI-740850, EBI-2348309; Cell membrane ; Peripheral membrane protein ; Cytoplasmic side Cytoplasm, cytosol Cytoplasmic vesicle Nucleus Note=Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytoplasmic puncta (By similarity). Interaction with FOXK1 and FOXK2 induces nuclear translocation (PubMed:25805136). The DIX domain mediates homooligomerization. Phosphorylated by CSNK1D (PubMed:21422228, PubMed:9192851). WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (PubMed:25805136). Belongs to the DSH family. neural tube closure positive regulation of protein phosphorylation heart morphogenesis outflow tract morphogenesis frizzled binding protein binding nucleus nucleoplasm cytoplasm cytosol plasma membrane transcription from RNA polymerase II promoter multicellular organism development segment specification heart development membrane Wnt signaling pathway aggresome lateral plasma membrane nuclear body protein kinase binding protein domain specific binding convergent extension involved in neural plate elongation clathrin-coated vesicle protein binding, bridging cytoplasmic vesicle cellular protein localization segmentation hippo signaling intracellular signal transduction non-canonical Wnt signaling pathway identical protein binding positive regulation of JUN kinase activity positive regulation of GTPase activity protein self-association canonical Wnt signaling pathway involved in regulation of cell proliferation apical part of cell clathrin-coated endocytic vesicle positive regulation of transcription, DNA-templated Rac GTPase binding positive regulation of sequence-specific DNA binding transcription factor activity convergent extension involved in organogenesis canonical Wnt signaling pathway Wnt signaling pathway, planar cell polarity pathway membrane organization positive regulation of protein tyrosine kinase activity negative regulation of canonical Wnt signaling pathway cochlea morphogenesis planar cell polarity pathway involved in neural tube closure beta-catenin destruction complex disassembly uc002gez.1 uc002gez.2 uc002gez.3 
ENST00000005386.8 RPAP3 ENST00000005386.8 RNA polymerase II associated protein 3, transcript variant 1 (from RefSeq NM_024604.3) B4DRW9 ENST00000005386.1 ENST00000005386.2 ENST00000005386.3 ENST00000005386.4 ENST00000005386.5 ENST00000005386.6 ENST00000005386.7 NM_024604 Q6PHR5 Q9H6T3 RPAP3_HUMAN uc001rpr.1 uc001rpr.2 uc001rpr.3 uc001rpr.4 uc001rpr.5 This gene encodes an RNA polymerase II-associated protein. The encoded protein may function in transcriptional regulation and may also regulate apoptosis. Alternatively spliced transcript variants have been described. [provided by RefSeq, Mar 2009]. Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. Tightly associated with the RNA polymerase II complex (PubMed:17643375). Component of the R2TP complex composed at least of RUVBL1, RUVBL2, RPAP3 and PIHD1 (PubMed:20864032). Component of the PAQosome complex which is responsible for the biogenesis of several protein complexes and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558). Interacts with PIH1D1 (PubMed:21078300). Interacts with TSC1 and TSC2 (PubMed:28561026). Interacts with PRPF8 and EFTUD2 in a ZNHIT2- dependent manner (PubMed:28561026). Q9H6T3; Q96MX6: DNAAF10; NbExp=5; IntAct=EBI-356928, EBI-2434101; Q9H6T3; P07900: HSP90AA1; NbExp=6; IntAct=EBI-356928, EBI-296047; Q9H6T3; Q9UHV9: PFDN2; NbExp=2; IntAct=EBI-356928, EBI-359873; Q9H6T3; P54274: TERF1; NbExp=2; IntAct=EBI-356928, EBI-710997; Q9H6T3; O94763: URI1; NbExp=2; IntAct=EBI-356928, EBI-357067; Q9H6T3; Q9UBK9: UXT; NbExp=2; IntAct=EBI-356928, EBI-357355; Q9H6T3; Q98140: ORF24; Xeno; NbExp=2; IntAct=EBI-356928, EBI-14033488; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9H6T3-1; Sequence=Displayed; Name=2; IsoId=Q9H6T3-2; Sequence=VSP_027957; Name=3; IsoId=Q9H6T3-3; Sequence=VSP_044882; Belongs to the RPAP3 family. protein binding cytosol R2TP complex uc001rpr.1 uc001rpr.2 uc001rpr.3 uc001rpr.4 uc001rpr.5 
ENST00000005756.5 UPP2 ENST00000005756.5 uridine phosphorylase 2, transcript variant 1 (from RefSeq NM_173355.4) B3KV87 ENST00000005756.1 ENST00000005756.2 ENST00000005756.3 ENST00000005756.4 NM_173355 O95045 UPP2 UPP2_HUMAN uc002tzp.1 uc002tzp.2 uc002tzp.3 uc002tzp.4 uc002tzp.5 Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (PubMed:12849978, PubMed:21855639). Shows broad substrate specificity and can also accept deoxyuridine and other analogous compounds (PubMed:12849978). Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24389; Evidence=; Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1- phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22825; Evidence=; A conditional disulfide bridge can form within the protein that dislocates a critical phosphate-coordinating arginine Arg- 100 away from the active site, disabling the enzyme. Kinetic parameters: KM=76 uM for uridine ; KM=300 uM for deoxyuridine ; KM=73 uM for thymidine ; KM=24 uM for 5-fluorouridine ; KM=427 uM for 5-fluoro-2(')-deoxyuridine ; Vmax=4.0 nmol/min/ug enzyme toward uridine ; Vmax=1.2 nmol/min/ug enzyme toward deoxyuridine ; Vmax=0.18 nmol/min/ug enzyme toward thymidine ; Vmax=1.6 nmol/min/ug enzyme toward 5-fluorouridine ; Vmax=0.8 nmol/min/ug enzyme toward 5-fluoro-2(')-deoxyuridine ; Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1. Homodimer. O95045; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-10191025, EBI-747107; O95045; O95045: UPP2; NbExp=3; IntAct=EBI-10191025, EBI-10191025; O95045-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11528386, EBI-739832; O95045-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11528386, EBI-16439278; O95045-2; Q13084: MRPL28; NbExp=3; IntAct=EBI-11528386, EBI-723426; O95045-2; Q8IUQ4-2: SIAH1; NbExp=6; IntAct=EBI-11528386, EBI-11522811; O95045-2; A0A0S2Z6U5: UPP2; NbExp=3; IntAct=EBI-11528386, EBI-16432858; O95045-2; O95045-2: UPP2; NbExp=6; IntAct=EBI-11528386, EBI-11528386; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95045-1; Sequence=Displayed; Name=2; IsoId=O95045-2; Sequence=VSP_043756; Predominantly expressed in kidney. Belongs to the PNP/UDP phosphorylase family. Sequence=AAH33529.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; catalytic activity uridine phosphorylase activity protein binding cytoplasm cytosol nucleoside metabolic process nucleotide catabolic process transferase activity transferase activity, transferring glycosyl groups transferase activity, transferring pentosyl groups identical protein binding pyrimidine nucleoside salvage UMP salvage type III intermediate filament uridine metabolic process pyrimidine nucleoside catabolic process uc002tzp.1 uc002tzp.2 uc002tzp.3 uc002tzp.4 uc002tzp.5 
ENST00000005995.8 PRSS21 ENST00000005995.8 serine protease 21, transcript variant 5 (from RefSeq NR_073012.2) ENST00000005995.1 ENST00000005995.2 ENST00000005995.3 ENST00000005995.4 ENST00000005995.5 ENST00000005995.6 ENST00000005995.7 ESP1 NR_073012 Q9NS34 Q9P2V6 Q9Y6M0 TEST1 TEST_HUMAN UNQ266/PRO303 uc002crt.1 uc002crt.2 uc002crt.3 uc002crt.4 uc002crt.5 uc002crt.6 This gene encodes a cell-surface anchored serine protease, which is a member of the trypsin family of serine proteases. The encoded protein is predicted to be active on peptide linkages involving the carboxyl group of lysine or arginine. The encoded protein localizes to the cytoplasm and the plasma membrane of premeiotic testicular germ cells and may be involved in progression of testicular tumors of germ cell origin. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jul 2012]. Could regulate proteolytic events associated with testicular germ cell maturation. Q9Y6M0; P36952: SERPINB5; NbExp=7; IntAct=EBI-7054564, EBI-2371394; Cell membrane ; Lipid-anchor, GPI- anchor Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=L; IsoId=Q9Y6M0-1; Sequence=Displayed; Name=2; Synonyms=S; IsoId=Q9Y6M0-2; Sequence=VSP_005389; Name=3; IsoId=Q9Y6M0-3; Sequence=VSP_005390; Expressed predominantly in premeiotic testicular germ cells, mostly late pachytene and diplotene spermatocytes. Belongs to the peptidase S1 family. serine-type endopeptidase activity protein binding extracellular region extracellular space cytoplasm plasma membrane proteolysis spermatogenesis peptidase activity serine-type peptidase activity membrane hydrolase activity anchored component of membrane uc002crt.1 uc002crt.2 uc002crt.3 uc002crt.4 uc002crt.5 uc002crt.6 
ENST00000006015.4 HOXA11 ENST00000006015.4 homeobox A11 (from RefSeq NM_005523.6) A4D190 ENST00000006015.1 ENST00000006015.2 ENST00000006015.3 HOX1I HXA11_HUMAN NM_005523 P31270 uc003syx.1 uc003syx.2 uc003syx.3 uc003syx.4 uc003syx.5 In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. This gene is involved in the regulation of uterine development and is required for female fertility. Mutations in this gene can cause radio-ulnar synostosis with amegakaryocytic thrombocytopenia. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC040948.1, AK313921.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000006015.4/ ENSP00000006015.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Nucleus. Radioulnar synostosis with amegakaryocytic thrombocytopenia 1 (RUSAT1) [MIM:605432]: The syndrome consists of an unusual association of bone marrow failure and skeletal defects. Patients have the same skeletal defects, the proximal fusion of the radius and ulna, resulting in extremely limited pronation and supination of the forearm. Some patients have also symptomatic thrombocytopenia, with bruising and bleeding problems since birth, necessitating correction by bone marrow or umbilical-cord stem-cell transplantation. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the Abd-B homeobox family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40847/HOXA11"; RNA polymerase II transcription factor activity, sequence-specific DNA binding skeletal system development metanephros development branching involved in ureteric bud morphogenesis organ induction DNA binding nucleus nucleoplasm transcription factor complex regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development spermatogenesis single fertilization mesodermal cell fate specification male gonad development anatomical structure morphogenesis anterior/posterior pattern specification dorsal/ventral pattern formation proximal/distal pattern formation regulation of gene expression positive regulation of cell development embryonic limb morphogenesis regulation of chondrocyte differentiation positive regulation of chondrocyte differentiation macromolecular complex protein-DNA complex embryonic forelimb morphogenesis embryonic digit morphogenesis sequence-specific DNA binding positive regulation of transcription, DNA-templated developmental growth uterus development embryonic skeletal joint morphogenesis bone development cartilage development involved in endochondral bone morphogenesis uc003syx.1 uc003syx.2 uc003syx.3 uc003syx.4 uc003syx.5 
ENST00000006053.7 CX3CL1 ENST00000006053.7 C-X3-C motif chemokine ligand 1, transcript variant 1 (from RefSeq NM_002996.6) A-152E5.2 CX3CL1 ENST00000006053.1 ENST00000006053.2 ENST00000006053.3 ENST00000006053.4 ENST00000006053.5 ENST00000006053.6 FKN NM_002996 NTT O00672 P78423 SCYD1 X3CL1_HUMAN uc002eli.1 uc002eli.2 uc002eli.3 uc002eli.4 uc002eli.5 This gene belongs to the CX3C subgroup of chemokines, characterized by the number of amino acids located between the conserved cysteine residues. This is the only member of the CX3C subgroup, which contains three amino acids between cysteine residues, resulting in a Cys-X-X-X-Cys configuration. The encoded protein contains an extended mucin-like stalk with a chemokine domain on top, and exists in both a membrane-anchored form where it acts as a binding molecule, or, in soluble form, as a chemotactic cytokine. The mature form of this protein can be cleaved at the cell surface, yielding different soluble forms that can interact with the G-protein coupled receptor, C-X3-C motif chemokine receptor 1 gene product. This gene plays a role in a wide range of diseases, including cancer, vasculitis, neuropathies, atherosclerosis, inflammatory diseases, and in human immunodeficiency virus infections. [provided by RefSeq, Sep 2017]. Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1 (PubMed:9782118, PubMed:12055230, PubMed:23125415, PubMed:9931005, PubMed:21829356). The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:9024663, PubMed:9177350, PubMed:9782118, PubMed:12055230). Regulates leukocyte adhesion and migration processes at the endothelium (PubMed:9024663, PubMed:9177350). Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (PubMed:23125415, PubMed:24789099). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (PubMed:23125415, PubMed:24789099). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (PubMed:23125415, PubMed:24789099). [Processed fractalkine]: The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. [Fractalkine]: The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. (Microbial infection) Mediates the cytoadherence of erythrocytes infected with parasite P.falciparum (strain 3D7) with endothelial cells by interacting with P.falciparum CBP1 and CBP2 expressed at the surface of erythrocytes (PubMed:27653778). The adhesion prevents the elimination of infected erythrocytes by the spleen (Probable). Monomer (PubMed:9931005). Forms a ternary complex with CX3CR1 and ITGAV:ITGB3 or ITGA4:ITGB1 (PubMed:23125415). (Microbial infection) Interacts with pox virus crmD; this inhibits cell migration mediated by CX3CL1. (Microbial infection) Interacts (via N-terminus) with human cytomegalovirus (HHV-5) US28. (Microbial infection) Interacts with P.falciparum (strain 3D7) CBP1 and CBP2 (via their extracellular domains); the interaction mediates the adhesion of infected erythrocytes with endothelial cells. P78423; P05556: ITGB1; NbExp=2; IntAct=EBI-15188013, EBI-703066; P78423; P05106: ITGB3; NbExp=6; IntAct=EBI-15188013, EBI-702847; P78423; P69332: US28; Xeno; NbExp=4; IntAct=EBI-15188013, EBI-16147206; Cell membrane ; Single-pass type I membrane protein [Processed fractalkine]: Secreted Expressed in the seminal plasma, endometrial fluid and follicular fluid (at protein level). Small intestine, colon, testis, prostate, heart, brain, lung, skeletal muscle, kidney and pancreas. Most abundant in the brain and heart. By TNF and IL1/interleukin-1 in pulmonary endothelial cells and umbilical vein endothelial cells. A soluble short 95 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. O-glycosylated with core 1 or possibly core 8 glycans. Belongs to the intercrine delta family. Name=Wikipedia; Note=CX3CL1 entry; URL="https://en.wikipedia.org/wiki/CX3CL1"; microglial cell activation positive regulation of cell-matrix adhesion positive regulation of neuroblast proliferation leukocyte migration involved in inflammatory response monocyte chemotaxis response to ischemia receptor binding cytokine activity integrin binding protein binding extracellular region extracellular space plasma membrane chemotaxis defense response inflammatory response immune response cell adhesion G-protein coupled receptor signaling pathway cell-cell signaling aging chemokine activity positive regulation of cell proliferation cell surface negative regulation of cell-substrate adhesion positive regulation of neuron projection development membrane integral component of membrane neuron remodeling cytokine-mediated signaling pathway negative regulation of cell migration neutrophil chemotaxis leukocyte chemotaxis regulation of lipopolysaccharide-mediated signaling pathway CX3C chemokine receptor binding positive regulation of actin filament bundle assembly negative regulation of interleukin-1 alpha production negative regulation of interleukin-1 beta production negative regulation of interleukin-6 production negative regulation of tumor necrosis factor production positive regulation of transforming growth factor beta1 production integrin activation autocrine signaling chemoattractant activity wound healing cell projection neuron projection neuronal cell body negative regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of MAPK cascade positive regulation of GTPase activity cell body CXCR1 chemokine receptor binding positive regulation of angiogenesis positive regulation of transcription from RNA polymerase II promoter CCR chemokine receptor binding regulation of synaptic plasticity eosinophil chemotaxis macrophage chemotaxis lymphocyte chemotaxis perinuclear region of cytoplasm positive regulation of smooth muscle cell proliferation positive regulation of inflammatory response regulation of neurogenesis leukocyte adhesive activation positive chemotaxis positive regulation of calcium-independent cell-cell adhesion positive regulation of NF-kappaB transcription factor activity positive regulation of release of sequestered calcium ion into cytosol positive regulation of protein kinase B signaling angiogenesis involved in wound healing cell chemotaxis microglial cell proliferation neuron cellular homeostasis chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor cell-cell adhesion synapse disassembly negative regulation of glutamate receptor signaling pathway positive regulation of I-kappaB phosphorylation negative regulation of microglial cell activation negative regulation of tumor necrosis factor secretion negative regulation of neuron migration negative regulation of apoptotic signaling pathway negative regulation of extrinsic apoptotic signaling pathway in absence of ligand uc002eli.1 uc002eli.2 uc002eli.3 uc002eli.4 uc002eli.5 
ENST00000006658.11 SPATA20 ENST00000006658.11 spermatogenesis associated 20, transcript variant 1 (from RefSeq NM_022827.4) ENST00000006658.1 ENST00000006658.10 ENST00000006658.2 ENST00000006658.3 ENST00000006658.4 ENST00000006658.5 ENST00000006658.6 ENST00000006658.7 ENST00000006658.8 ENST00000006658.9 NM_022827 Q2TA99 Q2XUZ6 Q6P0P1 Q8TB22 Q8WVW3 Q9H747 SPT20_HUMAN uc002ird.1 uc002ird.2 uc002ird.3 uc002ird.4 uc002ird.5 May play a role in fertility regulation. Secreted Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q8TB22-1; Sequence=Displayed; Name=2; IsoId=Q8TB22-2; Sequence=VSP_023290; Name=3; IsoId=Q8TB22-3; Sequence=VSP_023288; Name=4; IsoId=Q8TB22-4; Sequence=VSP_023289, VSP_023291, VSP_023292; [Isoform 3]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. catalytic activity extracellular region multicellular organism development spermatogenesis cell differentiation uc002ird.1 uc002ird.2 uc002ird.3 uc002ird.4 uc002ird.5 
ENST00000006750.8 CD79B ENST00000006750.8 CD79b molecule, transcript variant 1 (from RefSeq NM_000626.4) B29 CD79B_HUMAN ENST00000006750.1 ENST00000006750.2 ENST00000006750.3 ENST00000006750.4 ENST00000006750.5 ENST00000006750.6 ENST00000006750.7 IGB NM_000626 P40259 Q53FS2 Q9BU06 uc002jdq.1 uc002jdq.2 uc002jdq.3 The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-beta protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]. Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation. Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains (PubMed:35981043). Interacts with LYN (By similarity). P40259; O43765: SGTA; NbExp=6; IntAct=EBI-2873732, EBI-347996; P40259; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2873732, EBI-744081; P40259-1; P40259-1: CD79B; NbExp=3; IntAct=EBI-15869023, EBI-15869023; Cell membrane; Single-pass type I membrane protein. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. Event=Alternative splicing; Named isoforms=3; Name=Long; IsoId=P40259-1; Sequence=Displayed; Name=Short; IsoId=P40259-2; Sequence=VSP_002477; Name=3; IsoId=P40259-3; Sequence=VSP_047222; B-cells. The transmembrane helices of CD79A and CD79B chains and two IgM heavy chains assembly in a four-helix bundle structure that appears to be conserved among different BCR isotypes. Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr- kinases such as BLK, LYN and SYK. Agammaglobulinemia 6, autosomal recessive (AGM6) [MIM:612692]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. Note=The disease is caused by variants affecting the gene represented in this entry. Name=CD79Bbase; Note=CD79B mutation db; URL="http://structure.bmc.lu.se/idbase/CD79Bbase/"; adaptive immune response immune system process transmembrane signaling receptor activity protein binding nucleoplasm Golgi apparatus cytosol plasma membrane integral component of plasma membrane immune response signal transduction cell surface receptor signaling pathway response to bacterium external side of plasma membrane membrane integral component of membrane B cell receptor complex B cell differentiation identical protein binding protein homodimerization activity B cell receptor signaling pathway protein homooligomerization extracellular exosome uc002jdq.1 uc002jdq.2 uc002jdq.3 
ENST00000006777.11 RHBDD2 ENST00000006777.11 rhomboid domain containing 2, transcript variant 6 (from RefSeq NM_001346189.2) ENST00000006777.1 ENST00000006777.10 ENST00000006777.2 ENST00000006777.3 ENST00000006777.4 ENST00000006777.5 ENST00000006777.6 ENST00000006777.7 ENST00000006777.8 ENST00000006777.9 NM_001346189 Q6NTF9 Q7L534 Q9H5W6 Q9HBK7 Q9UDT2 RHBD2_HUMAN RHBDL7 uc003udw.1 uc003udw.2 uc003udw.3 The protein encoded by this gene is a member of the rhomboid family of membrane-bound proteases and is overexpressed in some breast cancers. Members of this family are involved in intramembrane proteolysis. In mouse, the orthologous protein associates with the Golgi body. [provided by RefSeq, Sep 2016]. Q6NTF9-3; O95870: ABHD16A; NbExp=3; IntAct=EBI-17589229, EBI-348517; Q6NTF9-3; Q13085-4: ACACA; NbExp=3; IntAct=EBI-17589229, EBI-12562760; Q6NTF9-3; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-17589229, EBI-2876502; Q6NTF9-3; Q07817: BCL2L1; NbExp=3; IntAct=EBI-17589229, EBI-78035; Q6NTF9-3; Q92843: BCL2L2; NbExp=3; IntAct=EBI-17589229, EBI-707714; Q6NTF9-3; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-17589229, EBI-752069; Q6NTF9-3; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-17589229, EBI-7062247; Q6NTF9-3; P27658: COL8A1; NbExp=3; IntAct=EBI-17589229, EBI-747133; Q6NTF9-3; P21964: COMT; NbExp=3; IntAct=EBI-17589229, EBI-372265; Q6NTF9-3; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-17589229, EBI-517508; Q6NTF9-3; Q6P2H7: DYNC1H1; NbExp=3; IntAct=EBI-17589229, EBI-17590191; Q6NTF9-3; Q14318: FKBP8; NbExp=3; IntAct=EBI-17589229, EBI-724839; Q6NTF9-3; P31512: FMO4; NbExp=3; IntAct=EBI-17589229, EBI-17589491; Q6NTF9-3; Q96A11: GAL3ST3; NbExp=3; IntAct=EBI-17589229, EBI-17590461; Q6NTF9-3; P23434: GCSH; NbExp=3; IntAct=EBI-17589229, EBI-715444; Q6NTF9-3; Q5U4N7: GDF5-AS1; NbExp=3; IntAct=EBI-17589229, EBI-17590774; Q6NTF9-3; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-17589229, EBI-739467; Q6NTF9-3; P33778: H2BC3; NbExp=3; IntAct=EBI-17589229, EBI-357986; Q6NTF9-3; Q99525: H4C7; NbExp=3; IntAct=EBI-17589229, EBI-10294329; Q6NTF9-3; P04792: HSPB1; NbExp=3; IntAct=EBI-17589229, EBI-352682; Q6NTF9-3; Q96BM0: IFI27L1; NbExp=3; IntAct=EBI-17589229, EBI-17589287; Q6NTF9-3; P24001: IL32; NbExp=3; IntAct=EBI-17589229, EBI-2866752; Q6NTF9-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-17589229, EBI-10975473; Q6NTF9-3; Q6P1Q0: LETMD1; NbExp=3; IntAct=EBI-17589229, EBI-1549822; Q6NTF9-3; P27338: MAOB; NbExp=3; IntAct=EBI-17589229, EBI-3911344; Q6NTF9-3; Q5VZR4: MFSD14CP; NbExp=3; IntAct=EBI-17589229, EBI-2867865; Q6NTF9-3; Q5XKP0: MICOS13; NbExp=3; IntAct=EBI-17589229, EBI-1053887; Q6NTF9-3; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-17589229, EBI-11988931; Q6NTF9-3; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-17589229, EBI-8852072; Q6NTF9-3; Q9H8L6: MMRN2; NbExp=3; IntAct=EBI-17589229, EBI-2623273; Q6NTF9-3; O95563: MPC2; NbExp=3; IntAct=EBI-17589229, EBI-719403; Q6NTF9-3; Q6IN84: MRM1; NbExp=3; IntAct=EBI-17589229, EBI-5454865; Q6NTF9-3; Q9NZE8-2: MRPL35; NbExp=3; IntAct=EBI-17589229, EBI-17590278; Q6NTF9-3; Q96E29: MTERF3; NbExp=3; IntAct=EBI-17589229, EBI-7825321; Q6NTF9-3; Q9HB07: MYG1; NbExp=3; IntAct=EBI-17589229, EBI-709754; Q6NTF9-3; Q9Y3Q0: NAALAD2; NbExp=3; IntAct=EBI-17589229, EBI-2863682; Q6NTF9-3; Q69YL0: NCBP2AS2; NbExp=3; IntAct=EBI-17589229, EBI-10986258; Q6NTF9-3; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-17589229, EBI-11978907; Q6NTF9-3; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-17589229, EBI-725252; Q6NTF9-3; Q8IXM6: NRM; NbExp=3; IntAct=EBI-17589229, EBI-10262547; Q6NTF9-3; Q96AL5: PBX3; NbExp=3; IntAct=EBI-17589229, EBI-741171; Q6NTF9-3; P17612: PRKACA; NbExp=3; IntAct=EBI-17589229, EBI-476586; Q6NTF9-3; P54725: RAD23A; NbExp=3; IntAct=EBI-17589229, EBI-746453; Q6NTF9-3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-17589229, EBI-396669; Q6NTF9-3; P60602: ROMO1; NbExp=3; IntAct=EBI-17589229, EBI-11909831; Q6NTF9-3; Q8WXG1: RSAD2; NbExp=3; IntAct=EBI-17589229, EBI-12736320; Q6NTF9-3; Q96QR1: SCGB3A1; NbExp=3; IntAct=EBI-17589229, EBI-9057632; Q6NTF9-3; O14521: SDHD; NbExp=3; IntAct=EBI-17589229, EBI-1224553; Q6NTF9-3; P50454: SERPINH1; NbExp=3; IntAct=EBI-17589229, EBI-350723; Q6NTF9-3; Q9BXI2: SLC25A2; NbExp=3; IntAct=EBI-17589229, EBI-17590310; Q6NTF9-3; Q00325-2: SLC25A3; NbExp=3; IntAct=EBI-17589229, EBI-5456178; Q6NTF9-3; O15079: SNPH; NbExp=3; IntAct=EBI-17589229, EBI-4401902; Q6NTF9-3; Q17RD7: SYT16; NbExp=3; IntAct=EBI-17589229, EBI-10238936; Q6NTF9-3; Q53QW1: TEX44; NbExp=3; IntAct=EBI-17589229, EBI-10278496; Q6NTF9-3; P37173: TGFBR2; NbExp=3; IntAct=EBI-17589229, EBI-296151; Q6NTF9-3; P07204: THBD; NbExp=3; IntAct=EBI-17589229, EBI-941422; Q6NTF9-3; O60830: TIMM17B; NbExp=3; IntAct=EBI-17589229, EBI-2372529; Q6NTF9-3; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-17589229, EBI-17249488; Q6NTF9-3; Q2NL82: TSR1; NbExp=3; IntAct=EBI-17589229, EBI-358058; Q6NTF9-3; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-17589229, EBI-12261790; Q6NTF9-3; Q05086-3: UBE3A; NbExp=3; IntAct=EBI-17589229, EBI-11026619; Q6NTF9-3; Q70CQ3: USP30; NbExp=3; IntAct=EBI-17589229, EBI-2512374; Q6NTF9-3; O76024: WFS1; NbExp=3; IntAct=EBI-17589229, EBI-720609; Golgi apparatus, cis-Golgi network membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q6NTF9-1; Sequence=Displayed; Name=2; IsoId=Q6NTF9-2; Sequence=VSP_055407; Name=3; IsoId=Q6NTF9-3; Sequence=VSP_055608; Belongs to the peptidase S54 family. Although strongly related to the peptidase S54 family, it lacks the conserved active sites, suggesting that it has no peptidase activity. Sequence=AAG09733.1; Type=Frameshift; Evidence=; Sequence=AAH06234.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Golgi membrane Hrd1p ubiquitin ligase ERAD-L complex serine-type endopeptidase activity nucleus nucleoplasm Golgi apparatus membrane integral component of membrane integral component of endoplasmic reticulum membrane ER-associated ubiquitin-dependent protein catabolic process endoplasmic reticulum unfolded protein response perinuclear region of cytoplasm misfolded protein binding ubiquitin-specific protease binding uc003udw.1 uc003udw.2 uc003udw.3 
ENST00000007264.7 RPUSD1 ENST00000007264.7 RNA pseudouridine synthase domain containing 1, transcript variant 1 (from RefSeq NM_058192.3) C16orf40 D3DU66 ENST00000007264.1 ENST00000007264.2 ENST00000007264.3 ENST00000007264.4 ENST00000007264.5 ENST00000007264.6 NM_058192 Q9UJJ7 RLUCL RUSD1_HUMAN uc002ckb.1 uc002ckb.2 uc002ckb.3 uc002ckb.4 Q9UJJ7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3922794, EBI-5235340; Belongs to the pseudouridine synthase RluA family. enzyme-directed rRNA pseudouridine synthesis pseudouridine synthesis molecular_function RNA binding cellular_component biological_process RNA modification pseudouridine synthase activity uc002ckb.1 uc002ckb.2 uc002ckb.3 uc002ckb.4 
ENST00000007390.3 TSR3 ENST00000007390.3 TSR3 ribosome maturation factor (from RefSeq NM_001001410.3) C16orf42 ENST00000007390.1 ENST00000007390.2 NM_001001410 Q6PJT8 Q9UJK0 TSR3 TSR3_HUMAN UND313L uc002cll.1 uc002cll.2 uc002cll.3 uc002cll.4 uc002cll.5 Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248) in 18S rRNA (Probable). It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA (Probable). Reaction=N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl- L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3- carboxypropyl]pseudouridine(1248) in human 18S rRNA + S-methyl-5'- thioadenosine; Xref=Rhea:RHEA:63292, Rhea:RHEA-COMP:11639, Rhea:RHEA- COMP:16308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63293; Evidence= Cytoplasm Belongs to the TDD superfamily. TSR3 family. rRNA modification cytosol rRNA processing transferase activity maturation of SSU-rRNA ribosome biogenesis uc002cll.1 uc002cll.2 uc002cll.3 uc002cll.4 uc002cll.5 
ENST00000007414.8 OSBPL7 ENST00000007414.8 oxysterol binding protein like 7 (from RefSeq NM_145798.3) D3DTT6 ENST00000007414.1 ENST00000007414.2 ENST00000007414.3 ENST00000007414.4 ENST00000007414.5 ENST00000007414.6 ENST00000007414.7 NM_145798 ORP7 OSBL7_HUMAN Q6PIV6 Q9BZF2 uc002ilx.1 uc002ilx.2 uc002ilx.3 This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Like most members, the encoded protein contains an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain. Two transcript variants encoding the same isoform have been identified. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC065482.1, SRR1803617.33078.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000007414.8/ ENSP00000007414.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Cytoplasm, cytosol Endoplasmic reticulum membrane Cell membrane Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BZF2-1; Sequence=Displayed; Name=2; IsoId=Q9BZF2-2; Sequence=VSP_057227, VSP_057228; Expressed in epithelium of small and large intestines (at protein level). Expressed in stomach, duodenum, jejunum, ascending colon, spleen, thymus, lymph node, trachea and leukocytes. Expressed in fetal lung and thymus. Belongs to the OSBP family. protein binding cytoplasm autophagosome endoplasmic reticulum endoplasmic reticulum membrane cytosol plasma membrane bile acid biosynthetic process lipid transport lipid binding regulation of autophagy cholesterol binding membrane sterol binding intracellular membrane-bounded organelle cellular response to cholesterol perinuclear endoplasmic reticulum positive regulation of proteasomal protein catabolic process uc002ilx.1 uc002ilx.2 uc002ilx.3 
ENST00000007510.9 ARHGAP33 ENST00000007510.9 Rho GTPase activating protein 33, transcript variant 3 (from RefSeq NM_001366178.1) ENST00000007510.1 ENST00000007510.2 ENST00000007510.3 ENST00000007510.4 ENST00000007510.5 ENST00000007510.6 ENST00000007510.7 ENST00000007510.8 NM_001366178 O14552 O14559 O14560 Q6ZSP6 Q96CP3 Q9NT23 RHG33_HUMAN SNX26 TCGAP uc060xjg.1 uc060xjg.2 This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. Alternative splice variants encoding different isoforms have been identified in this gene. [provided by RefSeq, Feb 2010]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2145743 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## inferred exon combination :: based on alignments, homology RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## May be involved in several stages of intracellular trafficking. Could play an important role in the regulation of glucose transport by insulin. May act as a downstream effector of RHOQ/TC10 in the regulation of insulin-stimulated glucose transport (By similarity). Specifically interacts with CDC42 and RHOQ/TC10 through its Rho-GAP domain (By similarity). Interacts with NEK6. O14559; P06241: FYN; NbExp=2; IntAct=EBI-1210010, EBI-515315; Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=O14559-1; Sequence=Displayed; Name=2; IsoId=O14559-10; Sequence=VSP_014287, VSP_014292; Name=3; IsoId=O14559-11; Sequence=VSP_014291; Name=4; IsoId=O14559-12; Sequence=VSP_014288, VSP_014289, VSP_014290; Belongs to the PX domain-containing GAP family. Sequence=AAB81198.1; Type=Erroneous gene model prediction; Evidence=; [Isoform 2]: Sequence=BAC86902.1; Type=Frameshift; Evidence=; GTPase activator activity protein binding cytoplasm cytosol plasma membrane signal transduction small GTPase mediated signal transduction response to toxic substance protein transport protein kinase binding macromolecular complex phosphatidylinositol binding dendritic spine positive regulation of GTPase activity regulation of small GTPase mediated signal transduction regulation of dendritic spine morphogenesis uc060xjg.1 uc060xjg.2 
ENST00000007516.8 NDUFAB1 ENST00000007516.8 NADH:ubiquinone oxidoreductase subunit AB1 (from RefSeq NM_005003.3) ACPM_HUMAN B2R4M1 ENST00000007516.1 ENST00000007516.2 ENST00000007516.3 ENST00000007516.4 ENST00000007516.5 ENST00000007516.6 ENST00000007516.7 NDUFAB1 NM_005003 O14561 Q9UNV1 uc002dlw.1 uc002dlw.2 uc002dlw.3 uc002dlw.4 uc002dlw.5 Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity) (PubMed:27626371). Accessory and non- catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (PubMed:27626371). Accessory protein, of the core iron-sulfur cluster (ISC) assembly complex, that regulates, in association with LYRM4, the stability and the cysteine desulfurase activity of NFS1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (PubMed:31664822). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN- dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). Mammalian complex I is composed of 45 different subunits (PubMed:12611891). Interacts with ETFRF1 (PubMed:27499296). Identified in a complex composed of MALSU1, MIEF1 upstream open reading frame protein and NDUFAB1; within the trimeric complex, MIEF1 upstream open reading frame protein functions as a bridging scaffold that interacts with MALSU1 on one side, and with NDUFAB1 on the other side. The complex interacts with the mitochondrial large ribosomal subunit (PubMed:28892042, PubMed:30215512). Interacts with alpha-1- microglobulin chain; this interaction is required for the maintenance of mitochondrial redox homeostasis. Component of the mitochondrial core iron-sulfur cluster (ISC) complex composed of NFS1, LYRM4, NDUFAB1, ISCU, FXN, and FDX2; this complex is an heterohexamer containing two copies of each monomer (Probable). Component of the cyteine desulfurase complex composed of NFS1, LYRM4 and NDUFAB1; this complex contributes to the stability and cysteine desulfurase activity of NFS1 (PubMed:31664822). O14561; Q08043: ACTN3; NbExp=3; IntAct=EBI-1246261, EBI-2880652; O14561; Q96PG8: BBC3; NbExp=3; IntAct=EBI-1246261, EBI-17289784; O14561; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-1246261, EBI-10243741; O14561; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-1246261, EBI-1104933; O14561; P26441: CNTF; NbExp=3; IntAct=EBI-1246261, EBI-1050897; O14561; Q9BSK4: FEM1A; NbExp=3; IntAct=EBI-1246261, EBI-2515349; O14561; Q13643: FHL3; NbExp=5; IntAct=EBI-1246261, EBI-741101; O14561; Q53EP0-3: FNDC3B; NbExp=5; IntAct=EBI-1246261, EBI-10242151; O14561; Q9BQA5: HINFP; NbExp=3; IntAct=EBI-1246261, EBI-749065; O14561; Q7L273: KCTD9; NbExp=3; IntAct=EBI-1246261, EBI-4397613; O14561; P25791-3: LMO2; NbExp=3; IntAct=EBI-1246261, EBI-11959475; O14561; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1246261, EBI-739832; O14561; Q6PF18: MORN3; NbExp=3; IntAct=EBI-1246261, EBI-9675802; O14561; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-1246261, EBI-12025760; O14561; Q16656-4: NRF1; NbExp=3; IntAct=EBI-1246261, EBI-11742836; O14561; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1246261, EBI-741158; O14561; O43482: OIP5; NbExp=3; IntAct=EBI-1246261, EBI-536879; O14561; Q969H6: POP5; NbExp=3; IntAct=EBI-1246261, EBI-366525; O14561; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-1246261, EBI-710402; O14561; P17980: PSMC3; NbExp=6; IntAct=EBI-1246261, EBI-359720; O14561; Q9GZT3: SLIRP; NbExp=4; IntAct=EBI-1246261, EBI-1050793; O14561; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-1246261, EBI-741515; O14561; O43711: TLX3; NbExp=5; IntAct=EBI-1246261, EBI-3939165; O14561; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-1246261, EBI-12815137; O14561; Q08AM6: VAC14; NbExp=3; IntAct=EBI-1246261, EBI-2107455; O14561; P17023: ZNF19; NbExp=3; IntAct=EBI-1246261, EBI-12884200; O14561; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-1246261, EBI-11741890; O14561; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-1246261, EBI-18036029; Mitochondrion Phosphopantetheinylation at Ser-112 is essential for interactions with LYR motif-containing proteins. In contrast to other accessory subunits of complex I, NDUFAB1 is the only subunit that is essential for cell viability in HEK293T cells. Since knockout cells lack assembled complex I and die in galactose media, this suggests that the essential role of NDUFAB1 is independent of complex I. Belongs to the acyl carrier protein (ACP) family. Sequence=AAC05814.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; acyl binding ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process fatty acid binding calcium ion binding protein binding nucleoplasm mitochondrion mitochondrial inner membrane mitochondrial respiratory chain complex I mitochondrial matrix mitochondrial electron transport, NADH to ubiquinone lipid metabolic process fatty acid metabolic process fatty acid biosynthetic process NADH dehydrogenase (ubiquinone) activity protein lipoylation mitochondrial membrane mitochondrial respiratory chain complex I assembly oxidation-reduction process respiratory chain mitochondrial large ribosomal subunit uc002dlw.1 uc002dlw.2 uc002dlw.3 uc002dlw.4 uc002dlw.5 
ENST00000007699.10 YBX2 ENST00000007699.10 Y-box binding protein 2 (from RefSeq NM_015982.4) CSDA3 D3DTP1 ENST00000007699.1 ENST00000007699.2 ENST00000007699.3 ENST00000007699.4 ENST00000007699.5 ENST00000007699.6 ENST00000007699.7 ENST00000007699.8 ENST00000007699.9 MSY2 NM_015982 Q8N4P0 Q9Y2T7 YBOX2_HUMAN uc002gfq.1 uc002gfq.2 uc002gfq.3 uc002gfq.4 This gene encodes a nucleic acid binding protein which is highly expressed in germ cells. The encoded protein binds to a Y-box element in the promoters of certain genes but also binds to mRNA transcribed from these genes. Pseudogenes for this gene are located on chromosome 10 and 15. [provided by RefSeq, Feb 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF096834.1, BC033800.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000007699.10/ ENSP00000007699.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Major constituent of messenger ribonucleoprotein particles (mRNPs). Involved in the regulation of the stability and/or translation of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to full-length mRNA with high affinity in a sequence-independent manner. Binds to short RNA sequences containing the consensus site 5'-UCCAUCA- 3' with low affinity and limited sequence specificity. Its binding with maternal mRNAs is necessary for its cytoplasmic retention. May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (By similarity). Found in a mRNP complex with PABPC1 and YBX3. Found in a mRNP complex with ZAR1 and ZAR1L. Cytoplasm Nucleus Expressed in oocytes and testicular germ cells in the stage of spermatogonia to spermatocyte. Also observed placental trophoblasts, as well as in vascular smooth muscle cells in the pulmonary artery, myocardium, and skeletal muscle. Undetectable in epithelial cells in respiratory, gastrointestinal, and urogenital tracts. Up-regulated in various carcinomas and germ cell tumors (at protein level). Phosphorylated during oocyte maturation and dephosphorylated following egg activation. Phosphorylated in vitro by a kinase activity associated with testicular mRNPs. Dephosphorylation leads to a decrease in its affinity to bind RNA in vitro (By similarity). fibrillar center nucleic acid binding DNA binding RNA binding nucleus cytoplasm transcription from RNA polymerase II promoter spermatogenesis translational attenuation oocyte development uc002gfq.1 uc002gfq.2 uc002gfq.3 uc002gfq.4 
ENST00000007735.4 KRT33A ENST00000007735.4 keratin 33A (from RefSeq NM_004138.4) B2RA87 ENST00000007735.1 ENST00000007735.2 ENST00000007735.3 HHA3-I HKA3A KRTHA3A KT33A_HUMAN NM_004138 O76009 Q6NTB9 Q6ZZB9 uc002hwk.1 uc002hwk.2 uc002hwk.3 uc002hwk.4 This gene encodes a member of the keratin gene family. This gene is one of multiple type I hair keratin genes that are clustered in a region of chromosome 17q12-q21 and have the same direction of transcription. As a type I hair keratin, the encoded protein is an acidic protein which heterodimerizes with type II keratins to form hair and nails. There are two isoforms of this protein, encoded by two separate genes, keratin 33A and keratin 33B. [provided by RefSeq, May 2012]. ##Evidence-Data-START## Transcript exon combination :: AJ633621.2, BC069135.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148874 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000007735.4/ ENSP00000007735.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Expressed in the hair follicles. There are two types of hair/microfibrillar keratin, I (acidic) and II (neutral to basic). Belongs to the intermediate filament family. structural molecule activity extracellular space cytosol intermediate filament keratinization cornification uc002hwk.1 uc002hwk.2 uc002hwk.3 uc002hwk.4 
ENST00000008391.4 TFAP2D ENST00000008391.4 transcription factor AP-2 delta (from RefSeq NM_172238.4) AP2D_HUMAN ENST00000008391.1 ENST00000008391.2 ENST00000008391.3 NM_172238 Q7Z6R9 Q8IWX0 TFAP2BL1 TFAP2D uc003paf.1 uc003paf.2 uc003paf.3 uc003paf.4 uc003paf.5 Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC (By similarity). Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members (By similarity). Q7Z6R9; O43184-4: ADAM12; NbExp=3; IntAct=EBI-11952651, EBI-12006944; Q7Z6R9; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-11952651, EBI-10173507; Q7Z6R9; O95994: AGR2; NbExp=3; IntAct=EBI-11952651, EBI-712648; Q7Z6R9; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-11952651, EBI-357530; Q7Z6R9; O95429: BAG4; NbExp=5; IntAct=EBI-11952651, EBI-2949658; Q7Z6R9; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-11952651, EBI-1383687; Q7Z6R9; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-11952651, EBI-3866279; Q7Z6R9; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-11952651, EBI-2802782; Q7Z6R9; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11952651, EBI-742887; Q7Z6R9; A8MTA8-2: CIMIP2B; NbExp=3; IntAct=EBI-11952651, EBI-12160437; Q7Z6R9; Q9BYD5: CNFN; NbExp=3; IntAct=EBI-11952651, EBI-12819063; Q7Z6R9; P67870: CSNK2B; NbExp=3; IntAct=EBI-11952651, EBI-348169; Q7Z6R9; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11952651, EBI-3867333; Q7Z6R9; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-11952651, EBI-11978259; Q7Z6R9; Q96NT3-2: GUCD1; NbExp=5; IntAct=EBI-11952651, EBI-11978177; Q7Z6R9; P13807: GYS1; NbExp=3; IntAct=EBI-11952651, EBI-740553; Q7Z6R9; P35452-2: HOXD12; NbExp=3; IntAct=EBI-11952651, EBI-17244356; Q7Z6R9; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-11952651, EBI-747204; Q7Z6R9; Q0VD86: INCA1; NbExp=5; IntAct=EBI-11952651, EBI-6509505; Q7Z6R9; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-11952651, EBI-10693436; Q7Z6R9; Q5T749: KPRP; NbExp=3; IntAct=EBI-11952651, EBI-10981970; Q7Z6R9; Q15323: KRT31; NbExp=3; IntAct=EBI-11952651, EBI-948001; Q7Z6R9; O76011: KRT34; NbExp=3; IntAct=EBI-11952651, EBI-1047093; Q7Z6R9; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11952651, EBI-11959885; Q7Z6R9; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-11952651, EBI-11749135; Q7Z6R9; P60409: KRTAP10-7; NbExp=5; IntAct=EBI-11952651, EBI-10172290; Q7Z6R9; P60410: KRTAP10-8; NbExp=5; IntAct=EBI-11952651, EBI-10171774; Q7Z6R9; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-11952651, EBI-1052037; Q7Z6R9; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11952651, EBI-11953334; Q7Z6R9; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-11952651, EBI-11992140; Q7Z6R9; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-11952651, EBI-12196745; Q7Z6R9; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-11952651, EBI-12805508; Q7Z6R9; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-11952651, EBI-10241353; Q7Z6R9; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-11952651, EBI-14065470; Q7Z6R9; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-11952651, EBI-3957672; Q7Z6R9; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-11952651, EBI-12111050; Q7Z6R9; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-11952651, EBI-11962084; Q7Z6R9; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-11952651, EBI-18394498; Q7Z6R9; Q9BYQ4: KRTAP9-2; NbExp=5; IntAct=EBI-11952651, EBI-1044640; Q7Z6R9; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-11952651, EBI-1043191; Q7Z6R9; P40692: MLH1; NbExp=5; IntAct=EBI-11952651, EBI-744248; Q7Z6R9; O43482: OIP5; NbExp=5; IntAct=EBI-11952651, EBI-536879; Q7Z6R9; P78337: PITX1; NbExp=3; IntAct=EBI-11952651, EBI-748265; Q7Z6R9; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-11952651, EBI-949255; Q7Z6R9; P28070: PSMB4; NbExp=3; IntAct=EBI-11952651, EBI-603350; Q7Z6R9; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-11952651, EBI-948156; Q7Z6R9; O15304-2: SIVA1; NbExp=3; IntAct=EBI-11952651, EBI-12372219; Q7Z6R9; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-11952651, EBI-10269374; Q7Z6R9; Q96LM6: SPMIP9; NbExp=3; IntAct=EBI-11952651, EBI-743976; Q7Z6R9; O43609: SPRY1; NbExp=3; IntAct=EBI-11952651, EBI-3866665; Q7Z6R9; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-11952651, EBI-11139477; Q7Z6R9; Q08117-2: TLE5; NbExp=5; IntAct=EBI-11952651, EBI-11741437; Q7Z6R9; Q63HR2: TNS2; NbExp=3; IntAct=EBI-11952651, EBI-949753; Q7Z6R9; Q13077: TRAF1; NbExp=3; IntAct=EBI-11952651, EBI-359224; Q7Z6R9; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-11952651, EBI-5235829; Q7Z6R9; Q86WV8: TSC1; NbExp=3; IntAct=EBI-11952651, EBI-12806590; Q7Z6R9; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-11952651, EBI-11975223; Q7Z6R9; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-11952651, EBI-2559305; Q7Z6R9; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-11952651, EBI-10188476; Q7Z6R9; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-11952651, EBI-12030590; Nucleus Highly expressed in brain, placenta, skeletal muscle, thymus, small intestine, and prostate, and expressed at lower levels in leukocyte, spleen, testis, ovary and colon. Barely detectable in heart, kidney, liver, lung or pancreas. Belongs to the AP-2 family. Name=Wikipedia; Note=Activating protein 2 entry; URL="https://en.wikipedia.org/wiki/Activating_protein_2"; nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus transcription factor complex regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter negative regulation of neuron apoptotic process positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter inferior colliculus development uc003paf.1 uc003paf.2 uc003paf.3 uc003paf.4 uc003paf.5 
ENST00000008527.10 CRY1 ENST00000008527.10 cryptochrome circadian regulator 1, transcript variant 16 (from RefSeq NR_182153.1) CRY1_HUMAN ENST00000008527.1 ENST00000008527.2 ENST00000008527.3 ENST00000008527.4 ENST00000008527.5 ENST00000008527.6 ENST00000008527.7 ENST00000008527.8 ENST00000008527.9 NR_182153 PHLL1 Q16526 uc001tmi.1 uc001tmi.2 uc001tmi.3 uc001tmi.4 uc001tmi.5 uc001tmi.6 Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post- translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-BMAL1 independently of PER proteins and is found at CLOCK-BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-BMAL1 induced transcription of ATF4, MTA1, KLF10 and NAMPT (By similarity). May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon-mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Inhibits hepatic gluconeogenesis by decreasing nuclear FOXO1 levels that down-regulates gluconeogenic gene expression (By similarity). Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4 (By similarity). Represses PPARD and its target genes in the skeletal muscle and limits exercise capacity (By similarity). Plays an essential role in the generation of circadian rhythms in the retina (By similarity). Represses the transcriptional activity of NR1I2 (By similarity). Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence=; Note=Binds 1 FAD per subunit. Only a minority of the protein molecules contain bound FAD. Contrary to the situation in photolyases, the FAD is bound in a shallow, surface-exposed pocket. ; Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate; Xref=ChEBI:CHEBI:15636; Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit.; KL001 (N-[3-(9H-carbazol-9-yl)-2-hydroxypropyl]-N- (2-furanylmethyl)-methanesulfonamide) binds to CRY1 and stabilizes it by inhibiting FBXL3- and ubiquitin-dependent degradation of CRY1 resulting in lengthening of the circadian periods. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, BMAL1 or BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins (By similarity). Interacts directly with TIMELESS (By similarity). Interacts directly with PER1 and PER3 (By similarity). Interacts directly with PER2; interaction with PER2 inhibits its ubiquitination and vice versa (PubMed:21613214). Interacts with FBXL21 (By similarity). Interacts with FBXL3 (PubMed:17463251). Interacts with PPP5C (via TPR repeats) (PubMed:16790549). Interacts with CLOCK-BMAL1 independently of PER2 and DNA (PubMed:28388406). Interacts with HDAC1, HDAC2 and SIN3B. Interacts with nuclear receptors AR, NR1D1, NR3C1/GR, RORA and RORC; the interaction with at least NR3C1/GR is ligand dependent (PubMed:22170608). Interacts with PRKDC (By similarity). Interacts with the G protein subunit alpha GNAS; the interaction may block GPCR-mediated regulation of cAMP concentrations (PubMed:20852621). Interacts with PRMT5 (PubMed:23133559). Interacts with EZH2 (By similarity). Interacts with MYBBP1A, DOCK7, HNRNPU, RPL7A, RPL8 and RPS3 (By similarity). Interacts with MAP1LC3B (By similarity). Interacts with CLOCK (By similarity). Interacts with BMAL1 (By similarity). Interacts weakly with HDAC3; this interaction is enhanced in the presence of FBXL3 (By similarity). Interacts with TRIM28, KCTD5 and DDB1 (By similarity). Interacts with FOXO1 (By similarity). Interacts with DTL and DDB1-CUL4A complex (PubMed:26431207). Interacts with HNF4A (PubMed:30530698). Interacts with PSMD2 in a KDM8-dependent manner (By similarity). Interacts with KDM8 in a FBXL3-dependent manner (By similarity). Interacts with PPARG in a ligand-dependent manner (By similarity). Interacts with PPARD (via domain NR LBD) and NR1I2 (via domain NR LBD) in a ligand-dependent manner (By similarity). Interacts with PPARA, NR1I3 and VDR (By similarity). Q16526; O14744: PRMT5; NbExp=3; IntAct=EBI-741297, EBI-351098; Cytoplasm. Nucleus Note=Translocated to the nucleus through interaction with other clock proteins such as PER2 or BMAL1. Expression is regulated by light and circadian rhythms and osicllates diurnally. Peak expression in the suprachiasma nucleus (SCN) and eye at the day/night transition (CT12). Levels decrease with BMAL1- CLOCK inhibition as part of the autoregulatory feedback loop. The LIR motifs (LC3-interacting region) 3 and 5 are required for its interaction with MAP1LC3B and for its autophagy-mediated degradation. Phosphorylation on Ser-247 by MAPK is important for the inhibition of CLOCK-BMAL1-mediated transcriptional activity. Phosphorylation by CSNK1E requires interaction with PER1 or PER2. Phosphorylation at Ser- 71 and Ser-280 by AMPK decreases protein stability. Phosphorylation at Ser-568 exhibits a robust circadian rhythm with a peak at CT8, increases protein stability, prevents SCF(FBXL3)-mediated degradation and is antagonized by interaction with PRKDC. Ubiquitinated by the SCF(FBXL3) and SCF(FBXL21) complexes, regulating the balance between degradation and stabilization. The SCF(FBXL3) complex is mainly nuclear and mediates ubiquitination and subsequent degradation of CRY1. In contrast, cytoplasmic SCF(FBXL21) complex-mediated ubiquitination leads to stabilize CRY1 and counteract the activity of the SCF(FBXL3) complex. The SCF(FBXL3) and SCF(FBXL21) complexes probably mediate ubiquitination at different Lys residues. Ubiquitination at Lys-11 and Lys-107 are specifically ubiquitinated by the SCF(FBXL21) complex but not by the SCF(FBXL3) complex. Ubiquitination may be inhibited by PER2 (PubMed:17463251, PubMed:22798407, PubMed:27565346). Deubiquitinated by USP7 (By similarity). Undergoes autophagy-mediated degradation in the liver in a time- dependent manner. Autophagic degradation of CRY1 (an inhibitor of gluconeogenesis) occurs during periods of reduced feeding allowing induction of gluconeogenesis and maintenance of blood glucose levels. Delayed sleep phase syndrome (DSPS) [MIM:614163]: A circadian rhythm sleep disorder characterized by sleep-onset insomnia and difficulty in awakening at the desired time. Patients with DSPS have chronic difficulty in adjusting their sleep-onset and wake-up times to occupational, school, and social activities. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. An adenine-to-cytosine transversion within the 5'splice site following exon 11 has been found in multiple members of a DSPD family and segregates with the disorder with autosomal dominant inheritance pattern. This variant is predicted to cause exon 11 skipping and in- frame deletion of 24 residues in the C-terminal region of CRY1. Functional studies show that the mutated protein acts as a more potent transcriptional repressor than wild-type, causes reduced expression of key transcriptional targets and lengthens the period of circadian molecular rhythms. Belongs to the DNA photolyase class-1 family. Name=Wikipedia; Note=Cryptochrome entry; URL="https://en.wikipedia.org/wiki/Cryptochrome"; negative regulation of transcription from RNA polymerase II promoter nucleotide binding DNA binding double-stranded DNA binding protein binding nucleus cytoplasm mitochondrion gluconeogenesis DNA damage induced protein phosphorylation circadian rhythm transcription factor binding response to light stimulus blue light signaling pathway photoreceptor activity blue light photoreceptor activity response to activity protein-chromophore linkage kinase binding protein kinase binding phosphatase binding lipid storage negative regulation of protein ubiquitination positive regulation of protein ubiquitination response to insulin circadian regulation of gene expression response to glucagon nuclear hormone receptor binding glucose homeostasis regulation of circadian rhythm negative regulation of circadian rhythm histone deacetylase binding entrainment of circadian clock by photoperiod negative regulation of gluconeogenesis negative regulation of G-protein coupled receptor protein signaling pathway negative regulation of transcription, DNA-templated rhythmic process response to stimulus E-box binding regulation of DNA damage checkpoint negative regulation of glucocorticoid receptor signaling pathway negative regulation of glucocorticoid secretion deoxyribodipyrimidine photo-lyase activity DNA (6-4) photolyase activity uc001tmi.1 uc001tmi.2 uc001tmi.3 uc001tmi.4 uc001tmi.5 uc001tmi.6 
ENST00000008938.5 PGLYRP1 ENST00000008938.5 peptidoglycan recognition protein 1 (from RefSeq NM_005091.3) ENST00000008938.1 ENST00000008938.2 ENST00000008938.3 ENST00000008938.4 NM_005091 O75594 PGLYRP PGRP PGRP1_HUMAN Q4VB36 SBBI68 TNFSF3L UNQ639/PRO1269 uc002pdx.1 uc002pdx.2 uc002pdx.3 uc002pdx.4 uc002pdx.5 Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram- positive bacteria and thus provides bactericidal activity (PubMed:9707603). Forms an equimolar complex with heat shock protein HSPA1A and induces programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane (PubMed:21247889, PubMed:26183779). In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement (PubMed:26654597). Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system (PubMed:30713770). Promotes also the activation of lymphocytes that become able to kill virus-infected cells as well as tumor cells by modulating the spectrum of their target-cell specificity (PubMed:29083508, PubMed:28977785). Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor (PubMed:28977785, PubMed:25595774). Homodimer; disulfide-linked (PubMed:16354652, PubMed:15769462). Interacts with HSPA1A; this interaction forms a cytotoxic complex that is released by lymphokine-activated killer cells (By similarity). Interacts with HSPBP1; this interaction blocks the cytotoxic activity of the PGLYRP1-HSPA1A complex (PubMed:21247889). Interacts with TNFRSF1A; this interaction is important for cell death induction (PubMed:26183779). Interacts with S100A4; this complex acts as a chemoattractant that promotes lymphocyte movement (PubMed:26654597, PubMed:30713770). Interacts with TREM1 (PubMed:25595774). Secreted Cytoplasmic granule Highly expressed in bone marrow. Weak expression found in kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils. N-glycosylated. N-glycosylation is required for bactericidal activity. Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. pattern recognition receptor signaling pathway immune system process extracellular region extracellular space zinc ion binding N-acetylmuramoyl-L-alanine amidase activity peptidoglycan catabolic process response to bacterium peptidoglycan receptor activity detection of bacterium antimicrobial humoral response killing of cells of other organism negative regulation of interferon-gamma production negative regulation of natural killer cell differentiation involved in immune response specific granule lumen defense response to bacterium peptidoglycan binding neutrophil degranulation growth of symbiont in host innate immune response negative regulation of inflammatory response defense response to Gram-positive bacterium positive regulation of cytolysis in other organism extracellular exosome phagocytic vesicle lumen tertiary granule lumen uc002pdx.1 uc002pdx.2 uc002pdx.3 uc002pdx.4 uc002pdx.5 
ENST00000009041.12 STARD3NL ENST00000009041.12 STARD3 N-terminal like, transcript variant 1 (from RefSeq NM_032016.4) A4D1X0 ENST00000009041.1 ENST00000009041.10 ENST00000009041.11 ENST00000009041.2 ENST00000009041.3 ENST00000009041.4 ENST00000009041.5 ENST00000009041.6 ENST00000009041.7 ENST00000009041.8 ENST00000009041.9 MENTHO NM_032016 O95772 STARD3NL STR3N_HUMAN UNQ855/PRO1864 uc003tfr.1 uc003tfr.2 uc003tfr.3 uc003tfr.4 uc003tfr.5 This gene encodes a late-endosomal protein that contains a conserved MENTAL (MLN64 N-terminal) domain. The encoded protein binds cholesterol molecules and may play a role in endosomal cholesterol transport through interactions with metastatic lymph node protein 64 (MLN64). [provided by RefSeq, Sep 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660807.259540.1, SRR1803613.194392.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB (PubMed:24105263). Homodimer (PubMed:16709157). Interacts (via the MENTAL domain) with STARD3NL (PubMed:16709157). Interacts (via FFAT motif) with VAPA. Interacts (via FFAT motif) with VAPB (PubMed:24105263). Interacts (via FFAT motif) with MOSPD2 (via MSP domain) (PubMed:29858488). O95772; Q9UBK5: HCST; NbExp=3; IntAct=EBI-3916943, EBI-2801937; O95772; Q8NHP6: MOSPD2; NbExp=5; IntAct=EBI-3916943, EBI-2812848; Late endosome membrane ; Multi-pass membrane protein Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2. Event=Alternative initiation; Named isoforms=2; Name=1; IsoId=O95772-1; Sequence=Displayed; Name=2; IsoId=O95772-2; Sequence=VSP_018819; The FFAT motif mediates interaction with VAPA, VAPB and MOSPD2. The MENTAL domain anchors the protein in endosome membranes and exposes the START domain in the cytosol (By similarity). It binds cholesterol and mediates homotypic as well as heterotypic interactions between STARD3 and STARD3NL (PubMed:15718238, PubMed:16709157). Belongs to the STARD3 family. protein binding lysosomal membrane endosome cytosol C21-steroid hormone biosynthetic process cholesterol binding membrane integral component of membrane late endosome membrane protein homodimerization activity intracellular membrane-bounded organelle organelle membrane contact site vesicle tethering to endoplasmic reticulum endoplasmic reticulum membrane uc003tfr.1 uc003tfr.2 uc003tfr.3 uc003tfr.4 uc003tfr.5 
ENST00000009180.10 CD9 ENST00000009180.10 CD9 molecule, transcript variant 1 (from RefSeq NM_001769.4) CD9 CD9_HUMAN D3DUQ9 ENST00000009180.1 ENST00000009180.2 ENST00000009180.3 ENST00000009180.4 ENST00000009180.5 ENST00000009180.6 ENST00000009180.7 ENST00000009180.8 ENST00000009180.9 GIG2 MIC3 NM_001769 P21926 Q5J7W6 Q96ES4 TSPAN29 uc285jyt.1 uc285jyt.2 This gene encodes a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Tetraspanins are cell surface glycoproteins with four transmembrane domains that form multimeric complexes with other cell surface proteins. The encoded protein functions in many cellular processes including differentiation, adhesion, and signal transduction, and expression of this gene plays a critical role in the suppression of cancer cell motility and metastasis. [provided by RefSeq, Jan 2011]. Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:8478605, PubMed:14575715, PubMed:18541721). Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (By similarity). In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (PubMed:12796480). Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). Acts as a receptor for PSG17 (By similarity). Involved in platelet activation and aggregation (PubMed:18541721). Regulates paranodal junction formation (By similarity). Involved in cell adhesion, cell motility and tumor metastasis (PubMed:8478605, PubMed:7511626). Forms both disulfide-linked homodimers and higher homooligomers as well as heterooligomers with other members of the tetraspanin family (PubMed:14556650). Interacts (via the second extracellular domain) with integrin ITGAV:ITGB3 (PubMed:19640571, PubMed:27993971). Interacts with integrin ITGA6:ITGB1; interaction takes place in oocytes and is involved in sperm-egg fusion (By similarity). Part of integrin-tetraspanin complexes composed of CD81, beta-1 and beta-2 integrins in the membrane of monocyte/macrophages (PubMed:12796480). Interacts with CD63; identified in a complex with CD63 and ITGB3 (PubMed:19640571). Associates with CR2/CD21 and with PTGFRN/CD9P1 (PubMed:11278880). Part of a complex composed of CD9, CD81, PTGFRN and IGSF8 (By similarity). Interacts directly with IGSF8 (PubMed:11504738). Interacts with PDPN; this interaction is homophilic and attenuates platelet aggregation and pulmonary metastasis induced by PDPN (PubMed:18541721). Interacts (on T cell side) with CD81 at immunological synapses between antigen-presenting cells and T cells (PubMed:23858057). P21926; O14672: ADAM10; NbExp=17; IntAct=EBI-4280101, EBI-1536151; P21926; P08473: MME; NbExp=6; IntAct=EBI-4280101, EBI-353759; P21926; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-4280101, EBI-12382569; P21926; Q9P2B2: PTGFRN; NbExp=10; IntAct=EBI-4280101, EBI-4290465; Cell membrane ; Multi-pass membrane protein Membrane ; Multi-pass membrane protein Secreted, extracellular exosome Note=Present at the cell surface of oocytes. Accumulates in the adhesion area between the sperm and egg following interaction between IZUMO1 and its receptor IZUMO1R/JUNO. Detected in platelets (at protein level) (PubMed:19640571). Expressed by a variety of hematopoietic and epithelial cells (PubMed:19640571). Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro). The protein exists in three forms with molecular masses between 22 and 27 kDa, and is known to carry covalently linked fatty acids (PubMed:11959120). Palmitoylation by ZDHHC2 regulates CD9 expression, association with other tetraspanin family proteins and function in cell adhesion (PubMed:18508921). Belongs to the tetraspanin (TM4SF) family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cd9/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/995/CD9"; platelet degranulation integrin binding protein binding extracellular region extracellular space plasma membrane integral component of plasma membrane focal adhesion cell adhesion single fertilization fusion of sperm to egg plasma membrane brain development negative regulation of cell proliferation response to water deprivation external side of plasma membrane cell surface oligodendrocyte development myoblast fusion involved in skeletal muscle regeneration membrane integral component of membrane apical plasma membrane platelet activation endocytic vesicle membrane clathrin-coated endocytic vesicle membrane paranodal junction assembly platelet alpha granule membrane receptor internalization macromolecular complex sperm-egg recognition negative regulation of cellular component movement extracellular exosome cellular response to low-density lipoprotein particle stimulus negative regulation of platelet aggregation extracellular vesicle regulation of macrophage migration uc285jyt.1 uc285jyt.2 
ENST00000009530.13 CD74 ENST00000009530.13 CD74 molecule, transcript variant 1 (from RefSeq NM_001025159.3) A8K7R1 B4DNE8 CD74 D3DQG3 D3DQG4 DHLAG ENST00000009530.1 ENST00000009530.10 ENST00000009530.11 ENST00000009530.12 ENST00000009530.2 ENST00000009530.3 ENST00000009530.4 ENST00000009530.5 ENST00000009530.6 ENST00000009530.7 ENST00000009530.8 ENST00000009530.9 HG2A_HUMAN NM_001025159 P04233 Q14597 Q29832 Q5U0J8 Q8SNA0 Q8WLP6 uc003lsc.1 uc003lsc.2 uc003lsc.3 uc003lsc.4 uc003lsc.5 uc003lsc.6 The protein encoded by this gene associates with class II major histocompatibility complex (MHC) and is an important chaperone that regulates antigen presentation for immune response. It also serves as cell surface receptor for the cytokine macrophage migration inhibitory factor (MIF) which, when bound to the encoded protein, initiates survival pathways and cell proliferation. This protein also interacts with amyloid precursor protein (APP) and suppresses the production of amyloid beta (Abeta). Multiple alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Aug 2011]. Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. Serves as cell surface receptor for the cytokine MIF. [Class-II-associated invariant chain peptide]: Binds to the peptide-binding site of MHC class II alpha/beta heterodimers forming an alpha-beta-CLIP complex, thereby preventing the loading of antigenic peptides to the MHC class II complex until its release by HLA-DM in the endosome. [Isoform p41]: Stabilizes the conformation of mature CTSL by binding to its active site and serving as a chaperone to help maintain a pool of mature enzyme in endocytic compartments and extracellular space of antigen-presenting cells (APCs). Has antiviral activity by stymieing the endosomal entry of Ebola virus and coronaviruses, including SARS-CoV-2 (PubMed:32855215). Disrupts cathepsin-mediated Ebola virus glycoprotein processing, which prevents viral fusion and entry. This antiviral activity is specific to p41 isoform (PubMed:32855215). Homotrimer. In the endoplasmic reticulum (ER) it forms a heterononameric MHC II-Ii complex: 3 MHC class II molecules (heterodimers of an alpha and a beta subunit) bind to the CD74 homotrimer (also known as invariant chain or HLA class II histocompatibility antigen gamma chain). In the endosomal/lysosomal system, the CD74 component undergoes sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide) attached to the MHC class II molecule (alpha-beta-CLIP complex). This processed complex interacts with HLA_DM and HLA_DO heterodimers in order to release CLIP and facilitate the binding of antigenic peptides to the MHC class II molecules. Interacts with CD44; this complex is essential for the MIF- induced signaling cascade that results in B cell survival. [Isoform p41]: Interacts with the mature form of CTSL; the complex survive in neutral pH environment. P04233; P16070: CD44; NbExp=9; IntAct=EBI-2622890, EBI-490245; P04233; P25025: CXCR2; NbExp=2; IntAct=EBI-2622890, EBI-2835281; P04233; P61073: CXCR4; NbExp=4; IntAct=EBI-2622890, EBI-489411; P04233; P60228: EIF3E; NbExp=2; IntAct=EBI-2622890, EBI-347740; P04233; Q14974: KPNB1; NbExp=2; IntAct=EBI-2622890, EBI-286758; P04233; P0A6Y8: dnaK; Xeno; NbExp=8; IntAct=EBI-2622890, EBI-542092; P04233-2; O15155: BET1; NbExp=3; IntAct=EBI-12222807, EBI-749204; P04233-2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-12222807, EBI-12256978; P04233-2; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12222807, EBI-11989440; P04233-2; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-12222807, EBI-2807956; P04233-2; P56851: EDDM3B; NbExp=3; IntAct=EBI-12222807, EBI-10215665; P04233-2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12222807, EBI-711490; P04233-2; P37268: FDFT1; NbExp=3; IntAct=EBI-12222807, EBI-714550; P04233-2; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-12222807, EBI-713304; P04233-2; Q9UBY5: LPAR3; NbExp=4; IntAct=EBI-12222807, EBI-12033434; P04233-2; Q8N912: NRAC; NbExp=4; IntAct=EBI-12222807, EBI-12051377; P04233-2; P0DJD7: PGA4; NbExp=3; IntAct=EBI-12222807, EBI-12957629; P04233-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-12222807, EBI-12188331; P04233-2; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-12222807, EBI-10485931; P04233-2; Q8WZA1: POMGNT1; NbExp=3; IntAct=EBI-12222807, EBI-3912424; P04233-2; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-12222807, EBI-14199621; P04233-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-12222807, EBI-10244780; P04233-2; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12222807, EBI-8652744; P04233-2; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-12222807, EBI-10329948; P04233-2; P78383: SLC35B1; NbExp=3; IntAct=EBI-12222807, EBI-12147661; P04233-2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-12222807, EBI-12188413; P04233-2; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-12222807, EBI-11523345; P04233-2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-12222807, EBI-10171534; P04233-2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-12222807, EBI-12887458; P04233-2; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-12222807, EBI-11956809; P04233-2; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12222807, EBI-2852148; P04233-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12222807, EBI-12111910; P04233-2; O00526: UPK2; NbExp=4; IntAct=EBI-12222807, EBI-10179682; Cell membrane ; Single-pass type II membrane protein Endoplasmic reticulum membrane. Golgi apparatus, trans-Golgi network. Endosome. Lysosome. Secreted te=Transits through a number of intracellular compartments in the endocytic pathway. It can either undergo proteolysis or reach the cell membrane. [Isoform p41]: Late endosome Lysosome Event=Alternative splicing, Alternative initiation; Named isoforms=5; Name=p45 ; Synonyms=Long; IsoId=P04233-1; Sequence=Displayed; Name=p35 ; Synonyms=Short; IsoId=P04233-2; Sequence=VSP_005331; Name=3; IsoId=P04233-3; Sequence=VSP_037869, VSP_037870; Name=p41 ; IsoId=P04233-4; Sequence=VSP_060904; Name=p33 ; IsoId=P04233-5; Sequence=VSP_060904, VSP_005331; Detected in urine (at protein level). [Isoform p41]: In B cells, represents 10% of total CD74 expression. [Isoform p33]: In B cells, represents 70% of total CD74 expression. Antiviral activity requires delivery of the thyroglobulin domain to the endosomal membrane. O-glycosylated with core 1 or possibly core 8 glycans (PubMed:22171320, PubMed:23234360). Contains chondroitin sulfate (PubMed:25326458). Note=A chromosomal aberration involving CD74 is found in a non-small cell lung tumor. Results in the formation of a CD74-ROS1 chimeric protein. Sequence=AAA36304.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Golgi membrane activation of MAPK activity prostaglandin biosynthetic process beta-amyloid binding positive regulation of protein phosphorylation positive regulation of cytokine-mediated signaling pathway adaptive immune response immune system process positive regulation of dendritic cell antigen processing and presentation negative regulation of peptide secretion positive regulation of type 2 immune response negative regulation of mature B cell apoptotic process cytokine receptor activity protein binding nucleus cytoplasm lysosome lysosomal membrane endosome late endosome multivesicular body vacuole endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus plasma membrane intracellular protein transport defense response immune response signal transduction cell proliferation external side of plasma membrane cell surface positive regulation of gene expression ER to Golgi transport vesicle membrane membrane integral component of membrane immunoglobulin mediated immune response antigen processing and presentation antigen processing and presentation of endogenous antigen antigen processing and presentation of exogenous peptide antigen via MHC class II cytokine binding MHC class II protein complex binding negative regulation of cell migration transport vesicle membrane endocytic vesicle membrane clathrin-coated endocytic vesicle membrane positive regulation of B cell proliferation positive regulation of prostaglandin biosynthetic process trans-Golgi network membrane macromolecular complex positive regulation of kinase activity macrophage migration inhibitory factor signaling pathway macrophage migration inhibitory factor receptor complex NOS2-CD74 complex macrophage migration inhibitory factor binding MHC class II protein binding CD4 receptor binding MHC class II protein complex MHC class II protein binding, via antigen binding groove identical protein binding regulation of macrophage activation negative regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling lysosomal lumen positive regulation of MAPK cascade negative regulation of DNA damage response, signal transduction by p53 class mediator protein binding involved in protein folding T cell selection positive thymic T cell selection negative thymic T cell selection positive regulation of chemokine biosynthetic process positive regulation of interleukin-6 biosynthetic process positive regulation of interleukin-8 biosynthetic process negative regulation of T cell differentiation positive regulation of T cell differentiation positive regulation of monocyte differentiation positive regulation of transcription, DNA-templated positive regulation of viral entry into host cell positive regulation of fibroblast proliferation positive regulation of peptidyl-tyrosine phosphorylation leukocyte migration nitric-oxide synthase binding chaperone mediated protein folding requiring cofactor protein heterotetramerization positive regulation of macrophage cytokine production macromolecular complex assembly extracellular exosome protein trimerization positive regulation of ERK1 and ERK2 cascade integral component of lumenal side of endoplasmic reticulum membrane positive regulation of neutrophil chemotaxis negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator positive regulation of chemokine (C-X-C motif) ligand 2 production positive regulation of macrophage migration inhibitory factor signaling pathway uc003lsc.1 uc003lsc.2 uc003lsc.3 uc003lsc.4 uc003lsc.5 uc003lsc.6 
ENST00000009589.8 RPS20 ENST00000009589.8 ribosomal protein S20, transcript variant 2 (from RefSeq NM_001023.4) B2R4F4 B4DW28 ENST00000009589.1 ENST00000009589.2 ENST00000009589.3 ENST00000009589.4 ENST00000009589.5 ENST00000009589.6 ENST00000009589.7 NM_001023 P17075 P60866 Q5M8S9 RS20_HUMAN uc003xsn.1 uc003xsn.2 uc003xsn.3 uc003xsn.4 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S10P family of ribosomal proteins. It is located in the cytoplasm. This gene is co-transcribed with the small nucleolar RNA gene U54, which is located in its second intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. Two transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Apr 2009]. Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Component of the 40S small ribosomal subunit. P60866; Q5S007: LRRK2; NbExp=4; IntAct=EBI-353105, EBI-5323863; P60866; Q15843: NEDD8; NbExp=3; IntAct=EBI-353105, EBI-716247; P60866; P36578: RPL4; NbExp=4; IntAct=EBI-353105, EBI-348313; P60866; Q6S8E0: ORF9b; Xeno; NbExp=2; IntAct=EBI-353105, EBI-25489144; Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P60866-1; Sequence=Displayed; Name=2; IsoId=P60866-2; Sequence=VSP_042724; Polyubiquitinated by ZNF598 via 'Lys-63'-linked ubiquitin chains when a ribosome has stalled, initiating the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide (PubMed:28065601, PubMed:28132843, PubMed:28685749, PubMed:32011234, PubMed:36302773). Deubiquitinated by OTUD3 and USP21, antagonizing ZNF598 activity (PubMed:32011234). Ufmylated by UFL1. Belongs to the universal ribosomal protein uS10 family. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay RNA binding structural constituent of ribosome protein binding nucleoplasm cytoplasm cytosol ribosome translation translational initiation SRP-dependent cotranslational protein targeting to membrane small ribosomal subunit membrane viral transcription cytosolic small ribosomal subunit extracellular exosome uc003xsn.1 uc003xsn.2 uc003xsn.3 uc003xsn.4 
ENST00000011292.8 CPA1 ENST00000011292.8 carboxypeptidase A1 (from RefSeq NM_001868.4) A4D1M1 CBPA1_HUMAN CPA CPA1 ENST00000011292.1 ENST00000011292.2 ENST00000011292.3 ENST00000011292.4 ENST00000011292.5 ENST00000011292.6 ENST00000011292.7 NM_001868 P15085 Q53XU0 Q9BS67 Q9UCF2 uc003vpx.1 uc003vpx.2 uc003vpx.3 uc003vpx.4 uc003vpx.5 This gene encodes a member of the carboxypeptidase A family of zinc metalloproteases. This enzyme is produced in the pancreas and preferentially cleaves C-terminal branched-chain and aromatic amino acids from dietary proteins. This gene and several family members are present in a gene cluster on chromosome 7. Mutations in this gene may be linked to chronic pancreatitis, while elevated protein levels may be associated with pancreatic cancer. [provided by RefSeq, Jan 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK291493.1, BT007313.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968832 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000011292.8/ ENSP00000011292.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (PubMed:8806703). Catalyzes the conversion of leukotriene C4 to leukotriene F4 via the hydrolysis of an amide bond (By similarity). Reaction=Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1; Evidence=; Reaction=H2O + leukotriene C4 = glycine + leukotriene F4; Xref=Rhea:RHEA:50740, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:57973, ChEBI:CHEBI:133618; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50741; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Monomer. May form a complex with proelastase 2. P15085; P19399; Xeno; NbExp=2; IntAct=EBI-1642148, EBI-15754788; Secreted. Belongs to the peptidase M14 family. carboxypeptidase activity metallocarboxypeptidase activity protein binding extracellular region extracellular space proteolysis peptidase activity metallopeptidase activity exopeptidase activity zinc ion binding hydrolase activity metal ion binding uc003vpx.1 uc003vpx.2 uc003vpx.3 uc003vpx.4 uc003vpx.5 
ENST00000011619.6 RANBP9 ENST00000011619.6 RAN binding protein 9 (from RefSeq NM_005493.3) A0PJA2 B2R8E1 ENST00000011619.1 ENST00000011619.2 ENST00000011619.3 ENST00000011619.4 ENST00000011619.5 NM_005493 O94764 Q6P3T7 Q7LBR2 Q7Z7F9 Q96S59 RANB9_HUMAN RANBPM uc003nbb.1 uc003nbb.2 uc003nbb.3 uc003nbb.4 This gene encodes a protein that binds RAN, a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The protein encoded by this gene has also been shown to interact with several other proteins, including met proto-oncogene, homeodomain interacting protein kinase 2, androgen receptor, and cyclin-dependent kinase 11. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF306510.1, BC052781.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000011619.6/ ENSP00000011619.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Acts as a mediator of cell spreading and actin cytoskeleton rearrangement (PubMed:18710924). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). May be involved in signaling of ITGB2/LFA-1 and other integrins (PubMed:14722085). Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway (PubMed:12147692). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation (PubMed:12361945, PubMed:18222118). Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity (PubMed:15558019). Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA. Part of a complex consisting of RANBP9, MKLN1 and GID8 (PubMed:12559565). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5 (PubMed:17467196, PubMed:29911972). Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles (PubMed:29911972). Interacts with GTP-bound Ran, AR, CDC2L1/p110C, CALB1, S100A7, USP11, MKLN1, SOS1 or SOS2, GID8, and FMR1 (PubMed:11470507, PubMed:9817760, PubMed:12361945, PubMed:12084015, PubMed:12421467, PubMed:12147692, PubMed:12684061, PubMed:14511641, PubMed:14684163, PubMed:15381419, PubMed:18710924). Interacts with the Dyrk kinases HIPK2, DYRK1A, and DYRK1B (PubMed:12220523, PubMed:14500717). Interacts with TP73 isoform Alpha but not with TP53 (PubMed:15558019). Interacts with the HGF receptor MET and the integrins ITGB1 and ITGB2, but not with ITGAL (PubMed:14722085). Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 (PubMed:14500717). Directly interacts with RANBP10 (PubMed:18222118). Interacts with YPEL5 (PubMed:20580816). Interacts with DDX4 (PubMed:27622290). Interacts with NGFR (By similarity). Interacts with TEX19 (By similarity). Q96S59; P05067: APP; NbExp=3; IntAct=EBI-636085, EBI-77613; Q96S59; Q9NRI5: DISC1; NbExp=7; IntAct=EBI-636085, EBI-529989; Q96S59; Q9Y463: DYRK1B; NbExp=4; IntAct=EBI-636085, EBI-634187; Q96S59; P49961: ENTPD1; NbExp=5; IntAct=EBI-636085, EBI-8074749; Q96S59; P35372: OPRM1; NbExp=5; IntAct=EBI-636085, EBI-2624570; Q96S59; P36873-2: PPP1CC; NbExp=3; IntAct=EBI-636085, EBI-3964623; Q96S59; P31151: S100A7; NbExp=3; IntAct=EBI-636085, EBI-357520; Q96S59; P31421: Grm2; Xeno; NbExp=4; IntAct=EBI-636085, EBI-7090147; Cytoplasm cleus ll membrane ; Peripheral membrane protein Note=The unphosphorylated form is predominantly cytoplasmic. A phosphorylated form is associated with the plasma membrane. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q96S59-1; Sequence=Displayed; Name=2; IsoId=Q96S59-2; Sequence=VSP_013175; Name=3; IsoId=Q96S59-3; Sequence=VSP_056049; Ubiquitously expressed, with highest levels in testes, placenta, heart, and muscle, and lowest levels in lung. Within the brain, expressed predominantly by neurons in the gray matter of cortex, the granular layer of cerebellum and the Purkinje cells. The SPRY domain mediates the interaction with MET, AR, and CDC2L1. Phosphorylated in response to stress. Can be phosphorylated by the cleaved p110 form of CDC2L1 (p110C). Ubiquitinated. Polyubiquitination targets the protein for rapid degradation via the ubiquitin system. Can be deubiquitinated by USP11. Belongs to the RANBP9/10 family. According to some authors RANBP9 is located in centrosomes and involved in microtubule assembly. Other authors infirmed these results. Sequence=AAH19886.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; Sequence=AAH52781.1; Type=Frameshift; Evidence=; Sequence=AAK15469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAA23216.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42040/RANBP9"; ubiquitin ligase complex MAPK cascade protein binding nucleus cytoplasm cytosol microtubule associated complex plasma membrane microtubule nucleation axon guidance Ran GTPase binding membrane enzyme binding macromolecular complex assembly negative regulation of ERK1 and ERK2 cascade uc003nbb.1 uc003nbb.2 uc003nbb.3 uc003nbb.4 
ENST00000011653.9 CD4 ENST00000011653.9 CD4 molecule, transcript variant 9 (from RefSeq NM_001382714.1) B2R737 CD4_HUMAN D3DUS5 ENST00000011653.1 ENST00000011653.2 ENST00000011653.3 ENST00000011653.4 ENST00000011653.5 ENST00000011653.6 ENST00000011653.7 ENST00000011653.8 NM_001382714 P01730 Q4ZGK2 Q5U066 Q9UDE5 uc001qqv.1 uc001qqv.2 uc001qqv.3 uc001qqv.4 This gene encodes the CD4 membrane glycoprotein of T lymphocytes. The CD4 antigen acts as a coreceptor with the T-cell receptor on the T lymphocyte to recognize antigens displayed by an antigen presenting cell in the context of class II MHC molecules. The CD4 antigen is also a primary receptor for entry of the human immunodeficiency virus through interactions with the HIV Env gp120 subunit. This gene is expressed not only in T lymphocytes, but also in B cells, macrophages, granulocytes, as well as in various regions of the brain. The protein functions to initiate or augment the early phase of T-cell activation, and may function as an important mediator of indirect neuronal damage in infectious and immune-mediated diseases of the central nervous system. Multiple alternatively spliced transcript variants encoding different isoforms have been identified in this gene. [provided by RefSeq, May 2020]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T- helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. (Microbial infection) Primary receptor for human immunodeficiency virus-1 (HIV-1) (PubMed:2214026, PubMed:16331979, PubMed:9641677, PubMed:12089508). Down-regulated by HIV-1 Vpu (PubMed:17346169). Acts as a receptor for Human Herpes virus 7/HHV-7 (PubMed:7909607). Forms disulfide-linked homodimers at the cell surface. Interacts with LCK (PubMed:16888650). Interacts with PTK2/FAK1 (PubMed:18078954). Binds to P4HB/PDI. Interacts with IL16; this interaction induces a CD4-dependent signaling in lymphocytes (PubMed:1673145). Interacts (via Ig-like V-type domain) with MHCII alpha chain (via alpha-2 domain) and beta chain (via beta-2 domain); this interaction increases the affinity of TCR for peptide-MHCII. CD4 oligomerization via Ig-like C2-type 2 and 3 domains appears to be required for stable binding to MHCII and adhesion between T cells and APCs (PubMed:27114505, PubMed:21900604, PubMed:7604010). (Microbial infection) Interacts with HIV-1 Envelope polyprotein gp160 and protein Vpu (PubMed:2214026, PubMed:16331979, PubMed:9641677, PubMed:7604010). (Microbial infection) Interacts with Human Herpes virus 7 surface proteins. P01730; P51681: CCR5; NbExp=3; IntAct=EBI-353826, EBI-489374; P01730; P01730: CD4; NbExp=2; IntAct=EBI-353826, EBI-353826; P01730; P13473-2: LAMP2; NbExp=3; IntAct=EBI-353826, EBI-21591415; P01730; P06239: LCK; NbExp=2; IntAct=EBI-353826, EBI-1348; P01730; P04150: NR3C1; NbExp=2; IntAct=EBI-353826, EBI-493507; P01730; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-353826, EBI-2623095; P01730; P04578: env; Xeno; NbExp=2; IntAct=EBI-353826, EBI-6163496; P01730; PRO_0000038427 [P04578]: env; Xeno; NbExp=3; IntAct=EBI-353826, EBI-6179761; P01730; Q1PHM6: env; Xeno; NbExp=2; IntAct=EBI-353826, EBI-15845606; P01730; Q2N0S6: env; Xeno; NbExp=3; IntAct=EBI-353826, EBI-16080048; P01730; P03407: nef; Xeno; NbExp=2; IntAct=EBI-353826, EBI-7355020; P01730; P05919: vpu; Xeno; NbExp=3; IntAct=EBI-353826, EBI-6164626; Cell membrane ingle-pass type I membrane protein te=Localizes to lipid rafts (PubMed:12517957, PubMed:9168119). Removed from plasma membrane by HIV- 1 Nef protein that increases clathrin-dependent endocytosis of this antigen to target it to lysosomal degradation. Cell surface expression is also down-modulated by HIV-1 Envelope polyprotein gp160 that interacts with, and sequesters CD4 in the endoplasmic reticulum. Highly expressed in T-helper cells. The presence of CD4 is a hallmark of T-helper cells which are specialized in the activation and growth of cytotoxic T-cells, regulation of B cells, or activation of phagocytes. CD4 is also present in other immune cells such as macrophages, dendritic cells or NK cells. The Ig-like V-type domain mediates the interaction with MHCII. Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. Phosphorylated by PKC; phosphorylation at Ser-433 plays an important role for CD4 internalization. The OKT monoclonal antibodies are widely used for the analysis of human peripheral blood T-lymphocytes. OKT4 reacts with T- helper/inducer lymphocytes. The OKT4 epitope of the CD4 cell-surface protein is polymorphic in white, black, and Japanese populations. The variable phenotypic expression is due a CD4 polymorphism. OKT4 positive individuals carry Arg-265 and OKT4 negative individuals carry Trp-265 [MIM:613949]. Immunodeficiency 79 (IMD79) [MIM:619238]: An autosomal recessive disorder characterized by childhood onset of recurrent and recalcitrant skin warts due to uncontrolled viral infection with human papillomavirus (HPV). Some patients may also have recurrent respiratory infections. Laboratory studies show a complete absence of CD4+ T cells. Note=The disease is caused by variants affecting the gene represented in this entry. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cd4/"; Name=Wikipedia; Note=CD4 entry; URL="https://en.wikipedia.org/wiki/CD4"; virus receptor activity cytokine production positive regulation of protein phosphorylation adaptive immune response immune system process transmembrane signaling receptor activity receptor binding extracellular matrix structural constituent protein binding early endosome endoplasmic reticulum lumen endoplasmic reticulum membrane plasma membrane integral component of plasma membrane induction by virus of host cell-cell fusion immune response cell adhesion signal transduction cell surface receptor signaling pathway enzyme linked receptor protein signaling pathway transmembrane receptor protein tyrosine kinase signaling pathway zinc ion binding external side of plasma membrane cell surface positive regulation of calcium ion transport into cytosol coreceptor activity membrane integral component of membrane viral process fusion of virus membrane with host plasma membrane cytokine-mediated signaling pathway immunoglobulin binding enzyme binding protein kinase binding T cell differentiation macrophage differentiation entry into host cell clathrin-coated vesicle membrane response to estradiol maintenance of protein location in cell response to vitamin D positive regulation of kinase activity helper T cell enhancement of adaptive immune response interleukin-15-mediated signaling pathway signaling receptor activity interleukin-16 binding interleukin-16 receptor activity T cell receptor complex positive regulation of T cell proliferation T cell activation MHC class II protein binding identical protein binding protein homodimerization activity positive regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of MAPK cascade T cell selection positive regulation of interleukin-2 biosynthetic process membrane raft positive regulation of monocyte differentiation positive regulation of protein kinase activity positive regulation of transcription, DNA-templated positive regulation of viral entry into host cell regulation of defense response to virus by virus positive regulation of peptidyl-tyrosine phosphorylation defense response to Gram-negative bacterium positive regulation of calcium-mediated signaling T cell receptor signaling pathway regulation of T cell activation positive regulation of T cell activation regulation of calcium ion transport membrane organization positive regulation of ERK1 and ERK2 cascade cellular response to granulocyte macrophage colony-stimulating factor stimulus protein tyrosine kinase binding uc001qqv.1 uc001qqv.2 uc001qqv.3 uc001qqv.4 
ENST00000011691.6 SS18L2 ENST00000011691.6 SS18 like 2, transcript variant 1 (from RefSeq NM_001370300.1) B2R5L1 ENST00000011691.1 ENST00000011691.2 ENST00000011691.3 ENST00000011691.4 ENST00000011691.5 NM_001370300 Q9UHA2 S18L2_HUMAN uc003clk.1 uc003clk.2 uc003clk.3 Synovial sarcomas occur most frequently in the extremities around large joints. More than 90% of cases have a recurrent and specific chromosomal translocation, t(X;18)(p11.2;q11.2), in which the 5-prime end of the SS18 gene (MIM 600192) is fused in-frame to the 3-prime end of the SSX1 (MIM 312820), SSX2 (MIM 300192), or SSX4 (MIM 300326) gene. The SS18L2 gene is homologous to SS18.[supplied by OMIM, Jul 2002]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.219285.1, SRR1660809.73432.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on expression, longest protein ##RefSeq-Attributes-END## Q9UHA2; Q15006: EMC2; NbExp=3; IntAct=EBI-10962400, EBI-359031; Q9UHA2; P63215: GNG3; NbExp=3; IntAct=EBI-10962400, EBI-1046668; Q9UHA2; Q86Y78: LYPD6; NbExp=3; IntAct=EBI-10962400, EBI-14035066; Q9UHA2; Q9P267-2: MBD5; NbExp=3; IntAct=EBI-10962400, EBI-17671489; Q9UHA2; Q86X19: TMEM17; NbExp=3; IntAct=EBI-10962400, EBI-11343485; Q9UHA2; Q9H869-2: YY1AP1; NbExp=4; IntAct=EBI-10962400, EBI-12150045; Belongs to the SS18 family. transcription coactivator activity protein binding nucleus positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter positive regulation of dendrite morphogenesis uc003clk.1 uc003clk.2 uc003clk.3 
ENST00000011898.10 TSPAN9 ENST00000011898.10 tetraspanin 9, transcript variant 1 (from RefSeq NM_006675.5) D3DUQ7 ENST00000011898.1 ENST00000011898.2 ENST00000011898.3 ENST00000011898.4 ENST00000011898.5 ENST00000011898.6 ENST00000011898.7 ENST00000011898.8 ENST00000011898.9 NET5 NM_006675 O75954 Q53FV2 Q6FGJ8 TSN9_HUMAN uc001qlp.1 uc001qlp.2 uc001qlp.3 uc001qlp.4 uc001qlp.5 The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. Alternatively spliced transcripts encoding the same protein have been identified. [provided by RefSeq, Nov 2009]. Found in a complex with GP6. Membrane ; Multi-pass membrane protein Note=Colocalizes with GP6 in tetraspanin microdomains on the platelet surface. Expressed in megakaryocytes and platelets (at protein level). Glycosylated. Belongs to the tetraspanin (TM4SF) family. molecular_function plasma membrane integral component of plasma membrane focal adhesion biological_process membrane integral component of membrane tetraspanin-enriched microdomain uc001qlp.1 uc001qlp.2 uc001qlp.3 uc001qlp.4 uc001qlp.5 
ENST00000012049.10 QPCTL ENST00000012049.10 glutaminyl-peptide cyclotransferase like, transcript variant 1 (from RefSeq NM_017659.4) ENST00000012049.1 ENST00000012049.2 ENST00000012049.3 ENST00000012049.4 ENST00000012049.5 ENST00000012049.6 ENST00000012049.7 ENST00000012049.8 ENST00000012049.9 NM_017659 Q53HE4 Q96F74 Q9NXS2 QPCTL_HUMAN uc010xxr.1 uc010xxr.2 uc010xxr.3 uc010xxr.4 Responsible for the biosynthesis of pyroglutamyl peptides. Reaction=N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl- [peptide] + NH4(+); Xref=Rhea:RHEA:23652, Rhea:RHEA-COMP:11736, Rhea:RHEA-COMP:11846, ChEBI:CHEBI:28938, ChEBI:CHEBI:64722, ChEBI:CHEBI:87215; EC=2.3.2.5; Evidence= Q9NXS2-3; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-13336719, EBI-2804156; Q9NXS2-3; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-13336719, EBI-10243654; Golgi apparatus membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NXS2-1; Sequence=Displayed; Name=2; IsoId=Q9NXS2-3; Sequence=VSP_054066; Belongs to the glutaminyl-peptide cyclotransferase family. It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn(2+)-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn(2+) ions, typically in a 1:1 stoichiometry (PubMed:21288892). However, a recent study suggests a Zn(2+)-independent catalytic mechanism (By similarity). Golgi membrane Golgi apparatus zinc ion binding membrane integral component of membrane glutaminyl-peptide cyclotransferase activity transferase activity transferase activity, transferring acyl groups peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase metal ion binding uc010xxr.1 uc010xxr.2 uc010xxr.3 uc010xxr.4 
ENST00000012443.9 PPP5C ENST00000012443.9 protein phosphatase 5 catalytic subunit, transcript variant 1 (from RefSeq NM_006247.4) ENST00000012443.1 ENST00000012443.2 ENST00000012443.3 ENST00000012443.4 ENST00000012443.5 ENST00000012443.6 ENST00000012443.7 ENST00000012443.8 NM_006247 P53041 PPP5 PPP5_HUMAN Q16722 Q53XV2 uc002pem.1 uc002pem.2 uc002pem.3 uc002pem.4 uc002pem.5 This gene encodes a serine/threonine phosphatase which is a member of the protein phosphatase catalytic subunit family. Proteins in this family participate in pathways regulated by reversible phosphorylation at serine and threonine residues; many of these pathways are involved in the regulation of cell growth and differentiation. The product of this gene has been shown to participate in signaling pathways in response to hormones or cellular stress, and elevated levels of this protein may be associated with breast cancer development. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2011]. Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:9000529, PubMed:30699359). Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:9000529, PubMed:30699359). Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1 (PubMed:14871926, PubMed:16260606, PubMed:21144835). Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress (PubMed:23102700). Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function (By similarity). Also dephosphorylates and inhibits the anti- adipogenic effect of NR3C1 (By similarity). Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E (PubMed:16790549). May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels (PubMed:22781750). Dephosphorylates and may play a role in the regulation of TAU/MAPT (PubMed:15546861). Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2 (By similarity). Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90 (PubMed:30699359). Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence= Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 Mg(2+) or Mn(2+) cations per subunit.; Autoinhibited. In the autoinhibited state, the TPR domain interacts with the catalytic region and prevents substrate access to the catalytic pocket. Allosterically activated by various polyunsaturated fatty acids, free long-chain fatty-acids and long-chain fatty acyl-CoA esters, arachidonic acid being the most effective activator. HSP90A and probably RAC1, GNA12 and GNA13 can also release the autoinhibition by the TPR repeat. Activation by RAC1, GNA12 and GNA13 is synergistic with the one produced by fatty acids binding. Inhibited by okadaic acid. Kinetic parameters: KM=1.847 uM for CSNK1E (at 30 degrees Celsius) ; KM=13.2 uM for MAPT/TAU (at pH 7.4 and 30 degrees Celsius) ; Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Part of a complex with HSP90/HSP90AA1 and steroid receptors (By similarity). Interacts (via TPR repeats) with HSP90AA1 (via TPR repeat-binding motif) or HSPA1A/HSPA1B; the interaction is direct and activates the phosphatase activity (PubMed:15383005, PubMed:15577939, PubMed:16531226). Dissociates from HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid (PubMed:15383005). Interacts with CPNE1 (via VWFA domain) (By similarity). Interacts with CDC16, CDC27 (PubMed:9405394). Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the phosphatase activity on MAP3K5 (PubMed:23102700). Interacts with ATM and ATR; both interactions are induced by DNA damage and enhance ATM and ATR kinase activity (PubMed:14871926). Interacts with RAD17; reduced by DNA damage (PubMed:14871926). Interacts with nuclear receptors such as NR3C1/GCR and PPARG (activated by agonist); regulates their transactivation activities (By similarity). Interacts (via TPR repeats) with S100 proteins S100A1, S100A2, S100A6, S100B and S100P; the interactions are calcium-dependent, strongly activate PPP5C phosphatase activity and compete with HSP90AA1 and MAP3K5 interactions (PubMed:22399290). Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3 phosphorylation and protein levels (PubMed:22781750). Interacts (via TPR repeats) with CRY1 and CRY2; the interaction with CRY2 down- regulates the phosphatase activity on CSNK1E (PubMed:16790549). Interacts (via TPR repeats) with the active form of RAC1, GNA12 or GNA13; these interactions activate the phosphatase activity and translocate PPP5C to the cell membrane (PubMed:19948726). Interacts with FLCN (PubMed:27353360). P53041; Q9UL18: AGO1; NbExp=2; IntAct=EBI-716663, EBI-527363; P53041; Q9H9G7: AGO3; NbExp=2; IntAct=EBI-716663, EBI-2267883; P53041; Q16543: CDC37; NbExp=5; IntAct=EBI-716663, EBI-295634; P53041; P50750: CDK9; NbExp=3; IntAct=EBI-716663, EBI-1383449; P53041; Q49AN0: CRY2; NbExp=3; IntAct=EBI-716663, EBI-2212355; P53041; P03372: ESR1; NbExp=4; IntAct=EBI-716663, EBI-78473; P53041; Q92731: ESR2; NbExp=4; IntAct=EBI-716663, EBI-78505; P53041; P07900: HSP90AA1; NbExp=12; IntAct=EBI-716663, EBI-296047; P53041; P08238: HSP90AB1; NbExp=8; IntAct=EBI-716663, EBI-352572; P53041; Q5SY16: NOL9; NbExp=2; IntAct=EBI-716663, EBI-1055462; P53041; P30153: PPP2R1A; NbExp=3; IntAct=EBI-716663, EBI-302388; P53041; P53041: PPP5C; NbExp=2; IntAct=EBI-716663, EBI-716663; P53041; P31948: STIP1; NbExp=4; IntAct=EBI-716663, EBI-1054052; Nucleus Cytoplasm Cell membrane Note=Predominantly nuclear (PubMed:15383005). But also present in the cytoplasm (PubMed:15383005). Translocates from the cytoplasm to the plasma membrane in a RAC1- dependent manner (PubMed:19948726). Ubiquitous. Activated by at least two different proteolytic cleavages producing a 56 kDa and a 50 kDa form. Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily. MAPK cascade mitotic cell cycle negative regulation of protein phosphorylation G-protein alpha-subunit binding RNA binding phosphoprotein phosphatase activity protein serine/threonine phosphatase activity protein binding ATP binding nucleus nucleoplasm cytoplasm cytosol plasma membrane DNA repair transcription, DNA-templated protein dephosphorylation cellular response to DNA damage stimulus microtubule binding lipid binding response to lead ion membrane histone dephosphorylation hydrolase activity phosphatase activity heat shock protein binding macromolecular complex peptidyl-threonine dephosphorylation identical protein binding neuron projection neuronal cell body positive regulation of I-kappaB kinase/NF-kappaB signaling perikaryon intracellular membrane-bounded organelle response to morphine ADP binding metal ion binding tau protein binding protein oligomerization protein heterooligomerization Hsp90 protein binding negative regulation of cell death peptidyl-serine dephosphorylation cellular response to hydrogen peroxide cellular response to cadmium ion cell periphery negative regulation of neuron death response to arachidonic acid proximal dendrite positive regulation of glucocorticoid receptor signaling pathway uc002pem.1 uc002pem.2 uc002pem.3 uc002pem.4 uc002pem.5 
ENST00000013070.11 UBR7 ENST00000013070.11 ubiquitin protein ligase E3 component n-recognin 7, transcript variant 3 (from RefSeq NR_038150.2) C14orf130 ENST00000013070.1 ENST00000013070.10 ENST00000013070.2 ENST00000013070.3 ENST00000013070.4 ENST00000013070.5 ENST00000013070.6 ENST00000013070.7 ENST00000013070.8 ENST00000013070.9 NR_038150 Q86U21 Q86UA9 Q8N806 Q96BY0 Q9NVV6 UBR7_HUMAN uc001ybm.1 uc001ybm.2 uc001ybm.3 uc001ybm.4 uc001ybm.5 This gene encodes a UBR box-containing protein that belongs to the E3 ubiquitin ligase family. The protein also contains a plant homeodomain (PHD) in the C-terminus. In mammals, the encoded protein recognizes N-degrons, the destabilizing N-terminal residues of short-lived proteins, which results in ubiquitinylation, and proteolysis via the proteasome. [provided by RefSeq, Jul 2016]. E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Protein modification; protein ubiquitination. Expressed in sperm (at protein level). Li-Campeau syndrome (LICAS) [MIM:619189]: An autosomal recessive neurodevelopmental disorder characterized by global developmental delay, intellectual disability, epilepsy, ptosis, hypothyroidism, and variable cardiac and genital anomalies. Additional features may include seizures, short stature, hypotonia, and brain imaging anomalies, such as cortical atrophy. Note=The disease is caused by variants affecting the gene represented in this entry. Sequence=AAH15046.1; Type=Erroneous initiation; Evidence=; Sequence=AAH51819.4; Type=Erroneous initiation; Evidence=; Sequence=BAA91639.1; Type=Erroneous initiation; Evidence=; molecular_function cytoplasm biological_process zinc ion binding protein ubiquitination transferase activity metal ion binding ubiquitin protein ligase activity uc001ybm.1 uc001ybm.2 uc001ybm.3 uc001ybm.4 uc001ybm.5 
ENST00000013222.5 INMT ENST00000013222.5 indolethylamine N-methyltransferase, transcript variant 1 (from RefSeq NM_006774.5) B8ZZ69 ENST00000013222.1 ENST00000013222.2 ENST00000013222.3 ENST00000013222.4 INMT_HUMAN NM_006774 O95050 Q3KP49 Q9P1Y2 Q9UBY4 Q9UHQ0 uc003tbs.1 N-methylation of endogenous and xenobiotic compounds is a major method by which they are degraded. This gene encodes an enzyme that N-methylates indoles such as tryptamine. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the downstream MINDY4 (aka FAM188B) gene. In rodents and other mammals such as cetartiodactyla this gene is in the opposite orientation compared to its orientation in human and other primates and this gene appears to have been lost in carnivora and chiroptera. [provided by RefSeq, Jul 2019]. Functions as a thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2- methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds (By similarity). Catalyzes the N-methylation of tryptamine and structurally related compounds. Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated tertiary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983; EC=2.1.1.49; Evidence=; Reaction=a secondary amine + S-adenosyl-L-methionine = a methylated secondary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:137419, ChEBI:CHEBI:137984; EC=2.1.1.49; Evidence=; Reaction=a primary amine + S-adenosyl-L-methionine = a methylated primary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65296, ChEBI:CHEBI:131823; EC=2.1.1.49; Evidence=; Reaction=dimethyl sulfide + S-adenosyl-L-methionine = S-adenosyl-L- homocysteine + trimethylsulfonium; Xref=Rhea:RHEA:19613, ChEBI:CHEBI:17434, ChEBI:CHEBI:17437, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.96; Evidence=; Kinetic parameters: KM=2.9 mM for tryptamine ; Monomer. O95050; Q53G59: KLHL12; NbExp=6; IntAct=EBI-10191038, EBI-740929; Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95050-1; Sequence=Displayed; Name=2; IsoId=O95050-2; Sequence=VSP_045922; Widely expressed. The highest levels were in thyroid, adrenal gland, adult and fetal lung. Intermediate levels in heart, placenta, skeletal muscle, testis, small intestine, pancreas, stomach, spinal cord, lymph node and trachea. Very low levels in adult and fetal kidney and liver, in adult spleen, thymus, ovary, colon and bone marrow. Not expressed in peripheral blood leukocytes and brain. Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family. thioether S-methyltransferase activity protein binding cytoplasm cytosol methyltransferase activity amine metabolic process response to toxic substance transferase activity amine N-methyltransferase activity methylation uc003tbs.1 
ENST00000014914.6 GPRC5A ENST00000014914.6 G protein-coupled receptor class C group 5 member A (from RefSeq NM_003979.4) B3KV45 ENST00000014914.1 ENST00000014914.2 ENST00000014914.3 ENST00000014914.4 ENST00000014914.5 GPCR5A NM_003979 O95357 Q8NFJ5 RAI3 RAI3_HUMAN RAIG1 uc001rba.1 uc001rba.2 uc001rba.3 uc001rba.4 uc001rba.5 This gene encodes a member of the type 3 G protein-coupling receptor family, characterized by the signature 7-transmembrane domain motif. The encoded protein may be involved in interaction between retinoid acid and G protein signalling pathways. Retinoic acid plays a critical role in development, cellular growth, and differentiation. This gene may play a role in embryonic development and epithelial cell differentiation. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7346977.2461861.1, SRR7346977.2565752.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000014914.6/ ENSP00000014914.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Orphan receptor. Could be involved in modulating differentiation and maintaining homeostasis of epithelial cells. This retinoic acid-inducible GPCR provide evidence for a possible interaction between retinoid and G-protein signaling pathways. Functions as a negative modulator of EGFR signaling (By similarity). May act as a lung tumor suppressor (PubMed:18000218). Interacts (via its transmembrane domain) with EGFR. Cell membrane ; Multi-pass membrane protein Cytoplasmic vesicle membrane ; Multi-pass membrane protein Note=Localized in perinuclear vesicles, probably Golgi- associated vesicles. Expressed at high level in fetal and adult lung tissues but repressed in most human lung cancers (PubMed:9857033, PubMed:18000218). Constitutively expressed in fetal kidney and adult placenta, kidney, prostate, testis, ovary, small intestine, colon, stomach, and spinal cord at low to moderate levels. Not detectable in fetal heart, brain, and liver and adult heart, brain, liver, skeletal muscle, pancreas, spleen, thymus, and peripheral leukocytes. According to PubMed:10783259, expressed at low but detectable level in pancreas and heart. By all-trans retinoic acid (ATRA). Phosphorylated in two conserved double-tyrosine motifs, Tyr- 317/Tyr-320 and Tyr-347/Tyr-350, by EGFR; leading to inactivation of the tumor suppressive function of GPRC5A in lung cancer cells. Tyr-317 and Tyr-320 are the preferred residues responsible for EGFR-mediated GPRC5A phosphorylation. Belongs to the G-protein coupled receptor 3 family. G-protein coupled receptor activity protein binding nucleolus plasma membrane integral component of plasma membrane signal transduction negative regulation of epidermal growth factor-activated receptor activity G-protein coupled receptor signaling pathway membrane integral component of membrane protein kinase activator activity cytoplasmic vesicle membrane cytoplasmic vesicle vesicle activation of protein kinase activity intracellular membrane-bounded organelle receptor complex cadherin binding extracellular exosome uc001rba.1 uc001rba.2 uc001rba.3 uc001rba.4 uc001rba.5 
ENST00000014930.9 HEBP1 ENST00000014930.9 heme binding protein 1 (from RefSeq NM_015987.5) A8K1G2 ENST00000014930.1 ENST00000014930.2 ENST00000014930.3 ENST00000014930.4 ENST00000014930.5 ENST00000014930.6 ENST00000014930.7 ENST00000014930.8 HBP HEBP1_HUMAN NM_015987 Q9NRV9 Q9Y5Z5 uc001rbd.1 uc001rbd.2 uc001rbd.3 uc001rbd.4 uc001rbd.5 The full-length protein encoded by this gene is an intracellular tetrapyrrole-binding protein. This protein includes a natural chemoattractant peptide of 21 amino acids at the N-terminus, which is a natural ligand for formyl peptide receptor-like receptor 2 (FPRL2) and promotes calcium mobilization and chemotaxis in monocytes and dendritic cells. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: ERR279873.4554.1, SRR3476690.869805.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000014930.9/ ENSP00000014930.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities. Monomer. Cytoplasm Forms a distorted beta-barrel structure, with two helices that are packed against the outer surface of the barrel. Porphyrins are expected to bind to a hydrophobic patch on the outer surface of the beta-barrel structure (By similarity). Belongs to the HEBP family. extracellular region cytoplasm G-protein coupled receptor signaling pathway circadian rhythm heme binding extracellular exosome uc001rbd.1 uc001rbd.2 uc001rbd.3 uc001rbd.4 uc001rbd.5 
ENST00000016171.6 COX15 ENST00000016171.6 cytochrome c oxidase assembly homolog COX15, transcript variant 11 (from RefSeq NR_164009.1) A8K6I9 COX15_HUMAN ENST00000016171.1 ENST00000016171.2 ENST00000016171.3 ENST00000016171.4 ENST00000016171.5 NR_164009 O60556 O75878 Q5TD00 Q5TD01 Q7KZN9 Q7Z3Q3 Q9NTN0 uc001kqb.1 uc001kqb.2 uc001kqb.3 uc001kqb.4 uc001kqb.5 uc001kqb.6 Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be essential for the biogenesis of COX formation and may function in the hydroxylation of heme O, according to the yeast mutant studies. This protein is predicted to contain 5 transmembrane domains localized in the mitochondrial inner membrane. Alternative splicing of this gene generates two transcript variants diverging in the 3' region. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7346977.2458739.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta ##RefSeq-Attributes-END## May be involved in the biosynthesis of heme A. Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1. Q7KZN9; P30041: PRDX6; NbExp=3; IntAct=EBI-3248549, EBI-2255129; Mitochondrion membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=COX15.1; IsoId=Q7KZN9-1; Sequence=Displayed; Name=2; Synonyms=COX15.2; IsoId=Q7KZN9-2; Sequence=VSP_011281; Predominantly found in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle, heart, and brain. Mitochondrial complex IV deficiency, nuclear type 6 (MC4DN6) [MIM:615119]: An autosomal recessive multisystem disorder with variable manifestations. Some patients present in the neonatal period with encephalomyopathic features, whereas others present later in the first year of life with developmental regression. Clinical features include microcephaly, encephalopathy, hypertrophic cardiomyopathy, persistent lactic acidosis, respiratory distress, hypotonia and seizures. Serum lactate is increased, and laboratory studies show decreased mitochondrial complex IV protein and activity levels. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the COX15/CtaA family. cytochrome-c oxidase activity protein binding nucleus mitochondrion mitochondrial inner membrane mitochondrial respiratory chain mitochondrial electron transport, cytochrome c to oxygen heme biosynthetic process heme a biosynthetic process respiratory gaseous exchange respiratory chain complex IV assembly membrane integral component of membrane oxidoreductase activity, acting on the CH-CH group of donors oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor heme binding mitochondrial membrane cellular respiration oxidation-reduction process binding, bridging cytochrome complex hydrogen ion transmembrane transport uc001kqb.1 uc001kqb.2 uc001kqb.3 uc001kqb.4 uc001kqb.5 uc001kqb.6 
ENST00000016913.8 MS4A12 ENST00000016913.8 membrane spanning 4-domains A12, transcript variant 1 (from RefSeq NM_017716.3) ENST00000016913.1 ENST00000016913.2 ENST00000016913.3 ENST00000016913.4 ENST00000016913.5 ENST00000016913.6 ENST00000016913.7 F5GX98 M4A12_HUMAN NM_017716 Q8N6L4 Q9NXJ0 uc001npr.1 uc001npr.2 uc001npr.3 uc001npr.4 The protein encoded by this gene is a cell surface protein found primarily in the apical membrane of colonocytes. Silencing of this gene in colon cancer cells inhibits the proliferation, cell motility, and chemotactic invasion of cells. This gene is part of a cluster of similar genes found on chromosome 11. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2009]. May be involved in signal transduction as a component of a multimeric receptor complex. Q9NXJ0; Q9BU27: FAM3A; NbExp=3; IntAct=EBI-10227644, EBI-10298603; Q9NXJ0; Q13021: MALL; NbExp=6; IntAct=EBI-10227644, EBI-750078; Q9NXJ0; Q9Y342: PLLP; NbExp=6; IntAct=EBI-10227644, EBI-3919291; Membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NXJ0-1; Sequence=Displayed; Name=2; IsoId=Q9NXJ0-2; Sequence=VSP_044899; Belongs to the MS4A family. protein binding membrane integral component of membrane uc001npr.1 uc001npr.2 uc001npr.3 uc001npr.4 
ENST00000016946.8 RGPD5 ENST00000016946.8 RANBP2 like and GRIP domain containing 5, transcript variant 1 (from RefSeq NM_005054.3) ENST00000016946.1 ENST00000016946.2 ENST00000016946.3 ENST00000016946.4 ENST00000016946.5 ENST00000016946.6 ENST00000016946.7 HEL161 NM_005054 V9HWE4 V9HWE4_HUMAN uc061mtq.1 uc061mtq.2 RAN is a small GTP-binding protein of the RAS superfamily that is associated with the nuclear membrane and is thought to control a variety of cellular functions through its interactions with other proteins. This gene shares a high degree of sequence identity with RANBP2, a large RAN-binding protein localized at the cytoplasmic side of the nuclear pore complex. It is believed that this RANBP2 gene family member arose from a duplication event 3 Mb distal to RANBP2. Alternative splicing has been observed for this locus and two variants are described. Additional splicing is suggested but complete sequence for further transcripts has not been determined. [provided by RefSeq, Jul 2008]. cell intracellular transport uc061mtq.1 uc061mtq.2 
ENST00000017003.7 XYLT2 ENST00000017003.7 xylosyltransferase 2, transcript variant 1 (from RefSeq NM_022167.4) ENST00000017003.1 ENST00000017003.2 ENST00000017003.3 ENST00000017003.4 ENST00000017003.5 ENST00000017003.6 NM_022167 Q6UY41 Q86V00 Q9H1B5 UNQ3058/PRO9878 XT2 XYLT2_HUMAN uc002iqo.1 uc002iqo.2 uc002iqo.3 uc002iqo.4 uc002iqo.5 uc002iqo.6 The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate. The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Dec 2013]. Catalyzes the first step in the biosynthesis of chondroitin sulfate, heparan sulfate and dermatan sulfate proteoglycans, such as DCN. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Reaction=L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)- L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:50192, Rhea:RHEA- COMP:9863, Rhea:RHEA-COMP:12567, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:132085; EC=2.4.2.26; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Active with either Mg(2+) or Mn(2+), but activity is highest when both are present. ; Glycan metabolism; chondroitin sulfate biosynthesis. Glycan metabolism; heparan sulfate biosynthesis. Monomer. Golgi apparatus membrane ; Single- pass type II membrane protein Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H1B5-1; Sequence=Displayed; Name=2; IsoId=Q9H1B5-2; Sequence=VSP_013758, VSP_013759; Widely expressed. Expressed at higher level in kidney and pancreas. Contains disulfide bonds. Spondyloocular syndrome (SOS) [MIM:605822]: A syndrome characterized by cataract, loss of vision due to retinal detachment, facial dysmorphism, facial hypotonia, normal height with disproportional short trunk, osteoporosis, immobile spine with thoracic kyphosis and reduced lumbal lordosis. Note=The disease is caused by variants affecting the gene represented in this entry. Pseudoxanthoma elasticum (PXE) [MIM:264800]: A multisystem disorder characterized by accumulation of mineralized and fragmented elastic fibers in the skin, vascular walls, and Burch membrane in the eye. Clinically, patients exhibit characteristic lesions of the posterior segment of the eye including peau d'orange, angioid streaks, and choroidal neovascularizations, of the skin including soft, ivory colored papules in a reticular pattern that predominantly affect the neck and large flexor surfaces, and of the cardiovascular system with peripheral and coronary arterial occlusive disease as well as gastrointestinal bleedings. Note=The gene represented in this entry acts as a disease modifier. PXE patients carrying causative ABCC6 mutations, manifest a more severe disease course characterized by earlier onset, frequent skin lesions and higher organ involvement, in the presence of XYLT2 variants. Belongs to the glycosyltransferase 14 family. XylT subfamily. Golgi membrane magnesium ion binding extracellular region extracellular space Golgi apparatus glycosaminoglycan biosynthetic process acetylglucosaminyltransferase activity heparan sulfate proteoglycan biosynthetic process membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups manganese ion binding protein xylosyltransferase activity proteoglycan biosynthetic process glycosaminoglycan metabolic process chondroitin sulfate biosynthetic process heparin biosynthetic process metal ion binding chondroitin sulfate proteoglycan biosynthetic process uc002iqo.1 uc002iqo.2 uc002iqo.3 uc002iqo.4 uc002iqo.5 uc002iqo.6 
ENST00000019103.8 SCTR ENST00000019103.8 secretin receptor (from RefSeq NM_002980.3) ENST00000019103.1 ENST00000019103.2 ENST00000019103.3 ENST00000019103.4 ENST00000019103.5 ENST00000019103.6 ENST00000019103.7 NM_002980 P47872 Q12961 Q13213 Q53T00 SCTR_HUMAN uc002tma.1 uc002tma.2 uc002tma.3 uc002tma.4 uc002tma.5 The protein encoded by this gene is a G protein-coupled receptor and belongs to the glucagon-VIP-secretin receptor family. It binds secretin which is the most potent regulator of pancreatic bicarbonate, electrolyte and volume secretion. Secretin and its receptor are suggested to be involved in pancreatic cancer and autism. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC035757.1, U28281.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000019103.8/ ENSP00000019103.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Receptor for secretin (SCT), which is involved in different processes such as regulation of the pH of the duodenal content, food intake and water homeostasis (PubMed:7612008, PubMed:25332973). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). Upon binding to secretin, regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation. Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation. Also able to stimulate lipolysis in white adipocytes. Also plays an important role in cellular osmoregulation by regulating renal water reabsorption. Also plays a role in the central nervous system: required for synaptic plasticity (By similarity). Cell membrane ; Multi-pass membrane protein Phosphorylated on Ser and Thr residues at the cytoplasmic C- terminus by G protein-coupled receptor kinases (GRKs). Belongs to the G-protein coupled receptor 2 family. diet induced thermogenesis transmembrane signaling receptor activity G-protein coupled receptor activity cytoplasmic microtubule plasma membrane signal transduction cell surface receptor signaling pathway G-protein coupled receptor signaling pathway brain development G-protein coupled peptide receptor activity cellular water homeostasis secretin receptor activity membrane integral component of membrane peptide hormone binding response to nutrient levels regulation of appetite positive regulation of cAMP-mediated signaling regulation of synaptic plasticity uc002tma.1 uc002tma.2 uc002tma.3 uc002tma.4 uc002tma.5 
ENST00000020673.6 PSD ENST00000020673.6 pleckstrin and Sec7 domain containing, transcript variant 1 (from RefSeq NM_002779.5) A5PKW4 B1AKX7 D3DR87 EFA6 EFA6A ENST00000020673.1 ENST00000020673.2 ENST00000020673.3 ENST00000020673.4 ENST00000020673.5 KIAA2011 NM_002779 PSD1 PSD1_HUMAN Q15673 Q8IVG0 TYL uc001kvg.1 uc001kvg.2 uc001kvg.3 uc001kvg.4 This gene encodes a Plekstrin homology and SEC7 domains-containing protein that functions as a guanine nucleotide exchange factor. The encoded protein regulates signal transduction by activating ADP-ribosylation factor 6. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2012]. Guanine nucleotide exchange factor for ARF6 (PubMed:23603394). Induces cytoskeletal remodeling (By similarity). Interacts with ACTN1. Interacts (ARF6-bound form) with KCNK1; does not interact with KCNK1 in the absence of ARF6 (By similarity). A5PKW4; P70398: Usp9x; Xeno; NbExp=3; IntAct=EBI-719999, EBI-2214043; Cell membrane Cell projection, ruffle membrane Cleavage furrow Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression. In later cytokinesis phases, fades away from the cleavage furrow and becomes uniformly distributed throughout the plasma membrane. Event=Alternative splicing; Named isoforms=2; Comment=Additional isoforms may exist.; Name=1; IsoId=A5PKW4-1; Sequence=Displayed; Name=2; IsoId=A5PKW4-2; Sequence=VSP_031186; Isoform 2 is expressed in the brain. Belongs to the PSD family. Sequence=BAC23107.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; guanyl-nucleotide exchange factor activity ARF guanyl-nucleotide exchange factor activity protein binding phospholipid binding plasma membrane signal transduction postsynaptic density membrane neuron projection development regulation of ARF protein signal transduction cleavage furrow ruffle membrane cell projection dendritic spine extrinsic component of postsynaptic endosome membrane postsynaptic density, intracellular component uc001kvg.1 uc001kvg.2 uc001kvg.3 uc001kvg.4 
ENST00000020926.8 SYT13 ENST00000020926.8 synaptotagmin 13, transcript variant 1 (from RefSeq NM_020826.3) A8K4P4 D3DQP1 ENST00000020926.1 ENST00000020926.2 ENST00000020926.3 ENST00000020926.4 ENST00000020926.5 ENST00000020926.6 ENST00000020926.7 KIAA1427 NM_020826 Q7L8C5 Q9BQS3 Q9H041 Q9P2C0 SYT13_HUMAN uc001myq.1 uc001myq.2 uc001myq.3 uc001myq.4 This gene encodes a member of the large synaptotagmin protein family. Family members have an extracellular N-terminal transmembrane domain and a cytoplasmic C terminus with two tandem C2 domains (C2A and C2B). Synaptotogmin family members can form homo- and heteromeric complexes with each other. They also have different biochemical properties and developmental profiles, and patterns of tissue distribution. Synaptotagmins function as membrane traffickers in multicellular organisms. Two alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [provided by RefSeq, Oct 2011]. May be involved in transport vesicle docking to the plasma membrane. Interacts with NRXN1. Membrane ; Single-pass membrane protein Expressed in brain, pancreas and kidney. The first C2 domain/C2A does not mediate Ca(2+)-dependent phospholipid binding. The second C2 domain/C2B domain binds phospholipids regardless of whether calcium is present. Belongs to the synaptotagmin family. Sequence=BAA92665.1; Type=Erroneous initiation; Evidence=; SNARE binding phosphatidylserine binding calcium ion binding calcium-dependent phospholipid binding plasma membrane integral component of plasma membrane regulation of dopamine secretion membrane integral component of membrane vesicle-mediated transport calcium ion regulated exocytosis regulation of calcium ion-dependent exocytosis transport vesicle clathrin binding axon neuron projection intracellular membrane-bounded organelle exocytic vesicle cellular response to calcium ion uc001myq.1 uc001myq.2 uc001myq.3 uc001myq.4 
ENST00000020945.4 SNAI2 ENST00000020945.4 snail family transcriptional repressor 2 (from RefSeq NM_003068.5) B2R6P6 ENST00000020945.1 ENST00000020945.2 ENST00000020945.3 NM_003068 O43623 Q53FC1 SLUG SLUGH SNAI2_HUMAN uc286arv.1 uc286arv.2 This gene encodes a member of the Snail family of C2H2-type zinc finger transcription factors. The encoded protein acts as a transcriptional repressor that binds to E-box motifs and is also likely to repress E-cadherin transcription in breast carcinoma. This protein is involved in epithelial-mesenchymal transitions and has antiapoptotic activity. Mutations in this gene may be associated with sporatic cases of neural tube defects. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK223368.1, SRR3476690.115526.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2467144, SAMEA2467146 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000020945.4/ ENSP00000020945.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcriptional repressor that modulates both activator- dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2-box- containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis. Interacts (via SNAG domain) with LIMD1 (via LIM domains), WTIP (via LIM domains) and AJUBA (via LIM domains) (By similarity). Interacts (via zinc fingers) with KPNA2, KPNB1, and TNPO1. May interact (via zinc fingers) with IPO7. O43623; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-9876238, EBI-12011224; O43623; P68400: CSNK2A1; NbExp=3; IntAct=EBI-9876238, EBI-347804; O43623; P21673: SAT1; NbExp=3; IntAct=EBI-9876238, EBI-711613; O43623; P36406: TRIM23; NbExp=3; IntAct=EBI-9876238, EBI-740098; O43623; P36508: ZNF76; NbExp=3; IntAct=EBI-9876238, EBI-7254550; Nucleus Cytoplasm. Note=Observed in discrete foci in interphase nuclei. These nuclear foci do not overlap with the nucleoli, the SP100 and the HP1 heterochromatin or the coiled body, suggesting SNAI2 is associated with active transcription or active splicing regions. Expressed in most adult human tissues, including spleen, thymus, prostate, testis, ovary, small intestine, colon, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Not detected in peripheral blood leukocyte. Expressed in the dermis and in all layers of the epidermis, with high levels of expression in the basal layers (at protein level). Expressed in osteoblasts (at protein level). Expressed in mesenchymal stem cells (at protein level). Expressed in breast tumor cells (at protein level). Repression activity depends on the C-terminal DNA-binding zinc fingers and on the N-terminal repression domain. GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation. Waardenburg syndrome 2D (WS2D) [MIM:608890]: WS2 is a genetically heterogeneous, autosomal dominant disorder characterized by sensorineural deafness, pigmentary disturbances, and absence of dystopia canthorum. The frequency of deafness is higher in WS2 than in WS1. Note=The disease is caused by variants affecting the gene represented in this entry. Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the snail C2H2-type zinc-finger protein family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/453/SNAI2"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding osteoblast differentiation epithelial to mesenchymal transition aortic valve morphogenesis epithelial to mesenchymal transition involved in endocardial cushion formation cell migration involved in endocardial cushion formation nucleic acid binding DNA binding chromatin binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm cytoplasm regulation of transcription, DNA-templated negative regulation of cell adhesion involved in substrate-bound cell migration Notch signaling pathway multicellular organism development sensory perception of sound response to radiation negative regulation of keratinocyte proliferation negative regulation of vitamin D biosynthetic process neural crest cell development cell migration positive regulation of cell migration negative regulation of chondrocyte differentiation regulation of chemokine production negative regulation of cell adhesion mediated by integrin positive regulation of histone acetylation desmosome disassembly negative regulation of apoptotic process pigmentation negative regulation of DNA damage response, signal transduction by p53 class mediator sequence-specific DNA binding positive regulation of fat cell differentiation regulation of osteoblast differentiation metal ion binding white fat cell differentiation palate development epithelium development cartilage morphogenesis regulation of branching involved in salivary gland morphogenesis Notch signaling involved in heart development negative regulation of vitamin D receptor signaling pathway E-box binding cellular response to epidermal growth factor stimulus cellular response to ionizing radiation negative regulation of canonical Wnt signaling pathway negative regulation of cell-cell adhesion by negative regulation of transcription from RNA polymerase II promoter negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage negative regulation of stem cell proliferation regulation of bicellular tight junction assembly negative regulation of anoikis negative regulation of extrinsic apoptotic signaling pathway in absence of ligand uc286arv.1 uc286arv.2 
ENST00000022615.9 VDAC3 ENST00000022615.9 voltage dependent anion channel 3, transcript variant 16 (from RefSeq NR_182163.1) ENST00000022615.1 ENST00000022615.2 ENST00000022615.3 ENST00000022615.4 ENST00000022615.5 ENST00000022615.6 ENST00000022615.7 ENST00000022615.8 NR_182163 Q9UIS0 Q9Y277 VDAC3_HUMAN uc003xpc.1 uc003xpc.2 uc003xpc.3 uc003xpc.4 uc003xpc.5 Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). Involved in male fertility and sperm mitochondrial sheath formation (By similarity). Interacts with ARMC12 in a TBC1D21-dependent manner. Interacts with MISFA. Q9Y277; P21796: VDAC1; NbExp=2; IntAct=EBI-354196, EBI-354158; Mitochondrion outer membrane Membrane Note=May localize to non-mitochondrial membranes. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y277-1; Sequence=Displayed; Name=2; IsoId=Q9Y277-2; Sequence=VSP_005079; Expressed in erythrocytes (at protein level) (PubMed:27641616). Widely expressed. Highest in testis (PubMed:9781040). Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. Belongs to the eukaryotic mitochondrial porin family. nucleotide binding behavioral fear response protein binding nucleus mitochondrion mitochondrial outer membrane ion transport chemical synaptic transmission neuron-neuron synaptic transmission learning voltage-gated anion channel activity porin activity inorganic anion transport adenine transport membrane integral component of membrane pore complex transmembrane transport extracellular exosome anion transmembrane transport regulation of cilium assembly uc003xpc.1 uc003xpc.2 uc003xpc.3 uc003xpc.4 uc003xpc.5 
ENST00000023064.9 SLC7A9 ENST00000023064.9 solute carrier family 7 member 9, transcript variant 1 (from RefSeq NM_014270.5) B2R9A6 BAT1 BAT1_HUMAN ENST00000023064.1 ENST00000023064.2 ENST00000023064.3 ENST00000023064.4 ENST00000023064.5 ENST00000023064.6 ENST00000023064.7 ENST00000023064.8 NM_014270 P82251 SLC7A9 uc002ntu.1 uc002ntu.2 uc002ntu.3 uc002ntu.4 uc002ntu.5 uc002ntu.6 uc002ntu.7 This gene encodes a protein that belongs to a family of light subunits of amino acid transporters. This protein plays a role in the high-affinity and sodium-independent transport of cystine and neutral and dibasic amino acids, and appears to function in the reabsorption of cystine in the kidney tubule. Mutations in this gene cause non-type I cystinuria, a disease that leads to cystine stones in the urinary system due to impaired transport of cystine and dibasic amino acids. Alternate transcript variants, which encode the same protein, have been found for this gene. [provided by RefSeq, Jul 2011]. Associates with SLC3A1 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1 (PubMed:8663357, PubMed:16825196, PubMed:32817565, PubMed:32494597). Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids (PubMed:8663357, PubMed:16825196, PubMed:32494597). Substrate exchange is driven by high concentration of intracellular neutral amino acids and the intracellular reduction of L-cystine to L- cysteine (PubMed:8663357). Required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane in renal proximal tubules. Reaction=L-arginine(in) + L-leucine(out) = L-arginine(out) + L- leucine(in); Xref=Rhea:RHEA:71059, ChEBI:CHEBI:32682, ChEBI:CHEBI:57427; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71060; Evidence=; Reaction=L-arginine(in) + L-histidine(out) = L-arginine(out) + L- histidine(in); Xref=Rhea:RHEA:71063, ChEBI:CHEBI:32682, ChEBI:CHEBI:57595; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71064; Evidence=; Reaction=L-arginine(in) + L-phenylalanine(out) = L-arginine(out) + L- phenylalanine(in); Xref=Rhea:RHEA:71067, ChEBI:CHEBI:32682, ChEBI:CHEBI:58095; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71068; Evidence=; Reaction=L-arginine(in) + L-cysteine(out) = L-arginine(out) + L- cysteine(in); Xref=Rhea:RHEA:71071, ChEBI:CHEBI:32682, ChEBI:CHEBI:35235; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71072; Evidence=; Reaction=L-arginine(in) + L-cystine(out) = L-arginine(out) + L- cystine(in); Xref=Rhea:RHEA:71075, ChEBI:CHEBI:32682, ChEBI:CHEBI:35491; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71076; Evidence=; Reaction=L-arginine(in) + L-lysine(out) = L-arginine(out) + L- lysine(in); Xref=Rhea:RHEA:70827, ChEBI:CHEBI:32551, ChEBI:CHEBI:32682; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70828; Evidence=; Kinetic parameters: KM=41 uM for L-cystine ; KM=85 uM for L-arginine ; KM=90 uM for L-leucine ; Disulfide-linked heterodimer composed of the catalytic light chain subunit SLC7A9 and the heavy chain subunit SLC3A1. The heterodimer is the minimal functional unit. Assembles in heterotetramers (dimers of heterodimers) and higher order oligomers; the oligomerization is mediated by SLC3A1 likely to prevent degradation and facilitate heteromer trafficking to the plasma membrane (PubMed:16825196, PubMed:32494597, PubMed:32817565). Interacts with CAV1 (By similarity). P82251; O43889-2: CREB3; NbExp=3; IntAct=EBI-3936589, EBI-625022; P82251; Q07837: SLC3A1; NbExp=2; IntAct=EBI-3936589, EBI-46442178; Apical cell membrane ; Multi-pass membrane protein ll membrane ; Multi-pass membrane protein Expressed in the brush border membrane in the kidney (at protein level). Kidney, small intestine, liver and placenta. Cystinuria (CSNU) [MIM:220100]: An autosomal disorder characterized by impaired epithelial cell transport of cystine and dibasic amino acids (lysine, ornithine, and arginine) in the proximal renal tubule and gastrointestinal tract. The impaired renal reabsorption of cystine and its low solubility causes the formation of calculi in the urinary tract, resulting in obstructive uropathy, pyelonephritis, and, rarely, renal failure. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the amino acid-polyamine-organocation (APC) superfamily. amino acid transmembrane transport protein binding plasma membrane integral component of plasma membrane amino acid transport amino acid transmembrane transporter activity neutral amino acid transmembrane transporter activity L-amino acid transmembrane transporter activity L-cystine transmembrane transporter activity neutral amino acid transport L-cystine transport membrane integral component of membrane apical plasma membrane transmembrane transporter activity brush border membrane peptide antigen binding leukocyte migration transmembrane transport macromolecular complex assembly L-alpha-amino acid transmembrane transport uc002ntu.1 uc002ntu.2 uc002ntu.3 uc002ntu.4 uc002ntu.5 uc002ntu.6 uc002ntu.7 
ENST00000025008.10 RB1CC1 ENST00000025008.10 RB1 inducible coiled-coil 1, transcript variant 1 (from RefSeq NM_014781.5) ENST00000025008.1 ENST00000025008.2 ENST00000025008.3 ENST00000025008.4 ENST00000025008.5 ENST00000025008.6 ENST00000025008.7 ENST00000025008.8 ENST00000025008.9 KIAA0203 NM_014781 Q86YR4 Q8TDY2 Q8WVU9 Q92601 RB1CC1 RBCC1_HUMAN RBICC uc003xre.1 uc003xre.2 uc003xre.3 uc003xre.4 uc003xre.5 uc003xre.6 The protein encoded by this gene interacts with signaling pathways to coordinately regulate cell growth, cell proliferation, apoptosis, autophagy, and cell migration. This tumor suppressor also enhances retinoblastoma 1 gene expression in cancer cells. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Nov 2009]. Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity). Part of a complex consisting of ATG13/KIAA0652, ULK1 and RB1CC1 (PubMed:19597335, PubMed:19211835). This complex associates with ATG101 (PubMed:19597335, PubMed:19211835). Interacts with PTK2/FAK1 and PTK2B/PYK2 (PubMed:10769033, PubMed:12221124). Interacts with GABARAP and GABARAPL1 (PubMed:23043107). Interacts with ATG16L1; the interaction is required for ULK1 complex-dependent autophagy (PubMed:24954904, PubMed:23262492, PubMed:23392225, PubMed:28890335). Interacts with RNF111, SKI and SMAD7 (By similarity). Interacts with COP1 in the cytoplasm of proliferating cells in response to UV stimulation (PubMed:23289756). Interacts with TP53 (PubMed:21775823). Interacts with C9orf72 (PubMed:27334615). Interacts with WDR45B (PubMed:28561066). Interacts with ATG13; this interaction is increased in the absence of TMEM39A (PubMed:31806350). Interacts with WIPI2 (PubMed:28890335). Interacts with TAX1BP1 (PubMed:33226137, PubMed:34471133). Interacts (via phosphorylated FFAT motif) with MOSPD2, VAPA and VAPB (PubMed:33124732). Q8TDY2; Q9BSB4: ATG101; NbExp=7; IntAct=EBI-1047793, EBI-2946739; Q8TDY2; O75143: ATG13; NbExp=10; IntAct=EBI-1047793, EBI-2798775; Q8TDY2; Q676U5: ATG16L1; NbExp=6; IntAct=EBI-1047793, EBI-535909; Q8TDY2; Q9H1Y0: ATG5; NbExp=3; IntAct=EBI-1047793, EBI-1047414; Q8TDY2; Q96LT7-1: C9orf72; NbExp=7; IntAct=EBI-1047793, EBI-16693635; Q8TDY2; Q96LT7-2: C9orf72; NbExp=6; IntAct=EBI-1047793, EBI-16693673; Q8TDY2; A7MCY6: TBKBP1; NbExp=2; IntAct=EBI-1047793, EBI-359969; Q8TDY2; O75385: ULK1; NbExp=11; IntAct=EBI-1047793, EBI-908831; Q8TDY2; Q8C0J2-3: Atg16l1; Xeno; NbExp=6; IntAct=EBI-1047793, EBI-16029274; Nucleus Cytoplasm Cytoplasm, cytosol Preautophagosomal structure Lysosome Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8TDY2-1; Sequence=Displayed; Name=2; IsoId=Q8TDY2-2; Sequence=VSP_040097; Expression levels correlated closely with those of RB1 in cancer cell lines as well as in various normal human tissues. Abundantly expressed in human musculoskeletal and cultured osteosarcoma cells. Expression was difficult to detect in immature proliferating chondroblasts or myogenic cells in embryos, but became obvious and prominent concomitantly with the maturation of osteocytes, chondrocytes, and skeletal muscle cells. Expression in these musculoskeletal cells increased with RB1 expression, which is linked to the terminal differentiation of many tissues and cells. The introduction of the wild-type protein decreased the formation of macroscopic colonies in a cell growth assay. The FFAT motif is involved in the interaction with MOSPD2, VAPA and VAPB and its phosphorylation regulates these interactions. Phosphorylation at Ser-734 of the FFAT motif activates interaction with MOSPD2, VAPA and VAPB. Probably involved in the tumorigenesis of breast cancer. RB1CC1 is frequently mutated in breast cancer and shows characteristics of a classical tumor suppressor gene. Belongs to the ATG17 family. Sequence=BAA13194.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; autophagosome assembly pre-autophagosomal structure mitophagy liver development positive regulation of protein phosphorylation protein binding nucleus cytoplasm lysosome endoplasmic reticulum membrane cytosol autophagy cell cycle heart development macroautophagy regulation of macroautophagy extrinsic component of membrane protein kinase binding pexophagy nuclear membrane pre-autophagosomal structure membrane piecemeal microautophagy of nucleus negative regulation of apoptotic process positive regulation of cell size positive regulation of JNK cascade reticulophagy glycophagy ATG1/ULK1 kinase complex negative regulation of extrinsic apoptotic signaling pathway uc003xre.1 uc003xre.2 uc003xre.3 uc003xre.4 uc003xre.5 uc003xre.6 
ENST00000025301.4 AKAP11 ENST00000025301.4 A-kinase anchoring protein 11 (from RefSeq NM_016248.4) AKA11_HUMAN AKAP220 ENST00000025301.1 ENST00000025301.2 ENST00000025301.3 KIAA0629 NM_016248 O75124 Q9NUK7 Q9UKA4 uc001uys.1 uc001uys.2 uc001uys.3 The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein is expressed at high levels throughout spermatogenesis and in mature sperm. It binds the RI and RII subunits of PKA in testis. It may serve a function in cell cycle control of both somatic cells and germ cells in addition to its putative role in spermatogenesis and sperm function. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF176555.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000025301.4/ ENSP00000025301.2 RefSeq Select criteria :: based on conservation, longest protein ##RefSeq-Attributes-END## Binds to type II regulatory subunits of protein kinase A and anchors/targets them. Q9UKA4; Q99732: LITAF; NbExp=3; IntAct=EBI-1049491, EBI-725647; Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic in premeiotic pachytene spermatocytes and in the centrosome of developing postmeiotic germ cells, while a midpiece/centrosome localization was found in elongating spermatocytes and mature sperm. Expressed in heart, brain, lung, liver, kidney, testis and ovary. Weakly expressed in skeletal muscle, pancreas and spleen. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Belongs to the AKAP110 family. Sequence=BAA92117.1; Type=Erroneous initiation; Evidence=; protein binding nucleolus cytoplasm peroxisome microtubule organizing center cytosol cytoskeleton plasma membrane protein localization protein phosphatase 1 binding intracellular signal transduction protein kinase A binding uc001uys.1 uc001uys.2 uc001uys.3 
ENST00000027335.8 CDH17 ENST00000027335.8 cadherin 17, transcript variant 14 (from RefSeq NR_182224.1) CAD17_HUMAN ENST00000027335.1 ENST00000027335.2 ENST00000027335.3 ENST00000027335.4 ENST00000027335.5 ENST00000027335.6 ENST00000027335.7 NR_182224 Q12864 Q15336 Q2M2E0 uc003ygh.1 uc003ygh.2 uc003ygh.3 uc003ygh.4 Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. LI-cadherin may have a role in the morphological organization of liver and intestine. Involved in intestinal peptide transport. Q12864; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12278850, EBI-947187; Cell membrane ; Single-pass type I membrane protein Expressed in the gastrointestinal tract and pancreatic duct. Not detected in kidney, lung, liver, brain, adrenal gland and skin. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40020/CDH17"; cell morphogenesis germinal center B cell differentiation marginal zone B cell differentiation integrin binding transporter activity proton-dependent oligopeptide secondary active transmembrane transporter activity calcium ion binding nucleus plasma membrane cell-cell adherens junction oligopeptide transport cell-cell junction assembly cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules integrin-mediated signaling pathway cytoskeletal protein binding cell surface membrane integral component of membrane basolateral plasma membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules catenin complex cell junction B cell differentiation positive regulation of integrin activation by cell surface receptor linked signal transduction adherens junction organization oligopeptide transmembrane transport protein homodimerization activity cell-cell adhesion mediated by cadherin cadherin binding metal ion binding spleen development cell-cell adhesion uc003ygh.1 uc003ygh.2 uc003ygh.3 uc003ygh.4 
ENST00000029410.10 B4GALT7 ENST00000029410.10 beta-1,4-galactosyltransferase 7 (from RefSeq NM_007255.3) B3KN39 B4GT7_HUMAN ENST00000029410.1 ENST00000029410.2 ENST00000029410.3 ENST00000029410.4 ENST00000029410.5 ENST00000029410.6 ENST00000029410.7 ENST00000029410.8 ENST00000029410.9 NM_007255 Q9UBV7 Q9UHN2 UNQ748/PRO1478 XGALT1 uc003mhy.1 uc003mhy.2 uc003mhy.3 uc003mhy.4 uc003mhy.5 This gene is a member of the beta-1,4-galactosyltransferase (beta4GalT) family. Family members encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose. Each beta4GalT member has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus which then remains uncleaved to function as a transmembrane anchor. The enzyme encoded by this gene attaches the first galactose in the common carbohydrate-protein linkage (GlcA-beta1,3-Gal-beta1,3-Gal-beta1,4-Xyl-beta1-O-Ser) found in proteoglycans. This enzyme differs from other beta4GalTs because it lacks the conserved Cys residues found in beta4GalT1-beta4GalT6 and it is located in cis-Golgi instead of trans-Golgi. Mutations in this gene have been associated with the progeroid form of Ehlers-Danlos syndrome. [provided by RefSeq, Oct 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.310844.1, SRR1163655.38696.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968189 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000029410.10/ ENSP00000029410.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts. Reaction=3-O-(beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:15297, Rhea:RHEA-COMP:12567, Rhea:RHEA- COMP:12570, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:132085, ChEBI:CHEBI:132088; EC=2.4.1.133; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Protein modification; protein glycosylation. Q9UBV7; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10319970, EBI-3867333; Q9UBV7; Q15323: KRT31; NbExp=3; IntAct=EBI-10319970, EBI-948001; Q9UBV7; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10319970, EBI-10172290; Q9UBV7; P53611: RABGGTB; NbExp=6; IntAct=EBI-10319970, EBI-536715; Q9UBV7; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10319970, EBI-8638294; Golgi apparatus, Golgi stack membrane; Single- pass type II membrane protein. Note=Cis cisternae of Golgi stack. High expression in heart, pancreas and liver, medium in placenta and kidney, low in brain, skeletal muscle and lung. Ehlers-Danlos syndrome, spondylodysplastic type, 1 (EDSSPD1) [MIM:130070]: A form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. EDSSPD1 is an autosomal recessive form characterized by short stature, developmental anomalies of the forearm bones and elbow, and bowing of extremities, in addition to the classic features of Ehlers-Danlos syndrome. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyltransferase 7 family. Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4- galactosyltransferase 7; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_442"; Golgi membrane beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity protein binding Golgi apparatus carbohydrate metabolic process glycosaminoglycan biosynthetic process proteoglycan metabolic process cellular protein modification process protein glycosylation protein N-linked glycosylation galactosyltransferase activity membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups manganese ion binding glycosaminoglycan metabolic process Golgi cisterna membrane xylosylprotein 4-beta-galactosyltransferase activity metal ion binding negative regulation of fibroblast proliferation supramolecular fiber organization uc003mhy.1 uc003mhy.2 uc003mhy.3 uc003mhy.4 uc003mhy.5 
ENST00000035307.7 CHPF2 ENST00000035307.7 chondroitin polymerizing factor 2, transcript variant 6 (from RefSeq NR_171547.1) B2DBD8 CHPF2_HUMAN CHSY3 CSGLCAT ENST00000035307.1 ENST00000035307.2 ENST00000035307.3 ENST00000035307.4 ENST00000035307.5 ENST00000035307.6 KIAA1402 NR_171547 Q6P2I4 Q6UXD2 Q9P2E5 UNQ299/PRO339 uc003wjr.1 uc003wjr.2 uc003wjr.3 uc003wjr.4 Transfers glucuronic acid (GlcUA) from UDP-GlcUA to N- acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. Has no N-acetylgalactosaminyltransferase activity. Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal- (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D- glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D- GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl- [protein] + H(+) + UDP; Xref=Rhea:RHEA:23428, Rhea:RHEA-COMP:12575, Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442; EC=2.4.1.226; Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D- GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)- beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta- D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D- GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)- beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996, Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444, ChEBI:CHEBI:138445; EC=2.4.1.226; Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9P2E5-1; Sequence=Displayed; Name=2; IsoId=Q9P2E5-2; Sequence=VSP_012724, VSP_012725; Ubiquitous. Highly expressed in placenta, small intestine and pancreas. Belongs to the chondroitin N- acetylgalactosaminyltransferase family. Sequence=BAA92640.1; Type=Erroneous initiation; Evidence=; Golgi membrane Golgi apparatus acetylgalactosaminyltransferase activity membrane integral component of membrane transferase activity chondroitin sulfate biosynthetic process Golgi cisterna membrane N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity uc003wjr.1 uc003wjr.2 uc003wjr.3 uc003wjr.4 
ENST00000037243.7 GABARAPL2 ENST00000037243.7 GABA type A receptor associated protein like 2 (from RefSeq NM_007285.7) ENST00000037243.1 ENST00000037243.2 ENST00000037243.3 ENST00000037243.4 ENST00000037243.5 ENST00000037243.6 FLC3A GABARAPL2 GBRL2_HUMAN GEF2 NM_007285 O08765 P60520 Q6FG91 Q9DCP8 Q9UQF7 uc002fen.1 uc002fen.2 uc002fen.3 uc002fen.4 Ubiquitin-like modifier involved in intra-Golgi traffic (By similarity). Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation (By similarity). It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy (PubMed:20418806, PubMed:23209295). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:20418806, PubMed:23209295). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20418806, PubMed:23209295). Monomer. Interacts with ATG3, ATG7, ATG13 and ULK1 (PubMed:11146101, PubMed:11825910, PubMed:11096062, PubMed:12507496, PubMed:23043107). Interacts with TP53INP1 and TP53INP2 (PubMed:19056683, PubMed:22421968, PubMed:22470510). Interacts with TBC1D25 (PubMed:21383079). Directly interacts with SQSTM1 and BNIP3 (PubMed:17580304, PubMed:23209295). Interacts with TECPR2 and PCM1 (PubMed:20562859, PubMed:24089205). Interacts with TBC1D5 (PubMed:22354992). Interacts with TRIM5 (PubMed:25127057). Interacts with MEFV and TRIM21 (PubMed:26347139). Interacts with WDFY3 (PubMed:24668264). Interacts with UBA5; promoting recruitment of UBA5 to the endoplasmic reticulum membrane (PubMed:26929408, PubMed:30990354). Interacts with GOSR1 (By similarity). Interacts with KBTBD6 and KBTBD7; the interaction is direct (PubMed:25684205). Interacts with reticulophagy regulators RETREG1, RETREG2 and RETREG3 (PubMed:34338405). Interacts with IRGM (PubMed:29420192). Interacts with DNM2 (PubMed:32315611). P60520; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-720116, EBI-741181; P60520; Q8IVF2-2: AHNAK2; NbExp=3; IntAct=EBI-720116, EBI-10217765; P60520; Q9P2R3: ANKFY1; NbExp=2; IntAct=EBI-720116, EBI-2513908; P60520; Q8N6T3: ARFGAP1; NbExp=3; IntAct=EBI-720116, EBI-716933; P60520; Q8N6T3-2: ARFGAP1; NbExp=3; IntAct=EBI-720116, EBI-6288865; P60520; O75143: ATG13; NbExp=3; IntAct=EBI-720116, EBI-2798775; P60520; Q676U5: ATG16L1; NbExp=2; IntAct=EBI-720116, EBI-535909; P60520; Q2TAZ0: ATG2A; NbExp=2; IntAct=EBI-720116, EBI-2514077; P60520; Q9NT62: ATG3; NbExp=5; IntAct=EBI-720116, EBI-988094; P60520; Q9Y4P1: ATG4B; NbExp=10; IntAct=EBI-720116, EBI-712014; P60520; O95352: ATG7; NbExp=7; IntAct=EBI-720116, EBI-987834; P60520; Q9BXK5: BCL2L13; NbExp=4; IntAct=EBI-720116, EBI-747430; P60520; O60238: BNIP3L; NbExp=3; IntAct=EBI-720116, EBI-849893; P60520; Q9NW68: BSDC1; NbExp=3; IntAct=EBI-720116, EBI-721848; P60520; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-720116, EBI-749920; P60520; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-720116, EBI-739580; P60520; Q8WXU2: DNAAF4; NbExp=2; IntAct=EBI-720116, EBI-2946907; P60520; P63167: DYNLL1; NbExp=3; IntAct=EBI-720116, EBI-349105; P60520; Q96FJ2: DYNLL2; NbExp=3; IntAct=EBI-720116, EBI-742371; P60520; P00533: EGFR; NbExp=3; IntAct=EBI-720116, EBI-297353; P60520; Q8IVP5: FUNDC1; NbExp=4; IntAct=EBI-720116, EBI-3059266; P60520; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-720116, EBI-2869338; P60520; P40939: HADHA; NbExp=4; IntAct=EBI-720116, EBI-356720; P60520; P54257: HAP1; NbExp=3; IntAct=EBI-720116, EBI-712814; P60520; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-720116, EBI-4311436; P60520; O00410: IPO5; NbExp=5; IntAct=EBI-720116, EBI-356424; P60520; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-720116, EBI-749265; P60520; Q86V97: KBTBD6; NbExp=2; IntAct=EBI-720116, EBI-2514778; P60520; Q8WVZ9: KBTBD7; NbExp=3; IntAct=EBI-720116, EBI-473695; P60520; Q8N8K9: KIAA1958; NbExp=7; IntAct=EBI-720116, EBI-10181113; P60520; Q96L93-6: KIF16B; NbExp=3; IntAct=EBI-720116, EBI-10988217; P60520; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-720116, EBI-10172290; P60520; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-720116, EBI-10172052; P60520; Q8N653: LZTR1; NbExp=3; IntAct=EBI-720116, EBI-2350056; P60520; Q9UH92: MLX; NbExp=5; IntAct=EBI-720116, EBI-741109; P60520; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-720116, EBI-8852072; P60520; Q14596: NBR1; NbExp=11; IntAct=EBI-720116, EBI-742698; P60520; P46934: NEDD4; NbExp=6; IntAct=EBI-720116, EBI-726944; P60520; P46934-3: NEDD4; NbExp=3; IntAct=EBI-720116, EBI-11980721; P60520; Q8TD19: NEK9; NbExp=7; IntAct=EBI-720116, EBI-1044009; P60520; O75323: NIPSNAP2; NbExp=6; IntAct=EBI-720116, EBI-307133; P60520; Q9NV35: NUDT15; NbExp=3; IntAct=EBI-720116, EBI-3924801; P60520; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-720116, EBI-1051317; P60520; Q15154: PCM1; NbExp=2; IntAct=EBI-720116, EBI-741421; P60520; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-720116, EBI-367363; P60520; Q8WWW0: RASSF5; NbExp=2; IntAct=EBI-720116, EBI-367390; P60520; Q14257: RCN2; NbExp=6; IntAct=EBI-720116, EBI-356710; P60520; Q9H6L5-1: RETREG1; NbExp=2; IntAct=EBI-720116, EBI-16159046; P60520; Q9H6L5-2: RETREG1; NbExp=3; IntAct=EBI-720116, EBI-13382642; P60520; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-720116, EBI-10192441; P60520; Q8IZE3-2: SCYL3; NbExp=3; IntAct=EBI-720116, EBI-11959369; P60520; Q9UH03: SEPTIN3; NbExp=2; IntAct=EBI-720116, EBI-727037; P60520; Q9H0K1: SIK2; NbExp=3; IntAct=EBI-720116, EBI-1181664; P60520; Q13501: SQSTM1; NbExp=24; IntAct=EBI-720116, EBI-307104; P60520; O95210: STBD1; NbExp=5; IntAct=EBI-720116, EBI-2947137; P60520; Q13188: STK3; NbExp=2; IntAct=EBI-720116, EBI-992580; P60520; Q13043: STK4; NbExp=2; IntAct=EBI-720116, EBI-367376; P60520; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-720116, EBI-529518; P60520; Q8TC07: TBC1D15; NbExp=2; IntAct=EBI-720116, EBI-1048247; P60520; Q3MII6: TBC1D25; NbExp=4; IntAct=EBI-720116, EBI-11899977; P60520; Q9UPU7: TBC1D2B; NbExp=3; IntAct=EBI-720116, EBI-2947180; P60520; B9A6K1: TBC1D5; NbExp=3; IntAct=EBI-720116, EBI-10217641; P60520; Q92609: TBC1D5; NbExp=5; IntAct=EBI-720116, EBI-742381; P60520; Q66K14-2: TBC1D9B; NbExp=3; IntAct=EBI-720116, EBI-10217736; P60520; O15040: TECPR2; NbExp=2; IntAct=EBI-720116, EBI-2946991; P60520; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-720116, EBI-10329860; P60520; Q15025: TNIP1; NbExp=6; IntAct=EBI-720116, EBI-357849; P60520; Q96A56: TP53INP1; NbExp=6; IntAct=EBI-720116, EBI-9986117; P60520; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-720116, EBI-11993364; P60520; Q969E8: TSR2; NbExp=11; IntAct=EBI-720116, EBI-746981; P60520; Q9GZZ9: UBA5; NbExp=17; IntAct=EBI-720116, EBI-747805; P60520; O75385: ULK1; NbExp=3; IntAct=EBI-720116, EBI-908831; P60520; Q8IZQ1: WDFY3; NbExp=3; IntAct=EBI-720116, EBI-1569256; P60520; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-720116, EBI-2515601; P60520; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-720116, EBI-10251462; P60520; Q9Z2F7: Bnip3l; Xeno; NbExp=2; IntAct=EBI-720116, EBI-1774669; Cytoplasmic vesicle, autophagosome doplasmic reticulum membrane Golgi apparatus Ubiquitous. Expressed at high levels in the brain, heart, prostate, ovary, spleen and skeletal muscle. Expressed at very low levels in lung, thymus and small intestine. The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, GABARAPL2-I (PubMed:15169837, PubMed:20818167, PubMed:30661429, PubMed:31709703). The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, GABARAPL2-II (PubMed:15169837, PubMed:31709703). During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (PubMed:33909989). ATG4 proteins also mediate the delipidation of PE- conjugated forms required for GABARAPL2 recycling when autophagosomes fuse with lysosomes (PubMed:29458288, PubMed:31709703, PubMed:33909989). In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989). ATG4B constitutes the major protein for proteolytic activation (PubMed:30661429). ATG4D is the main enzyme for delipidation activity (By similarity). (Microbial infection) The Legionella effector RavZ is a deconjugating enzyme that hydrolyzes the amide bond between the C- terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that is resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine (PubMed:31722778). RavZ is also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). Phosphorylation at Ser-87 and Ser-88 by TBK1 prevents interaction with ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) (PubMed:31709703). Phosphorylation by TBK1 on autophagosomes prevents their delipidation by ATG4 and premature removal from nascent autophagosomes (PubMed:31709703). Belongs to the ATG8 family. autophagosome assembly Golgi membrane SNARE binding autophagosome membrane mitophagy protein binding intracellular cytoplasm autophagosome Golgi apparatus cytosol intra-Golgi vesicle-mediated transport autophagy cellular response to nitrogen starvation microtubule binding protein transport macroautophagy cytoplasmic vesicle ubiquitin protein ligase binding positive regulation of ATPase activity beta-tubulin binding GABA receptor binding ATPase binding autophagosome maturation negative regulation of proteasomal protein catabolic process uc002fen.1 uc002fen.2 uc002fen.3 uc002fen.4 
ENST00000037502.11 MYOC ENST00000037502.11 myocilin (from RefSeq NM_000261.2) B2RD84 ENST00000037502.1 ENST00000037502.10 ENST00000037502.2 ENST00000037502.3 ENST00000037502.4 ENST00000037502.5 ENST00000037502.6 ENST00000037502.7 ENST00000037502.8 ENST00000037502.9 GLC1A MYOC_HUMAN NM_000261 O00620 Q7Z6Q9 Q99972 TIGR uc001ghu.1 uc001ghu.2 uc001ghu.3 uc001ghu.4 uc001ghu.5 MYOC encodes the protein myocilin, which is believed to have a role in cytoskeletal function. MYOC is expressed in many occular tissues, including the trabecular meshwork, and was revealed to be the trabecular meshwork glucocorticoid-inducible response protein (TIGR). The trabecular meshwork is a specialized eye tissue essential in regulating intraocular pressure, and mutations in MYOC have been identified as the cause of hereditary juvenile-onset open-angle glaucoma. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189667.323867.1, U85257.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2153980, SAMEA2154125 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000037502.11/ ENSP00000037502.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin- associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork. Homodimer (via N-terminus). Can also form higher oligomers (PubMed:9497363). Interacts with OLFM3, FN1, NRCAM, GLDN and NFASC (PubMed:12019210, PubMed:11773026, PubMed:23897819). Interacts (via N- terminus) with MYL2 (PubMed:11773029). Interacts with SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates Wnt signaling (PubMed:19188438). Interacts with SNTA1; regulates muscle hypertrophy. Interacts with ERBB2 and ERBB3; activates ERBB2-ERBB3 signaling pathway. Interacts with SNCG; affects its secretion and its aggregation (By similarity). Q99972; P10916: MYL2; NbExp=7; IntAct=EBI-11692272, EBI-725770; Q99972; O43765: SGTA; NbExp=3; IntAct=EBI-11692272, EBI-347996; Q99972; P09486: SPARC; NbExp=3; IntAct=EBI-11692272, EBI-2800983; Q99972; Q14515: SPARCL1; NbExp=2; IntAct=EBI-11692272, EBI-2682673; Secreted lgi apparatus Cytoplasmic vesicle Secreted, extracellular space. Secreted, extracellular space, extracellular matrix creted, extracellular exosome Mitochondrion Mitochondrion intermembrane space Mitochondrion inner membrane Mitochondrion outer membrane Rough endoplasmic reticulum Cell projection. Cell projection, cilium Note=Located preferentially in the ciliary rootlet and basal body of the connecting cilium of photoreceptor cells, and in the rough endoplasmic reticulum (PubMed:9169133). It is only imported to mitochondria in the trabecular meshwork (PubMed:17516541). Localizes to the Golgi apparatus in Schlemm's canal endothelial cells (PubMed:11053284). Appears in the extracellular space of trabecular meshwork cells by an unconventional mechanism, likely associated with exosome-like vesicles (PubMed:15944158). Localizes in trabecular meshwork extracellular matrix (PubMed:15944158). [Myocilin, C-terminal fragment]: Secreted. [Myocilin, N-terminal fragment]: Endoplasmic reticulum. Note=Remains retained in the endoplasmic reticulum. Detected in aqueous humor (PubMed:12697062). Detected in the eye (at protein level) (PubMed:11431441). Widely expressed. Highly expressed in various types of muscle, ciliary body, papillary sphincter, skeletal muscle, heart, and bone marrow-derived mesenchymal stem cells. Expressed predominantly in the retina. In normal eyes, found in the inner uveal meshwork region and the anterior portion of the meshwork. In contrast, in many glaucomatous eyes, it is found in more regions of the meshwork and seems to be expressed at higher levels than in normal eyes, regardless of the type or clinical severity of glaucoma. The myocilin 35 kDa fragment is detected in aqueous humor and to a lesser extent in iris and ciliary body. Up-regulated by dexamethasone, a glucocorticoid. Different isoforms may arise by post-translational modifications. Glycosylated. Palmitoylated. Undergoes a calcium-dependent proteolytic cleavage at Arg-226 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal leucine zipper- like domain. Glaucoma 1, open angle, A (GLC1A) [MIM:137750]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. te=The disease is caused by variants affecting the gene represented in this entry. Glaucoma 3, primary congenital, A (GLC3A) [MIM:231300]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. MYOC mutations may contribute to GLC3A via digenic inheritance with CYP1B1 and/or another locus associated with the disease (PubMed:15733270). Sequence=BAA24532.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; osteoblast differentiation regulation of cell-matrix adhesion negative regulation of cell-matrix adhesion fibronectin binding frizzled binding protein binding extracellular region extracellular space mitochondrion mitochondrial outer membrane mitochondrial inner membrane mitochondrial intermembrane space endoplasmic reticulum rough endoplasmic reticulum Golgi apparatus cilium positive regulation of phosphatidylinositol 3-kinase signaling skeletal muscle hypertrophy membrane myelination in peripheral nervous system positive regulation of cell migration receptor tyrosine kinase binding neuron projection development cytoplasmic vesicle myosin light chain binding node of Ranvier negative regulation of Rho protein signal transduction non-canonical Wnt signaling pathway via JNK cascade ERBB2-ERBB3 signaling pathway cell projection regulation of MAPK cascade clustering of voltage-gated sodium channels metal ion binding regulation of stress fiber assembly positive regulation of stress fiber assembly negative regulation of stress fiber assembly positive regulation of focal adhesion assembly positive regulation of protein kinase B signaling positive regulation of mitochondrial depolarization bone development extracellular exosome positive regulation of substrate adhesion-dependent cell spreading uc001ghu.1 uc001ghu.2 uc001ghu.3 uc001ghu.4 uc001ghu.5 
ENST00000038176.8 NSMAF ENST00000038176.8 neutral sphingomyelinase activation associated factor, transcript variant 30 (from RefSeq NR_182089.1) B4DFB0 E9PCH0 ENST00000038176.1 ENST00000038176.2 ENST00000038176.3 ENST00000038176.4 ENST00000038176.5 ENST00000038176.6 ENST00000038176.7 FAN FAN_HUMAN NR_182089 Q8IW26 Q92636 uc003xtt.1 uc003xtt.2 uc003xtt.3 uc003xtt.4 uc003xtt.5 Couples the p55 TNF-receptor (TNF-R55 / TNFR1) to neutral sphingomyelinase (N-SMASE). Specifically binds to the N-smase activation domain of TNF-R55. May regulate ceramide production by N- SMASE. Q92636; P60709: ACTB; NbExp=2; IntAct=EBI-2947053, EBI-353944; Q92636; Q9NPI6: DCP1A; NbExp=2; IntAct=EBI-2947053, EBI-374238; Q92636; Q8IZD4: DCP1B; NbExp=2; IntAct=EBI-2947053, EBI-521595; Q92636; O95166: GABARAP; NbExp=2; IntAct=EBI-2947053, EBI-712001; Q92636; Q9H0R8: GABARAPL1; NbExp=7; IntAct=EBI-2947053, EBI-746969; Q92636; P50552: VASP; NbExp=2; IntAct=EBI-2947053, EBI-748201; Q92636; Q9SJF3: At1g08370; Xeno; NbExp=2; IntAct=EBI-2947053, EBI-7786643; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q92636-1; Sequence=Displayed; Name=2; IsoId=Q92636-2; Sequence=VSP_042036; Ubiquitous. protein binding cytoplasm cytosol ceramide metabolic process signal transduction sphingomyelin phosphodiesterase activator activity positive regulation of apoptotic process positive regulation of catalytic activity positive regulation of ceramide biosynthetic process uc003xtt.1 uc003xtt.2 uc003xtt.3 uc003xtt.4 uc003xtt.5 
ENST00000039007.5 OTC ENST00000039007.5 ornithine transcarbamylase, transcript variant 1 (from RefSeq NM_000531.6) A8K9P2 D3DWB0 ENST00000039007.1 ENST00000039007.2 ENST00000039007.3 ENST00000039007.4 NM_000531 OTC OTC_HUMAN P00480 Q3KNR1 Q6B0I1 Q9NYJ5 uc004def.1 uc004def.2 uc004def.3 uc004def.4 uc004def.5 uc004def.6 This nuclear gene encodes a mitochondrial matrix enzyme. Missense, nonsense, and frameshift mutations in this enzyme lead to ornithine transcarbamylase deficiency, which causes hyperammonemia. Since the gene for this enzyme maps close to that for Duchenne muscular dystrophy, it may play a role in that disease also. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189664.144333.1, SRR5189664.63751.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000039007.5/ ENSP00000039007.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline (PubMed:6372096, PubMed:8112735, PubMed:2556444). The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion (PubMed:2556444). Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence= PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19515; Evidence=; Negatively regulated by lysine acetylation. Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine and carbamoyl phosphate: step 1/1. Homotrimer. Mitochondrion matrix Mainly expressed in liver and intestinal mucosa. Acetylation at Lys-88 negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. Ornithine carbamoyltransferase deficiency (OTCD) [MIM:311250]: An X-linked disorder of the urea cycle which causes a form of hyperammonemia. Mutations with no residual enzyme activity are always expressed in hemizygote males by a very severe neonatal hyperammonemic coma that generally proves to be fatal. Heterozygous females are either asymptomatic or express orotic aciduria spontaneously or after protein intake. The disorder is treatable with supplemental dietary arginine and low protein diet. The arbitrary classification of patients into the 'neonatal' group (clinical hyperammonemia in the first few days of life) and 'late' onset (clinical presentation after the neonatal period) has been used to differentiate severe from mild forms. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family. urea cycle liver development ornithine carbamoyltransferase activity phospholipid binding cytoplasm mitochondrion mitochondrial inner membrane mitochondrial matrix cellular amino acid metabolic process arginine biosynthetic process ornithine metabolic process ornithine catabolic process midgut development cellular amino acid biosynthetic process response to zinc ion amino acid binding transferase activity carboxyl- or carbamoyltransferase activity citrulline biosynthetic process response to nutrient levels response to insulin phosphate ion binding arginine biosynthetic process via ornithine response to drug anion homeostasis protein homotrimerization response to biotin ammonia homeostasis uc004def.1 uc004def.2 uc004def.3 uc004def.4 uc004def.5 uc004def.6 
ENST00000039989.9 TTC17 ENST00000039989.9 tetratricopeptide repeat domain 17, transcript variant 1 (from RefSeq NM_018259.6) ENST00000039989.1 ENST00000039989.2 ENST00000039989.3 ENST00000039989.4 ENST00000039989.5 ENST00000039989.6 ENST00000039989.7 ENST00000039989.8 G3XAB3 NM_018259 Q8NEC0 Q96AE7 TTC17_HUMAN uc001mxi.1 uc001mxi.2 uc001mxi.3 uc001mxi.4 uc001mxi.5 Plays a role in primary ciliogenesis by modulating actin polymerization. Interacts with CATIP. Cytoplasm Cell membrane Cytoplasm, cytoskeleton Note=Colocalized with CATIP at F-actin rich zones and at dynamic plasma membrane protrusions. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96AE7-1; Sequence=Displayed; Name=2; IsoId=Q96AE7-2; Sequence=VSP_056857, VSP_056858, VSP_056859; Expressed in germ cells as well as in somatic cells of the testis (at protein level). Belongs to the TTC17 family. protein binding cytoplasm cytosol cytoskeleton plasma membrane actin cytoskeleton membrane cell projection organization actin filament polymerization cilium organization uc001mxi.1 uc001mxi.2 uc001mxi.3 uc001mxi.4 uc001mxi.5 
ENST00000040584.6 HOXC8 ENST00000040584.6 homeobox C8 (from RefSeq NM_022658.4) A8K4J4 ENST00000040584.1 ENST00000040584.2 ENST00000040584.3 ENST00000040584.4 ENST00000040584.5 HOX3A HXC8_HUMAN NM_022658 O15221 O15362 P31273 uc001ser.1 uc001ser.2 uc001ser.3 uc001ser.4 uc001ser.5 This gene belongs to the homeobox family of genes. The homeobox genes encode a highly conserved family of transcription factors that play an important role in morphogenesis in all multicellular organisms. Mammals possess four similar homeobox gene clusters, HOXA, HOXB, HOXC and HOXD, which are located on different chromosomes and consist of 9 to 11 genes arranged in tandem. This gene is one of several homeobox HOXC genes located in a cluster on chromosome 12. The product of this gene may play a role in the regulation of cartilage differentiation. It could also be involved in chondrodysplasias or other cartilage disorders. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC053898.1, AK290959.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000040584.6/ ENSP00000040584.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Interacts with HOMEZ (PubMed:12925734). Forms a DNA-binding heterodimer with transcription factor PBX1 (PubMed:7791786). P31273; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-1752118, EBI-11976299; P31273; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1752118, EBI-10173507; P31273; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-1752118, EBI-8643161; P31273; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-1752118, EBI-11954519; P31273; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-1752118, EBI-2548012; P31273; A2RRN7: CADPS; NbExp=3; IntAct=EBI-1752118, EBI-10179719; P31273; Q9BSQ5: CCM2; NbExp=3; IntAct=EBI-1752118, EBI-1573056; P31273; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-1752118, EBI-739624; P31273; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-1752118, EBI-718615; P31273; P05813: CRYBA1; NbExp=3; IntAct=EBI-1752118, EBI-7043337; P31273; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1752118, EBI-3867333; P31273; Q92997: DVL3; NbExp=3; IntAct=EBI-1752118, EBI-739789; P31273; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-1752118, EBI-948630; P31273; Q16610: ECM1; NbExp=3; IntAct=EBI-1752118, EBI-947964; P31273; P49356: FNTB; NbExp=3; IntAct=EBI-1752118, EBI-602349; P31273; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1752118, EBI-5916454; P31273; Q9H4Y5: GSTO2; NbExp=3; IntAct=EBI-1752118, EBI-10194609; P31273; P13807: GYS1; NbExp=3; IntAct=EBI-1752118, EBI-740553; P31273; Q9UBX0: HESX1; NbExp=3; IntAct=EBI-1752118, EBI-8470369; P31273; P31249: HOXD3; NbExp=3; IntAct=EBI-1752118, EBI-3957655; P31273; O75031: HSF2BP; NbExp=3; IntAct=EBI-1752118, EBI-7116203; P31273; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-1752118, EBI-747204; P31273; Q7L273: KCTD9; NbExp=3; IntAct=EBI-1752118, EBI-4397613; P31273; Q5T749: KPRP; NbExp=3; IntAct=EBI-1752118, EBI-10981970; P31273; O76011: KRT34; NbExp=5; IntAct=EBI-1752118, EBI-1047093; P31273; Q92764: KRT35; NbExp=3; IntAct=EBI-1752118, EBI-1058674; P31273; O76013-2: KRT36; NbExp=3; IntAct=EBI-1752118, EBI-11958506; P31273; Q6A162: KRT40; NbExp=3; IntAct=EBI-1752118, EBI-10171697; P31273; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1752118, EBI-11959885; P31273; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1752118, EBI-11749135; P31273; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1752118, EBI-10172290; P31273; P60410: KRTAP10-8; NbExp=5; IntAct=EBI-1752118, EBI-10171774; P31273; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1752118, EBI-10172052; P31273; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-1752118, EBI-1052037; P31273; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-1752118, EBI-10210845; P31273; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-1752118, EBI-10241252; P31273; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-1752118, EBI-12196745; P31273; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-1752118, EBI-12111050; P31273; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-1752118, EBI-11962084; P31273; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-1752118, EBI-10261141; P31273; Q5SW96: LDLRAP1; NbExp=8; IntAct=EBI-1752118, EBI-747813; P31273; O95751: LDOC1; NbExp=3; IntAct=EBI-1752118, EBI-740738; P31273; P50458: LHX2; NbExp=3; IntAct=EBI-1752118, EBI-12179869; P31273; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-1752118, EBI-12039345; P31273; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-1752118, EBI-18273118; P31273; Q13387-4: MAPK8IP2; NbExp=3; IntAct=EBI-1752118, EBI-12345753; P31273; P50221: MEOX1; NbExp=3; IntAct=EBI-1752118, EBI-2864512; P31273; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1752118, EBI-16439278; P31273; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-1752118, EBI-10174029; P31273; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-1752118, EBI-748610; P31273; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-1752118, EBI-10271199; P31273; Q8IV28: NID2; NbExp=3; IntAct=EBI-1752118, EBI-10261509; P31273; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1752118, EBI-22310682; P31273; O43482: OIP5; NbExp=3; IntAct=EBI-1752118, EBI-536879; P31273; Q02548: PAX5; NbExp=3; IntAct=EBI-1752118, EBI-296331; P31273; P26367: PAX6; NbExp=3; IntAct=EBI-1752118, EBI-747278; P31273; Q06710: PAX8; NbExp=3; IntAct=EBI-1752118, EBI-2683132; P31273; P40424: PBX1; NbExp=3; IntAct=EBI-1752118, EBI-301611; P31273; P40425: PBX2; NbExp=3; IntAct=EBI-1752118, EBI-348489; P31273; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-1752118, EBI-10302990; P31273; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-1752118, EBI-9640281; P31273; Q99471: PFDN5; NbExp=3; IntAct=EBI-1752118, EBI-357275; P31273; O15496: PLA2G10; NbExp=3; IntAct=EBI-1752118, EBI-726466; P31273; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-1752118, EBI-949255; P31273; Q16633: POU2AF1; NbExp=3; IntAct=EBI-1752118, EBI-943588; P31273; P78424: POU6F2; NbExp=3; IntAct=EBI-1752118, EBI-12029004; P31273; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-1752118, EBI-3957793; P31273; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-1752118, EBI-11320284; P31273; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-1752118, EBI-2340624; P31273; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-1752118, EBI-10269374; P31273; Q15036: SNX17; NbExp=8; IntAct=EBI-1752118, EBI-1752620; P31273; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-1752118, EBI-1644036; P31273; O60806: TBX19; NbExp=3; IntAct=EBI-1752118, EBI-12096770; P31273; Q9Y458: TBX22; NbExp=3; IntAct=EBI-1752118, EBI-6427217; P31273; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-1752118, EBI-750487; P31273; Q08117-2: TLE5; NbExp=3; IntAct=EBI-1752118, EBI-11741437; P31273; Q63HR2: TNS2; NbExp=3; IntAct=EBI-1752118, EBI-949753; P31273; Q13077: TRAF1; NbExp=3; IntAct=EBI-1752118, EBI-359224; P31273; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-1752118, EBI-492476; P31273; P14373: TRIM27; NbExp=3; IntAct=EBI-1752118, EBI-719493; P31273; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-1752118, EBI-5235829; P31273; Q15654: TRIP6; NbExp=3; IntAct=EBI-1752118, EBI-742327; P31273; Q86WV8: TSC1; NbExp=3; IntAct=EBI-1752118, EBI-12806590; P31273; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-1752118, EBI-11975223; P31273; O95231: VENTX; NbExp=3; IntAct=EBI-1752118, EBI-10191303; P31273; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-1752118, EBI-12040603; P31273; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-1752118, EBI-11419867; P31273; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-1752118, EBI-7850213; P31273; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-1752118, EBI-527853; Nucleus. Belongs to the Antp homeobox family. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus nucleoplasm regulation of transcription, DNA-templated multicellular organism development anterior/posterior pattern specification microtubule cytoskeleton neuron differentiation sequence-specific DNA binding skeletal system morphogenesis uc001ser.1 uc001ser.2 uc001ser.3 uc001ser.4 uc001ser.5 
ENST00000040663.8 MRI1 ENST00000040663.8 methylthioribose-1-phosphate isomerase 1, transcript variant 1 (from RefSeq NM_001031727.4) ENST00000040663.1 ENST00000040663.2 ENST00000040663.3 ENST00000040663.4 ENST00000040663.5 ENST00000040663.6 ENST00000040663.7 MRDI MRI1 MTNA_HUMAN NM_001031727 Q8NDC9 Q9BV20 UNQ6390/PRO21135 uc002mxe.1 uc002mxe.2 uc002mxe.3 uc002mxe.4 uc002mxe.5 This enzyme functions in the methionine salvage pathway by catalyzing the interconversion of methylthioribose-1-phosphate and methythioribulose-1-phosphate. Elevated expression of the encoded protein is associated with metastatic melanoma and this protein promotes melanoma cell invasion independent of its enzymatic activity. Mutations in this gene may be associated with vanishing white matter disease (VMWD). [provided by RefSeq, Jul 2016]. Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Independently from catalytic activity, promotes cell invasion in response to constitutive RhoA activation by promoting FAK tyrosine phosphorylation and stress fiber turnover. Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio- D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533, ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence= Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6. Q9BV20; P46379-2: BAG6; NbExp=3; IntAct=EBI-747381, EBI-10988864; Q9BV20; P55212: CASP6; NbExp=3; IntAct=EBI-747381, EBI-718729; Q9BV20; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-747381, EBI-3866319; Q9BV20; Q9Y624: F11R; NbExp=3; IntAct=EBI-747381, EBI-742600; Q9BV20; P13473-2: LAMP2; NbExp=3; IntAct=EBI-747381, EBI-21591415; Q9BV20; Q9BV20: MRI1; NbExp=7; IntAct=EBI-747381, EBI-747381; Q9BV20; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-747381, EBI-2811583; Q9BV20; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-747381, EBI-79165; Q9BV20; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-747381, EBI-742388; Q9BV20; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-747381, EBI-5280197; Q9BV20; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-747381, EBI-2623095; Nucleus toplasm ll projection Note=Primarily nuclear, but cytoplasmic in cancer cells, with enrichment at leading edge of the plasma membrane in late stage tumor cells. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BV20-1; Sequence=Displayed; Name=2; IsoId=Q9BV20-2; Sequence=VSP_030935; By RhoA activation in cancer cells (at protein level). Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily. fibrillar center nucleus nucleoplasm cytoplasm cytosol cellular amino acid biosynthetic process methionine biosynthetic process isomerase activity L-methionine biosynthetic process from S-adenosylmethionine L-methionine biosynthetic process from methylthioadenosine identical protein binding cell projection cellular metabolic process cellular biosynthetic process S-methyl-5-thioribose-1-phosphate isomerase activity uc002mxe.1 uc002mxe.2 uc002mxe.3 uc002mxe.4 uc002mxe.5 
ENST00000040738.10 BOD1L1 ENST00000040738.10 biorientation of chromosomes in cell division 1 like 1 (from RefSeq NM_148894.3) BD1L1_HUMAN BOD1L BOD1L1 ENST00000040738.1 ENST00000040738.2 ENST00000040738.3 ENST00000040738.4 ENST00000040738.5 ENST00000040738.6 ENST00000040738.7 ENST00000040738.8 ENST00000040738.9 FAM44A KIAA1327 NM_148894 Q6P0M8 Q8NFC6 Q96AL1 Q9H6G0 Q9NTD6 Q9P2L9 uc003gmz.1 uc003gmz.2 uc003gmz.3 Component of the fork protection machinery required to protect stalled/damaged replication forks from uncontrolled DNA2- dependent resection. Acts by stabilizing RAD51 at stalled replication forks and protecting RAD51 nucleofilaments from the antirecombinogenic activities of FBH1 and BLM (PubMed:26166705, PubMed:29937342). Does not regulate spindle orientation (PubMed:26166705). Interacts (via COMPASS-Shg1 domain) with SETD1A at stalled replication forks; this interaction mediates FANCD2-dependent nucleosome remodeling at reversed forks protecting them from nucleolytic degradation. Q8NFC6; P61964: WDR5; NbExp=4; IntAct=EBI-2654318, EBI-540834; Chromosome Note=Localizes at replication forks: following DNA damage, localizes to damaged replication forks undergoing resection. Belongs to the BOD1 family. Sequence=AAH16987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAB15299.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; Sequence=CAB70705.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; spindle pole condensed chromosome outer kinetochore protein phosphatase inhibitor activity nucleoplasm chromosome centrosome spindle microtubule DNA repair cellular response to DNA damage stimulus replication fork processing negative regulation of phosphoprotein phosphatase activity protein phosphatase 2A binding uc003gmz.1 uc003gmz.2 uc003gmz.3 
ENST00000040877.2 TARBP1 ENST00000040877.2 TAR (HIV-1) RNA binding protein 1 (from RefSeq NM_005646.4) ENST00000040877.1 NM_005646 Q13395 Q9H581 TARB1_HUMAN TRM3 TRP185 uc001hwd.1 uc001hwd.2 uc001hwd.3 uc001hwd.4 HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. This element forms a stable stem-loop structure and can be bound by either the protein encoded by this gene or by RNA polymerase II. This protein may act to disengage RNA polymerase II from TAR during transcriptional elongation. Alternatively spliced transcripts of this gene may exist, but their full-length natures have not been determined. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U38847.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000040877.2/ ENSP00000040877.1 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. (Microbial infection) In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II (PubMed:7638159, PubMed:8626763, PubMed:8846792). Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA (PubMed:7638159, PubMed:8626763, PubMed:8846792). Monomer and homodimer. Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. RNA binding nucleus regulation of transcription from RNA polymerase II promoter RNA processing methyltransferase activity RNA methyltransferase activity tRNA (guanine) methyltransferase activity transferase activity tRNA methylation methylation uc001hwd.1 uc001hwd.2 uc001hwd.3 uc001hwd.4 
ENST00000042381.9 RIPOR1 ENST00000042381.9 RHO family interacting cell polarization regulator 1, transcript variant 1 (from RefSeq NM_024519.4) B4DEQ9 B4DIM2 E9PBS3 ENST00000042381.1 ENST00000042381.2 ENST00000042381.3 ENST00000042381.4 ENST00000042381.5 ENST00000042381.6 ENST00000042381.7 ENST00000042381.8 FAM65A KIAA1930 NM_024519 Q4G0A4 Q6ZS17 Q7Z5R7 Q8NDA4 Q96J39 Q96PV8 Q9H8D9 RIPR1_HUMAN uc002eth.1 uc002eth.2 uc002eth.3 uc002eth.4 uc002eth.5 Downstream effector protein for Rho-type small GTPases that plays a role in cell polarity and directional migration (PubMed:27807006). Acts as an adapter protein, linking active Rho proteins to STK24 and STK26 kinases, and hence positively regulates Golgi reorientation in polarized cell migration upon Rho activation (PubMed:27807006). Involved in the subcellular relocation of STK26 from the Golgi to cytoplasm punctae in a Rho- and PDCD10-dependent manner upon serum stimulation (PubMed:27807006). Interacts (via N-terminus) with RHOA (GTP-bound form); this interaction links active RHOA to STK24 and STK26 kinases (PubMed:27807006). Interacts with RHOB (PubMed:27807006). Interacts with RHOC (PubMed:27807006). Interacts (via C-terminus) with PDCD10; this interaction occurs in a Rho-independent manner (PubMed:27807006). Interacts (via C-terminus) with STK24; this interaction occurs in a PDCD10-dependent and Rho-independent manner (PubMed:27807006). Interacts (via C-terminus) with STK26; this interaction occurs in a PDCD10-dependent and Rho-independent manner (PubMed:27807006). Interacts (via N-terminus) with 14-3-3 proteins; these interactions occur in a Rho-dependent manner (PubMed:27807006). Cytoplasm Golgi apparatus Note=Localizes to the podocyte major processes and cell body (By similarity). Colocalized with STK26 in the Golgi of serum-starved cells and relocated to cytoplasmic punctae, probably vesicular compartments, along with STK26 upon serum stimulation in a Rho- and PDCD10-dependent manner (PubMed:27807006). Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q6ZS17-1; Sequence=Displayed; Name=2; IsoId=Q6ZS17-2; Sequence=VSP_025903; Name=3; IsoId=Q6ZS17-3; Sequence=VSP_043315, VSP_025903; Name=4; IsoId=Q6ZS17-4; Sequence=VSP_045002, VSP_025903; Belongs to the RIPOR family. Sequence=BAB14678.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence=; Sequence=BAB67823.1; Type=Frameshift; Evidence=; protein binding cytoplasm Golgi apparatus Rho protein signal transduction cellular response to starvation response to wounding vesicle membrane membrane positive regulation of cell migration cell leading edge protein localization to Golgi apparatus negative regulation of Rho protein signal transduction establishment of Golgi localization extracellular exosome 14-3-3 protein binding positive regulation of intracellular protein transport cellular response to chemokine negative regulation of Rho guanyl-nucleotide exchange factor activity uc002eth.1 uc002eth.2 uc002eth.3 uc002eth.4 uc002eth.5 
ENST00000043402.8 RTN4R ENST00000043402.8 reticulon 4 receptor (from RefSeq NM_023004.6) D3DX28 ENST00000043402.1 ENST00000043402.2 ENST00000043402.3 ENST00000043402.4 ENST00000043402.5 ENST00000043402.6 ENST00000043402.7 NM_023004 NOGOR Q9BZR6 RTN4R_HUMAN UNQ330/PRO526 uc002zrv.1 uc002zrv.2 uc002zrv.3 uc002zrv.4 uc002zrv.5 This gene encodes the receptor for reticulon 4, oligodendrocyte myelin glycoprotein and myelin-associated glycoprotein. This receptor mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AL834449.1, ERR279866.1216.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000043402.8/ ENSP00000043402.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor for RTN4, OMG and MAG (PubMed:12037567, PubMed:12068310, PubMed:12426574, PubMed:12089450, PubMed:16712417, PubMed:18411262, PubMed:12839991, PubMed:19052207). Functions as a receptor for the sialylated gangliosides GT1b and GM1 (PubMed:18411262). Besides, functions as a receptor for chondroitin sulfate proteoglycans (By similarity). Can also bind heparin (By similarity). Intracellular signaling cascades are triggered via the coreceptor NGFR (PubMed:12426574). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:16712417, PubMed:22325200). Mediates axonal growth inhibition (PubMed:12839991, PubMed:19052207, PubMed:28892071). Plays a role in regulating axon regeneration and neuronal plasticity in the adult central nervous system. Plays a role in postnatal brain development. Required for normal axon migration across the brain midline and normal formation of the corpus callosum. Protects motoneurons against apoptosis; protection against apoptosis is probably mediated via interaction with MAG. Acts in conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell motility during cortical development. Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). Homodimer (PubMed:18411262). Interacts with MAG (PubMed:12089450, PubMed:12839991, PubMed:18411262, PubMed:19052207). Interacts with RTN4 (PubMed:12839991, PubMed:19052207). Interacts with NGFR (PubMed:12426574, PubMed:18411262, PubMed:19052207). Interacts with LINGO1 (PubMed:14966521, PubMed:19052207). Interacts with KIAA0319L (PubMed:20697954). Interacts with OLFM1; this inhibits interaction with LINGO1 and NGFR (By similarity). Interacts with OMG (PubMed:12068310, PubMed:12839991, PubMed:19052207). Q9BZR6; P49639: HOXA1; NbExp=3; IntAct=EBI-5240240, EBI-740785; Q9BZR6; Q8IZA0: KIAA0319L; NbExp=4; IntAct=EBI-5240240, EBI-5240269; Q9BZR6; P32242: OTX1; NbExp=3; IntAct=EBI-5240240, EBI-740446; Cell membrane ipid- anchor, GPI-anchor Membrane raft Cell projection, dendrite Cell projection, axon Perikaryon Note=Detected along dendrites and axons, close to synapses, but clearly excluded from synapses. Widespread in the brain but highest levels in the gray matter. Low levels in heart and kidney; not expressed in oligodendrocytes (white matter). N-glycosylated. O-glycosylated. Contains terminal sialic acid groups on its glycan chains. Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. te=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the Nogo receptor family. Name=Protein Spotlight; Note=Nerve regrowth: nipped by a no-go - Issue 69 of April 2006; URL="https://web.expasy.org/spotlight/back_issues/069"; protein binding endoplasmic reticulum plasma membrane integral component of plasma membrane cell surface receptor signaling pathway axonogenesis heparin binding lipid binding cell surface negative regulation of neuron projection development membrane corpus callosum development neuronal signal transduction axon dendrite growth cone negative regulation of axon extension anchored component of membrane anchored component of external side of plasma membrane positive regulation of Rho protein signal transduction chondroitin sulfate binding signaling receptor activity neuregulin receptor activity cell projection neuron projection neuronal cell body dendritic shaft perikaryon positive regulation of GTPase activity axonal growth cone macromolecular complex binding membrane raft negative regulation of axon regeneration negative regulation of axonogenesis extracellular exosome presynapse glutamatergic synapse ganglioside GM1 binding ganglioside GT1b binding uc002zrv.1 uc002zrv.2 uc002zrv.3 uc002zrv.4 uc002zrv.5 
ENST00000044462.12 PSMA4 ENST00000044462.12 proteasome 20S subunit alpha 4, transcript variant 1 (from RefSeq NM_002789.6) D3DW86 ENST00000044462.1 ENST00000044462.10 ENST00000044462.11 ENST00000044462.2 ENST00000044462.3 ENST00000044462.4 ENST00000044462.5 ENST00000044462.6 ENST00000044462.7 ENST00000044462.8 ENST00000044462.9 HC9 NM_002789 P25789 PSA4_HUMAN PSC9 Q53XP2 Q567Q5 Q8TBD1 uc002bdu.1 uc002bdu.2 uc002bdu.3 uc002bdu.4 uc002bdu.5 uc002bdu.6 This gene encodes a core alpha subunit of the 20S proteosome, which is a highly ordered ring-shaped structure composed of four rings of 28 non-identical subunits. Proteasomes cleave peptides in an ATP- and ubiquitin-dependent manner. [provided by RefSeq, Aug 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803615.40060.1, SRR1803615.115885.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000044462.12/ ENSP00000044462.7 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP- dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin- independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. (Microbial infection) Interaction with HTLV-1 TAX protein favors NFKB1 activation. P25789; P54253: ATXN1; NbExp=7; IntAct=EBI-359310, EBI-930964; P25789; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-359310, EBI-11530605; P25789; Q08379: GOLGA2; NbExp=3; IntAct=EBI-359310, EBI-618309; P25789; Q16665: HIF1A; NbExp=4; IntAct=EBI-359310, EBI-447269; P25789; P42858: HTT; NbExp=4; IntAct=EBI-359310, EBI-466029; P25789; Q13422: IKZF1; NbExp=3; IntAct=EBI-359310, EBI-745305; P25789; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-359310, EBI-11522367; P25789; P25786: PSMA1; NbExp=7; IntAct=EBI-359310, EBI-359352; P25789; P25787: PSMA2; NbExp=8; IntAct=EBI-359310, EBI-603262; P25789; P25788: PSMA3; NbExp=4; IntAct=EBI-359310, EBI-348380; P25789; P60900: PSMA6; NbExp=5; IntAct=EBI-359310, EBI-357793; P25789; O14818: PSMA7; NbExp=11; IntAct=EBI-359310, EBI-603272; P25789; Q04864-2: REL; NbExp=3; IntAct=EBI-359310, EBI-10829018; P25789; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-359310, EBI-1105213; P25789; O00635: TRIM38; NbExp=3; IntAct=EBI-359310, EBI-2130415; P25789; Q99PV5: Bhlhe41; Xeno; NbExp=2; IntAct=EBI-359310, EBI-6143801; Cytoplasm cleus te=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9 (PubMed:34711951). Colocalizes with TRIM5 in the cytoplasmic bodies (By similarity). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P25789-1; Sequence=Displayed; Name=2; IsoId=P25789-2; Sequence=VSP_043102; Down-regulated by antioxidants BO-653 and probucol. Belongs to the peptidase T1A family. MAPK cascade protein polyubiquitination proteasome complex P-body stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent endopeptidase activity threonine-type endopeptidase activity protein binding nucleus nucleoplasm cytoplasm cytosol proteasome core complex proteolysis ubiquitin-dependent protein catabolic process regulation of cellular amino acid metabolic process peptidase activity proteasomal protein catabolic process proteasomal ubiquitin-independent protein catabolic process negative regulation of G2/M transition of mitotic cell cycle viral process protein deubiquitination hydrolase activity proteasome core complex, alpha-subunit complex anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process intracellular membrane-bounded organelle regulation of mRNA stability post-translational protein modification T cell receptor signaling pathway proteolysis involved in cellular protein catabolic process transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia extracellular exosome interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation uc002bdu.1 uc002bdu.2 uc002bdu.3 uc002bdu.4 uc002bdu.5 uc002bdu.6 
ENST00000046087.7 ZPBP ENST00000046087.7 zona pellucida binding protein, transcript variant 1 (from RefSeq NM_007009.3) A4D253 C9JPU1 ENST00000046087.1 ENST00000046087.2 ENST00000046087.3 ENST00000046087.4 ENST00000046087.5 ENST00000046087.6 NM_007009 Q15941 Q75KX9 Q75MI3 Q9BS86 ZPBP1 ZPBP1_HUMAN uc003tou.1 uc003tou.2 uc003tou.3 uc003tou.4 uc003tou.5 ZPBP is one of several proteins that are thought to participate in secondary binding between acrosome-reacted sperm and the egg-specific extracellular matrix, the zona pellucida (McLeskey et al., 1998 [PubMed 9378618]).[supplied by OMIM, Aug 2008]. Plays a role in acrosome compaction and sperm morphogenesis (PubMed:21911476). Is implicated in sperm-oocyte interaction during fertilization (By similarity). Cytoplasmic vesicle, secretory vesicle, acrosome Cytoplasmic vesicle, secretory vesicle, acrosome membrane ; Peripheral membrane protein Secreted Note=First localized in acrosome granule, later migrates to the inner and outer acrosomal membrane. Released after the acrosomal reaction. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BS86-1; Sequence=Displayed; Name=2; IsoId=Q9BS86-2; Sequence=VSP_045491; Expressed specifically in testis. N-glycosylated. Spermatogenic failure 66 (SPGF66) [MIM:619799]: An autosomal recessive male infertility disorder characterized by globozoospermia. Affected individuals have a normal sperm count, but spermatozoa are round-headed and lack the acrosome. In addition to pure globozoospermia, some patients have a mixture of acrosomeless spermatozoa and spermatozoa with small or detached acrosomes, which is defined as acrosomal hypoplasia. te=The disease may be caused by variants affecting the gene represented in this entry. Belongs to the zona pellucida-binding protein Sp38 family. Sequence=AAS07517.1; Type=Erroneous initiation; Evidence=; acrosomal membrane extracellular region nucleus binding of sperm to zona pellucida membrane cytoplasmic vesicle uc003tou.1 uc003tou.2 uc003tou.3 uc003tou.4 uc003tou.5 
ENST00000046640.9 CTNS ENST00000046640.9 cystinosin, lysosomal cystine transporter, transcript variant 2 (from RefSeq NM_004937.3) CTNS CTNS_HUMAN D3DTJ5 ENST00000046640.1 ENST00000046640.2 ENST00000046640.3 ENST00000046640.4 ENST00000046640.5 ENST00000046640.6 ENST00000046640.7 ENST00000046640.8 NM_004937 O60931 Q8IZ01 Q9UNK6 uc002fwb.1 uc002fwb.2 uc002fwb.3 uc002fwb.4 uc002fwb.5 This gene encodes a seven-transmembrane domain protein that functions to transport cystine out of lysosomes. Its activity is driven by the H+ electrochemical gradient of the lysosomal membrane. Mutations in this gene cause cystinosis, a lysosomal storage disorder. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2009]. Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from lysosomes (PubMed:11689434, PubMed:18337546, PubMed:22232659, PubMed:29467429, PubMed:33208952, PubMed:15128704, PubMed:36113465). Plays an important role in melanin synthesis by catalyzing cystine export from melanosomes, possibly by inhibiting pheomelanin synthesis (PubMed:22649030). In addition to cystine export, also acts as a positive regulator of mTORC1 signaling in kidney proximal tubular cells, via interactions with components of the v-ATPase and Ragulator complexes (PubMed:36113465). Also involved in small GTPase-regulated vesicle trafficking and lysosomal localization of LAMP2A, independently of cystine transporter activity (By similarity). Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in); Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173; Evidence= [Isoform 1]: Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in); Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173; Evidence=; [Isoform 2]: Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in); Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173; Evidence=; Switches between a lumen- and a cytosol-open conformation: pH induces conformational changes and shifts the equilibrium to facilitate the transition between the lumen- and cytosol-open conformation, thereby promoting cystine transport (PubMed:36113465). Protonation of specific aspartate residues (Asp-205, Asp-305 and Asp-346) favors the cytosol-open conformation (PubMed:36113465). Kinetic parameters: KM=75 uM for cystine (at pH 5.0) ; KM=278 uM for cystine ; Interacts with components of the V-ATPase complex (By similarity). Interacts with components of the Ragulator complex (PubMed:36113465). Interacts with RRAGA/RagA and RRAGC/RagC (By similarity). Interacts with AP-3 complex subunit mu (AP3M1 or AP3M2) (PubMed:25753619). O60931-2; Q14749: GNMT; NbExp=3; IntAct=EBI-19888994, EBI-744239; [Isoform 1]: Lysosome membrane ulti-pass membrane protein Melanosome membrane ; Multi-pass membrane protein Note=AP-3 complex is required for localization to the lysosome. [Isoform 2]: Lysosome membrane ; Multi-pass membrane protein Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O60931-1; Sequence=Displayed; Name=2; Synonyms=cystinosin-LKG ; IsoId=O60931-2; Sequence=VSP_038377; Strongly expressed in pancreas, kidney (adult and fetal), skeletal muscle, melanocytes and keratinocytes (PubMed:22649030). Expressed at lower levels in placenta and heart. Weakly expressed in lung, liver and brain (adult and fetal) (PubMed:22649030). [Isoform 2]: Represents 5-20 % of CTNS transcripts, with the exception of the testis that expresses both isoforms in equal proportions. The lysosomal targeting motif, together with the second PQ-loop mediate targeting to the lysosome. Cystinosis, nephropathic type (CTNS) [MIM:219800]: A form of cystinosis, a lysosomal storage disease due to defective transport of cystine across the lysosomal membrane. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. The classical nephropathic form has onset in the first year of life and is characterized by a polyuro-polydipsic syndrome, marked height-weight growth delay, generalized impaired proximal tubular reabsorptive capacity, with severe fluid-electrolyte balance alterations, renal failure, ocular symptoms and other systemic complications. te=The disease is caused by variants affecting the gene represented in this entry. Cystinosis, adult, non-nephropathic type (CTNSANN) [MIM:219750]: A form of cystinosis, a lysosomal storage disease due to defective transport of cystine across the lysosomal membrane. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. Cystinosis adult non-nephropathic type is characterized by ocular features and a benign course. Patients manifest mild photophobia due to conjunctival and corneal cystine crystals. Note=The disease is caused by variants affecting the gene represented in this entry. Cystinosis, late-onset juvenile or adolescent nephropathic type (CTNSJAN) [MIM:219900]: A form of cystinosis, a lysosomal storage disease due to defective transport of cystine across the lysosomal membrane. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. Late-onset juvenile or adolescent nephropathic cystinosis is an intermediated form, manifesting first at age 10 to 12 years with proteinuria due to glomerular damage rather than with the manifestations of tubular damage that occur first in infantile cystinosis. There is no excess amino aciduria and stature is normal. Photophobia, late development of pigmentary retinopathy, and chronic headaches are features. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the cystinosin family. lens development in camera-type eye lysosome lysosomal membrane late endosome vacuolar membrane plasma membrane cellular amino acid metabolic process glutathione metabolic process ion transport brain development long-term memory grooming behavior adult walking behavior visual learning negative regulation of hydrogen peroxide biosynthetic process positive regulation of mitochondrial membrane potential L-cystine transmembrane transporter activity L-cystine transport membrane integral component of membrane melanin biosynthetic process melanosome intracellular membrane-bounded organelle intermediate filament cytoskeleton ATP metabolic process cognition transmembrane transport extracellular exosome negative regulation of reactive oxygen species biosynthetic process early endosome uc002fwb.1 uc002fwb.2 uc002fwb.3 uc002fwb.4 uc002fwb.5 
ENST00000046794.10 LCP2 ENST00000046794.10 lymphocyte cytosolic protein 2 (from RefSeq NM_005565.5) A8KA25 ENST00000046794.1 ENST00000046794.2 ENST00000046794.3 ENST00000046794.4 ENST00000046794.5 ENST00000046794.6 ENST00000046794.7 ENST00000046794.8 ENST00000046794.9 LCP2_HUMAN NM_005565 Q13094 Q53XV4 uc003man.1 uc003man.2 uc003man.3 This gene encodes an adapter protein that acts as a substrate of the T cell antigen receptor (TCR)-activated protein tyrosine kinase pathway. The encoded protein associates with growth factor receptor bound protein 2, and is thought to play a role TCR-mediated intracellular signal transduction. A similar protein in mouse plays a role in normal T-cell development and activation. Mice lacking this gene show subcutaneous and intraperitoneal fetal hemorrhaging, dysfunctional platelets and impaired viability. [provided by RefSeq, Nov 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC016618.1, SRR1163658.196053.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000046794.10/ ENSP00000046794.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Involved in T-cell antigen receptor mediated signaling. Interacts with SLA. Interacts with CBLB (By similarity). Interacts with GRB2 (PubMed:7706237). Interacts with SHB (PubMed:12084069). Interacts with PRAM1 (PubMed:11301322). Interacts (via SH2 domain) with CD6 (via tyrosine phosphorylated C-terminus) (PubMed:16914752, PubMed:24584089). Interacts with FYB1 and the phosphorylated form of FYB2 (PubMed:27335501). Q13094; P30203: CD6; NbExp=3; IntAct=EBI-346946, EBI-2873748; Q13094; P00533: EGFR; NbExp=3; IntAct=EBI-346946, EBI-297353; Q13094; Q9H5J4: ELOVL6; NbExp=3; IntAct=EBI-346946, EBI-12821617; Q13094; P51116: FXR2; NbExp=7; IntAct=EBI-346946, EBI-740459; Q13094; O15117: FYB1; NbExp=9; IntAct=EBI-346946, EBI-1753267; Q13094; Q08379: GOLGA2; NbExp=6; IntAct=EBI-346946, EBI-618309; Q13094; O75791: GRAP2; NbExp=40; IntAct=EBI-346946, EBI-740418; Q13094; P62993: GRB2; NbExp=18; IntAct=EBI-346946, EBI-401755; Q13094; Q08881: ITK; NbExp=3; IntAct=EBI-346946, EBI-968552; Q13094; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-346946, EBI-739832; Q13094; Q8IVH8: MAP4K3; NbExp=5; IntAct=EBI-346946, EBI-1758170; Q13094; P16333: NCK1; NbExp=21; IntAct=EBI-346946, EBI-389883; Q13094; O43639: NCK2; NbExp=10; IntAct=EBI-346946, EBI-713635; Q13094; P19174: PLCG1; NbExp=3; IntAct=EBI-346946, EBI-79387; Q13094; Q92783: STAM; NbExp=3; IntAct=EBI-346946, EBI-752333; Q13094; O75886: STAM2; NbExp=9; IntAct=EBI-346946, EBI-373258; Q13094; P15498: VAV1; NbExp=9; IntAct=EBI-346946, EBI-625518; Q13094; O89100: Grap2; Xeno; NbExp=4; IntAct=EBI-346946, EBI-642151; Q13094; Q99JP0: Map4k3; Xeno; NbExp=2; IntAct=EBI-346946, EBI-5324222; Q13094; P08487: PLCG1; Xeno; NbExp=5; IntAct=EBI-346946, EBI-8013886; Cytoplasm Highly expressed in spleen, thymus and peripheral blood leukocytes. Highly expressed also in T-cell and monocytic cell lines, expressed at lower level in B-cell lines. Not detected in fibroblast or neuroblastoma cell lines. The SH2 domain mediates interaction with phosphorylated CD6 (PubMed:16914752). The SH2 domain mediates interaction with SHB (PubMed:12084069). Phosphorylated after T-cell receptor activation by ZAP70, ITK and TXK, which leads to the up-regulation of Th1 preferred cytokine IL-2. SYK-dependent phosphorylation is required for recruitment of PI3K signaling components. Immunodeficiency 81 (IMD81) [MIM:619374]: An autosomal recessive disorder characterized by recurrent infections, including fungal infections, associated with T cell, neutrophil, and NK cell dysfunction. B cells may also show maturation abnormalities. Other features include autoimmune hemolytic anemia and abnormal platelet aggregation. Note=The disease is caused by variants affecting the gene represented in this entry. protein binding cytoplasm cytosol cell-cell junction immune response transmembrane receptor protein tyrosine kinase signaling pathway platelet activation intracellular signal transduction TCR signalosome Fc-epsilon receptor signaling pathway plasma membrane raft mast cell activation positive regulation of protein kinase activity cytokine secretion T cell receptor signaling pathway uc003man.1 uc003man.2 uc003man.3 
ENST00000052754.10 DCN ENST00000052754.10 decorin, transcript variant A2 (from RefSeq NM_133503.4) DCN DKFZp686J19238 ENST00000052754.1 ENST00000052754.2 ENST00000052754.3 ENST00000052754.4 ENST00000052754.5 ENST00000052754.6 ENST00000052754.7 ENST00000052754.8 ENST00000052754.9 NM_133503 Q6FH10 Q6FH10_HUMAN hCG_24110 uc001tbu.1 uc001tbu.2 uc001tbu.3 uc001tbu.4 uc001tbu.5 This gene encodes a member of the small leucine-rich proteoglycan family of proteins. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate the mature protein. This protein plays a role in collagen fibril assembly. Binding of this protein to multiple cell surface receptors mediates its role in tumor suppression, including a stimulatory effect on autophagy and inflammation and an inhibitory effect on angiogenesis and tumorigenesis. This gene and the related gene biglycan are thought to be the result of a gene duplication. Mutations in this gene are associated with congenital stromal corneal dystrophy in human patients. [provided by RefSeq, Nov 2015]. May affect the rate of fibrils formation. Binds to type I and type II collagen, fibronectin and TGF- beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT. Secreted, extracellular space, extracellular matrix Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily. kidney development placenta development collagen binding glycosaminoglycan binding extracellular region collagen type VI trimer skeletal muscle tissue development aging response to mechanical stimulus positive regulation of autophagy peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan extracellular matrix structural constituent conferring compression resistance extracellular matrix response to lipopolysaccharide wound healing protein N-terminus binding extracellular matrix binding uc001tbu.1 uc001tbu.2 uc001tbu.3 uc001tbu.4 uc001tbu.5 
ENST00000053243.6 TNFRSF17 ENST00000053243.6 TNF receptor superfamily member 17 (from RefSeq NM_001192.3) BCM BCMA ENST00000053243.1 ENST00000053243.2 ENST00000053243.3 ENST00000053243.4 ENST00000053243.5 NM_001192 Q02223 Q2TQ40 TNR17_HUMAN uc002dbv.1 uc002dbv.2 uc002dbv.3 uc002dbv.4 The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is preferentially expressed in mature B lymphocytes, and may be important for B cell development and autoimmune response. This receptor has been shown to specifically bind to the tumor necrosis factor (ligand) superfamily, member 13b (TNFSF13B/TALL-1/BAFF), and to lead to NF-kappaB and MAPK8/JNK activation. This receptor also binds to various TRAF family members, and thus may transduce signals for cell survival and proliferation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163658.304475.1, BC058291.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000053243.6/ ENSP00000053243.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor for TNFSF13B/BLyS/BAFF and TNFSF13/APRIL. Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK. Associates with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6. Q02223; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-519945, EBI-2807956; Q02223; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-519945, EBI-981985; Q02223; P55061: TMBIM6; NbExp=3; IntAct=EBI-519945, EBI-1045825; Cell membrane; Single-pass type III membrane protein. Endomembrane system; Single-pass type III membrane protein. Note=Perinuclear Golgi-like structures. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q02223-1; Sequence=Displayed; Name=2; Synonyms=TV4; IsoId=Q02223-2; Sequence=VSP_047678; Expressed in mature B-cells, but not in T-cells or monocytes. Note=A chromosomal aberration involving TNFRSF17 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(4;16)(q26;p13) with IL2. [Isoform 2]: Observed only in some CD19+ cell. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tnfrsf17/"; adaptive immune response lymphocyte homeostasis immune system process plasma membrane signal transduction multicellular organism development endomembrane system membrane integral component of membrane tumor necrosis factor-mediated signaling pathway signaling receptor activity uc002dbv.1 uc002dbv.2 uc002dbv.3 uc002dbv.4 
ENST00000053468.4 MRPS10 ENST00000053468.4 mitochondrial ribosomal protein S10 (from RefSeq NM_018141.4) B2RE89 ENST00000053468.1 ENST00000053468.2 ENST00000053468.3 MSTP040 NM_018141 P82664 Q9H3E5 Q9NVR3 RT10_HUMAN uc003osa.1 uc003osa.2 uc003osa.3 uc003osa.4 uc003osa.5 uc003osa.6 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S10P family. Pseudogenes corresponding to this gene are found on chromosomes 1q, 3p, and 9p. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.110737.1, SRR1803613.110112.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000053468.4/ ENSP00000053468.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Component of the mitochondrial small ribosomal subunit (mt- SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins. Mitochondrion Belongs to the universal ribosomal protein uS10 family. molecular_function mitochondrion mitochondrial inner membrane mitochondrial small ribosomal subunit ribosome biological_process mitochondrial translational elongation mitochondrial translational termination uc003osa.1 uc003osa.2 uc003osa.3 uc003osa.4 uc003osa.5 uc003osa.6 
ENST00000053867.8 GRN ENST00000053867.8 granulin precursor (from RefSeq NM_002087.4) D3DX55 ENST00000053867.1 ENST00000053867.2 ENST00000053867.3 ENST00000053867.4 ENST00000053867.5 ENST00000053867.6 ENST00000053867.7 GRN GRN_HUMAN NM_002087 P23781 P23782 P23783 P23784 P28799 Q53HQ8 Q53Y88 Q540U8 Q9BWE7 Q9H8S1 Q9UCH0 uc002igp.1 uc002igp.2 uc002igp.3 uc002igp.4 Granulins are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. The 88 kDa precursor protein, progranulin, is also called proepithelin and PC cell-derived growth factor. Cleavage of the signal peptide produces mature granulin which can be further cleaved into a variety of active, 6 kDa peptides. These smaller cleavage products are named granulin A, granulin B, granulin C, etc. Epithelins 1 and 2 are synonymous with granulins A and B, respectively. Both the peptides and intact granulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X62320.1, AK000607.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000053867.8/ ENSP00000053867.2 RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein regulatory uORF :: PMID: 25056957 ##RefSeq-Attributes-END## Secreted protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation (PubMed:28541286, PubMed:28073925, PubMed:18378771, PubMed:28453791, PubMed:12526812). Regulates protein trafficking to lysosomes and, also the activity of lysosomal enzymes (PubMed:28453791, PubMed:28541286). Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB (PubMed:28073925). In addition, functions as a wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structures (By similarity). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases (PubMed:12526812). Moreover, modulates inflammation in neurons by preserving neurons survival, axonal outgrowth and neuronal integrity (PubMed:18378771). [Granulin-4]: Promotes proliferation of the epithelial cell line A431 in culture. [Granulin-3]: Inhibits epithelial cell proliferation and induces epithelial cells to secrete IL-8. [Granulin-7]: Stabilizes CTSD through interaction with CTSD leading to maintain its aspartic-type peptidase activity. Progranulin is secreted as a homodimer (PubMed:23364791). Interacts with SLPI; interaction protects progranulin from proteolysis (PubMed:12526812). Interacts (via region corresponding to granulin-7 peptide) with CTSD; stabilizes CTSD and increases its proteolytic activity (PubMed:28453791). Interacts (via region corresponding to granulin-7 peptide) with SORT1; this interaction mediates endocytosis and lysosome delivery of progranulin; interaction occurs at the neuronal cell surface in a stressed nervous system (PubMed:21092856). Interacts with PSAP; facilitates lysosomal delivery of progranulin from the extracellular space and the biosynthetic pathway (PubMed:26370502). Forms a complex with PSAP and M6PR; PSAP bridges the binding between progranulin and M6PR (PubMed:26370502). Forms a complex with PSAP and SORT1; progranulin bridges the interaction between PSAP and SORT1; facilitates lysosomal targeting of PSAP via SORT1; interaction enhances PSAP uptake in primary cortical neurons (PubMed:28541286). Interacts (via regions corresponding to granulin-2 and granulin-7 peptides) with GBA1; this interaction prevents aggregation of GBA1-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271). Interacts (via region corresponding to granulin-7 peptide) with HSPA1A; mediates recruitment of HSPA1A to GBA1 and prevents GBA1 aggregation in response to stress (PubMed:27789271). P28799; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-747754, EBI-10173507; P28799; Q9UIJ7: AK3; NbExp=3; IntAct=EBI-747754, EBI-3916527; P28799; Q9NYG5: ANAPC11; NbExp=3; IntAct=EBI-747754, EBI-2130187; P28799; D3DTF8: APLN; NbExp=3; IntAct=EBI-747754, EBI-22002556; P28799; Q8N6T3: ARFGAP1; NbExp=3; IntAct=EBI-747754, EBI-716933; P28799; Q8N6T3-3: ARFGAP1; NbExp=3; IntAct=EBI-747754, EBI-10694449; P28799; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-747754, EBI-14199987; P28799; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-747754, EBI-25843552; P28799; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-747754, EBI-10254793; P28799; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-747754, EBI-9089489; P28799; P46379-2: BAG6; NbExp=3; IntAct=EBI-747754, EBI-10988864; P28799; Q16611: BAK1; NbExp=3; IntAct=EBI-747754, EBI-519866; P28799; Q8IXM2: BAP18; NbExp=3; IntAct=EBI-747754, EBI-4280811; P28799; Q14457: BECN1; NbExp=3; IntAct=EBI-747754, EBI-949378; P28799; Q96LC9: BMF; NbExp=3; IntAct=EBI-747754, EBI-3919268; P28799; Q9GZL8: BPESC1; NbExp=3; IntAct=EBI-747754, EBI-25861458; P28799; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-747754, EBI-2837444; P28799; Q9Y297: BTRC; NbExp=3; IntAct=EBI-747754, EBI-307461; P28799; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-747754, EBI-747505; P28799; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-747754, EBI-7317823; P28799; Q6P5X5-2: C22orf39; NbExp=3; IntAct=EBI-747754, EBI-10692329; P28799; Q53FE4: C4orf17; NbExp=3; IntAct=EBI-747754, EBI-715110; P28799; Q9BRJ6: C7orf50; NbExp=3; IntAct=EBI-747754, EBI-751612; P28799; O00555: CACNA1A; NbExp=2; IntAct=EBI-747754, EBI-766279; P28799; Q96NX5: CAMK1G; NbExp=3; IntAct=EBI-747754, EBI-3920838; P28799; O75808: CAPN15; NbExp=3; IntAct=EBI-747754, EBI-6149008; P28799; Q8N5R6: CCDC33; NbExp=3; IntAct=EBI-747754, EBI-740841; P28799; P50750-2: CDK9; NbExp=3; IntAct=EBI-747754, EBI-12029902; P28799; O14646-2: CHD1; NbExp=3; IntAct=EBI-747754, EBI-10961487; P28799; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-747754, EBI-744045; P28799; Q99967: CITED2; NbExp=3; IntAct=EBI-747754, EBI-937732; P28799; Q9Y240: CLEC11A; NbExp=3; IntAct=EBI-747754, EBI-3957044; P28799; Q96DZ5: CLIP3; NbExp=3; IntAct=EBI-747754, EBI-12823145; P28799; Q16740: CLPP; NbExp=3; IntAct=EBI-747754, EBI-1056029; P28799; Q9BT09: CNPY3; NbExp=3; IntAct=EBI-747754, EBI-2835965; P28799; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-747754, EBI-25836090; P28799; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-747754, EBI-350590; P28799; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-747754, EBI-713677; P28799; Q02930-3: CREB5; NbExp=3; IntAct=EBI-747754, EBI-10192698; P28799; Q49AN0: CRY2; NbExp=3; IntAct=EBI-747754, EBI-2212355; P28799; P01040: CSTA; NbExp=3; IntAct=EBI-747754, EBI-724303; P28799; P07339: CTSD; NbExp=4; IntAct=EBI-747754, EBI-2115097; P28799; P42830: CXCL5; NbExp=3; IntAct=EBI-747754, EBI-12175919; P28799; Q8TB03: CXorf38; NbExp=3; IntAct=EBI-747754, EBI-12024320; P28799; P00167: CYB5A; NbExp=3; IntAct=EBI-747754, EBI-1047284; P28799; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-747754, EBI-3867333; P28799; Q16643: DBN1; NbExp=5; IntAct=EBI-747754, EBI-351394; P28799; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-747754, EBI-25842815; P28799; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-747754, EBI-12019838; P28799; Q07687: DLX2; NbExp=3; IntAct=EBI-747754, EBI-3908234; P28799; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-747754, EBI-9679045; P28799; P49184: DNASE1L1; NbExp=3; IntAct=EBI-747754, EBI-20894690; P28799; Q16610: ECM1; NbExp=3; IntAct=EBI-747754, EBI-947964; P28799; O75530-2: EED; NbExp=3; IntAct=EBI-747754, EBI-11132357; P28799; O60841: EIF5B; NbExp=3; IntAct=EBI-747754, EBI-928530; P28799; Q6UXG2-3: ELAPOR1; NbExp=3; IntAct=EBI-747754, EBI-12920100; P28799; Q8TE68-3: EPS8L1; NbExp=3; IntAct=EBI-747754, EBI-21574901; P28799; Q9H6S3: EPS8L2; NbExp=3; IntAct=EBI-747754, EBI-3940939; P28799; O15540: FABP7; NbExp=3; IntAct=EBI-747754, EBI-10697159; P28799; Q9UNN5: FAF1; NbExp=3; IntAct=EBI-747754, EBI-718246; P28799; Q6SJ93: FAM111B; NbExp=3; IntAct=EBI-747754, EBI-6309082; P28799; Q96AQ9: FAM131C; NbExp=4; IntAct=EBI-747754, EBI-741921; P28799; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-747754, EBI-10247271; P28799; Q5HYJ3-3: FAM76B; NbExp=6; IntAct=EBI-747754, EBI-11956087; P28799; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-747754, EBI-5461838; P28799; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-747754, EBI-8468186; P28799; Q9NW38: FANCL; NbExp=3; IntAct=EBI-747754, EBI-2339898; P28799; Q53R41: FASTKD1; NbExp=3; IntAct=EBI-747754, EBI-3957005; P28799; Q8NFZ0: FBH1; NbExp=3; IntAct=EBI-747754, EBI-724767; P28799; Q9UBX5: FBLN5; NbExp=3; IntAct=EBI-747754, EBI-947897; P28799; P15976-2: GATA1; NbExp=3; IntAct=EBI-747754, EBI-9090198; P28799; P23769-2: GATA2; NbExp=3; IntAct=EBI-747754, EBI-21856389; P28799; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-747754, EBI-8799578; P28799; P10075: GLI4; NbExp=3; IntAct=EBI-747754, EBI-14061927; P28799; O76003: GLRX3; NbExp=9; IntAct=EBI-747754, EBI-374781; P28799; Q9Y223-2: GNE; NbExp=6; IntAct=EBI-747754, EBI-11975289; P28799; Q9HBQ8: GOLGA2P5; NbExp=3; IntAct=EBI-747754, EBI-22000587; P28799; Q7Z602: GPR141; NbExp=3; IntAct=EBI-747754, EBI-21649723; P28799; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-747754, EBI-347538; P28799; O75409: H2AP; NbExp=3; IntAct=EBI-747754, EBI-6447217; P28799; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-747754, EBI-2868501; P28799; P68431: H3C12; NbExp=3; IntAct=EBI-747754, EBI-79722; P28799; A8K0U2: hCG_2001421; NbExp=3; IntAct=EBI-747754, EBI-25843825; P28799; Q03014: HHEX; NbExp=3; IntAct=EBI-747754, EBI-747421; P28799; P49639: HOXA1; NbExp=18; IntAct=EBI-747754, EBI-740785; P28799; P09017: HOXC4; NbExp=3; IntAct=EBI-747754, EBI-3923226; P28799; P22692: IGFBP4; NbExp=3; IntAct=EBI-747754, EBI-2831948; P28799; Q14005-2: IL16; NbExp=3; IntAct=EBI-747754, EBI-17178971; P28799; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-747754, EBI-743980; P28799; Q9UNL4: ING4; NbExp=3; IntAct=EBI-747754, EBI-2866661; P28799; Q8IXL9: IQCF2; NbExp=3; IntAct=EBI-747754, EBI-10238842; P28799; Q9Y6F6-3: IRAG1; NbExp=3; IntAct=EBI-747754, EBI-25840037; P28799; Q86U28: ISCA2; NbExp=3; IntAct=EBI-747754, EBI-10258659; P28799; Q14145: KEAP1; NbExp=3; IntAct=EBI-747754, EBI-751001; P28799; Q12756: KIF1A; NbExp=3; IntAct=EBI-747754, EBI-2679809; P28799; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-747754, EBI-2796400; P28799; P57682: KLF3; NbExp=4; IntAct=EBI-747754, EBI-8472267; P28799; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-747754, EBI-714379; P28799; O76011: KRT34; NbExp=3; IntAct=EBI-747754, EBI-1047093; P28799; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-747754, EBI-11959885; P28799; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-747754, EBI-11741292; P28799; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-747754, EBI-10172290; P28799; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-747754, EBI-10171774; P28799; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-747754, EBI-1052037; P28799; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-747754, EBI-10210845; P28799; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-747754, EBI-11953846; P28799; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-747754, EBI-10241252; P28799; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-747754, EBI-11992140; P28799; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-747754, EBI-10241353; P28799; Q6PEX3: KRTAP26-1; NbExp=8; IntAct=EBI-747754, EBI-3957672; P28799; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-747754, EBI-3958099; P28799; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-747754, EBI-12111050; P28799; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-747754, EBI-11962084; P28799; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-747754, EBI-10261141; P28799; Q14847-2: LASP1; NbExp=3; IntAct=EBI-747754, EBI-9088686; P28799; O95447: LCA5L; NbExp=3; IntAct=EBI-747754, EBI-8473670; P28799; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-747754, EBI-11962058; P28799; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-747754, EBI-10245913; P28799; Q5T752: LCE1D; NbExp=3; IntAct=EBI-747754, EBI-11741311; P28799; Q5T753: LCE1E; NbExp=3; IntAct=EBI-747754, EBI-11955335; P28799; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-747754, EBI-10246607; P28799; O14633: LCE2B; NbExp=3; IntAct=EBI-747754, EBI-11478468; P28799; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-747754, EBI-10246750; P28799; Q5T5A8: LCE3C; NbExp=3; IntAct=EBI-747754, EBI-10245291; P28799; Q5T5B0: LCE3E; NbExp=3; IntAct=EBI-747754, EBI-10245456; P28799; Q5TA78: LCE4A; NbExp=4; IntAct=EBI-747754, EBI-10246358; P28799; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-747754, EBI-10258746; P28799; Q68G74: LHX8; NbExp=3; IntAct=EBI-747754, EBI-8474075; P28799; A2RU56: LOC401296; NbExp=3; IntAct=EBI-747754, EBI-9088215; P28799; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-747754, EBI-749562; P28799; Q14693: LPIN1; NbExp=3; IntAct=EBI-747754, EBI-5278370; P28799; Q6Q4G3-4: LVRN; NbExp=3; IntAct=EBI-747754, EBI-25862057; P28799; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-747754, EBI-12056869; P28799; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-747754, EBI-373144; P28799; Q99683: MAP3K5; NbExp=3; IntAct=EBI-747754, EBI-476263; P28799; P61244-4: MAX; NbExp=3; IntAct=EBI-747754, EBI-25848049; P28799; O95243-2: MBD4; NbExp=3; IntAct=EBI-747754, EBI-6448717; P28799; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-747754, EBI-16439278; P28799; P41218: MNDA; NbExp=3; IntAct=EBI-747754, EBI-2829677; P28799; Q86VF5-3: MOGAT3; NbExp=3; IntAct=EBI-747754, EBI-25840143; P28799; Q9Y2R5: MRPS17; NbExp=3; IntAct=EBI-747754, EBI-1046443; P28799; O43196-4: MSH5; NbExp=3; IntAct=EBI-747754, EBI-25860238; P28799; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-747754, EBI-10699187; P28799; Q96A32: MYL11; NbExp=3; IntAct=EBI-747754, EBI-1390771; P28799; Q9NPC7: MYNN; NbExp=3; IntAct=EBI-747754, EBI-3446748; P28799; O15069: NACAD; NbExp=3; IntAct=EBI-747754, EBI-7108375; P28799; Q99608: NDN; NbExp=3; IntAct=EBI-747754, EBI-718177; P28799; Q9P032: NDUFAF4; NbExp=3; IntAct=EBI-747754, EBI-2606839; P28799; Q12986: NFX1; NbExp=3; IntAct=EBI-747754, EBI-2130062; P28799; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-747754, EBI-718372; P28799; Q9UBE8: NLK; NbExp=7; IntAct=EBI-747754, EBI-366978; P28799; Q96AM0: NLRP1; NbExp=3; IntAct=EBI-747754, EBI-25860999; P28799; Q6IAD4: NOTCH1; NbExp=3; IntAct=EBI-747754, EBI-25860267; P28799; Q14995: NR1D2; NbExp=3; IntAct=EBI-747754, EBI-6144053; P28799; Q7Z417: NUFIP2; NbExp=10; IntAct=EBI-747754, EBI-1210753; P28799; O43482: OIP5; NbExp=3; IntAct=EBI-747754, EBI-536879; P28799; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-747754, EBI-1058491; P28799; P32242: OTX1; NbExp=10; IntAct=EBI-747754, EBI-740446; P28799; Q15077: P2RY6; NbExp=3; IntAct=EBI-747754, EBI-10235794; P28799; P07237: P4HB; NbExp=4; IntAct=EBI-747754, EBI-395883; P28799; O75781-2: PALM; NbExp=3; IntAct=EBI-747754, EBI-16399860; P28799; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-747754, EBI-17159452; P28799; Q86SE9-2: PCGF5; NbExp=3; IntAct=EBI-747754, EBI-25861637; P28799; O15534: PER1; NbExp=3; IntAct=EBI-747754, EBI-2557276; P28799; Q96FX8: PERP; NbExp=3; IntAct=EBI-747754, EBI-17183069; P28799; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-747754, EBI-12339509; P28799; Q9BWX1: PHF7; NbExp=3; IntAct=EBI-747754, EBI-4307517; P28799; A2BDE7: PHLDA1; NbExp=3; IntAct=EBI-747754, EBI-14084211; P28799; O75925: PIAS1; NbExp=3; IntAct=EBI-747754, EBI-629434; P28799; Q9BZM1: PLA2G12A; NbExp=3; IntAct=EBI-747754, EBI-3916751; P28799; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-747754, EBI-21503705; P28799; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-747754, EBI-12891828; P28799; Q9Y342: PLLP; NbExp=3; IntAct=EBI-747754, EBI-3919291; P28799; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-747754, EBI-18063495; P28799; Q9H1D9: POLR3F; NbExp=3; IntAct=EBI-747754, EBI-710067; P28799; Q12837: POU4F2; NbExp=6; IntAct=EBI-747754, EBI-17236143; P28799; P09565: PP9974; NbExp=3; IntAct=EBI-747754, EBI-10196507; P28799; P54646: PRKAA2; NbExp=3; IntAct=EBI-747754, EBI-1383852; P28799; O43741: PRKAB2; NbExp=4; IntAct=EBI-747754, EBI-1053424; P28799; P11908: PRPS2; NbExp=3; IntAct=EBI-747754, EBI-4290895; P28799; P07602: PSAP; NbExp=5; IntAct=EBI-747754, EBI-716699; P28799; P40306: PSMB10; NbExp=3; IntAct=EBI-747754, EBI-603329; P28799; P28062-2: PSMB8; NbExp=3; IntAct=EBI-747754, EBI-372312; P28799; Q8TBK9: PTMA; NbExp=3; IntAct=EBI-747754, EBI-1056327; P28799; Q8WUK0: PTPMT1; NbExp=3; IntAct=EBI-747754, EBI-7199479; P28799; Q14671: PUM1; NbExp=3; IntAct=EBI-747754, EBI-948453; P28799; Q7Z7K5: PXN; NbExp=3; IntAct=EBI-747754, EBI-25841978; P28799; P47897: QARS1; NbExp=3; IntAct=EBI-747754, EBI-347462; P28799; Q96PK6: RBM14; NbExp=3; IntAct=EBI-747754, EBI-954272; P28799; Q96PM5-4: RCHY1; NbExp=3; IntAct=EBI-747754, EBI-21252376; P28799; Q8TCX5: RHPN1; NbExp=3; IntAct=EBI-747754, EBI-746325; P28799; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-747754, EBI-25829984; P28799; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-747754, EBI-749039; P28799; Q9UBS8: RNF14; NbExp=3; IntAct=EBI-747754, EBI-2130308; P28799; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-747754, EBI-751555; P28799; P62244: RPS15A; NbExp=3; IntAct=EBI-747754, EBI-347895; P28799; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-747754, EBI-10248967; P28799; Q8N488: RYBP; NbExp=3; IntAct=EBI-747754, EBI-752324; P28799; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-747754, EBI-4403649; P28799; P34741: SDC2; NbExp=3; IntAct=EBI-747754, EBI-1172957; P28799; P60896: SEM1; NbExp=3; IntAct=EBI-747754, EBI-79819; P28799; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-747754, EBI-9089805; P28799; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-747754, EBI-745901; P28799; Q13530: SERINC3; NbExp=3; IntAct=EBI-747754, EBI-1045571; P28799; O43765: SGTA; NbExp=7; IntAct=EBI-747754, EBI-347996; P28799; Q9NUL5-3: SHFL; NbExp=3; IntAct=EBI-747754, EBI-22000547; P28799; O60902-3: SHOX2; NbExp=3; IntAct=EBI-747754, EBI-9092164; P28799; Q9GZS3: SKIC8; NbExp=3; IntAct=EBI-747754, EBI-358545; P28799; O15198-2: SMAD9; NbExp=3; IntAct=EBI-747754, EBI-12273450; P28799; P49901: SMCP; NbExp=3; IntAct=EBI-747754, EBI-750494; P28799; Q9HCE7-2: SMURF1; NbExp=3; IntAct=EBI-747754, EBI-9845742; P28799; Q96DI7: SNRNP40; NbExp=3; IntAct=EBI-747754, EBI-538492; P28799; Q99523: SORT1; NbExp=3; IntAct=EBI-747754, EBI-1057058; P28799; A0A024R4B0: SPATA3; NbExp=3; IntAct=EBI-747754, EBI-14123856; P28799; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-747754, EBI-8635958; P28799; P20155: SPINK2; NbExp=3; IntAct=EBI-747754, EBI-10200479; P28799; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-747754, EBI-10174456; P28799; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-747754, EBI-7082156; P28799; O43597: SPRY2; NbExp=3; IntAct=EBI-747754, EBI-742487; P28799; Q9C004: SPRY4; NbExp=3; IntAct=EBI-747754, EBI-354861; P28799; Q6PJ21: SPSB3; NbExp=3; IntAct=EBI-747754, EBI-3937206; P28799; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-747754, EBI-357085; P28799; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-747754, EBI-723091; P28799; Q17RD7-3: SYT16; NbExp=3; IntAct=EBI-747754, EBI-25861603; P28799; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-747754, EBI-745958; P28799; P17735: TAT; NbExp=3; IntAct=EBI-747754, EBI-12046643; P28799; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-747754, EBI-529518; P28799; P62380: TBPL1; NbExp=3; IntAct=EBI-747754, EBI-716225; P28799; Q8IYN2: TCEAL8; NbExp=3; IntAct=EBI-747754, EBI-2116184; P28799; Q13569: TDG; NbExp=3; IntAct=EBI-747754, EBI-348333; P28799; P28347-2: TEAD1; NbExp=3; IntAct=EBI-747754, EBI-12151837; P28799; Q8NA77: TEX19; NbExp=3; IntAct=EBI-747754, EBI-13323487; P28799; O60830: TIMM17B; NbExp=3; IntAct=EBI-747754, EBI-2372529; P28799; Q04724: TLE1; NbExp=3; IntAct=EBI-747754, EBI-711424; P28799; Q08117-2: TLE5; NbExp=3; IntAct=EBI-747754, EBI-11741437; P28799; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-747754, EBI-25830583; P28799; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-747754, EBI-10242677; P28799; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-747754, EBI-25831574; P28799; P19438: TNFRSF1A; NbExp=4; IntAct=EBI-747754, EBI-299451; P28799; P20333: TNFRSF1B; NbExp=5; IntAct=EBI-747754, EBI-358983; P28799; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-747754, EBI-17716262; P28799; Q9BVS5: TRMT61B; NbExp=3; IntAct=EBI-747754, EBI-3197877; P28799; Q96Q11-3: TRNT1; NbExp=3; IntAct=EBI-747754, EBI-25861172; P28799; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-747754, EBI-739485; P28799; O14817: TSPAN4; NbExp=3; IntAct=EBI-747754, EBI-8652667; P28799; A0A024RCB9: TSSC4; NbExp=3; IntAct=EBI-747754, EBI-25860845; P28799; Q99614: TTC1; NbExp=3; IntAct=EBI-747754, EBI-742074; P28799; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-747754, EBI-9090990; P28799; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-747754, EBI-9088812; P28799; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-747754, EBI-5457544; P28799; Q6EMK4: VASN; NbExp=3; IntAct=EBI-747754, EBI-10249550; P28799; P45880: VDAC2; NbExp=3; IntAct=EBI-747754, EBI-354022; P28799; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-747754, EBI-2850578; P28799; Q8NEZ2-2: VPS37A; NbExp=3; IntAct=EBI-747754, EBI-10270911; P28799; P58304: VSX2; NbExp=3; IntAct=EBI-747754, EBI-6427899; P28799; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-747754, EBI-12040603; P28799; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-747754, EBI-12111538; P28799; O95070: YIF1A; NbExp=3; IntAct=EBI-747754, EBI-2799703; P28799; P25490: YY1; NbExp=4; IntAct=EBI-747754, EBI-765538; P28799; O43167-2: ZBTB24; NbExp=3; IntAct=EBI-747754, EBI-25842419; P28799; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-747754, EBI-711679; P28799; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-747754, EBI-2602314; P28799; Q15973: ZNF124; NbExp=3; IntAct=EBI-747754, EBI-2555767; P28799; P52744: ZNF138; NbExp=3; IntAct=EBI-747754, EBI-10746567; P28799; Q9UJW8-4: ZNF180; NbExp=3; IntAct=EBI-747754, EBI-12055755; P28799; Q16600: ZNF239; NbExp=3; IntAct=EBI-747754, EBI-8787052; P28799; Q8WUU4: ZNF296; NbExp=3; IntAct=EBI-747754, EBI-8834821; P28799; Q8N895: ZNF366; NbExp=3; IntAct=EBI-747754, EBI-2813661; P28799; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-747754, EBI-12010736; P28799; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-747754, EBI-25831733; P28799; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-747754, EBI-10486136; P28799; Q96C55: ZNF524; NbExp=3; IntAct=EBI-747754, EBI-10283126; P28799; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-747754, EBI-8490788; P28799; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-747754, EBI-10172590; P28799; Q96I27-2: ZNF625; NbExp=3; IntAct=EBI-747754, EBI-12038525; P28799; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-747754, EBI-12939666; P28799; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-747754, EBI-745276; P28799; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-747754, EBI-11090299; P28799; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-747754, EBI-25845217; P28799; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-747754, EBI-10251462; P28799; Q3KP31: ZNF791; NbExp=3; IntAct=EBI-747754, EBI-2849119; P28799; Q16670: ZSCAN26; NbExp=3; IntAct=EBI-747754, EBI-3920053; P28799; O15535: ZSCAN9; NbExp=3; IntAct=EBI-747754, EBI-751531; P28799; A0A384ME25; NbExp=3; IntAct=EBI-747754, EBI-10211777; P28799; Q7L8T7; NbExp=3; IntAct=EBI-747754, EBI-25831943; P28799; Q7Z783; NbExp=3; IntAct=EBI-747754, EBI-9088990; P28799; P09022: Hoxa1; Xeno; NbExp=2; IntAct=EBI-747754, EBI-3957603; P28799-2; D3DTF8: APLN; NbExp=3; IntAct=EBI-25860013, EBI-22002556; P28799-2; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-25860013, EBI-718459; P28799-2; A0A024R9H7: CCDC26; NbExp=3; IntAct=EBI-25860013, EBI-10271580; P28799-2; P50750-2: CDK9; NbExp=3; IntAct=EBI-25860013, EBI-12029902; P28799-2; Q02930-3: CREB5; NbExp=3; IntAct=EBI-25860013, EBI-10192698; P28799-2; P80370: DLK1; NbExp=3; IntAct=EBI-25860013, EBI-21555397; P28799-2; O14531: DPYSL4; NbExp=3; IntAct=EBI-25860013, EBI-719542; P28799-2; Q92997: DVL3; NbExp=3; IntAct=EBI-25860013, EBI-739789; P28799-2; O15540: FABP7; NbExp=3; IntAct=EBI-25860013, EBI-10697159; P28799-2; Q96AQ9: FAM131C; NbExp=3; IntAct=EBI-25860013, EBI-741921; P28799-2; Q5HYJ3-3: FAM76B; NbExp=3; IntAct=EBI-25860013, EBI-11956087; P28799-2; Q8N7T0: hCG_1820408; NbExp=3; IntAct=EBI-25860013, EBI-25858908; P28799-2; P49639: HOXA1; NbExp=3; IntAct=EBI-25860013, EBI-740785; P28799-2; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-25860013, EBI-10246607; P28799-2; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-25860013, EBI-10699187; P28799-2; Q14995: NR1D2; NbExp=3; IntAct=EBI-25860013, EBI-6144053; P28799-2; P09565: PP9974; NbExp=3; IntAct=EBI-25860013, EBI-10196507; P28799-2; Q14671: PUM1; NbExp=3; IntAct=EBI-25860013, EBI-948453; P28799-2; Q7Z7K5: PXN; NbExp=3; IntAct=EBI-25860013, EBI-25841978; P28799-2; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-25860013, EBI-4403649; P28799-2; P34741: SDC2; NbExp=3; IntAct=EBI-25860013, EBI-1172957; P28799-2; Q9NTG7: SIRT3; NbExp=3; IntAct=EBI-25860013, EBI-724621; P28799-2; O95416: SOX14; NbExp=3; IntAct=EBI-25860013, EBI-9087806; P28799-2; A0A024R4B0: SPATA3; NbExp=3; IntAct=EBI-25860013, EBI-14123856; P28799-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25860013, EBI-5235340; P28799-2; P17735: TAT; NbExp=3; IntAct=EBI-25860013, EBI-12046643; P28799-2; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-25860013, EBI-3923210; P28799-2; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-25860013, EBI-25831574; P28799-2; Q9Y2B4: TP53TG5; NbExp=3; IntAct=EBI-25860013, EBI-21870909; P28799-2; P25490: YY1; NbExp=3; IntAct=EBI-25860013, EBI-765538; P28799-2; Q9C0A1: ZFHX2; NbExp=3; IntAct=EBI-25860013, EBI-25850811; P28799-2; Q9UJW8-4: ZNF180; NbExp=3; IntAct=EBI-25860013, EBI-12055755; P28799-2; Q8N895: ZNF366; NbExp=3; IntAct=EBI-25860013, EBI-2813661; P28799-2; A0A087WZY1; NbExp=3; IntAct=EBI-25860013, EBI-13387614; P28799-2; Q7L8T7; NbExp=3; IntAct=EBI-25860013, EBI-25831943; PRO_0000012695; P07339: CTSD; NbExp=2; IntAct=EBI-21335602, EBI-2115097; PRO_0000012696; P07339: CTSD; NbExp=2; IntAct=EBI-21335615, EBI-2115097; PRO_0000012697; P07339: CTSD; NbExp=2; IntAct=EBI-21335629, EBI-2115097; PRO_0000012698; P07339: CTSD; NbExp=2; IntAct=EBI-21335642, EBI-2115097; PRO_0000012699; P07339: CTSD; NbExp=2; IntAct=EBI-21335656, EBI-2115097; PRO_0000012700; P07339: CTSD; NbExp=2; IntAct=EBI-21335669, EBI-2115097; PRO_0000012701; P07339: CTSD; NbExp=2; IntAct=EBI-21335682, EBI-2115097; Secreted sosome Note=Endocytosed by SORT1 and delivred to lysosomes (PubMed:21092856, PubMed:28073925). Targeted to lysosome by PSAP via M6PR and LRP1, in both biosynthetic and endocytic pathways (PubMed:26370502, PubMed:28073925). Co-localized with GBA1 in the intracellular trafficking compartments until to lysosome (By similarity). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P28799-1; Sequence=Displayed; Name=2; IsoId=P28799-2; Sequence=VSP_001837; Name=3; IsoId=P28799-3; Sequence=VSP_053472, VSP_053473; In myelogenous leukemic cell lines of promonocytic, promyelocytic, and proerythroid lineage, in fibroblasts, and very strongly in epithelial cell lines. Present in inflammatory cells and bone marrow. Highest levels in kidney. Increased in response to lysosome alkalization. Cleaved by ELANE; proteolysis is blocked by SLPI and is concentration- and time-dependent and induces CXCL8/IL-8 production; granulin-3 and granulin-4 are resistant to ELANE (PubMed:12526812, PubMed:28743268). Cleaved by CTSL in lysosome thus regulating the maturation and turnover of progranulin within the lysosome (PubMed:28743268). Ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:607485]: Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease. te=The disease is caused by variants affecting the gene represented in this entry. Ceroid lipofuscinosis, neuronal, 11 (CLN11) [MIM:614706]: A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the granulin family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40757/GRN"; astrocyte activation involved in immune response microglial cell activation involved in immune response RNA binding cytokine activity protein binding extracellular region extracellular space lysosome lysosomal membrane endosome late endosome endoplasmic reticulum Golgi apparatus trans-Golgi network plasma membrane lysosome organization lysosomal transport lysosomal lumen acidification signal transduction growth factor activity positive regulation of endothelial cell migration membrane positive regulation of cell migration azurophil granule lumen neutrophil degranulation negative regulation of neuron apoptotic process positive regulation of neuron apoptotic process positive regulation of angiogenesis positive regulation of axon regeneration positive regulation of epithelial cell proliferation protein stabilization chaperone binding negative regulation of respiratory burst involved in inflammatory response extracellular exosome positive regulation of defense response to bacterium negative regulation of neutrophil activation positive regulation of protein folding negative regulation of microglial cell activation positive regulation of aspartic-type peptidase activity positive regulation of lysosome organization uc002igp.1 uc002igp.2 uc002igp.3 uc002igp.4 
ENST00000054650.9 THAP3 ENST00000054650.9 THAP domain containing 3, transcript variant 7 (from RefSeq NM_001394499.1) ENST00000054650.1 ENST00000054650.2 ENST00000054650.3 ENST00000054650.4 ENST00000054650.5 ENST00000054650.6 ENST00000054650.7 ENST00000054650.8 NM_001394499 Q569K1 Q5TH66 Q5TH67 Q8N8T6 Q8WTV1 Q9BSC7 Q9Y3H2 Q9Y3H3 THAP3_HUMAN uc001aoc.1 uc001aoc.2 uc001aoc.3 uc001aoc.4 uc001aoc.5 Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Component of a THAP1/THAP3-HCFC1-OGT complex that contains at least, either THAP1 or THAP3, HCFC1 and OGT. Interacts directly with OGT and HCFC1 (via its HBM). Q8WTV1; P46379-2: BAG6; NbExp=3; IntAct=EBI-17438286, EBI-10988864; Q8WTV1; P28329-3: CHAT; NbExp=3; IntAct=EBI-17438286, EBI-25837549; Q8WTV1; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-17438286, EBI-12593112; Q8WTV1; O14645: DNALI1; NbExp=3; IntAct=EBI-17438286, EBI-395638; Q8WTV1; P15311: EZR; NbExp=3; IntAct=EBI-17438286, EBI-1056902; Q8WTV1; P22607: FGFR3; NbExp=3; IntAct=EBI-17438286, EBI-348399; Q8WTV1; Q14957: GRIN2C; NbExp=3; IntAct=EBI-17438286, EBI-8285963; Q8WTV1; O14901: KLF11; NbExp=3; IntAct=EBI-17438286, EBI-948266; Q8WTV1; Q13449: LSAMP; NbExp=3; IntAct=EBI-17438286, EBI-4314821; Q8WTV1; P28331-2: NDUFS1; NbExp=3; IntAct=EBI-17438286, EBI-6190702; Q8WTV1; P61970: NUTF2; NbExp=3; IntAct=EBI-17438286, EBI-591778; Q8WTV1; Q16512: PKN1; NbExp=3; IntAct=EBI-17438286, EBI-602382; Q8WTV1; P24928: POLR2A; NbExp=3; IntAct=EBI-17438286, EBI-295301; Q8WTV1; P63000: RAC1; NbExp=3; IntAct=EBI-17438286, EBI-413628; Q8WTV1; P14678-2: SNRPB; NbExp=3; IntAct=EBI-17438286, EBI-372475; Q8WTV1; Q13148: TARDBP; NbExp=6; IntAct=EBI-17438286, EBI-372899; Q8WTV1; P14679-2: TYR; NbExp=3; IntAct=EBI-17438286, EBI-25894402; Q8WTV1; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-17438286, EBI-607755; Q8WTV1; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-17438286, EBI-741480; Q8WTV1; P14927: UQCRB; NbExp=3; IntAct=EBI-17438286, EBI-743128; Q8WTV1; P31930: UQCRC1; NbExp=3; IntAct=EBI-17438286, EBI-1052596; Q8WTV1; P61758: VBP1; NbExp=3; IntAct=EBI-17438286, EBI-357430; Q8WTV1; Q9Y649; NbExp=3; IntAct=EBI-17438286, EBI-25900580; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q8WTV1-1; Sequence=Displayed; Name=2; IsoId=Q8WTV1-3; Sequence=VSP_015136; Name=3; IsoId=Q8WTV1-4; Sequence=VSP_015137, VSP_015138, VSP_015139; Highly expressed in heart, skeletal muscle and placenta. Weaker expression in brain, kidney and liver. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding nucleic acid binding DNA binding protein binding regulation of transcription from RNA polymerase II promoter metal ion binding uc001aoc.1 uc001aoc.2 uc001aoc.3 uc001aoc.4 uc001aoc.5 
ENST00000054666.11 VAMP3 ENST00000054666.11 vesicle associated membrane protein 3 (from RefSeq NM_004781.4) ENST00000054666.1 ENST00000054666.10 ENST00000054666.2 ENST00000054666.3 ENST00000054666.4 ENST00000054666.5 ENST00000054666.6 ENST00000054666.7 ENST00000054666.8 ENST00000054666.9 NM_004781 Q6FGG2 Q6FGG2_HUMAN VAMP3 hCG_21813 uc001aol.1 uc001aol.2 uc001aol.3 uc001aol.4 Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.201507.1, SRR3476690.404792.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000054666.11/ ENSP00000054666.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. Early endosome membrane ; Single-pass type IV membrane protein Endosome membrane ; Single-pass type I membrane protein Endosome membrane ; Single-pass type IV membrane protein Membrane ; Single-pass type I membrane protein Membrane ; Single-pass type IV membrane protein Recycling endosome membrane ; Single-pass type I membrane protein Synapse, synaptosome Belongs to the synaptobrevin family. SNARE binding positive regulation of receptor recycling cytosol plasma membrane cell surface membrane integral component of membrane vesicle-mediated transport apical plasma membrane syntaxin-1 binding calcium ion regulated exocytosis secretory granule integral component of synaptic vesicle membrane clathrin-coated vesicle membrane SNARE complex cytoplasmic vesicle substrate adhesion-dependent cell spreading SNARE complex assembly Golgi to plasma membrane protein transport intracellular organelle intracellular membrane-bounded organelle phagocytic vesicle perinuclear region of cytoplasm recycling endosome macromolecular complex assembly cellular response to interferon-gamma uc001aol.1 uc001aol.2 uc001aol.3 uc001aol.4 
ENST00000054950.4 RCN1 ENST00000054950.4 reticulocalbin 1 (from RefSeq NM_002901.4) ENST00000054950.1 ENST00000054950.2 ENST00000054950.3 HEL-S-84 NM_002901 V9HW95 V9HW95_HUMAN uc010reb.1 uc010reb.2 uc010reb.3 uc010reb.4 Reticulocalbin 1 is a calcium-binding protein located in the lumen of the ER. The protein contains six conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand. High conservation of amino acid residues outside of these motifs, in comparison to mouse reticulocalbin, is consistent with a possible biochemical function besides that of calcium binding. In human endothelial and prostate cancer cell lines this protein localizes to the plasma membrane.[provided by RefSeq, Jan 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK129791.1, FJ224346.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000054950.4/ ENSP00000054950.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Belongs to the CREC family. calcium ion binding endoplasmic reticulum uc010reb.1 uc010reb.2 uc010reb.3 uc010reb.4 
ENST00000055077.8 RFC2 ENST00000055077.8 replication factor C subunit 2, transcript variant 1 (from RefSeq NM_181471.3) B5BU07 D3DXG3 ENST00000055077.1 ENST00000055077.2 ENST00000055077.3 ENST00000055077.4 ENST00000055077.5 ENST00000055077.6 ENST00000055077.7 NM_181471 P32846 P35250 Q9BU93 RFC2_HUMAN uc003uaj.1 uc003uaj.2 uc003uaj.3 uc003uaj.4 uc003uaj.5 uc003uaj.6 This gene encodes a member of the activator 1 small subunits family. The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins, proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). Replication factor C, also called activator 1, is a protein complex consisting of five distinct subunits. This gene encodes the 40 kD subunit, which has been shown to be responsible for binding ATP and may help promote cell survival. Disruption of this gene is associated with Williams syndrome. Alternatively spliced transcript variants encoding distinct isoforms have been described. A pseudogene of this gene has been defined on chromosome 2. [provided by RefSeq, Jul 2013]. The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit binds ATP (By similarity). Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA. RFC2 also interacts with PRKAR1A; the complex may be involved in cell survival (PubMed:15655353). Interacts with DDX11 (PubMed:18499658). P35250; P10644: PRKAR1A; NbExp=7; IntAct=EBI-476409, EBI-476431; P35250; P35251: RFC1; NbExp=4; IntAct=EBI-476409, EBI-476616; P35250; P35249: RFC4; NbExp=8; IntAct=EBI-476409, EBI-476655; P35250-2; O14964: HGS; NbExp=3; IntAct=EBI-12936957, EBI-740220; P35250-2; P25786: PSMA1; NbExp=3; IntAct=EBI-12936957, EBI-359352; P35250-2; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-12936957, EBI-2510804; P35250-2; Q15915: ZIC1; NbExp=3; IntAct=EBI-12936957, EBI-11963196; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P35250-1; Sequence=Displayed; Name=2; IsoId=P35250-2; Sequence=VSP_005660; Note=RFC2 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region (PubMed:11003705). Belongs to the activator 1 small subunits family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rfc2/"; nucleotide binding DNA binding protein binding ATP binding nucleus nucleoplasm DNA replication factor C complex DNA replication DNA-dependent DNA replication transcription-coupled nucleotide-excision repair nucleotide-excision repair, DNA incision, 5'-to lesion nucleotide-excision repair, DNA gap filling enzyme binding translesion synthesis Ctf18 RFC-like complex telomere maintenance via semi-conservative replication DNA duplex unwinding nucleotide-excision repair, DNA incision error-prone translesion synthesis DNA damage response, detection of DNA damage error-free translesion synthesis positive regulation of DNA-directed DNA polymerase activity regulation of signal transduction by p53 class mediator DNA clamp loader activity single-stranded DNA-dependent ATP-dependent DNA helicase activity uc003uaj.1 uc003uaj.2 uc003uaj.3 uc003uaj.4 uc003uaj.5 uc003uaj.6 
ENST00000055335.11 PPP1R3F ENST00000055335.11 protein phosphatase 1 regulatory subunit 3F, transcript variant 1 (from RefSeq NM_033215.5) A2VDJ8 B3KPW2 E9PCM3 ENST00000055335.1 ENST00000055335.10 ENST00000055335.2 ENST00000055335.3 ENST00000055335.4 ENST00000055335.5 ENST00000055335.6 ENST00000055335.7 ENST00000055335.8 ENST00000055335.9 NM_033215 PPR3F_HUMAN Q6ZSY5 uc004dnh.1 uc004dnh.2 uc004dnh.3 uc004dnh.4 This gene encodes a protein that has been identified as one of several type-1 protein phosphatase (PP1) regulatory subunits. One or two of these subunits, together with the well-conserved catalytic subunit, can form the PP1 holoenzyme, where the regulatory subunit functions to regulate substrate specificity and/or targeting to a particular cellular compartment. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2010]. Glycogen-targeting subunit for protein phosphatase 1 (PP1). Membrane ; Single-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6ZSY5-1; Sequence=Displayed; Name=2; IsoId=Q6ZSY5-2; Sequence=VSP_045003, VSP_045004; Expressed in brain, skeletal muscle and heart. Sequence=AAI31589.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=BAG51824.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; regulation of glycogen biosynthetic process membrane integral component of membrane protein phosphatase binding regulation of glycogen (starch) synthase activity glycogen binding uc004dnh.1 uc004dnh.2 uc004dnh.3 uc004dnh.4 
ENST00000055682.12 NEXMIF ENST00000055682.12 neurite extension and migration factor (from RefSeq NM_001008537.3) A7YY87 ENST00000055682.1 ENST00000055682.10 ENST00000055682.11 ENST00000055682.2 ENST00000055682.3 ENST00000055682.4 ENST00000055682.5 ENST00000055682.6 ENST00000055682.7 ENST00000055682.8 ENST00000055682.9 KIAA2022 NEXMIF NEXMI_HUMAN NM_001008537 Q5JUX9 Q5QGS0 Q8IVE9 uc004eby.1 uc004eby.2 uc004eby.3 uc004eby.4 uc004eby.5 uc004eby.6 An inversion on the X chromosome which disrupts this gene and a G-protein coupled purinergic receptor gene located in the pseudoautosomal region of the X chromosome has been linked to X linked cognitive disability.[provided by RefSeq, Mar 2009]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY563507.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2152798, SAMEA2155984 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000055682.12/ ENSP00000055682.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Involved in neurite outgrowth by regulating cell-cell adhesion via the N-cadherin signaling pathway. May act by regulating expression of protein-coding genes, such as N-cadherins and integrin beta-1 (ITGB1). Nucleus Cytoplasm Highly expressed in fetal and adult brain, predominantly in the cerebral cortex and the cerebellum. Also expressed in other tissues but to a lesser extent. Intellectual developmental disorder, X-linked 98 (XLID98) [MIM:300912]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. XLID98 patients show delayed psychomotor development, absent or poor speech development, and postnatal growth retardation, often with microcephaly. Some patients show autistic behavioral features, such as stereotypic hand movements and repetitive behaviors. Additional, more variable features include spasticity, axial hypotonia, seizures, drooling, gastroesophageal reflux, and lack of sphincter control. te=The disease is caused by variants affecting the gene represented in this entry. A chromosomal aberration involving NEXMIF is found in patients with severe intellectual disability. Pericentric inversion inv(X)(p22.3;q13.2) with P2RY8 leading to inactivation of NEXMIF (PubMed:15466006). XLID98 transmission pattern is consistent with X- linked recessive inheritance (PubMed:23615299). In some cases, de novo heterozygous loss-of-function mutations have been found in affected females, while some female carriers are asymptomatic (PubMed:26576034, PubMed:27358180, PubMed:27568816). The female phenotype partially overlaps with the reported male phenotype but includes epilepsy as a relevant feature. The variability of disease manifestation in female carriers is probably due to skewed X inactivation with differential expression in the brain (PubMed:26576034, PubMed:27358180, PubMed:27568816). Sequence=BAC23118.1; Type=Erroneous initiation; Evidence=; negative regulation of cell-matrix adhesion nucleus cytoplasm multicellular organism development nervous system development negative regulation of cell adhesion mediated by integrin negative regulation of cell-cell adhesion mediated by cadherin negative regulation of neuron migration uc004eby.1 uc004eby.2 uc004eby.3 uc004eby.4 uc004eby.5 uc004eby.6 
ENST00000056217.10 ARHGEF5 ENST00000056217.10 Rho guanine nucleotide exchange factor 5 (from RefSeq NM_005435.4) A6NNJ2 ARHG5_HUMAN ENST00000056217.1 ENST00000056217.2 ENST00000056217.3 ENST00000056217.4 ENST00000056217.5 ENST00000056217.6 ENST00000056217.7 ENST00000056217.8 ENST00000056217.9 NM_005435 Q12774 Q6ZML7 TIM uc003wel.1 uc003wel.2 uc003wel.3 uc003wel.4 uc003wel.5 Rho GTPases play a fundamental role in numerous cellular processes initiated by extracellular stimuli that work through G protein coupled receptors. The encoded protein may form a complex with G proteins and stimulate Rho-dependent signals. This protein may be involved in the control of cytoskeletal organization. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK160365.1, BC136661.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1968189 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000056217.10/ ENSP00000056217.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Guanine nucleotide exchange factor which activates Rho GTPases (PubMed:15601624). Strongly activates RHOA (PubMed:15601624). Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1 (By similarity). Involved in regulation of cell shape and actin cytoskeletal organization (PubMed:15601624). Plays a role in actin organization by generating a loss of actin stress fibers and the formation of membrane ruffles and filopodia (PubMed:14662653). Required for SRC-induced podosome formation (By similarity). Involved in positive regulation of immature dendritic cell migration (By similarity). Interacts with SRC (By similarity). Forms a ternary complex with SRC and the PI3K 85 kDa subunit (By similarity). Interacts with and is activated by the heterodimer formed by GNB1 and GNG2 (By similarity). Interacts with ODAM (via C-terminus) (PubMed:25911094). Interacts with RHOA (By similarity). Q12774; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-602199, EBI-739580; Q12774; Q9Y2V7: COG6; NbExp=5; IntAct=EBI-602199, EBI-3866319; Q12774; Q5JST6: EFHC2; NbExp=6; IntAct=EBI-602199, EBI-2349927; Q12774; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-602199, EBI-6255981; Q12774; P62993: GRB2; NbExp=7; IntAct=EBI-602199, EBI-401755; Q12774; O75031: HSF2BP; NbExp=3; IntAct=EBI-602199, EBI-7116203; Q12774; Q96EW2: HSPBAP1; NbExp=6; IntAct=EBI-602199, EBI-720457; Q12774; P25791-3: LMO2; NbExp=3; IntAct=EBI-602199, EBI-11959475; Q12774; Q96KN4: LRATD1; NbExp=5; IntAct=EBI-602199, EBI-11477916; Q12774; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-602199, EBI-11323212; Q12774; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-602199, EBI-10172526; Q12774; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-602199, EBI-79165; Q12774; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-602199, EBI-949255; Q12774; O15160: POLR1C; NbExp=5; IntAct=EBI-602199, EBI-1055079; Q12774; P61586: RHOA; NbExp=2; IntAct=EBI-602199, EBI-446668; Q12774; P31947: SFN; NbExp=4; IntAct=EBI-602199, EBI-476295; Q12774; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-602199, EBI-10269374; Q12774; Q9NVG8: TBC1D13; NbExp=6; IntAct=EBI-602199, EBI-12264956; Q12774; P15884-3: TCF4; NbExp=3; IntAct=EBI-602199, EBI-13636688; Q12774; P14373: TRIM27; NbExp=6; IntAct=EBI-602199, EBI-719493; Q12774; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-602199, EBI-2130429; Q12774; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-602199, EBI-527853; Cytoplasm cleus Cell projection, podosome Event=Alternative splicing; Named isoforms=2; Comment=A number of additional isoforms are detected in primary breast tumors but not in normal tissues. ; Name=1; IsoId=Q12774-1; Sequence=Displayed; Name=2; IsoId=Q12774-2; Sequence=VSP_035175; Ubiquitously expressed with highest levels in placenta. High levels are also found in colon, kidney, trachea, prostate, liver, pancreas, pituitary gland, thyroid gland and mammary gland. In fetal tissues, expressed at high levels in kidney, lung and liver (PubMed:15601624). Expressed at low levels in lung and heart (PubMed:14662653). The PH domain binds to phosphoinositides and is essential for podosome formation. Activation of SRC induces tyrosine phosphorylation of ARHGEF5. Sequence=BAD18708.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; podosome myeloid dendritic cell chemotaxis guanyl-nucleotide exchange factor activity Rho guanyl-nucleotide exchange factor activity protein binding GTP binding nucleus nucleoplasm cytoplasm cytosol plasma membrane G-protein coupled receptor signaling pathway lipid binding actin cytoskeleton organization cell junction regulation of actin cytoskeleton organization regulation of Rho protein signal transduction intracellular signal transduction cell projection positive regulation of apoptotic process regulation of GTPase activity positive regulation of JUN kinase activity positive regulation of GTPase activity regulation of small GTPase mediated signal transduction positive regulation of sequence-specific DNA binding transcription factor activity regulation of cytoskeleton organization positive regulation of stress fiber assembly positive regulation of podosome assembly cell periphery positive regulation of protein import regulation of ERK1 and ERK2 cascade uc003wel.1 uc003wel.2 uc003wel.3 uc003wel.4 uc003wel.5 
ENST00000056233.4 NFE2L3 ENST00000056233.4 NFE2 like bZIP transcription factor 3 (from RefSeq NM_004289.7) ENST00000056233.1 ENST00000056233.2 ENST00000056233.3 NF2L3_HUMAN NM_004289 NRF3 Q6NUS0 Q7Z498 Q86UJ4 Q86VR5 Q9UQA4 Q9Y4A8 uc003sxq.1 uc003sxq.2 uc003sxq.3 uc003sxq.4 uc003sxq.5 This gene encodes a member of the cap 'n' collar basic-region leucine zipper family of transcription factors. The encoded protein heterodimerizes with small musculoaponeurotic fibrosarcoma factors to bind antioxidant response elements in target genes. This protein is a membrane bound glycoprotein that is targeted to the endoplasmic reticulum and the nuclear envelope. Pseudogenes of this gene are found on chromosomes 16, 17, and 18. [provided by RefSeq, Mar 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC068455.1, AF134891.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000056233.4/ ENSP00000056233.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Activates erythroid-specific, globin gene expression. Heterodimer with MAFG, MAFK and other small MAF proteins that binds to the MAF recognition elements (MARE). Q9Y4A8; Q9ULX9: MAFF; NbExp=3; IntAct=EBI-10890629, EBI-721128; Q9Y4A8; O15525: MAFG; NbExp=5; IntAct=EBI-10890629, EBI-713514; Q9Y4A8; Q16621: NFE2; NbExp=4; IntAct=EBI-10890629, EBI-726369; Nucleus Highly expressed in human placenta and also in B- cell and monocyte cell lines. Low expression in heart, brain, lung, skeletal muscle, kidney and pancreas. Belongs to the bZIP family. CNC subfamily. Sequence=AAP22344.1; Type=Erroneous gene model prediction; Evidence=; Sequence=BAA76288.1; Type=Erroneous initiation; Evidence=; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin transcription regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding transcription coactivator activity protein binding nucleus cytoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter transcription from RNA polymerase II promoter positive regulation of transcription, DNA-templated uc003sxq.1 uc003sxq.2 uc003sxq.3 uc003sxq.4 uc003sxq.5 
ENST00000057513.8 TNIP3 ENST00000057513.8 TNFAIP3 interacting protein 3, transcript variant 1 (from RefSeq NM_024873.6) A1A574 A8K2Z4 ABIN3 B4DVF5 B4E023 ENST00000057513.1 ENST00000057513.2 ENST00000057513.3 ENST00000057513.4 ENST00000057513.5 ENST00000057513.6 ENST00000057513.7 LIND NM_024873 Q96KP6 Q96PQ3 Q9H780 TNIP3 TNIP3_HUMAN uc010ing.1 uc010ing.2 uc010ing.3 uc010ing.4 uc010ing.5 Binds to zinc finger protein TNFAIP3 and inhibits NF-kappa-B activation induced by tumor necrosis factor, Toll-like receptor 4 (TLR4), interleukin-1 and 12-O-tetradecanoylphorbol-13-acetate. Overexpression inhibits NF-kappa-B-dependent gene expression in response to lipopolysaccharide at a level downstream of TRAF6 and upstream of IKBKB. NF-kappa-B inhibition is independent of TNFAIP3 binding. Interacts with TNFAIP3. Interacts with polyubiquitin. Q96KP6; Q86V38: ATN1; NbExp=3; IntAct=EBI-2509913, EBI-11954292; Q96KP6; P48745: CCN3; NbExp=3; IntAct=EBI-2509913, EBI-3904822; Q96KP6; P02489: CRYAA; NbExp=3; IntAct=EBI-2509913, EBI-6875961; Q96KP6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2509913, EBI-3867333; Q96KP6; Q15038: DAZAP2; NbExp=9; IntAct=EBI-2509913, EBI-724310; Q96KP6; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2509913, EBI-10976677; Q96KP6; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2509913, EBI-719941; Q96KP6; P42858: HTT; NbExp=9; IntAct=EBI-2509913, EBI-466029; Q96KP6; Q92876: KLK6; NbExp=3; IntAct=EBI-2509913, EBI-2432309; Q96KP6; O00505: KPNA3; NbExp=3; IntAct=EBI-2509913, EBI-358297; Q96KP6; Q6A162: KRT40; NbExp=4; IntAct=EBI-2509913, EBI-10171697; Q96KP6; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2509913, EBI-10171774; Q96KP6; Q99732: LITAF; NbExp=3; IntAct=EBI-2509913, EBI-725647; Q96KP6; P02545: LMNA; NbExp=3; IntAct=EBI-2509913, EBI-351935; Q96KP6; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-2509913, EBI-741037; Q96KP6; P43356: MAGEA2B; NbExp=3; IntAct=EBI-2509913, EBI-5650739; Q96KP6; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2509913, EBI-11522433; Q96KP6; P35240: NF2; NbExp=3; IntAct=EBI-2509913, EBI-1014472; Q96KP6; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2509913, EBI-945833; Q96KP6; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2509913, EBI-22310682; Q96KP6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2509913, EBI-741158; Q96KP6; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2509913, EBI-14066006; Q96KP6; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-2509913, EBI-750734; Q96KP6; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2509913, EBI-25882629; Q96KP6; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2509913, EBI-5235340; Q96KP6; Q86VP1: TAX1BP1; NbExp=7; IntAct=EBI-2509913, EBI-529518; Q96KP6; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2509913, EBI-11955057; Q96KP6; P21580: TNFAIP3; NbExp=3; IntAct=EBI-2509913, EBI-527670; Q96KP6; Q15025: TNIP1; NbExp=6; IntAct=EBI-2509913, EBI-357849; Q96KP6; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-2509913, EBI-2340370; Q96KP6; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-2509913, EBI-742740; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q96KP6-1; Sequence=Displayed; Name=2; IsoId=Q96KP6-2; Sequence=VSP_045101, VSP_045103; Name=3; IsoId=Q96KP6-3; Sequence=VSP_045102, VSP_045103; Highly expressed in lung, lymph node, thymus and fetal liver. Expressed at lower levels in bone marrow, brain, kidney, spleen, leukocytes and tonsils. Could be detected in heart, salivary gland, adrenal gland, pancreas, ovary and fetal brain. High levels detected in liver, colon, small intestine, muscle, stomach, testis, placenta, thyroid, uterus, prostate, skin and PBL. By Listeria infection. Expression is slightly down-regulated by dexamethasone and slightly up-regulated by IL-10. Strongly induced mRNA and protein expression by lipopolysaccharide. Sequence=BAB15018.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAB15018.1; Type=Frameshift; Evidence=; Sequence=CAC85929.1; Type=Frameshift; Evidence=; MyD88-independent toll-like receptor signaling pathway protein binding cytosol inflammatory response protein deubiquitination polyubiquitin binding toll-like receptor 4 signaling pathway negative regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of transcription from RNA polymerase II promoter cellular response to lipopolysaccharide uc010ing.1 uc010ing.2 uc010ing.3 uc010ing.4 uc010ing.5 
ENST00000060969.6 SIKE1 ENST00000060969.6 suppressor of IKBKE 1, transcript variant 4 (from RefSeq NR_049742.2) ENST00000060969.1 ENST00000060969.2 ENST00000060969.3 ENST00000060969.4 ENST00000060969.5 NR_049742 Q5TEZ7 Q5TEZ9 Q68DZ4 Q9BRV8 Q9H778 SIKE SIKE1_HUMAN uc001efo.1 uc001efo.2 uc001efo.3 uc001efo.4 uc001efo.5 uc001efo.6 SIKE interacts with IKK-epsilon (IKBKE; MIM 605048) and TBK1 (MIM 604834) and acts as a suppressor of TLR3 (MIM 603029) and virus-triggered interferon activation pathways (Huang et al., 2005 [PubMed 16281057]).[supplied by OMIM, Mar 2008]. Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3- mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and RIGI. Does not inhibit NF- kappa-B activation pathways. Interacts with IKBKE and TBK1 via its coiled coil region. Interaction with TBK1 is disrupted upon viral infection or TLR3 stimulation (PubMed:16281057). Interacts with CDC42BPB (PubMed:25743393). Q9BRV8; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-1773646, EBI-11954144; Q9BRV8; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-1773646, EBI-2350265; Q9BRV8; P78358: CTAG1B; NbExp=3; IntAct=EBI-1773646, EBI-1188472; Q9BRV8; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1773646, EBI-741158; Q9BRV8; Q9UIL1-3: SCOC; NbExp=3; IntAct=EBI-1773646, EBI-10692913; Q9BRV8; Q13033-2: STRN3; NbExp=4; IntAct=EBI-1773646, EBI-1053876; Q9BRV8; O75558: STX11; NbExp=3; IntAct=EBI-1773646, EBI-714135; Q9BRV8; Q9Y228: TRAF3IP3; NbExp=2; IntAct=EBI-1773646, EBI-765817; Q9BRV8; P40222: TXLNA; NbExp=3; IntAct=EBI-1773646, EBI-359793; Q9BRV8; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-1773646, EBI-6116822; Q9BRV8; Q53FD0-2: ZC2HC1C; NbExp=6; IntAct=EBI-1773646, EBI-14104088; Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BRV8-1; Sequence=Displayed; Name=2; IsoId=Q9BRV8-2; Sequence=VSP_027543; Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and leukocytes. Present in all cell lines tested (at protein level). Belongs to the SIKE family. protein binding cytoplasm cytosol Rho GTPase binding protein kinase binding uc001efo.1 uc001efo.2 uc001efo.3 uc001efo.4 uc001efo.5 uc001efo.6 
ENST00000061240.7 TLL1 ENST00000061240.7 tolloid like 1, transcript variant 1 (from RefSeq NM_012464.5) B2RMU2 ENST00000061240.1 ENST00000061240.2 ENST00000061240.3 ENST00000061240.4 ENST00000061240.5 ENST00000061240.6 NM_012464 O43897 Q96AN3 Q9NQS4 TLL TLL1_HUMAN uc003irh.1 uc003irh.2 uc003irh.3 uc003irh.4 This gene encodes an astacin-like, zinc-dependent, metalloprotease that belongs to the peptidase M12A family. This protease processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Studies in mice suggest that this gene plays multiple roles in the development of mammalian heart, and is essential for the formation of the interventricular septum. Allelic variants of this gene are associated with atrial septal defect type 6. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2011]. Protease which processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43897-1; Sequence=Displayed; Name=2; IsoId=O43897-2; Sequence=VSP_017197, VSP_017198; Atrial septal defect 6 (ASD6) [MIM:613087]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria. Note=The disease is caused by variants affecting the gene represented in this entry. skeletal system development metalloendopeptidase activity calcium ion binding extracellular region proteolysis multicellular organism development peptidase activity metallopeptidase activity zinc ion binding hydrolase activity extracellular matrix disassembly cell differentiation metal ion binding uc003irh.1 uc003irh.2 uc003irh.3 uc003irh.4 
ENST00000064571.3 CBLN4 ENST00000064571.3 cerebellin 4 precursor (from RefSeq NM_080617.6) A8K0S5 CBLN4_HUMAN CBLNL1 ENST00000064571.1 ENST00000064571.2 NM_080617 Q9NTU7 UNQ718/PRO1382 uc002xxa.1 uc002xxa.2 uc002xxa.3 uc002xxa.4 uc002xxa.5 uc002xxa.6 This gene encodes a member of a family of small secreted proteins containing C1Q domains. Members of this family are involved in regulation of neurexin signalling during synapse development. The mouse homolog of the protein encoded by this gene competes with netrin to bind to the deleted in colorectal cancer receptor. [provided by RefSeq, Aug 2012]. ##Evidence-Data-START## Transcript exon combination :: BC050026.1, SRR1803617.233939.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1970526, SAMEA2142586 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000064571.3/ ENSP00000064571.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as a synaptic organizer in specific subsets of neurons in the brain (By similarity). Essential for the formation and maintenance of inhibitory GABAergic synapses (By similarity). Promotes the development of dendrite-targeting inhibitory GABAergic synapses made by somatostatin-positive interneurons (By similarity). May contribute to the function of ventral medial habenula region of the brain implicated in the regulation of anxiety-related behaviors (By similarity). May play a role in CBLN3 export from the endoplasmic reticulum and secretion (By similarity). Homohexamer; disulfide-linked homotrimers. The trimers are assembled via the globular C1q domains. The trimers associate via N- terminal cysteine residues to form disulfide-linked hexamers (By similarity). May form oligomers with CBLN1, CBLN2 and CBLN3 prior to secretion (By similarity). Strongly interacts with DCC in a NTN1- displaceable fashion (By similarity). Weakly binds to NRXN1 and NRXN2 long and short isoforms produced by alternative promoter usage. Interaction with NRXN3 short isoform is hardly detectable; no interaction at all with NRXN3 long isoform (By similarity). Secreted Synapse Note=Detected at GABAergic synapses. Sialoglycoprotein. extracellular region extracellular space protein secretion cell junction synapse uc002xxa.1 uc002xxa.2 uc002xxa.3 uc002xxa.4 uc002xxa.5 uc002xxa.6 
ENST00000064724.8 CLDN11 ENST00000064724.8 claudin 11, transcript variant 1 (from RefSeq NM_005602.6) B2R7C1 CLD11_HUMAN D3DNQ5 ENST00000064724.1 ENST00000064724.2 ENST00000064724.3 ENST00000064724.4 ENST00000064724.5 ENST00000064724.6 ENST00000064724.7 NM_005602 O75508 OSP OTM Q5U0P3 uc003fgx.1 uc003fgx.2 uc003fgx.3 uc003fgx.4 uc003fgx.5 This gene encodes a member of the claudin family. Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical barrier to prevent solutes and water from passing freely through the paracellular space between epithelial or endothelial cell sheets, and also play critical roles in maintaining cell polarity and signal transductions. The protein encoded by this gene is a major component of central nervous system (CNS) myelin and plays an important role in regulating proliferation and migration of oligodendrocytes. Mouse studies showed that the gene deficiency results in deafness and loss of the Sertoli cell epithelial phenotype in the testis. This protein is a tight junction protein at the human blood-testis barrier (BTB), and the BTB disruption is related to a dysfunction of this gene. Alternatively spliced transcript variants encoding different isoforms have been identified.[provided by RefSeq, Aug 2010]. Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Interacts with tetraspanin-3/TSPAN3 (By similarity). Interacts with OCLN (PubMed:20375010). O75508; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-12820543, EBI-19125216; O75508; Q86V38: ATN1; NbExp=3; IntAct=EBI-12820543, EBI-11954292; O75508; Q6UWD8: C16orf54; NbExp=3; IntAct=EBI-12820543, EBI-18041102; O75508; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12820543, EBI-12142257; O75508; Q92876: KLK6; NbExp=3; IntAct=EBI-12820543, EBI-2432309; O75508; P26715: KLRC1; NbExp=3; IntAct=EBI-12820543, EBI-9018187; O75508; A0PJX4: SHISA3; NbExp=3; IntAct=EBI-12820543, EBI-10171518; O75508; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-12820543, EBI-741850; O75508; O43278-2: SPINT1; NbExp=3; IntAct=EBI-12820543, EBI-12078338; O75508; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-12820543, EBI-11742770; O75508; O43557: TNFSF14; NbExp=3; IntAct=EBI-12820543, EBI-524131; O75508; P21754-3: ZP3; NbExp=3; IntAct=EBI-12820543, EBI-17458299; Cell junction, tight junction. Cell membrane ; Multi-pass membrane protein Leukodystrophy, hypomyelinating, 22 (HLD22) [MIM:619328]: An autosomal dominant disorder characterized by global developmental delay, mildly impaired intellectual development, motor impairment, limb spasticity, dysarthria, and eye abnormalities including hypermetropia. Brain imaging shows hypomyelinating leukodystrophy. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the claudin family. structural molecule activity protein binding plasma membrane bicellular tight junction membrane integral component of membrane calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules cell junction identical protein binding uc003fgx.1 uc003fgx.2 uc003fgx.3 uc003fgx.4 uc003fgx.5 
ENST00000064780.7 RELT ENST00000064780.7 RELT TNF receptor, transcript variant 2 (from RefSeq NM_152222.2) ENST00000064780.1 ENST00000064780.2 ENST00000064780.3 ENST00000064780.4 ENST00000064780.5 ENST00000064780.6 NM_152222 Q86V34 Q969Z4 Q96JU1 Q9BUX7 TNFRSF19L TR19L_HUMAN uc001otv.1 uc001otv.2 uc001otv.3 uc001otv.4 uc001otv.5 The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is especially abundant in hematologic tissues. It has been shown to activate the NF-kappaB pathway and selectively bind TNF receptor-associated factor 1 (TRAF1). This receptor is capable of stimulating T-cell proliferation in the presence of CD3 signaling, which suggests its regulatory role in immune response. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported. [provided by RefSeq, Jul 2008]. May play a role in apoptosis (PubMed:28688764, PubMed:19969290). Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed (PubMed:16530727). Involved in dental enamel formation (PubMed:30506946). Interacts with TRAF1 (PubMed:11313261). Interacts with RELL1, RELL2 and OXSR1 (PubMed:16389068). Interacts with PLSCR1 (PubMed:22052202). Interacts with STK39 (PubMed:16530727). Cell membrane ; Single-pass type I membrane protein Cytoplasm Cytoplasm, perinuclear region Spleen, lymph node, brain, breast and peripheral blood leukocytes (at protein level) (PubMed:28688764). Expressed highly in bone marrow and fetal liver. Very low levels in skeletal muscle, testis and colon. Not detected in kidney and pancreas. Phosphorylated in vitro by OXSR1 (PubMed:16389068). Phosphorylated by STK39 (PubMed:16530727). Amelogenesis imperfecta 3C (AI3C) [MIM:618386]: An autosomal recessive form of amelogenesis imperfecta, a defect of enamel formation. AI3C is characterized by generalized enamel hypocalcification affecting primary and secondary dentition. The surface of the enamel is rough and often stained. After eruption, the occlusal enamel on the molars disappears due to attrition, leaving a ring of intact enamel remaining on the sides. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the RELT family. Sequence=BAB84954.1; Type=Frameshift; Evidence=; protein binding nucleus cytoplasm plasma membrane apoptotic process membrane integral component of membrane perinuclear region of cytoplasm uc001otv.1 uc001otv.2 uc001otv.3 uc001otv.4 uc001otv.5 
ENST00000066544.8 CDC27 ENST00000066544.8 cell division cycle 27, transcript variant 10 (from RefSeq NR_148340.2) ANAPC3 CDC27_HUMAN D0S1430E D17S978E ENST00000066544.1 ENST00000066544.2 ENST00000066544.3 ENST00000066544.4 ENST00000066544.5 ENST00000066544.6 ENST00000066544.7 G3V1C4 NR_148340 P30260 Q16349 Q96F35 uc002ild.1 uc002ild.2 uc002ild.3 uc002ild.4 uc002ild.5 uc002ild.6 The protein encoded by this gene shares strong similarity with Saccharomyces cerevisiae protein Cdc27, and the gene product of Schizosaccharomyces pombe nuc 2. This protein is a component of the anaphase-promoting complex (APC), which is composed of eight protein subunits and is highly conserved in eukaryotic cells. This complex catalyzes the formation of cyclin B-ubiquitin conjugate, which is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. The protein encoded by this gene and three other members of the APC complex contain tetratricopeptide (TPR) repeats, which are important for protein-protein interactions. This protein was shown to interact with mitotic checkpoint proteins including Mad2, p55CDC and BUBR1, and it may thus be involved in controlling the timing of mitosis. Alternative splicing of this gene results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 2, 22 and Y. [provided by RefSeq, May 2014]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.250251.1 [ECO:0000332] ##Evidence-Data-END## Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Protein modification; protein ubiquitination. Homodimer. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (PubMed:26083744, PubMed:25043029). Interacts with RB. Interacts with FAM168B/MANI (By similarity). Interacts with MCPH1 (PubMed:22139841). P30260; Q9UJX5: ANAPC4; NbExp=8; IntAct=EBI-994813, EBI-2554854; P30260; P24385: CCND1; NbExp=3; IntAct=EBI-994813, EBI-375001; P30260; Q12834: CDC20; NbExp=13; IntAct=EBI-994813, EBI-367462; P30260; P12830: CDH1; NbExp=2; IntAct=EBI-994813, EBI-727477; P30260; P21964-2: COMT; NbExp=3; IntAct=EBI-994813, EBI-10200977; P30260; Q9UKT4: FBXO5; NbExp=2; IntAct=EBI-994813, EBI-852298; P30260; O43524: FOXO3; NbExp=2; IntAct=EBI-994813, EBI-1644164; P30260; Q9UM11: FZR1; NbExp=12; IntAct=EBI-994813, EBI-724997; P30260; Q13257: MAD2L1; NbExp=9; IntAct=EBI-994813, EBI-78203; P30260; Q9UI95: MAD2L2; NbExp=2; IntAct=EBI-994813, EBI-77889; P30260; P16333: NCK1; NbExp=3; IntAct=EBI-994813, EBI-389883; P30260; P51955: NEK2; NbExp=2; IntAct=EBI-994813, EBI-633182; P30260; P60484: PTEN; NbExp=7; IntAct=EBI-994813, EBI-696162; Nucleus Cytoplasm, cytoskeleton, spindle Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P30260-1; Sequence=Displayed; Name=2; IsoId=P30260-2; Sequence=VSP_047225; Phosphorylated. Phosphorylation on Ser-426 and Thr-446 occurs specifically during mitosis. [Isoform 2]: May be due to competing acceptor splice site. Belongs to the APC3/CDC27 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc27/"; protein binding nucleus nucleoplasm anaphase-promoting complex cytoplasm centrosome cytosol ubiquitin-dependent protein catabolic process metaphase/anaphase transition of mitotic cell cycle protein ubiquitination protein phosphatase binding anaphase-promoting complex-dependent catabolic process protein K11-linked ubiquitination regulation of mitotic cell cycle phase transition spindle microtubule uc002ild.1 uc002ild.2 uc002ild.3 uc002ild.4 uc002ild.5 uc002ild.6 
ENST00000072644.7 YIPF1 ENST00000072644.7 Yip1 domain family member 1, transcript variant 2 (from RefSeq NR_036639.2) B2RCM7 D3DQ40 ENST00000072644.1 ENST00000072644.2 ENST00000072644.3 ENST00000072644.4 ENST00000072644.5 ENST00000072644.6 NR_036639 Q9NWJ1 Q9Y548 YIPF1_HUMAN uc001cvu.1 uc001cvu.2 uc001cvu.3 uc001cvu.4 uc001cvu.5 uc001cvu.6 Interacts with YIPF6; this interaction may stabilize YIPF1. May also form a ternary complex with YIPF2 and YIPF6. Q9Y548; Q8NCL9: APCDD1L; NbExp=3; IntAct=EBI-7850136, EBI-12904424; Q9Y548; Q13520: AQP6; NbExp=3; IntAct=EBI-7850136, EBI-13059134; Q9Y548; P07307-3: ASGR2; NbExp=3; IntAct=EBI-7850136, EBI-12808270; Q9Y548; O00501: CLDN5; NbExp=3; IntAct=EBI-7850136, EBI-18400628; Q9Y548; Q8TAZ6: CMTM2; NbExp=3; IntAct=EBI-7850136, EBI-2339374; Q9Y548; P34972: CNR2; NbExp=3; IntAct=EBI-7850136, EBI-2835940; Q9Y548; Q15125: EBP; NbExp=3; IntAct=EBI-7850136, EBI-3915253; Q9Y548; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-7850136, EBI-781551; Q9Y548; O14843: FFAR3; NbExp=3; IntAct=EBI-7850136, EBI-17762181; Q9Y548; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-7850136, EBI-13345167; Q9Y548; O15529: GPR42; NbExp=3; IntAct=EBI-7850136, EBI-18076404; Q9Y548; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-7850136, EBI-13067820; Q9Y548; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-7850136, EBI-1055254; Q9Y548; P48051: KCNJ6; NbExp=3; IntAct=EBI-7850136, EBI-12017638; Q9Y548; O15243: LEPROT; NbExp=3; IntAct=EBI-7850136, EBI-15672507; Q9Y548; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-7850136, EBI-373355; Q9Y548; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-7850136, EBI-10192441; Q9Y548; Q99942: RNF5; NbExp=3; IntAct=EBI-7850136, EBI-348482; Q9Y548; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-7850136, EBI-17640454; Q9Y548; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-7850136, EBI-18159983; Q9Y548; Q2M3R5: SLC35G1; NbExp=3; IntAct=EBI-7850136, EBI-13311257; Q9Y548; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-7850136, EBI-13292283; Q9Y548; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-7850136, EBI-6268651; Q9Y548; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-7850136, EBI-12947623; Q9Y548; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-7850136, EBI-8638294; Q9Y548; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-7850136, EBI-10314986; Q9Y548; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-7850136, EBI-11724433; Q9Y548; Q9Y320: TMX2; NbExp=3; IntAct=EBI-7850136, EBI-6447886; Q9Y548; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-7850136, EBI-11343401; Q9Y548; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-7850136, EBI-1055364; Q9Y548; Q96EC8: YIPF6; NbExp=8; IntAct=EBI-7850136, EBI-751210; Q9Y548; Q9NXF8-2: ZDHHC7; NbExp=3; IntAct=EBI-7850136, EBI-12948063; Golgi apparatus, cis-Golgi network membrane ; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane Late endosome membrane Note=Mainly localizes within medial-/trans-Golgi and trans-Golgi network (TGN), while less so within cis-Golgi. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y548-1; Sequence=Displayed; Name=2; IsoId=Q9Y548-2; Sequence=VSP_019437; Belongs to the YIP1 family. Sequence=AAH09674.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Golgi trans cisterna protein binding endosome Golgi apparatus Golgi medial cisterna trans-Golgi network membrane integral component of membrane vesicle-mediated transport Rab GTPase binding transport vesicle late endosome membrane uc001cvu.1 uc001cvu.2 uc001cvu.3 uc001cvu.4 uc001cvu.5 uc001cvu.6 
ENST00000072869.9 ADCK2 ENST00000072869.9 aarF domain containing kinase 2 (from RefSeq NM_052853.4) AARF ADCK2_HUMAN ENST00000072869.1 ENST00000072869.2 ENST00000072869.3 ENST00000072869.4 ENST00000072869.5 ENST00000072869.6 ENST00000072869.7 ENST00000072869.8 NM_052853 Q7Z695 Q96CN6 Q9Y6T5 uc003vvy.1 uc003vvy.2 uc003vvy.3 The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr) (Probable). Involved in the mitochondrial import of CoQ precursors, plays a role in muscle mitochondrial function and fatty acid beta-oxidation (PubMed:31480808). Q7Z695; P05141: SLC25A5; NbExp=4; IntAct=EBI-21505425, EBI-355133; Mitochondrion Membrane ; Single-pass membrane protein Belongs to the protein kinase superfamily. ADCK protein kinase family. Sequence=AAH14107.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence=; nucleotide binding protein serine/threonine kinase activity ATP binding protein phosphorylation membrane integral component of membrane kinase activity phosphorylation transferase activity uc003vvy.1 uc003vvy.2 uc003vvy.3 
ENST00000075120.12 SLC2A3 ENST00000075120.12 solute carrier family 2 member 3 (from RefSeq NM_006931.3) B2R606 D3DUU6 ENST00000075120.1 ENST00000075120.10 ENST00000075120.11 ENST00000075120.2 ENST00000075120.3 ENST00000075120.4 ENST00000075120.5 ENST00000075120.6 ENST00000075120.7 ENST00000075120.8 ENST00000075120.9 GLUT3 GTR3_HUMAN NM_006931 P11169 Q6I9U2 Q9UG15 SLC2A3 uc001qtr.1 uc001qtr.2 uc001qtr.3 uc001qtr.4 uc001qtr.5 Facilitative glucose transporter (PubMed:9477959, PubMed:26176916). Can also mediate the uptake of various other monosaccharides across the cell membrane (PubMed:9477959, PubMed:26176916). Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate (PubMed:9477959, PubMed:26176916). Does not mediate fructose transport (PubMed:9477959, PubMed:26176916). Required for mesendoderm differentiation (By similarity). Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence= Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915, ChEBI:CHEBI:4139; Evidence=; Deoxyglucose transport is inhibit by D-glucose, D- galactose and maltose (PubMed:8457197). Galactose transport is inhibited by D-glucose and maltose (PubMed:8457197). Kinetic parameters: KM=1.4 mM for deoxyglucose KM=8.5 mM for D-galactose ; Interacts with SMIM43; the interaction may promote SLC2A3- mediated glucose transport to meet the energy needs of mesendoderm differentiation. P11169; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-725116, EBI-6942903; Cell membrane ulti-pass membrane protein Perikaryon Cell projection Note=Localized to densely spaced patches along neuronal processes. Highly expressed in brain (PubMed:8457197). Expressed in many tissues. Transport is mediated via a series of conformation changes, switching between a conformation where the substrate-binding cavity is accessible from the outside, and a another conformation where it is accessible from the cytoplasm. Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily. glucose transmembrane transporter activity protein binding glucose binding plasma membrane integral component of plasma membrane carbohydrate metabolic process carbohydrate transport membrane integral component of membrane L-ascorbic acid metabolic process transmembrane transporter activity secretory granule membrane specific granule membrane cell projection perikaryon neutrophil degranulation transmembrane transport extracellular exosome tertiary granule membrane ficolin-1-rich granule membrane glucose transmembrane transport uc001qtr.1 uc001qtr.2 uc001qtr.3 uc001qtr.4 uc001qtr.5 
ENST00000075322.11 ENPP2 ENST00000075322.11 ectonucleotide pyrophosphatase/phosphodiesterase 2, transcript variant 2 (from RefSeq NM_001040092.3) A8UHA1 ATX E9PHP7 ENPP2_HUMAN ENST00000075322.1 ENST00000075322.10 ENST00000075322.2 ENST00000075322.3 ENST00000075322.4 ENST00000075322.5 ENST00000075322.6 ENST00000075322.7 ENST00000075322.8 ENST00000075322.9 NM_001040092 PDNP2 Q13822 Q13827 Q14555 Q15117 Q9UCQ8 Q9UCR0 Q9UCR1 Q9UCR2 Q9UCR3 Q9UCR4 uc003yot.1 uc003yot.2 uc003yot.3 uc003yot.4 The protein encoded by this gene functions as both a phosphodiesterase, which cleaves phosphodiester bonds at the 5' end of oligonucleotides, and a phospholipase, which catalyzes production of lysophosphatidic acid (LPA) in extracellular fluids. LPA evokes growth factor-like responses including stimulation of cell proliferation and chemotaxis. This gene product stimulates the motility of tumor cells and has angiogenic properties, and its expression is upregulated in several kinds of carcinomas. The gene product is secreted and further processed to make the biologically active form. Several alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Aug 2008]. Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:15769751, PubMed:26371182, PubMed:27754931, PubMed:14500380, PubMed:12354767). Major substrate is lysophosphatidylcholine (PubMed:12176993, PubMed:27754931, PubMed:14500380). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility (PubMed:14500380). Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:15769751, PubMed:12176993). Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation (PubMed:11559573). Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein (PubMed:1733949). May have a role in induction of parturition (PubMed:12176993). Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor (PubMed:1733949, PubMed:11559573). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (PubMed:21393252). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3- phosphocholine (lyso-PAF) (PubMed:21393252). Reaction=1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl- sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:15965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603, ChEBI:CHEBI:58014, ChEBI:CHEBI:76168; EC=3.1.4.39; Evidence= Reaction=1-O-(9Z-octadecenyl)-sn-glycero-3-phosphocholine + H2O = 1-O- (9Z-octadecenyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41684, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64396, ChEBI:CHEBI:78402; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41685; Evidence=; Reaction=a 2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn- glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:41712, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57875, ChEBI:CHEBI:64982; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41713; Evidence=; Reaction=a 2-acyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn- glycerol 3-phosphate + H(+) + L-serine; Xref=Rhea:RHEA:41716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:64982, ChEBI:CHEBI:65214; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41717; Evidence=; Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl- sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:38991, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72682, ChEBI:CHEBI:74966; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38992; Evidence=; Reaction=H2O + sphing-4-enine-phosphocholine = choline + H(+) + sphing- 4-enine 1-phosphate; Xref=Rhea:RHEA:38919, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58906, ChEBI:CHEBI:60119; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38920; Evidence=; Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z- octadecenoyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38916; Evidence=; Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1- tetradecanoyl-sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:38983, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64489, ChEBI:CHEBI:72683; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38984; Evidence=; Reaction=1-decanoyl-sn-glycero-3-phosphocholine + H2O = 1-decanoyl-sn- glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41131, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77724, ChEBI:CHEBI:77726; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41132; Evidence=; Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- hexadecanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:38975, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72998; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38976; Evidence=; Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- octadecanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:38979, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73858, ChEBI:CHEBI:74565; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38980; Evidence=; Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41135, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28733, ChEBI:CHEBI:74547; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41136; Evidence=; Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41139, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344, ChEBI:CHEBI:74938; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41140; Evidence=; Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O- hexadecyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144; Evidence=; Reaction=1-hexanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexanoyl-sn- glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41400, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78215, ChEBI:CHEBI:78223; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41401; Evidence=; Reaction=1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O = 1,2- dioctanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41416, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78228, ChEBI:CHEBI:78229; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41417; Evidence=; Reaction=1,2-didecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2- didecanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41412, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78226, ChEBI:CHEBI:78227; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41413; Evidence=; Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-(1Z- alkenyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41588, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77283, ChEBI:CHEBI:77287; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41589; Evidence=; Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:38927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603, ChEBI:CHEBI:74544, ChEBI:CHEBI:74971; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38928; Evidence=; Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 1- (9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + L-serine; Xref=Rhea:RHEA:38931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:74544, ChEBI:CHEBI:74617; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38932; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence= Note=Binds 2 Zn(2+) ions per subunit. Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence= Note=Binds 1 Ca(2+) ion per subunit. Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA (Probable). Kinetic parameters: KM=0.5 mM for 16:0-LPC (at pH 8.5) KM=5.5 mM for pNP-TMP (at pH 8.5) KM=11.3 mM for pNppp (isoform 1) KM=5.7 mM for pNppp (isoform 2) KM=19.8 mM for pNppp (isoform 3) KM=96 uM for sn-1 lyso-PAF ; KM=51 uM for sn-2 lyso-PAF ; KM=0.10 mM for lysophosphatidylcholine ; KM=0.23 mM for sphingosylphosphorylcholine ; Vmax=1.9 nmol/min/ug enzyme with pNppp as substrate (isoform 1) ; Vmax=0.67 nmol/min/ug enzyme with pNppp as substrate (isoform 2) ; Vmax=1.6 nmol/min/ug enzyme with pNppp as substrate (isoform 3) ; Vmax=0.11 umol/min/mg enzyme with sn-1 lyso-PAF as substrate ; Vmax=0.025 umol/min/mg enzyme with sn-2 lyso-PAF as substrate ; Vmax=11.8 nmol/min/ug enzyme with lysophosphatidylcholine as substrate ; Vmax=6.1 nmol/min/ug enzyme with sphingosylphosphorylcholine as substrate ; pH dependence: Optimum pH is 9.0 (isoform 1), 8.0 (isoform 3). Isoform 1 is less sensitive to pH. Isoform 1, isoform 2 and isoform 3 all retain some activity at pH 9.5. Temperature dependence: Isoform 1 and isoform 3 are active from 45 to 60 degrees Celsius. ; Secreted Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=ATXter, Beta; IsoId=Q13822-1; Sequence=Displayed; Name=2; Synonyms=ATXmel, Alpha; IsoId=Q13822-2; Sequence=VSP_006750; Name=3; Synonyms=Gamma; IsoId=Q13822-3; Sequence=VSP_036398; Detected in blood plasma (at protein level) (PubMed:12176993, PubMed:26371182). Predominantly expressed in brain, placenta, ovary, and small intestine. Expressed in a number of carcinomas such as hepatocellular and prostate carcinoma, neuroblastoma and non-small-cell lung cancer. Expressed in body fluids such as plasma, cerebral spinal fluid (CSF), saliva, follicular and amniotic fluids. Not detected in leukocytes. Isoform 1 is more highly expressed in peripheral tissues than in the central nervous system (CNS). Adipocytes only express isoform 1. Isoform 3 is more highly expressed in the brain than in peripheral tissues. Up-regulated in massively obese subjects with glucose intolerance, and during adipogenesis. N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. The interdomain disulfide bond between Cys-414 and Cys-806 is essential for catalytic activity. Belongs to the nucleotide pyrophosphatase/phosphodiesterase family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40455/ENPP2"; nucleic acid binding catalytic activity phosphodiesterase I activity nucleotide diphosphatase activity lysophospholipase activity scavenger receptor activity calcium ion binding extracellular region extracellular space plasma membrane lipid metabolic process phospholipid metabolic process endocytosis chemotaxis immune response transcription factor binding zinc ion binding phospholipid catabolic process positive regulation of epithelial cell migration lipid catabolic process hydrolase activity polysaccharide binding regulation of cell migration phosphatidylcholine catabolic process regulation of angiogenesis metal ion binding alkylglycerophosphoethanolamine phosphodiesterase activity cell motility positive regulation of peptidyl-tyrosine phosphorylation nucleic acid phosphodiester bond hydrolysis positive regulation of lamellipodium morphogenesis uc003yot.1 uc003yot.2 uc003yot.3 uc003yot.4 
ENST00000075503.8 STYK1 ENST00000075503.8 serine/threonine/tyrosine kinase 1 (from RefSeq NM_018423.3) B2R9T2 ENST00000075503.1 ENST00000075503.2 ENST00000075503.3 ENST00000075503.4 ENST00000075503.5 ENST00000075503.6 ENST00000075503.7 NM_018423 NOK Q52LR3 Q6J9G0 Q9BXY2 Q9NSH1 STYK1_HUMAN uc001qys.1 uc001qys.2 uc001qys.3 Receptor protein tyrosine kinases, like STYK1, play important roles in diverse cellular and developmental processes, such as cell proliferation, differentiation, and survival (Liu et al., 2004 [PubMed 15150103]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AL353940.1, SRR1660809.181095.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000075503.8/ ENSP00000075503.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphatidylinositol 3'-kinases (PI3K) pathways (By similarity). Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence=; Q6J9G0; P49841: GSK3B; NbExp=2; IntAct=EBI-6424915, EBI-373586; Q6J9G0; P08238: HSP90AB1; NbExp=3; IntAct=EBI-6424915, EBI-352572; Membrane ; Single-pass membrane protein Widely expressed. Highly expressed in brain, placenta and prostate. Expressed in tumor cells such as hepatoma cells L-02, cervix carcinoma cells HeLa, ovary cancer cells Ho8910 and chronic myelogenous leukemia cells K-562, but not in other tumor cells such as epidermoid carcinoma (A-431). Undetectable in most normal lung tissues, widely expressed in lung cancers. Belongs to the protein kinase superfamily. Tyr protein kinase family. nucleotide binding protein kinase activity protein tyrosine kinase activity non-membrane spanning protein tyrosine kinase activity protein binding ATP binding plasma membrane protein phosphorylation membrane integral component of membrane kinase activity phosphorylation transferase activity peptidyl-tyrosine phosphorylation uc001qys.1 uc001qys.2 uc001qys.3 
ENST00000078429.9 GNA11 ENST00000078429.9 G protein subunit alpha 11 (from RefSeq NM_002067.5) ENST00000078429.1 ENST00000078429.2 ENST00000078429.3 ENST00000078429.4 ENST00000078429.5 ENST00000078429.6 ENST00000078429.7 ENST00000078429.8 GA11 GNA11_HUMAN NM_002067 O15109 P29992 Q14350 Q6IB00 uc010xhe.1 uc010xhe.2 uc010xhe.3 uc010xhe.4 uc010xhe.5 uc010xhe.6 The protein encoded by this gene belongs to the family of guanine nucleotide-binding proteins (G proteins), which function as modulators or transducers in various transmembrane signaling systems. G proteins are composed of 3 units: alpha, beta and gamma. This gene encodes one of the alpha subunits (subunit alpha-11). Mutations in this gene have been associated with hypocalciuric hypercalcemia type II (HHC2) and hypocalcemia dominant 2 (HYPOC2). Patients with HHC2 and HYPOC2 exhibit decreased or increased sensitivity, respectively, to changes in extracellular calcium concentrations. [provided by RefSeq, Dec 2013]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: ERR279833.10491.1, SRR1163658.278623.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000078429.9/ ENSP00000078429.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (PubMed:31073061). Acts as an activator of phospholipase C (PubMed:31073061). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (PubMed:27852822). Together with GNAQ, required for heart development (By similarity). G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:35061538). Interacts with RGS22 (PubMed:18703424). Interacts with NTSR1 (PubMed:21725197). (Microbial infection) Interacts with human cytomegalovirus (HHV-5) US28. Cell membrane ; Lipid-anchor Cytoplasm Note=In testicular cells, expressed exclusively in the cytoplasm. Expressed in testis. (Microbial infection) Deamidated at Gln-209 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA. Hypocalciuric hypercalcemia, familial 2 (HHC2) [MIM:145981]: A form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis that is transmitted as an autosomal dominant trait with a high degree of penetrance. It is characterized biochemically by lifelong elevation of serum calcium concentrations and is associated with inappropriately low urinary calcium excretion and a normal or mildly elevated circulating parathyroid hormone level. Hypermagnesemia is typically present. Affected individuals are usually asymptomatic and the disorder is considered benign. However, chondrocalcinosis and pancreatitis occur in some adults. Note=The disease is caused by variants affecting the gene represented in this entry. Hypocalcemia, autosomal dominant 2 (HYPOC2) [MIM:615361]: A form of hypocalcemia, a disorder of mineral homeostasis characterized by blood calcium levels below normal, and low or normal serum parathyroid hormone concentrations. Disease manifestations include hypocalcemia, paresthesias, carpopedal spasm, seizures, hypercalciuria with nephrocalcinosis or kidney stones, and ectopic and basal ganglia calcifications. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the G-alpha family. G(q) subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/43272/GNA11"; nucleotide binding skeletal system development action potential G-protein coupled receptor binding photoreceptor outer segment GTPase activity protein binding GTP binding cytoplasm lysosomal membrane heterotrimeric G-protein complex plasma membrane signal transduction G-protein coupled receptor signaling pathway adenylate cyclase-modulating G-protein coupled receptor signaling pathway G-protein coupled acetylcholine receptor signaling pathway heart development phototransduction, visible light entrainment of circadian clock membrane guanyl nucleotide binding platelet activation G-protein beta/gamma-subunit complex binding type 2A serotonin receptor binding regulation of melanocyte differentiation metal ion binding developmental pigmentation phospholipase C-activating dopamine receptor signaling pathway extracellular exosome cellular response to pH uc010xhe.1 uc010xhe.2 uc010xhe.3 uc010xhe.4 uc010xhe.5 uc010xhe.6 
ENST00000078445.7 CREB3L3 ENST00000078445.7 cAMP responsive element binding protein 3 like 3, transcript variant 1 (from RefSeq NM_032607.3) B2R7S6 B7ZL69 CR3L3_HUMAN CREBH ENST00000078445.1 ENST00000078445.2 ENST00000078445.3 ENST00000078445.4 ENST00000078445.5 ENST00000078445.6 HYST1481 M0QYW7 NM_032607 Q68CJ9 Q6ZMC5 Q96TB9 uc002lzl.1 uc002lzl.2 uc002lzl.3 uc002lzl.4 uc002lzl.5 This gene encodes a member of the basic-leucine zipper family and the AMP-dependent transcription factor family. The encoded protein is localized to the endoplasmic reticulum and acts as a transcription factor activated by cyclic AMP stimulation. The encoded protein binds the cyclic AMP response element (CRE) and the box-B element and has been linked to acute inflammatory response, hepatocellular carcinoma, triglyceride metabolism, and hepcidin expression. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2012]. Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. In vitro, binds to the cAMP response element (CRE) and box-B element. Activates transcription through box-B element. Activates transcription through CRE (By similarity). May function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression. Regulates FGF21 transcription (By similarity). Plays a crucial role in the regulation of triglyceride metabolism and is required for the maintenance of normal plasma triglyceride concentrations (PubMed:21666694). Binds DNA as a dimer (By similarity). May form homodimers (PubMed:16469704). Interacts with ATF6 (PubMed:16469704). Interacts with SYNV1/HRD1; this interaction leads to CREB3L3 ubiquitination and proteasomal degradation (By similarity). Q68CJ9; P18850: ATF6; NbExp=2; IntAct=EBI-852194, EBI-852157; Q68CJ9; Q96LK0: CEP19; NbExp=3; IntAct=EBI-852194, EBI-741885; Q68CJ9; O43889: CREB3; NbExp=3; IntAct=EBI-852194, EBI-625002; Q68CJ9; Q96BA8: CREB3L1; NbExp=2; IntAct=EBI-852194, EBI-6942903; Q68CJ9; Q68CJ9: CREB3L3; NbExp=2; IntAct=EBI-852194, EBI-852194; Q68CJ9; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-852194, EBI-10269179; Q68CJ9; Q9C005: DPY30; NbExp=3; IntAct=EBI-852194, EBI-744973; Q68CJ9; Q969F0: FATE1; NbExp=3; IntAct=EBI-852194, EBI-743099; Q68CJ9; O00155: GPR25; NbExp=3; IntAct=EBI-852194, EBI-10178951; Q68CJ9; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-852194, EBI-348259; Q68CJ9; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-852194, EBI-12070086; Q68CJ9; Q16649: NFIL3; NbExp=2; IntAct=EBI-852194, EBI-3951858; Q68CJ9; Q02094: RHAG; NbExp=3; IntAct=EBI-852194, EBI-14772355; Q68CJ9; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-852194, EBI-8636004; Q68CJ9; O43765: SGTA; NbExp=3; IntAct=EBI-852194, EBI-347996; Q68CJ9; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-852194, EBI-744081; Q68CJ9; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-852194, EBI-10314552; Q68CJ9; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-852194, EBI-2823239; Q68CJ9; Q13190: STX5; NbExp=3; IntAct=EBI-852194, EBI-714206; Q68CJ9; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-852194, EBI-11955057; Q68CJ9; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-852194, EBI-11528917; Q68CJ9; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-852194, EBI-765817; Q68CJ9; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-852194, EBI-751210; Endoplasmic reticulum membrane ; Single-pass type II membrane protein [Processed cyclic AMP-responsive element-binding protein 3-like protein 3]: Nucleus Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q68CJ9-1; Sequence=Displayed; Name=2; IsoId=Q68CJ9-2; Sequence=VSP_025637; Name=3; IsoId=Q68CJ9-4; Sequence=VSP_054876; Name=4; IsoId=Q68CJ9-5; Sequence=VSP_055635, VSP_055636; Exclusively expressed in liver. Underexpressed in hepatocellular carcinoma tissues. Controlled by regulated intramembrane proteolysis (RIP). Following ER stress a fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (PS1 and PS2). N- and O-glycosylated. N-glycosylation is required for optimal proteolytic activation. O-glycosylated with core 1 or possibly core 8 glycans. Ubiquitinated at Lys-294 by SYNV1/HRD1 via 'Lys-27'-linked ubiquitin. Hypertriglyceridemia 2 (HYTG2) [MIM:619324]: An autosomal dominant form of hypertriglyceridemia, a disorder characterized by elevated plasma triglyceride levels. HYTG2 patients also have increased total cholesterol levels and low levels of high density lipoprotein (HDL) cholesterol. Reduced penetrance has been observed. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the bZIP family. ATF subfamily. Sequence=BAD18804.1; Type=Frameshift; Evidence=; Sequence=BAD18804.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence=; Golgi membrane nuclear chromatin transcription regulatory region sequence-specific DNA binding RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding positive regulation of acute inflammatory response DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm endoplasmic reticulum endoplasmic reticulum membrane cytosol regulation of transcription, DNA-templated response to unfolded protein membrane integral component of membrane endoplasmic reticulum unfolded protein response cAMP response element binding protein homodimerization activity positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress uc002lzl.1 uc002lzl.2 uc002lzl.3 uc002lzl.4 uc002lzl.5 
ENST00000080059.12 HDAC7 ENST00000080059.12 histone deacetylase 7, transcript variant 8 (from RefSeq NR_160436.1) B3KY08 B4DWI0 B4E0Q5 ENST00000080059.1 ENST00000080059.10 ENST00000080059.11 ENST00000080059.2 ENST00000080059.3 ENST00000080059.4 ENST00000080059.5 ENST00000080059.6 ENST00000080059.7 ENST00000080059.8 ENST00000080059.9 HDAC7A HDAC7_HUMAN NR_160436 Q6P1W9 Q6W9G7 Q7Z4K2 Q7Z5I1 Q8WUI4 Q96K01 Q9BR73 Q9H7L0 Q9NW41 Q9NWA9 Q9NYK9 Q9UFU7 uc010slo.1 uc010slo.2 uc010slo.3 uc010slo.4 Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to mouse HDAC7 gene whose protein promotes repression mediated via the transcriptional corepressor SMRT. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7346977.1964967.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3 (PubMed:17360565). Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (PubMed:28167758). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758). Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl- [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA- COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C (By similarity). Interacts with KAT5 and EDNRA. Interacts with KDM5B. Interacts with ZMYND15 (By similarity). Interacts with PML (isoform PML-4). Interacts with FOXP3. Interacts with RARA (PubMed:28167758). Q8WUI4; P00533: EGFR; NbExp=3; IntAct=EBI-1048378, EBI-297353; Q8WUI4; Q9BZS1-1: FOXP3; NbExp=2; IntAct=EBI-1048378, EBI-9695448; Q8WUI4; Q9BZS1-2: FOXP3; NbExp=2; IntAct=EBI-1048378, EBI-16338471; Q8WUI4; Q9BZL6: PRKD2; NbExp=6; IntAct=EBI-1048378, EBI-1384325; Q8WUI4; P31947: SFN; NbExp=3; IntAct=EBI-1048378, EBI-476295; Q8WUI4; P63104: YWHAZ; NbExp=4; IntAct=EBI-1048378, EBI-347088; Q8WUI4; P08393: ICP0; Xeno; NbExp=3; IntAct=EBI-1048378, EBI-6148881; Q8WUI4; Q8CFN5: Mef2c; Xeno; NbExp=2; IntAct=EBI-1048378, EBI-643797; Q8WUI4-5; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-10276431, EBI-739580; Q8WUI4-5; Q04864: REL; NbExp=3; IntAct=EBI-10276431, EBI-307352; Q8WUI4-5; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-10276431, EBI-10226430; Q8WUI4-6; Q8WXI4-2: ACOT11; NbExp=3; IntAct=EBI-12094670, EBI-17721098; Q8WUI4-6; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-12094670, EBI-713602; Q8WUI4-6; Q03989: ARID5A; NbExp=3; IntAct=EBI-12094670, EBI-948603; Q8WUI4-6; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-12094670, EBI-10693038; Q8WUI4-6; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-12094670, EBI-18036948; Q8WUI4-6; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-12094670, EBI-739580; Q8WUI4-6; P60953: CDC42; NbExp=3; IntAct=EBI-12094670, EBI-81752; Q8WUI4-6; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-12094670, EBI-2350265; Q8WUI4-6; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12094670, EBI-742054; Q8WUI4-6; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-12094670, EBI-12260294; Q8WUI4-6; Q9UBI6: GNG12; NbExp=3; IntAct=EBI-12094670, EBI-358636; Q8WUI4-6; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12094670, EBI-5916454; Q8WUI4-6; A5PKX9: INADL; NbExp=3; IntAct=EBI-12094670, EBI-12035052; Q8WUI4-6; Q9BXK1: KLF16; NbExp=3; IntAct=EBI-12094670, EBI-5457991; Q8WUI4-6; Q6ZNG9: KRBA2; NbExp=3; IntAct=EBI-12094670, EBI-13309813; Q8WUI4-6; O43679: LDB2; NbExp=3; IntAct=EBI-12094670, EBI-2865580; Q8WUI4-6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12094670, EBI-16439278; Q8WUI4-6; Q9BRT3: MIEN1; NbExp=5; IntAct=EBI-12094670, EBI-6137472; Q8WUI4-6; O95411: MYO18A; NbExp=3; IntAct=EBI-12094670, EBI-302378; Q8WUI4-6; O00746: NME4; NbExp=3; IntAct=EBI-12094670, EBI-744871; Q8WUI4-6; Q9BQI9: NRIP2; NbExp=6; IntAct=EBI-12094670, EBI-3913975; Q8WUI4-6; B7ZLY0: PHC2; NbExp=3; IntAct=EBI-12094670, EBI-14568740; Q8WUI4-6; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-12094670, EBI-710402; Q8WUI4-6; P63000: RAC1; NbExp=4; IntAct=EBI-12094670, EBI-413628; Q8WUI4-6; P15153: RAC2; NbExp=3; IntAct=EBI-12094670, EBI-489652; Q8WUI4-6; P60763: RAC3; NbExp=3; IntAct=EBI-12094670, EBI-767084; Q8WUI4-6; Q04864-2: REL; NbExp=3; IntAct=EBI-12094670, EBI-10829018; Q8WUI4-6; Q0D2K3: RIPPLY1; NbExp=6; IntAct=EBI-12094670, EBI-10226430; Q8WUI4-6; P62070: RRAS2; NbExp=3; IntAct=EBI-12094670, EBI-491037; Q8WUI4-6; O15427: SLC16A3; NbExp=3; IntAct=EBI-12094670, EBI-7600166; Q8WUI4-6; O94964-4: SOGA1; NbExp=3; IntAct=EBI-12094670, EBI-14083835; Q8WUI4-6; O95164: UBL3; NbExp=3; IntAct=EBI-12094670, EBI-12876508; Nucleus. Cytoplasm. Note=In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. Treatment with EDN1 results in shuttling from the nucleus to the perinuclear region. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation. Event=Alternative splicing; Named isoforms=10; Name=1; IsoId=Q8WUI4-1; Sequence=Displayed; Name=2; IsoId=Q8WUI4-2; Sequence=VSP_007429, VSP_007431; Name=3; IsoId=Q8WUI4-3; Sequence=VSP_008772; Name=4; IsoId=Q8WUI4-4; Sequence=VSP_007430; Name=5; IsoId=Q8WUI4-5; Sequence=VSP_038104; Name=6; IsoId=Q8WUI4-6; Sequence=VSP_038105; Name=7; IsoId=Q8WUI4-7; Sequence=VSP_038104, VSP_008772; Name=8; IsoId=Q8WUI4-8; Sequence=VSP_038106, VSP_038107; Name=9; IsoId=Q8WUI4-9; Sequence=VSP_038102; Name=10; IsoId=Q8WUI4-10; Sequence=VSP_038103; The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm. May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-155 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-155 is a prerequisite for phosphorylation at Ser-181. Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor. Belongs to the histone deacetylase family. HD type 2 subfamily. Sequence=AAF63491.1; Type=Frameshift; Evidence=; Sequence=BAA91474.1; Type=Erroneous initiation; Evidence=; Sequence=BAA91545.1; Type=Erroneous initiation; Evidence=; Sequence=BAB15759.1; Type=Erroneous initiation; Evidence=; Sequence=BAB55363.1; Type=Erroneous initiation; Evidence=; Sequence=BAC56929.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence=; histone deacetylase complex negative regulation of transcription from RNA polymerase II promoter vasculogenesis chromatin binding transcription corepressor activity histone deacetylase activity protein kinase C binding protein binding nucleus nucleoplasm cytoplasm cytosol chromatin organization cell-cell junction assembly histone deacetylation hydrolase activity protein kinase binding NAD-dependent histone deacetylase activity (H3-K14 specific) negative regulation of interleukin-2 production activating transcription factor binding negative regulation of osteoblast differentiation negative regulation of transcription, DNA-templated metal ion binding repressing transcription factor binding histone H3 deacetylation 14-3-3 protein binding positive regulation of cell migration involved in sprouting angiogenesis negative regulation of NIK/NF-kappaB signaling uc010slo.1 uc010slo.2 uc010slo.3 uc010slo.4 
ENST00000081029.8 MRPS35 ENST00000081029.8 mitochondrial ribosomal protein S35, transcript variant 1 (from RefSeq NM_021821.4) ENST00000081029.1 ENST00000081029.2 ENST00000081029.3 ENST00000081029.4 ENST00000081029.5 ENST00000081029.6 ENST00000081029.7 HDCMD11P MDS023 MRPS28 MRPS35 NM_021821 P82673 PSEC0213 Q32LZ1 Q6P4C6 Q7L1M6 Q8NBP4 Q96AI0 Q9H044 Q9HC14 Q9P1R5 RT35_HUMAN uc001rih.1 uc001rih.2 uc001rih.3 uc001rih.4 uc001rih.5 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that has had confusing nomenclature in the literature. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Pseudogenes corresponding to this gene are found on chromosomes 3p, 5q, and 10q. [provided by RefSeq, Jul 2010]. Component of the mitochondrial small ribosomal subunit (mt- SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins. Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1 ; IsoId=P82673-1; Sequence=Displayed; Name=2 ; IsoId=P82673-2; Sequence=VSP_054096, VSP_054097; Belongs to the mitochondrion-specific ribosomal protein mS35 family. Sequence=AAG14958.1; Type=Frameshift; Evidence=; RNA binding structural constituent of ribosome mitochondrion mitochondrial inner membrane mitochondrial small ribosomal subunit ribosome mitochondrial translation DNA damage response, detection of DNA damage mitochondrial translational elongation mitochondrial translational termination uc001rih.1 uc001rih.2 uc001rih.3 uc001rih.4 uc001rih.5 
ENST00000083182.8 APPBP2 ENST00000083182.8 amyloid beta precursor protein binding protein 2, transcript variant 1 (from RefSeq NM_006380.5) A8K862 APBP2_HUMAN APPBP2 ENST00000083182.1 ENST00000083182.2 ENST00000083182.3 ENST00000083182.4 ENST00000083182.5 ENST00000083182.6 ENST00000083182.7 KIAA0228 NM_006380 O95095 PAT1 Q8WVC9 Q92624 uc002iys.1 uc002iys.2 uc002iys.3 uc002iys.4 The protein encoded by this gene interacts with microtubules and is functionally associated with beta-amyloid precursor protein transport and/or processing. The beta-amyloid precursor protein is a cell surface protein with signal-transducing properties, and it is thought to play a role in the pathogenesis of Alzheimer's disease. The encoded protein may be involved in regulating cell death. This gene has been found to be highly expressed in breast cancer. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]. Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948, PubMed:29775578). The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29779948, PubMed:29775578). The CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa- Xaa-Gly degron at the C-terminus, leading to their ubiquitination and degradation (PubMed:29779948, PubMed:29775578). The CRL2(APPBP2) complex mediates ubiquitination and degradation of truncated SELENOV selenoproteins produced by failed UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron (PubMed:26138980). May play a role in intracellular protein transport: may be involved in the translocation of APP along microtubules toward the cell surface (PubMed:9843960). E3 ubiquitin-protein ligase activity of the CRL2(APPBP2) complex is inhibited by APP. Protein modification; protein ubiquitination. Component of a CRL2 E3 ubiquitin-protein ligase complex, also named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter APPBP2 (PubMed:29779948, PubMed:29775578). Interacts with APP; APP interaction inhibits the E3 ubiquitin-protein ligase activity of the CRL2(APPBP2) complex (PubMed:9843960, PubMed:29775578). Q92624; P22760: AADAC; NbExp=3; IntAct=EBI-743771, EBI-13217105; Q92624; P12814: ACTN1; NbExp=3; IntAct=EBI-743771, EBI-351710; Q92624; P23526: AHCY; NbExp=3; IntAct=EBI-743771, EBI-1053240; Q92624; Q9UIJ7: AK3; NbExp=6; IntAct=EBI-743771, EBI-3916527; Q92624; O75891-4: ALDH1L1; NbExp=3; IntAct=EBI-743771, EBI-12400198; Q92624; Q8IUW1: ANKRD10; NbExp=3; IntAct=EBI-743771, EBI-10261416; Q92624; Q9NXR5: ANKRD10; NbExp=3; IntAct=EBI-743771, EBI-10316475; Q92624; P05067: APP; NbExp=3; IntAct=EBI-743771, EBI-77613; Q92624; Q6P1M9: ARMCX5; NbExp=6; IntAct=EBI-743771, EBI-10252512; Q92624; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-743771, EBI-12069500; Q92624; Q4VC05-2: BCL7A; NbExp=3; IntAct=EBI-743771, EBI-12065992; Q92624; Q9UBW5: BIN2; NbExp=3; IntAct=EBI-743771, EBI-2042570; Q92624; Q9BTE2: C16orf35; NbExp=3; IntAct=EBI-743771, EBI-10298364; Q92624; Q9BV19: C1orf50; NbExp=6; IntAct=EBI-743771, EBI-2874661; Q92624; Q5I0X4: C6orf226; NbExp=6; IntAct=EBI-743771, EBI-10244057; Q92624; B4DJ51: CALM1; NbExp=3; IntAct=EBI-743771, EBI-10171450; Q92624; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-743771, EBI-9083477; Q92624; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-743771, EBI-2836773; Q92624; Q00536: CDK16; NbExp=3; IntAct=EBI-743771, EBI-726261; Q92624; P35523: CLCN1; NbExp=6; IntAct=EBI-743771, EBI-10206780; Q92624; Q17RW2: COL24A1; NbExp=6; IntAct=EBI-743771, EBI-2529266; Q92624; Q9UQ03: CORO2B; NbExp=6; IntAct=EBI-743771, EBI-723376; Q92624; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-743771, EBI-9087876; Q92624; P78368: CSNK1G2; NbExp=3; IntAct=EBI-743771, EBI-748380; Q92624; P09228: CST2; NbExp=3; IntAct=EBI-743771, EBI-8832659; Q92624; Q2NKJ3: CTC1; NbExp=3; IntAct=EBI-743771, EBI-2562802; Q92624; P81605: DCD; NbExp=3; IntAct=EBI-743771, EBI-395625; Q92624; Q13268: DHRS2; NbExp=3; IntAct=EBI-743771, EBI-354324; Q92624; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-743771, EBI-8645574; Q92624; P16444: DPEP1; NbExp=3; IntAct=EBI-743771, EBI-749514; Q92624; Q14117: DPYS; NbExp=3; IntAct=EBI-743771, EBI-12275416; Q92624; Q96HE7: ERO1A; NbExp=3; IntAct=EBI-743771, EBI-2564539; Q92624; Q12841: FSTL1; NbExp=8; IntAct=EBI-743771, EBI-2349801; Q92624; P58549: FXYD7; NbExp=6; IntAct=EBI-743771, EBI-10216171; Q92624; Q14435-2: GALNT3; NbExp=3; IntAct=EBI-743771, EBI-10232904; Q92624; Q8N6F7: GCSAM; NbExp=6; IntAct=EBI-743771, EBI-10267082; Q92624; A0A0C4DFY5: GPRC5C; NbExp=3; IntAct=EBI-743771, EBI-12364679; Q92624; P09211: GSTP1; NbExp=6; IntAct=EBI-743771, EBI-353467; Q92624; Q04756: HGFAC; NbExp=3; IntAct=EBI-743771, EBI-1041722; Q92624; Q8NE63: HIPK4; NbExp=3; IntAct=EBI-743771, EBI-6381114; Q92624; A4FTV9: HIST1H2AK; NbExp=3; IntAct=EBI-743771, EBI-10173457; Q92624; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-743771, EBI-3918847; Q92624; P34932: HSPA4; NbExp=6; IntAct=EBI-743771, EBI-356933; Q92624; Q14164: IKBKE; NbExp=4; IntAct=EBI-743771, EBI-307369; Q92624; P16144-2: ITGB4; NbExp=3; IntAct=EBI-743771, EBI-11051601; Q92624; P18084: ITGB5; NbExp=3; IntAct=EBI-743771, EBI-1223434; Q92624; P50053-2: KHK; NbExp=3; IntAct=EBI-743771, EBI-12204387; Q92624; Q6ZMV9: KIF6; NbExp=3; IntAct=EBI-743771, EBI-751100; Q92624; O14901: KLF11; NbExp=3; IntAct=EBI-743771, EBI-948266; Q92624; Q6PF15: KLHL35; NbExp=6; IntAct=EBI-743771, EBI-9477654; Q92624; Q9NS86: LANCL2; NbExp=6; IntAct=EBI-743771, EBI-2510837; Q92624; Q496Y0: LONRF3; NbExp=3; IntAct=EBI-743771, EBI-2690768; Q92624; Q9Y383: LUC7L2; NbExp=6; IntAct=EBI-743771, EBI-352851; Q92624; Q9P127: LUZP4; NbExp=6; IntAct=EBI-743771, EBI-10198848; Q92624; Q9Y2E5: MAN2B2; NbExp=3; IntAct=EBI-743771, EBI-12243024; Q92624; Q9GZU1: MCOLN1; NbExp=3; IntAct=EBI-743771, EBI-721209; Q92624; Q9UQ53: MGAT4B; NbExp=3; IntAct=EBI-743771, EBI-725713; Q92624; P42568: MLLT3; NbExp=4; IntAct=EBI-743771, EBI-716132; Q92624; C0H5X0: MMP28; NbExp=3; IntAct=EBI-743771, EBI-12286419; Q92624; P43246: MSH2; NbExp=3; IntAct=EBI-743771, EBI-355888; Q92624; Q13421-3: MSLN; NbExp=3; IntAct=EBI-743771, EBI-12303989; Q92624; Q969V5: MUL1; NbExp=6; IntAct=EBI-743771, EBI-744120; Q92624; Q15746-7: MYLK; NbExp=3; IntAct=EBI-743771, EBI-12189939; Q92624; P23511: NFYA; NbExp=3; IntAct=EBI-743771, EBI-389739; Q92624; O14745: NHERF1; NbExp=3; IntAct=EBI-743771, EBI-349787; Q92624; Q9BRL4: PCTK1; NbExp=3; IntAct=EBI-743771, EBI-10296950; Q92624; Q7Z6Z6: PNPLA5; NbExp=3; IntAct=EBI-743771, EBI-12241582; Q92624; Q8IXY8: PPIL6; NbExp=3; IntAct=EBI-743771, EBI-12226639; Q92624; Q12972: PPP1R8; NbExp=3; IntAct=EBI-743771, EBI-716633; Q92624; Q12972-2: PPP1R8; NbExp=3; IntAct=EBI-743771, EBI-12252736; Q92624; P54646: PRKAA2; NbExp=3; IntAct=EBI-743771, EBI-1383852; Q92624; P22694: PRKACB; NbExp=3; IntAct=EBI-743771, EBI-2679622; Q92624; P07602: PSAP; NbExp=3; IntAct=EBI-743771, EBI-716699; Q92624; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-743771, EBI-14199621; Q92624; Q8N2H3: PYROXD2; NbExp=3; IntAct=EBI-743771, EBI-3919450; Q92624; Q96AH8: RAB7B; NbExp=3; IntAct=EBI-743771, EBI-3924400; Q92624; Q15382: RHEB; NbExp=3; IntAct=EBI-743771, EBI-1055287; Q92624; Q5EBL4-3: RILPL1; NbExp=3; IntAct=EBI-743771, EBI-12072024; Q92624; Q8TEB7: RNF128; NbExp=3; IntAct=EBI-743771, EBI-2341619; Q92624; Q969K3: RNF34; NbExp=3; IntAct=EBI-743771, EBI-2340642; Q92624; O60942: RNGTT; NbExp=3; IntAct=EBI-743771, EBI-1237132; Q92624; Q15050: RRS1; NbExp=7; IntAct=EBI-743771, EBI-749186; Q92624; P59797: SELENOV; NbExp=3; IntAct=EBI-743771, EBI-10216195; Q92624; Q8WU57: SELI; NbExp=3; IntAct=EBI-743771, EBI-751012; Q92624; Q4U2R8: SLC22A6; NbExp=3; IntAct=EBI-743771, EBI-749741; Q92624; Q9BV35: SLC25A23; NbExp=3; IntAct=EBI-743771, EBI-2933255; Q92624; Q9NS82: SLC7A10; NbExp=3; IntAct=EBI-743771, EBI-12068238; Q92624; Q9Y5X3: SNX5; NbExp=3; IntAct=EBI-743771, EBI-715760; Q92624; Q9Y5X3-2: SNX5; NbExp=3; IntAct=EBI-743771, EBI-12229025; Q92624; P0CI01: SPDYE6; NbExp=3; IntAct=EBI-743771, EBI-11960469; Q92624; O15466: ST8SIA5; NbExp=3; IntAct=EBI-743771, EBI-10182857; Q92624; Q9UMZ2: SYNRG; NbExp=3; IntAct=EBI-743771, EBI-7240490; Q92624; Q9UMZ2-8: SYNRG; NbExp=3; IntAct=EBI-743771, EBI-12353261; Q92624; Q9BT88: SYT11; NbExp=3; IntAct=EBI-743771, EBI-751770; Q92624; Q15544: TAF11; NbExp=6; IntAct=EBI-743771, EBI-1027005; Q92624; Q96LR4: TAFA4; NbExp=3; IntAct=EBI-743771, EBI-10290841; Q92624; Q12788: TBL3; NbExp=4; IntAct=EBI-743771, EBI-715766; Q92624; Q9BQ70: TCF25; NbExp=3; IntAct=EBI-743771, EBI-745182; Q92624; Q05952: TNP2; NbExp=3; IntAct=EBI-743771, EBI-12039775; Q92624; Q8IZ69: TRMT2A; NbExp=3; IntAct=EBI-743771, EBI-2515774; Q92624; Q712K3: UBE2R2; NbExp=3; IntAct=EBI-743771, EBI-2340879; Q92624; Q9NYU1: UGGT2; NbExp=3; IntAct=EBI-743771, EBI-1054215; Q92624; P42768: WAS; NbExp=3; IntAct=EBI-743771, EBI-346375; Q92624; Q96S15: WDR24; NbExp=4; IntAct=EBI-743771, EBI-746424; Q92624; Q96NZ8: WFIKKN1; NbExp=3; IntAct=EBI-743771, EBI-2363713; Q92624; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-743771, EBI-742550; Q92624; Q9BV97: ZNF747; NbExp=3; IntAct=EBI-743771, EBI-4395497; Q92624; Q9H669; NbExp=3; IntAct=EBI-743771, EBI-10307430; Nucleus Cytoplasm, cytoskeleton Membrane ; Peripheral membrane protein Note=Associated with membranes and microtubules. Rapidly degraded by the proteasome upon overexpression of a C- terminal fragment of APP. Sequence=BAA13217.1; Type=Erroneous initiation; Evidence=; microtubule motor activity protein binding nucleus cytoplasm cytoskeleton microtubule microtubule associated complex intracellular protein transport protein transport membrane cytoplasmic vesicle membrane intracellular transport uc002iys.1 uc002iys.2 uc002iys.3 uc002iys.4 
ENST00000084798.9 CA11 ENST00000084798.9 carbonic anhydrase 11, transcript variant 2 (from RefSeq NR_136241.2) CAH11_HUMAN CARP2 ENST00000084798.1 ENST00000084798.2 ENST00000084798.3 ENST00000084798.4 ENST00000084798.5 ENST00000084798.6 ENST00000084798.7 ENST00000084798.8 NR_136241 O60596 O75493 Q6FHI1 Q9UEC4 UNQ211/PRO237 uc002pjz.1 uc002pjz.2 uc002pjz.3 Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA XI is likely a secreted protein, however, radical changes at active site residues completely conserved in CA isozymes with catalytic activity, make it unlikely that it has carbonic anhydrase activity. It shares properties in common with two other acatalytic CA isoforms, CA VIII and CA X. CA XI is most abundantly expressed in brain, and may play a general role in the central nervous system. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7410570.656759.1, SRR3476690.395550.1 [ECO:0000332] ##Evidence-Data-END## Does not have a catalytic activity. Secreted Expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid. Belongs to the alpha-carbonic anhydrase family. extracellular region zinc ion binding basolateral plasma membrane carbonate dehydratase activity uc002pjz.1 uc002pjz.2 uc002pjz.3 
ENST00000085219.10 CD22 ENST00000085219.10 CD22 molecule, transcript variant 1 (from RefSeq NM_001771.4) CD22 ENST00000085219.1 ENST00000085219.2 ENST00000085219.3 ENST00000085219.4 ENST00000085219.5 ENST00000085219.6 ENST00000085219.7 ENST00000085219.8 ENST00000085219.9 NM_001771 Q0EAF5 Q0EAF5_HUMAN uc010edt.1 uc010edt.2 uc010edt.3 uc010edt.4 uc010edt.5 uc010edt.6 Membrane ; Single- pass type I membrane protein membrane integral component of membrane uc010edt.1 uc010edt.2 uc010edt.3 uc010edt.4 uc010edt.5 uc010edt.6 
ENST00000086933.3 GSC2 ENST00000086933.3 goosecoid homeobox 2 (from RefSeq NM_005315.2) ENST00000086933.1 ENST00000086933.2 GSC2_HUMAN GSCL NM_005315 O15499 uc011ags.1 uc011ags.2 uc011ags.3 uc011ags.4 Goosecoidlike (GSCL), a homeodomain-containing gene, resides in the critical region for VCFS/DGS on 22q11. Velocardiofacial syndrome (VCFS) is a developmental disorder characterized by conotruncal heart defects, craniofacial anomalies, and learning disabilities. VCFS is phenotypically related to DiGeorge syndrome (DGS) and both syndromes are associated with hemizygous 22q11 deletions. Because many of the tissues and structures affected in VCFS/DGS derive from the pharyngeal arches of the developing embryo, it is believed that haploinsufficiency of a gene involved in embryonic development may be responsible for its etiology. The gene is expressed in a limited number of adult tissues, as well as in early human development. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May have a role in development. May regulate its own transcription. May bind the bicoid consensus sequence TAATCC. O15499; P05187: ALPP; NbExp=3; IntAct=EBI-19954058, EBI-1211484; O15499; P08758: ANXA5; NbExp=3; IntAct=EBI-19954058, EBI-296601; O15499; Q12797-6: ASPH; NbExp=3; IntAct=EBI-19954058, EBI-12092171; O15499; Q8N1M1-5: BEST3; NbExp=3; IntAct=EBI-19954058, EBI-20140863; O15499; Q12982: BNIP2; NbExp=3; IntAct=EBI-19954058, EBI-752094; O15499; Q8N9M1-2: C19orf47; NbExp=3; IntAct=EBI-19954058, EBI-10979594; O15499; Q13901: C1D; NbExp=3; IntAct=EBI-19954058, EBI-3844053; O15499; P27797: CALR; NbExp=3; IntAct=EBI-19954058, EBI-1049597; O15499; P55273: CDKN2D; NbExp=3; IntAct=EBI-19954058, EBI-745859; O15499; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-19954058, EBI-752069; O15499; P27658: COL8A1; NbExp=3; IntAct=EBI-19954058, EBI-747133; O15499; O75575-2: CRCP; NbExp=3; IntAct=EBI-19954058, EBI-12880830; O15499; P68400: CSNK2A1; NbExp=3; IntAct=EBI-19954058, EBI-347804; O15499; Q9Y463: DYRK1B; NbExp=3; IntAct=EBI-19954058, EBI-634187; O15499; Q9H6Z9: EGLN3; NbExp=3; IntAct=EBI-19954058, EBI-1175354; O15499; P63241: EIF5A; NbExp=3; IntAct=EBI-19954058, EBI-373150; O15499; Q16134: ETFDH; NbExp=3; IntAct=EBI-19954058, EBI-2870454; O15499; A6H8Z2: FAM221B; NbExp=3; IntAct=EBI-19954058, EBI-12006844; O15499; O75344: FKBP6; NbExp=3; IntAct=EBI-19954058, EBI-744771; O15499; Q8NCW6-2: GALNT11; NbExp=3; IntAct=EBI-19954058, EBI-13364322; O15499; O75603: GCM2; NbExp=3; IntAct=EBI-19954058, EBI-10188645; O15499; Q6ZYL4: GTF2H5; NbExp=3; IntAct=EBI-19954058, EBI-6380438; O15499; Q9H1H1: GTSF1L; NbExp=3; IntAct=EBI-19954058, EBI-19128683; O15499; P43080: GUCA1A; NbExp=3; IntAct=EBI-19954058, EBI-6873005; O15499; P33402: GUCY1A2; NbExp=3; IntAct=EBI-19954058, EBI-6911715; O15499; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-19954058, EBI-2549423; O15499; Q2M1V0: ISX; NbExp=3; IntAct=EBI-19954058, EBI-6426064; O15499; O15550: KDM6A; NbExp=3; IntAct=EBI-19954058, EBI-4292203; O15499; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-19954058, EBI-6426443; O15499; O76011: KRT34; NbExp=3; IntAct=EBI-19954058, EBI-1047093; O15499; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-19954058, EBI-3958099; O15499; Q5T5B0: LCE3E; NbExp=3; IntAct=EBI-19954058, EBI-10245456; O15499; Q8WV07: LTO1; NbExp=3; IntAct=EBI-19954058, EBI-12249832; O15499; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-19954058, EBI-77889; O15499; P45984: MAPK9; NbExp=3; IntAct=EBI-19954058, EBI-713568; O15499; Q9Y4F3: MARF1; NbExp=3; IntAct=EBI-19954058, EBI-5235902; O15499; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-19954058, EBI-10172526; O15499; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-19954058, EBI-10288852; O15499; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-19954058, EBI-2513715; O15499; Q9Y3D9: MRPS23; NbExp=3; IntAct=EBI-19954058, EBI-1054270; O15499; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-19954058, EBI-744782; O15499; Q9UNF0: PACSIN2; NbExp=3; IntAct=EBI-19954058, EBI-742503; O15499; Q08493-2: PDE4C; NbExp=3; IntAct=EBI-19954058, EBI-12169289; O15499; O43741: PRKAB2; NbExp=3; IntAct=EBI-19954058, EBI-1053424; O15499; Q96BW5: PTER; NbExp=3; IntAct=EBI-19954058, EBI-4291023; O15499; Q9H7N4: SCAF1; NbExp=3; IntAct=EBI-19954058, EBI-1222181; O15499; O00560: SDCBP; NbExp=3; IntAct=EBI-19954058, EBI-727004; O15499; Q9BVW5: TIPIN; NbExp=3; IntAct=EBI-19954058, EBI-2515360; O15499; O14787-2: TNPO2; NbExp=3; IntAct=EBI-19954058, EBI-12076664; O15499; Q969E8: TSR2; NbExp=3; IntAct=EBI-19954058, EBI-746981; O15499; Q712K3: UBE2R2; NbExp=3; IntAct=EBI-19954058, EBI-2340879; O15499; Q3SXR9: VCX2; NbExp=3; IntAct=EBI-19954058, EBI-11983741; O15499; Q13426: XRCC4; NbExp=3; IntAct=EBI-19954058, EBI-717592; O15499; P62699: YPEL5; NbExp=3; IntAct=EBI-19954058, EBI-11721624; O15499; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-19954058, EBI-12010736; O15499; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-19954058, EBI-6427977; Nucleus Detected in adult testis and pituitary, and in 9-10 week fetal tissue (thorax). Probably expressed in other tissues at low levels. Expressed in early human development as well as in a limited number of adult tissues. Belongs to the paired homeobox family. Bicoid subfamily. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter anatomical structure morphogenesis sequence-specific DNA binding uc011ags.1 uc011ags.2 uc011ags.3 uc011ags.4 
ENST00000155093.8 ZFY ENST00000155093.8 zinc finger protein Y-linked, transcript variant 1 (from RefSeq NM_003411.4) B4DVF7 ENST00000155093.1 ENST00000155093.2 ENST00000155093.3 ENST00000155093.4 ENST00000155093.5 ENST00000155093.6 ENST00000155093.7 NM_003411 P08048 Q14021 Q15558 Q1RME9 Q24JR0 Q96TF3 ZFY_HUMAN uc004fqj.1 uc004fqj.2 uc004fqj.3 uc004fqj.4 uc004fqj.5 This gene encodes a zinc finger-containing protein that may function as a transcription factor. This gene was once a candidate gene for the testis-determining factor (TDF) and was erroneously referred to as TDF. [provided by RefSeq, Jul 2008]. Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'. P08048; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-12239601, EBI-9679045; P08048; Q9H8E8: KAT14; NbExp=3; IntAct=EBI-12239601, EBI-750907; P08048; Q969R5: L3MBTL2; NbExp=6; IntAct=EBI-12239601, EBI-739909; Nucleus. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P08048-1; Sequence=Displayed; Name=2; IsoId=P08048-2; Sequence=VSP_042774, VSP_042775; Name=3; IsoId=P08048-3; Sequence=VSP_042824, VSP_042825, VSP_042826; The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. Belongs to the krueppel C2H2-type zinc-finger protein family. ZFX/ZFY subfamily. Was originally thought to be the testis determining factor (TDF). RNA polymerase II transcription factor activity, sequence-specific DNA binding nucleic acid binding DNA binding protein binding nucleus nucleoplasm nucleolus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter metal ion binding uc004fqj.1 uc004fqj.2 uc004fqj.3 uc004fqj.4 uc004fqj.5 
ENST00000155840.12 KCNQ1 ENST00000155840.12 potassium voltage-gated channel subfamily Q member 1, transcript variant 4 (from RefSeq NM_001406837.1) ENST00000155840.1 ENST00000155840.10 ENST00000155840.11 ENST00000155840.2 ENST00000155840.3 ENST00000155840.4 ENST00000155840.5 ENST00000155840.6 ENST00000155840.7 ENST00000155840.8 ENST00000155840.9 KCNA8 KCNA9 KCNQ1 KCNQ1_HUMAN KVLQT1 NM_001406837 O00347 O60607 O94787 P51787 Q14D14 Q7Z6G9 Q92960 Q9UMN8 Q9UMN9 uc001lwn.1 uc001lwn.2 uc001lwn.3 uc001lwn.4 uc001lwn.5 uc001lwn.6 uc001lwn.7 Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (PubMed:10646604, PubMed:25441029). Associates with KCNE beta subunits that modulates current kinetics (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505, PubMed:19687231). Induces a voltage-dependent current by rapidly activating and slowly deactivating potassium-selective outward current (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505, PubMed:25441029). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (PubMed:10713961). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (PubMed:10646604). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP- induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (PubMed:11101505). When associated with KCNE4, inhibits voltage-gated potassium channel activity (PubMed:19687231). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (PubMed:12324418). Also forms a heterotetramer with KCNQ5; has a voltage-gated potassium channel activity (PubMed:24855057). Binds with phosphatidylinositol 4,5- bisphosphate (PubMed:25037568). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability. [Isoform 2]: Non-functional alone but modulatory when coexpressed with the full-length isoform 1. Tetramer (PubMed:18165683, PubMed:19693805, PubMed:25441029). Heterotetramer with KCNE1; targets to the membrane raft (PubMed:25037568, PubMed:19693805, PubMed:20533308). Interacts (via C- terminus) with CALM; forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner (PubMed:18165683, PubMed:25441029). Interacts with AKAP9; targets protein kinase A (PKA) catalytic and regulatory subunits and protein phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex, allowing PKA-mediated phosphorylation and increase of delayed rectifier potassium channel activity (PubMed:11799244, PubMed:25037568). Interacts with KCNE2; forms a heterooligomer complex that targets to the membrane raft and leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (PubMed:11101505, PubMed:20533308). Interacts with AP2M1; mediates estrogen-induced internalization via clathrin-coated vesicles (PubMed:23529131). Interacts with NEDD4L; promotes internalization and decreases I(Ks) currents (PubMed:23529131, PubMed:22024150). Interacts with USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restore plasma membrane localization (PubMed:22024150). Heterotetramer with KCNQ5; has a voltage-gated potassium channel activity (PubMed:24855057). Interacts with KCNE3; alters membrane raft localization (PubMed:20533308). Interacts with KCNE4; impairs KCNQ1 localization in lipid rafts and inhibits voltage-gated potassium channel activity (PubMed:19687231, PubMed:20533308). Interacts with KCNE5; impairs KCNQ1 localization in lipid rafts and only conducts current upon strong and continued depolarization (PubMed:20533308, PubMed:12324418). Interacts with SLC5A3; forms coregulatory channel- transporter complexes that modulate Na(+)-coupled myo-inositol influx through the transporter. P51787; P15382: KCNE1; NbExp=4; IntAct=EBI-359667, EBI-7043557; P51787-1; P62158: CALM3; NbExp=6; IntAct=EBI-15885881, EBI-397435; Cell membrane ulti-pass membrane protein Cytoplasmic vesicle membrane Early endosome Membrane raft Endoplasmic reticulum Basolateral cell membrane Apical cell membrane ; Multi-pass membrane protein Note=Colocalized with KCNE3 at the plasma membrane (PubMed:10646604). Upon 17beta-oestradiol treatment, colocalizes with RAB5A at early endosome (PubMed:23529131). Heterotetramer with KCNQ5 is highly retained at the endoplasmic reticulum and is localized outside of lipid raft microdomains (PubMed:24855057). During the early stages of epithelial cell polarization induced by the calcium switch, it is removed from the plasma membrane to the endoplasmic reticulum, where it is retained, and redistributed to the basolateral cell surface in a PI3K-dependent manner at a later stage (PubMed:21228319). Colocalizes with SLC5A3 at the apical membrane of choroid plexus epithelium. Event=Alternative splicing; Named isoforms=2; Comment=Additional isoforms seem to exist.; Name=1; IsoId=P51787-1; Sequence=Displayed; Name=2; Synonyms=TKvLQT1; IsoId=P51787-2; Sequence=VSP_000981, VSP_000982; Abundantly expressed in heart, pancreas, prostate, kidney, small intestine and peripheral blood leukocytes. Less abundant in placenta, lung, spleen, colon, thymus, testis and ovaries. The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. The coiled-coil domain mediates tetramerization. The segment S6 is involved in the inhibition of voltage-gated potassium channel activity by KCNE4. The C-terminal assembly domain promotes self-interactiona; allows functional channel. The C-terminal coiled-coil domain interacts with a single CALM molecule via the first two membrane-proximal helical regions, with CALM forming a clamp-like structure. Binding of CALM C-terminus to the first helical region is calcium-independent but is essential for assembly of the structure. Binding of CALM N-terminus to the second helical region is calcium-dependent and regulates electrophysiological activity of the channel. Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9. Ubiquitinated by NEDD4L; promotes internalization (PubMed:22024150). The ubiquitinylated form is internalized through a clathrin-mediated endocytosis by interacting with AP2M1 and is recycled back to the cell membrane via RAB4A and RAB11A (PubMed:23529131). Deubiquitinated by USP2; counteracts the NEDD4L-specific down- regulation of I(Ks) and restores the membrane localization. Long QT syndrome 1 (LQT1) [MIM:192500]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. te=The disease is caused by variants affecting the gene represented in this entry. Jervell and Lange-Nielsen syndrome 1 (JLNS1) [MIM:220400]: An autosomal recessive disorder characterized by congenital deafness, prolongation of the QT interval, syncopal attacks due to ventricular arrhythmias, and a high risk of sudden death. te=The disease is caused by variants affecting the gene represented in this entry. Atrial fibrillation, familial, 3 (ATFB3) [MIM:607554]: An autosomal dominant form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. Note=The disease is caused by variants affecting the gene represented in this entry. Short QT syndrome 2 (SQT2) [MIM:609621]: An autosomal dominant form of short QT syndrome, a heart disorder characterized by idiopathic persistently and uniformly short QT interval on ECG in the absence of structural heart disease in affected individuals. It can cause syncope and sudden death. Note=The disease is caused by variants affecting the gene represented in this entry. Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. te=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mutagenesis experiments were carried out by expressing in Xenopus oocytes or COS-7 cells KCNQ1 mutants either individually (homomultimers) or in combination with both wild-type KCNQ1 (mut/wt homomultimers) and minK (heteromultimers). Belongs to the potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.1/KCNQ1 sub-subfamily. Sequence=AAC51781.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence=; Sequence=BAA34739.1; Type=Frameshift; Evidence=; Name=Wikipedia; Note=KvLQT1 entry; URL="https://en.wikipedia.org/wiki/KvLQT1"; ion channel activity voltage-gated ion channel activity voltage-gated potassium channel activity delayed rectifier potassium channel activity potassium channel activity protein binding calmodulin binding phosphatidylinositol-4,5-bisphosphate binding cytoplasm lysosome endosome early endosome late endosome endoplasmic reticulum plasma membrane regulation of gene expression by genetic imprinting ion transport potassium ion transport sensory perception of sound regulation of heart contraction voltage-gated potassium channel complex protein phosphatase 1 binding positive regulation of heart rate outward rectifier potassium channel activity membrane integral component of membrane basolateral plasma membrane gene silencing cytoplasmic vesicle membrane cytoplasmic vesicle protein kinase A catalytic subunit binding protein kinase A regulatory subunit binding ion channel complex regulation of ion transmembrane transport cellular response to drug ion channel binding membrane raft inner ear development intestinal absorption transmembrane transport cardiac muscle contraction regulation of membrane repolarization regulation of ventricular cardiac muscle cell membrane repolarization regulation of atrial cardiac muscle cell membrane repolarization positive regulation of cardiac muscle contraction regulation of gastric acid secretion cardiac conduction renal absorption cellular response to cAMP potassium ion transmembrane transport cellular response to epinephrine stimulus cardiovascular system development ventricular cardiac muscle cell action potential voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization membrane repolarization membrane repolarization during action potential membrane repolarization during cardiac muscle cell action potential atrial cardiac muscle cell action potential voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization regulation of heart rate by cardiac conduction scaffold protein binding potassium ion export across plasma membrane membrane repolarization during atrial cardiac muscle cell action potential membrane repolarization during ventricular cardiac muscle cell action potential positive regulation of potassium ion transmembrane transport negative regulation of delayed rectifier potassium channel activity voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization negative regulation of voltage-gated potassium channel activity uc001lwn.1 uc001lwn.2 uc001lwn.3 uc001lwn.4 uc001lwn.5 uc001lwn.6 uc001lwn.7 
ENST00000155926.9 TRIB2 ENST00000155926.9 tribbles pseudokinase 2, transcript variant 1 (from RefSeq NM_021643.4) B2R851 D6W510 ENST00000155926.1 ENST00000155926.2 ENST00000155926.3 ENST00000155926.4 ENST00000155926.5 ENST00000155926.6 ENST00000155926.7 ENST00000155926.8 NM_021643 Q92519 TRB2 TRIB2 TRIB2_HUMAN uc002rbv.1 uc002rbv.2 uc002rbv.3 uc002rbv.4 uc002rbv.5 uc002rbv.6 This gene encodes one of three members of the Tribbles family. The Tribbles members share a Trb domain, which is homologous to protein serine-threonine kinases, but lacks the active site lysine and probably lacks a catalytic function. The Tribbles proteins interact and modulate the activity of signal transduction pathways in a number of physiological and pathological processes. This Tribbles member induces apoptosis of cells mainly of the hematopoietic origin. It has been identified as a protein up-regulated by inflammatory stimuli in myeloid (THP-1) cells, and also as an oncogene that inactivates the transcription factor C/EBPalpha (CCAAT/enhancer-binding protein alpha) and causes acute myelogenous leukemia. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Mar 2009]. Interacts with MAPK kinases and regulates activation of MAP kinases. Does not display kinase activity (By similarity). Interacts with COP1 (PubMed:27041596). Q92519; Q9HBI0: PARVG; NbExp=5; IntAct=EBI-947178, EBI-3921217; Q92519; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-947178, EBI-5235340; Cytoplasm Cytoplasm, cytoskeleton Note=May associate with the cytoskeleton. Highly expressed in peripheral blood leukocytes. The protein kinase domain is predicted to be catalytically inactive. Antibodies against TRIB2 are present in sera from patients with autoimmune uveitis. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Tribbles subfamily. protein kinase inhibitor activity nucleus cytoplasm cytoskeleton protein phosphorylation negative regulation of protein kinase activity transcription factor binding mitogen-activated protein kinase kinase binding ubiquitin protein ligase binding positive regulation of proteasomal ubiquitin-dependent protein catabolic process regulation of MAP kinase activity negative regulation of interleukin-10 biosynthetic process negative regulation of fat cell differentiation ubiquitin-protein transferase regulator activity nucleotide binding protein kinase activity uc002rbv.1 uc002rbv.2 uc002rbv.3 uc002rbv.4 uc002rbv.5 uc002rbv.6 
ENST00000156109.7 GPKOW ENST00000156109.7 G-patch domain and KOW motifs (from RefSeq NM_015698.6) ENST00000156109.1 ENST00000156109.2 ENST00000156109.3 ENST00000156109.4 ENST00000156109.5 ENST00000156109.6 GPATC5 GPATCH5 GPKOW_HUMAN NM_015698 Q59EK5 Q92917 Q9BQA8 T54 uc004dmr.1 uc004dmr.2 uc004dmr.3 uc004dmr.4 uc004dmr.5 uc004dmr.6 This gene encodes a putative RNA-binding protein containing G-patch and KOW (Kyprides, Ouzounis, Woese) domains. The encoded protein interacts directly with protein kinase A and protein kinase X and is also found associated with the spliceosome. [provided by RefSeq, Aug 2013]. ##Evidence-Data-START## Transcript exon combination :: SRR1660803.255113.1, SRR3476690.303268.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000156109.7/ ENSP00000156109.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## RNA-binding protein involved in pre-mRNA splicing. As a component of the minor spliceosome, involved in the splicing of U12- type introns in pre-mRNAs (Probable). Component of the minor spliceosome, which splices U12-type introns (PubMed:33509932). Interacts with PRKX (PubMed:16491121). Interacts with DHX16 (PubMed:25296192). Interacts with PRKACB (PubMed:21880142). Q92917; Q9P291: ARMCX1; NbExp=3; IntAct=EBI-746309, EBI-2843626; Q92917; Q9BRD0: BUD13; NbExp=12; IntAct=EBI-746309, EBI-2561235; Q92917; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-746309, EBI-2808286; Q92917; Q6P9H4: CNKSR3; NbExp=3; IntAct=EBI-746309, EBI-10253274; Q92917; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-746309, EBI-742054; Q92917; O60231: DHX16; NbExp=3; IntAct=EBI-746309, EBI-311446; Q92917; Q92620: DHX38; NbExp=2; IntAct=EBI-746309, EBI-1043041; Q92917; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-746309, EBI-2349927; Q92917; Q96IJ6: GMPPA; NbExp=3; IntAct=EBI-746309, EBI-750953; Q92917; Q08379: GOLGA2; NbExp=9; IntAct=EBI-746309, EBI-618309; Q92917; P46439: GSTM5; NbExp=3; IntAct=EBI-746309, EBI-4312072; Q92917; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-746309, EBI-10961706; Q92917; O75031: HSF2BP; NbExp=3; IntAct=EBI-746309, EBI-7116203; Q92917; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-746309, EBI-81279; Q92917; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-746309, EBI-2556193; Q92917; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-746309, EBI-739832; Q92917; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-746309, EBI-18273118; Q92917; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-746309, EBI-1216080; Q92917; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-746309, EBI-742610; Q92917; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-746309, EBI-16439278; Q92917; Q14696: MESD; NbExp=3; IntAct=EBI-746309, EBI-6165891; Q92917; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-746309, EBI-10172526; Q92917; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-746309, EBI-11522433; Q92917; O43189: PHF1; NbExp=3; IntAct=EBI-746309, EBI-530034; Q92917; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-746309, EBI-14066006; Q92917; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-746309, EBI-79165; Q92917; P62487: POLR2G; NbExp=3; IntAct=EBI-746309, EBI-347928; Q92917; P22694-2: PRKACB; NbExp=4; IntAct=EBI-746309, EBI-5258763; Q92917; P31321: PRKAR1B; NbExp=3; IntAct=EBI-746309, EBI-2805516; Q92917; P51817: PRKX; NbExp=2; IntAct=EBI-746309, EBI-4302903; Q92917; O43172: PRPF4; NbExp=2; IntAct=EBI-746309, EBI-718395; Q92917; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-746309, EBI-538479; Q92917; P98175: RBM10; NbExp=2; IntAct=EBI-746309, EBI-721525; Q92917; Q04864-2: REL; NbExp=3; IntAct=EBI-746309, EBI-10829018; Q92917; Q9HAT0: ROPN1; NbExp=6; IntAct=EBI-746309, EBI-1378139; Q92917; Q6FGM0: SH3GL1; NbExp=3; IntAct=EBI-746309, EBI-10173690; Q92917; Q99961: SH3GL1; NbExp=8; IntAct=EBI-746309, EBI-697911; Q92917; O60504: SORBS3; NbExp=3; IntAct=EBI-746309, EBI-741237; Q92917; A6NLX3: SPDYE4; NbExp=3; IntAct=EBI-746309, EBI-12047907; Q92917; P23193: TCEA1; NbExp=3; IntAct=EBI-746309, EBI-2608271; Q92917; Q15560: TCEA2; NbExp=7; IntAct=EBI-746309, EBI-710310; Q92917; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-746309, EBI-750109; Q92917; Q12933: TRAF2; NbExp=7; IntAct=EBI-746309, EBI-355744; Q92917; P36406: TRIM23; NbExp=4; IntAct=EBI-746309, EBI-740098; Q92917; P14373: TRIM27; NbExp=3; IntAct=EBI-746309, EBI-719493; Q92917; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-746309, EBI-2799833; Q92917; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-746309, EBI-12030590; Q92917; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-746309, EBI-527853; Nucleus Phosphorylation regulates its ability to bind RNA. Belongs to the MOS2 family. Sequence=AAB18640.1; Type=Frameshift; Evidence=; mRNA splicing, via spliceosome nucleic acid binding RNA binding protein binding nucleus nucleoplasm spliceosomal complex mRNA processing RNA splicing uc004dmr.1 uc004dmr.2 uc004dmr.3 uc004dmr.4 uc004dmr.5 uc004dmr.6 
ENST00000156471.10 AQR ENST00000156471.10 aquarius intron-binding spliceosomal factor (from RefSeq NM_014691.3) A0JP17 A5YKK3 AQR_HUMAN ENST00000156471.1 ENST00000156471.2 ENST00000156471.3 ENST00000156471.4 ENST00000156471.5 ENST00000156471.6 ENST00000156471.7 ENST00000156471.8 ENST00000156471.9 KIAA0560 NM_014691 O60306 Q2YDX9 Q6IRU8 Q6PIC8 uc001ziv.1 uc001ziv.2 uc001ziv.3 uc001ziv.4 uc001ziv.5 Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:25599396, PubMed:28502770, PubMed:28076346). Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis (PubMed:16949364). Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly (PubMed:16949364). May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing (PubMed:16949364). Has ATP-dependent RNA helicase activity and can unwind double-stranded RNA molecules with a 3' overhang (in vitro) (PubMed:25599396). Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence=; Identified in the spliceosome C complex (PubMed:11991638, PubMed:16949364, PubMed:25599396, PubMed:28502770, PubMed:28076346). Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE (PubMed:17981804). Identified in a pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a preassembled complex (PubMed:25599396). The IB complex does not contain PRPF19 (PubMed:25599396). Within the spliceosome, interacts with SNRPA1, SF3B1, SF3B3, SF3A1 and SF3A2 (PubMed:25599396). O60306; Q9ULR0: ISY1; NbExp=6; IntAct=EBI-2512328, EBI-2557660; O60306; Q9UNP9: PPIE; NbExp=9; IntAct=EBI-2512328, EBI-591818; O60306; Q9HCS7: XAB2; NbExp=6; IntAct=EBI-2512328, EBI-295232; O60306; Q96NB3: ZNF830; NbExp=11; IntAct=EBI-2512328, EBI-3920997; Nucleus cleus, nucleoplasm Note=Localizes to speckle-like regions of the nucleoplasm. Contains an N-terminal domain with structural similarity to ARM repeat regions; this domain functions as a scaffold for protein-protein interactions, but is not required for RNA binding or for ATP-dependent RNA helicase activity. Belongs to the CWF11 family. Sequence=BAA25486.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleotide binding mRNA splicing, via spliceosome RNA binding RNA helicase activity mRNA binding helicase activity protein binding ATP binding nucleus nucleoplasm spliceosomal complex transcription-coupled nucleotide-excision repair mRNA processing RNA splicing membrane hydrolase activity U2-type catalytic step 2 spliceosome catalytic step 2 spliceosome uc001ziv.1 uc001ziv.2 uc001ziv.3 uc001ziv.4 uc001ziv.5 
ENST00000156626.12 ST6GALNAC1 ENST00000156626.12 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 1, transcript variant 1 (from RefSeq NM_018414.5) ENST00000156626.1 ENST00000156626.10 ENST00000156626.11 ENST00000156626.2 ENST00000156626.3 ENST00000156626.4 ENST00000156626.5 ENST00000156626.6 ENST00000156626.7 ENST00000156626.8 ENST00000156626.9 NM_018414 Q6UW90 Q9NSC6 Q9NSC7 SIA7A_HUMAN SIAT7A ST6GALNAC1 UNQ543/PRO848 uc002jsh.1 uc002jsh.2 uc002jsh.3 uc002jsh.4 uc002jsh.5 uc002jsh.6 Glycosylation of proteins affects cell-cell interaction, interactions with the matrix, and the functions of intracellular molecules. ST6GALNAC1 transfers a sialic acid, N-acetylneuraminic acid (NeuAc), in an alpha-2,6 linkage to O-linked GalNAc residues. The cancer-associated sialyl-Tn (sTn) antigen is formed by ST6GALNAC1-catalyzed sialylation of GalNAc residues on mucins (Ikehara et al., 1999 [PubMed 10536037]; Sewell et al., 2006 [PubMed 16319059]).[supplied by OMIM, Mar 2008]. Protein sialyltransferase specifically expressed in goblet cells that plays a key role in intestinal host-commensal homeostasis (PubMed:35303419). Conjugates sialic acid with an alpha-2-6 linkage to N-acetylgalactosamine (GalNAc) glycan chains linked to serine or threonine in glycoproteins (PubMed:16319059, PubMed:35303419). Catalyzes the formation of the sialyl-Tn (S-Tn) antigen, an antigen found in intestinal goblet cells, as well as ulcerative colitis (UC) and various cancers (PubMed:16319059, PubMed:35303419). Protein sialylation in globlet cells is essential for mucus integrity and is required to protect the intestinal mucus against excessive bacterial proteolytic degradation (PubMed:35303419). Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl- (1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D- galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:11136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:133470, ChEBI:CHEBI:140764; EC=2.4.3.3; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11137; Evidence=; Protein modification; protein glycosylation. Q9NSC7; P13569: CFTR; NbExp=5; IntAct=EBI-2854712, EBI-349854; Golgi apparatus membrane ; Single-pass type II membrane protein Expression is restricted to the gastrointestinal tract (PubMed:16319059). Highly expressed in goblet cells (PubMed:35303419). Also expressed in various tumor cells (PubMed:16319059). Glycosylated; autosialylated. Note=Inflammatory bowel disease (PubMed:35303419). A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology (PubMed:35303419). It is subdivided into Crohn disease and ulcerative colitis phenotypes (PubMed:35303419). Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon (PubMed:35303419). Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas (PubMed:35303419). In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed (PubMed:35303419). Both diseases include extraintestinal inflammation of the skin, eyes, or joints (PubMed:35303419). Disease susceptibility is associated with variants affecting the gene represented in this entry (PubMed:35303419). Belongs to the glycosyltransferase 29 family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44087/ST6GALNAC1"; Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc I; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_630"; Name=Protein Spotlight; Note=The slime inside us - Issue 257 of April 2023; URL="https://www.proteinspotlight.org/back_issues/257/"; Golgi membrane alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity Golgi apparatus protein glycosylation sialyltransferase activity oligosaccharide biosynthetic process membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups sialylation uc002jsh.1 uc002jsh.2 uc002jsh.3 uc002jsh.4 uc002jsh.5 uc002jsh.6 
ENST00000157600.8 LMCD1 ENST00000157600.8 LIM and cysteine rich domains 1, transcript variant 1 (from RefSeq NM_014583.4) B4DG80 ENST00000157600.1 ENST00000157600.2 ENST00000157600.3 ENST00000157600.4 ENST00000157600.5 ENST00000157600.6 ENST00000157600.7 LMCD1_HUMAN NM_014583 Q9NZU5 uc010hci.1 uc010hci.2 uc010hci.3 uc010hci.4 uc010hci.5 This gene encodes a member of the LIM-domain family of zinc finger proteins. The encoded protein contains an N-terminal cysteine-rich domain and two C-terminal LIM domains. The presence of LIM domains suggests involvement in protein-protein interactions. The protein may act as a co-regulator of transcription along with other transcription factors. Alternate splicing results in multiple transcript variants of this gene. [provided by RefSeq, May 2013]. Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6- mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC promoter (By similarity). Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway. Interacts with GATA1 and GATA4 (By similarity). Interacts with beta-dystroglycan. Interacts with GATA6. Q9NZU5; P47224: RABIF; NbExp=3; IntAct=EBI-5774016, EBI-713992; Q9NZU5; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-5774016, EBI-750487; Cytoplasm Nucleus Note=May shuttle between the cytoplasm and the nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NZU5-1; Sequence=Displayed; Name=2; IsoId=Q9NZU5-2; Sequence=VSP_053895; Expressed in the heart (at protein level). Expressed in many tissues with highest abundance in skeletal muscle. The LIM zinc-binding domains and the Cys-rich region mediate interaction with GATA6. negative regulation of transcription from RNA polymerase II promoter transcription corepressor activity nucleus nucleoplasm cytoplasm zinc ion binding regulation of cardiac muscle hypertrophy cellular protein metabolic process metal ion binding positive regulation of calcineurin-NFAT signaling cascade uc010hci.1 uc010hci.2 uc010hci.3 uc010hci.4 uc010hci.5 
ENST00000157812.7 PSMC4 ENST00000157812.7 proteasome 26S subunit, ATPase 4, transcript variant 1 (from RefSeq NM_006503.4) ENST00000157812.1 ENST00000157812.2 ENST00000157812.3 ENST00000157812.4 ENST00000157812.5 ENST00000157812.6 MIP224 NM_006503 P43686 PRS6B_HUMAN Q96FV5 Q9UBM3 Q9UEX3 TBP7 uc002omq.1 uc002omq.2 uc002omq.3 uc002omq.4 uc002omq.5 uc002omq.6 The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a member of the triple-A family of ATPases that is a component of the 19S regulatory subunit and plays a role in 26S proteasome assembly. The encoded protein interacts with gankyrin, a liver oncoprotein, and may also play a role in Parkinson's disease through interactions with synphilin-1. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jul 2012]. Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC4 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC4 and few additional components (PubMed:27428775, PubMed:27342858). Interacts with NR1I3. Interacts with PAAF1 (PubMed:15831487). Interacts with TRIM5 (PubMed:22078707). Interacts with ZFAND1 (PubMed:29804830). P43686; P27797: CALR; NbExp=3; IntAct=EBI-743997, EBI-1049597; P43686; P36957: DLST; NbExp=5; IntAct=EBI-743997, EBI-351007; P43686; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-743997, EBI-1055945; P43686; P62191: PSMC1; NbExp=2; IntAct=EBI-743997, EBI-357598; P43686; P62195: PSMC5; NbExp=15; IntAct=EBI-743997, EBI-357745; P43686; P62333: PSMC6; NbExp=5; IntAct=EBI-743997, EBI-357669; P43686; O75832: PSMD10; NbExp=23; IntAct=EBI-743997, EBI-752185; P43686; Q9Z2X2: Psmd10; Xeno; NbExp=4; IntAct=EBI-743997, EBI-8377084; P43686-2; P00441: SOD1; NbExp=3; IntAct=EBI-21522939, EBI-990792; Cytoplasm. Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P43686-1; Sequence=Displayed; Name=2; IsoId=P43686-2; Sequence=VSP_000022; Belongs to the AAA ATPase family. MAPK cascade nucleotide binding protein polyubiquitination proteasome complex blastocyst development stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent protein binding ATP binding nucleus nucleoplasm cytoplasm cytosol proteolysis regulation of cellular amino acid metabolic process proteasome regulatory particle, base subcomplex negative regulation of G2/M transition of mitotic cell cycle membrane inclusion body protein deubiquitination hydrolase activity ATPase activity proteasome accessory complex protein catabolic process anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process cytosolic proteasome complex tumor necrosis factor-mediated signaling pathway proteasome-activating ATPase activity NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process regulation of mRNA stability post-translational protein modification synapse positive regulation of RNA polymerase II transcriptional preinitiation complex assembly T cell receptor signaling pathway transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway positive regulation of proteasomal protein catabolic process regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation uc002omq.1 uc002omq.2 uc002omq.3 uc002omq.4 uc002omq.5 uc002omq.6 
ENST00000158009.6 FNDC8 ENST00000158009.6 fibronectin type III domain containing 8 (from RefSeq NM_017559.4) B2R9G6 ENST00000158009.1 ENST00000158009.2 ENST00000158009.3 ENST00000158009.4 ENST00000158009.5 FNDC8_HUMAN NM_017559 Q8TC99 Q9UFC2 uc002hix.1 uc002hix.2 uc002hix.3 uc002hix.4 uc002hix.5 Q8TC99; Q15013: MAD2L1BP; NbExp=3; IntAct=EBI-12903902, EBI-712181; Q8TC99; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-12903902, EBI-348259; Q8TC99; Q92569: PIK3R3; NbExp=3; IntAct=EBI-12903902, EBI-79893; Q8TC99; Q147U7: SMCO1; NbExp=3; IntAct=EBI-12903902, EBI-11735944; Q8TC99; P36508: ZNF76; NbExp=3; IntAct=EBI-12903902, EBI-7254550; nucleus uc002hix.1 uc002hix.2 uc002hix.3 uc002hix.4 uc002hix.5 
ENST00000158762.8 ACAP1 ENST00000158762.8 ArfGAP with coiled-coil, ankyrin repeat and PH domains 1 (from RefSeq NM_014716.4) ACAP1_HUMAN CENTB1 ENST00000158762.1 ENST00000158762.2 ENST00000158762.3 ENST00000158762.4 ENST00000158762.5 ENST00000158762.6 ENST00000158762.7 KIAA0050 NM_014716 Q15027 Q53XN9 uc002ggd.1 uc002ggd.2 uc002ggd.3 uc002ggd.4 GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration. GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. Banana-shaped homodimer laterally assembling into tetramers, the tetramers further pack helically onto the membrane. Interacts with GTP-bound ARF6. Interacts with third cytoplasmic loop of SLC2A4/GLUT4. Interacts with CLTC. Interacts with GULP1. Forms a complex with GDP- bound ARF6 and GULP1. Interacts with ITGB1; required for ITGB1 recycling. Q15027; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-751746, EBI-11958845; Q15027; P62993: GRB2; NbExp=3; IntAct=EBI-751746, EBI-401755; Q15027; Q92993: KAT5; NbExp=3; IntAct=EBI-751746, EBI-399080; Q15027; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-751746, EBI-11742507; Q15027; O76041: NEBL; NbExp=3; IntAct=EBI-751746, EBI-2880203; Q15027; P17252: PRKCA; NbExp=3; IntAct=EBI-751746, EBI-1383528; Q15027; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-751746, EBI-9090795; Q15027; P14927: UQCRB; NbExp=3; IntAct=EBI-751746, EBI-743128; Q15027; P22695: UQCRC2; NbExp=3; IntAct=EBI-751746, EBI-1051424; Q15027; P61981: YWHAG; NbExp=3; IntAct=EBI-751746, EBI-359832; Recycling endosome membrane ; Peripheral membrane protein ; Cytoplasmic side Highest level in lung and spleen. Low level in heart, kidney, liver and pancreas. PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate ACAP1-binding to PIP2 or PIP3 containing membranes. Only one PH domain of one ACAP1 dimer inserts into the membrane, while the other PH domain acts primaryly to interact with adjacent ACAP1 dimers. The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions. Phosphorylation at Ser-554 by PKB is required for interaction with ITGB1, export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration. Cells overexpressing ACAP1 show an accumulation of ITGB1 in recycling endosomes and inhibition of stimulation-dependent cell migration. Cells with reduced levels of ACAP1 or AKT1 and AKT2 show inhibition of stimulation-dependent cell migration. Cells overexpressing ACAP1 and PIP5K1C show formation of tubular structures derived from endosomal membranes. Sequence=BAA06418.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; GTPase activator activity protein binding endosome protein transport membrane positive regulation of GTPase activity metal ion binding recycling endosome membrane uc002ggd.1 uc002ggd.2 uc002ggd.3 uc002ggd.4 
ENST00000158771.9 DERL2 ENST00000158771.9 derlin 2, transcript variant 5 (from RefSeq NR_130906.2) CGI-101 DER2 DERL2 DERL2_HUMAN ENST00000158771.1 ENST00000158771.2 ENST00000158771.3 ENST00000158771.4 ENST00000158771.5 ENST00000158771.6 ENST00000158771.7 ENST00000158771.8 FLANA NR_130906 Q9GZP9 Q9Y3A7 SBBI53 uc002gcc.1 uc002gcc.2 uc002gcc.3 Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. DERL2 is involved in the degradation of misfolded glycoproteins in the ER (Oda et al., 2006 [PubMed 16449189]).[supplied by OMIM, Mar 2008]. Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins (PubMed:16186509, PubMed:16449189). May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908). (Microbial infection) In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. Forms homo- and heterooligomers with DERL3 and, to a lesser extent, with DERL1 (PubMed:16186509). Interacts with the SEL1L/SYVN1 and VCP/SELENOS protein complexes (PubMed:16186509). Mediates association between VCP and EDEM1, as well as that between VCP and the misfolded glycoproteins (PubMed:16449189). Interacts with OS9 (PubMed:19084021). Interacts with SELENOK and SELENOS (PubMed:22016385). Interacts with the signal recognition particle/SRP and the SRP receptor; in the process of endoplasmic reticulum stress- induced pre-emptive quality control (PubMed:26565908). Interacts with CCDC47 (By similarity). Q9GZP9; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-7962814, EBI-517508; Q9GZP9; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-7962814, EBI-713304; Q9GZP9; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-7962814, EBI-10172290; Q9GZP9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-7962814, EBI-10171774; Q9GZP9; Q00013: MPP1; NbExp=3; IntAct=EBI-7962814, EBI-711788; Q9GZP9; P43378: PTPN9; NbExp=3; IntAct=EBI-7962814, EBI-742898; Q9GZP9; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-7962814, EBI-3232108; Q9GZP9; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-7962814, EBI-2854842; Endoplasmic reticulum membrane ; Multi-pass membrane protein Ubiquitous. Overexpressed in various hepatocarcinomas. Up-regulated in response to endoplasmic reticulum stress via the ERN1-XBP1 pathway of the unfolded protein response (UPR). Belongs to the derlin family. Sequence=AAD34096.1; Type=Frameshift; Evidence=; Hrd1p ubiquitin ligase ERAD-L complex suckling behavior protein binding early endosome late endosome endoplasmic reticulum endoplasmic reticulum membrane response to unfolded protein positive regulation of cell proliferation membrane integral component of membrane integral component of endoplasmic reticulum membrane positive regulation of cell growth ER-associated ubiquitin-dependent protein catabolic process endoplasmic reticulum unfolded protein response retrograde protein transport, ER to cytosol endoplasmic reticulum quality control compartment misfolded protein binding negative regulation of retrograde protein transport, ER to cytosol endoplasmic reticulum mannose trimming ubiquitin-specific protease binding signal recognition particle receptor complex signal recognition particle uc002gcc.1 uc002gcc.2 uc002gcc.3 
ENST00000159060.3 NOX3 ENST00000159060.3 NADPH oxidase 3 (from RefSeq NM_015718.3) ENST00000159060.1 ENST00000159060.2 MOX2 NM_015718 NOX3_HUMAN Q9HBJ9 Q9HBY0 uc003qqm.1 uc003qqm.2 uc003qqm.3 uc003qqm.4 uc003qqm.5 This gene encodes a member of the NOX family of NADPH oxidases. These enzymes have the capacity to generate superoxide and other reactive oxygen species (ROS) and transport electrons across the plasma membrane. The ROS generated by family members have been implicated in numerous biological functions including host defense, posttranlational processing of proteins, cellular signaling, regulation of gene expression, and cell differentiation. The protein encoded by this gene is expressed predominantly in the inner ear and is involved in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity.[provided by RefSeq, May 2009]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF190122.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA2142680, SAMEA2144333 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000159060.3/ ENSP00000159060.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor, upon formation of a complex with CYBA/p22phox (PubMed:15181005, PubMed:15824103). Plays a role in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity (By similarity). Reaction=NADPH + 2 O2 = H(+) + NADP(+) + 2 superoxide; Xref=Rhea:RHEA:63180, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18421, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Activated by the ototoxic drug cisplatin (By similarity). Activated by NOXO1. Cooperatively activated by NCF1 and NCF2 or NOXA1 in a phorbol 12-myristate 13-acetate (PMA)-dependent manner. Inhibited by diphenyleneiodonium chloride. Interacts with CYBA/p22phox (PubMed:15824103). Heterodimerization with CYBA/p22phox is essential for its activity and cell membrane localization (By similarity). Q9HBY0; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-13069010, EBI-2680384; Cell membrane ; Multi-pass membrane protein Expressed in fetal kidney and to a lower extent in liver, lung and spleen. N-glycosylated in a CYBA/p22phox-dependent manner. temperature homeostasis cytoplasm plasma membrane defense response detection of gravity response to gravity membrane integral component of membrane superoxide-generating NADPH oxidase activity oxidoreductase activity superoxide anion generation NADPH oxidase complex otolith development oxidation-reduction process extracellular exosome uc003qqm.1 uc003qqm.2 uc003qqm.3 uc003qqm.4 uc003qqm.5 
ENST00000159087.7 ANO8 ENST00000159087.7 anoctamin 8 (from RefSeq NM_020959.3) A6NIJ0 ANO8_HUMAN ENST00000159087.1 ENST00000159087.2 ENST00000159087.3 ENST00000159087.4 ENST00000159087.5 ENST00000159087.6 KIAA1623 NM_020959 Q9HCE9 TMEM16H uc002ngf.1 uc002ngf.2 uc002ngf.3 Does not exhibit calcium-activated chloride channel (CaCC) activity. Cell membrane ulti-pass membrane protein Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9HCE9-1; Sequence=Displayed; Name=2; IsoId=Q9HCE9-2; Sequence=VSP_020351, VSP_020352; Expressed in embryonic stem cells, fetal brain and neural tissues. The term 'anoctamin' was coined because these channels are anion selective and have eight (OCT) transmembrane segments. There is some dissatisfaction in the field with the Ano nomenclature because it is not certain that all the members of this family are anion channels or have the 8-transmembrane topology. Belongs to the anoctamin family. Sequence=BAB13449.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; intracellular calcium activated chloride channel activity endoplasmic reticulum lumen plasma membrane chloride transport membrane integral component of membrane ion transmembrane transport post-translational protein modification cellular protein metabolic process uc002ngf.1 uc002ngf.2 uc002ngf.3 
ENST00000159111.9 KDM4B ENST00000159111.9 lysine demethylase 4B, transcript variant 1 (from RefSeq NM_015015.3) A0A0C4DFL8 A0A0C4DFL8_HUMAN ENST00000159111.1 ENST00000159111.2 ENST00000159111.3 ENST00000159111.4 ENST00000159111.5 ENST00000159111.6 ENST00000159111.7 ENST00000159111.8 KDM4B NM_015015 uc002mbq.1 uc002mbq.2 uc002mbq.3 uc002mbq.4 uc002mbq.5 uc002mbq.6 Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)- [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L- lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA- COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.66; Evidence=; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence=; Nucleus Belongs to the JHDM3 histone demethylase family. nucleus cytosol nuclear pericentric heterochromatin histone demethylase activity histone demethylase activity (H3-K9 specific) histone H3-K9 demethylation metal ion binding histone H3-K36 demethylation negative regulation of histone H3-K9 trimethylation uc002mbq.1 uc002mbq.2 uc002mbq.3 uc002mbq.4 uc002mbq.5 uc002mbq.6 
ENST00000160262.10 ICAM3 ENST00000160262.10 intercellular adhesion molecule 3, transcript variant 1 (from RefSeq NM_002162.5) ENST00000160262.1 ENST00000160262.2 ENST00000160262.3 ENST00000160262.4 ENST00000160262.5 ENST00000160262.6 ENST00000160262.7 ENST00000160262.8 ENST00000160262.9 ICAM3_HUMAN NM_002162 P32942 Q6PD68 uc002mob.1 uc002mob.2 uc002mob.3 uc002mob.4 The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2-9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein. This protein is constitutively and abundantly expressed by all leucocytes and may be the most important ligand for LFA-1 in the initiation of the immune response. It functions not only as an adhesion molecule, but also as a potent signalling molecule. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Feb 2016]. ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2) (PubMed:1448173). ICAM3 is also a ligand for integrin alpha-D/beta-2. In association with integrin alpha- L/beta-2, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590). Interacts with moesin/MSN. P32942; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-725421, EBI-12244618; P32942; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-725421, EBI-12256978; P32942; O14493: CLDN4; NbExp=3; IntAct=EBI-725421, EBI-9316372; P32942; P56851: EDDM3B; NbExp=3; IntAct=EBI-725421, EBI-10215665; P32942; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-725421, EBI-10317425; P32942; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-725421, EBI-8652744; P32942; P11686: SFTPC; NbExp=3; IntAct=EBI-725421, EBI-10197617; P32942; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-725421, EBI-8640191; P32942; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-725421, EBI-12188413; P32942; P30536: TSPO; NbExp=3; IntAct=EBI-725421, EBI-6623146; Membrane; Single-pass type I membrane protein. Leukocytes. Upon stimulation by a physiologic stimuli becomes rapidly and transiently phosphorylated on serine residues. N-glycosylated; glycans consist of a mixture of tri- and tetra- antennary complex-type chains and high-mannose chains. Belongs to the immunoglobulin superfamily. ICAM family. Name=Functional Glycomics Gateway - Glycan Binding; Note=ICAM-3; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_263"; stimulatory C-type lectin receptor signaling pathway receptor binding integrin binding protein binding plasma membrane integral component of plasma membrane phagocytosis cell adhesion membrane integral component of membrane extracellular matrix organization regulation of immune response extracellular exosome cell-cell adhesion uc002mob.1 uc002mob.2 uc002mob.3 uc002mob.4 
ENST00000160298.9 CAMSAP3 ENST00000160298.9 calmodulin regulated spectrin associated protein family member 3, transcript variant 2 (from RefSeq NM_020902.2) CAMP3_HUMAN CAMSAP3 ENST00000160298.1 ENST00000160298.2 ENST00000160298.3 ENST00000160298.4 ENST00000160298.5 ENST00000160298.6 ENST00000160298.7 ENST00000160298.8 KIAA1543 NM_020902 Q8NDF1 Q9P1Y5 uc002mgv.1 uc002mgv.2 uc002mgv.3 uc002mgv.4 uc002mgv.5 uc002mgv.6 Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19041755, PubMed:23169647). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153). Required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites (PubMed:19041755). Required for orienting the apical-to-basal polarity of microtubules in epithelial cells: acts by tethering non-centrosomal microtubules to the apical cortex, leading to their longitudinal orientation (PubMed:27802168, PubMed:26715742). Plays a key role in early embryos, which lack centrosomes: accumulates at the microtubule bridges that connect pairs of cells and enables the formation of a non-centrosomal microtubule- organizing center that directs intracellular transport in the early embryo (By similarity). Couples non-centrosomal microtubules with actin: interaction with MACF1 at the minus ends of non-centrosomal microtubules, tethers the microtubules to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). Plays a key role in the generation of non-centrosomal microtubules by accumulating in the pericentrosomal region and cooperating with KATNA1 to release non-centrosomal microtubules from the centrosome (PubMed:28386021). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:28089391). Through interaction with AKAP9, involved in translocation of Golgi vesicles in epithelial cells, where microtubules are mainly non-centrosomal (PubMed:28089391). Plays an important role in motile cilia function by facilitatating proper orientation of basal bodies and formation of central microtubule pairs in motile cilia (By similarity). Interacts with PLEKHA7 (PubMed:19041755). Interacts with CAMSAP2 (By similarity). Interacts with KATNA1 and KATNB1; leading to regulate the length of CAMSAP3-decorated microtubule stretches (PubMed:24486153, PubMed:28386021). Interacts with AKAP9; regulating Golgi assembly in epithelial cells (PubMed:28089391). Interacts with MACF1 (PubMed:27693509, PubMed:27802168). Interacts with AKNA (By similarity). Q9P1Y5-2; O43143: DHX15; NbExp=3; IntAct=EBI-18121830, EBI-1237044; Q9P1Y5-2; A1L4K1: FSD2; NbExp=3; IntAct=EBI-18121830, EBI-5661036; Q9P1Y5-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-18121830, EBI-7116203; Cytoplasm, cytoskeleton ll junction, adherens junction Cytoplasm Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body Note=Scattered in the cytoplasm, associated with the minus-end of microtubules and also detected at the centrosomes (PubMed:19041755, PubMed:24486153, PubMed:27693509). Decorates the minus-end of microtubules by decreasing the rate of tubulin incorporation and remaining bound (PubMed:24486153). Localizes along zonula adherens only at mature cell-cell contacts (PubMed:19041755). In early embryos, accumulates at the microtubule bridges that connect pairs of cells: this structure is present in early embryos, which lack centrosomes (By similarity). This cytokinetic bridge does not undergo stereotypical abscission after cell division (By similarity). Accumulates to the pericentrosomal region following interaction with KATNA1 (PubMed:28386021). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9P1Y5-1; Sequence=Displayed; Name=2; IsoId=Q9P1Y5-2; Sequence=VSP_041473; The CKK domain binds microtubules and specifically recognizes the minus-end of microtubules. 'Nezha' is a deity in Chinese mythology. Belongs to the CAMSAP1 family. microtubule cytoskeleton organization in utero embryonic development protein binding calmodulin binding cytoplasm cytoskeleton microtubule adherens junction zonula adherens negative regulation of microtubule depolymerization microtubule binding embryo development ending in birth or egg hatching negative regulation of phosphatase activity cell junction regulation of cell migration spectrin binding establishment or maintenance of microtubule cytoskeleton polarity regulation of microtubule polymerization cytoplasmic microtubule organization neuron projection development regulation of organelle organization microtubule anchoring microtubule minus-end establishment of epithelial cell apical/basal polarity zonula adherens maintenance microtubule minus-end binding actin filament binding regulation of focal adhesion assembly regulation of microtubule cytoskeleton organization epithelial cell-cell adhesion protein transport along microtubule regulation of Golgi organization centrosome uc002mgv.1 uc002mgv.2 uc002mgv.3 uc002mgv.4 uc002mgv.5 uc002mgv.6 
ENST00000160373.8 CTTNBP2 ENST00000160373.8 cortactin binding protein 2, transcript variant 1 (from RefSeq NM_033427.3) C7orf8 CORTBP2 CTTB2_HUMAN ENST00000160373.1 ENST00000160373.2 ENST00000160373.3 ENST00000160373.4 ENST00000160373.5 ENST00000160373.6 ENST00000160373.7 KIAA1758 NM_033427 O43389 Q7LG11 Q8WZ74 Q9C0A5 uc003vjf.1 uc003vjf.2 uc003vjf.3 uc003vjf.4 uc003vjf.5 This gene encodes a protein with six ankyrin repeats and several proline-rich regions. A similar gene in rat interacts with a central regulator of the actin cytoskeleton. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AF377960.1, BC106000.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000160373.8/ ENSP00000160373.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, thus controls dendritic spinogenesis and dendritic spine maintenance. Interacts with CTTN/cortactin SH3 domain. Interacts with STRN, STRN4/zinedin and MOB4/phocein; this interaction may regulate dendritic spine distribution of STRN and STRN4 in hippocampal neurons. Activation of glutamate receptors weakens the interaction with STRN and STRN4. Q8WZ74; Q8WYA1-3: BMAL2; NbExp=3; IntAct=EBI-1774260, EBI-12268276; Q8WZ74; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-1774260, EBI-12845222; Q8WZ74; O75031: HSF2BP; NbExp=3; IntAct=EBI-1774260, EBI-7116203; Q8WZ74; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1774260, EBI-6509505; Q8WZ74; P02533: KRT14; NbExp=3; IntAct=EBI-1774260, EBI-702178; Q8WZ74; P43364: MAGEA11; NbExp=3; IntAct=EBI-1774260, EBI-739552; Q8WZ74; A8MW99: MEI4; NbExp=3; IntAct=EBI-1774260, EBI-19944212; Q8WZ74; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-1774260, EBI-2692890; Cytoplasm, cell cortex Cell projection, dendritic spine Note=Remains associated with dendritic spines even after glutamate stimulation. Highest expression in brain. Also expressed in kidney, pancreas, lung, heart, liver, skeletal muscle and placenta. cytoplasm cell cortex brain development synaptic vesicle SH3 domain binding cell projection dendritic spine regulation of synapse organization postsynaptic actin cytoskeleton glutamatergic synapse regulation of modification of postsynaptic actin cytoskeleton uc003vjf.1 uc003vjf.2 uc003vjf.3 uc003vjf.4 uc003vjf.5 
ENST00000160382.10 ACTL6B ENST00000160382.10 actin like 6B, transcript variant 2 (from RefSeq NR_134539.2) A4D2D0 ACL6B_HUMAN ACTL6 ACTL6B BAF53B ENST00000160382.1 ENST00000160382.2 ENST00000160382.3 ENST00000160382.4 ENST00000160382.5 ENST00000160382.6 ENST00000160382.7 ENST00000160382.8 ENST00000160382.9 NR_134539 O75421 O94805 uc003uvy.1 uc003uvy.2 uc003uvy.3 uc003uvy.4 uc003uvy.5 The protein encoded by this gene is a member of a family of actin-related proteins (ARPs) which share significant amino acid sequence identity to conventional actins. Both actins and ARPs have an actin fold, which is an ATP-binding cleft, as a common feature. The ARPs are involved in diverse cellular processes, including vesicular transport, spindle orientation, nuclear migration and chromatin remodeling. This gene encodes a subunit of the BAF (BRG1/brm-associated factor) complex in mammals, which is functionally related to SWI/SNF complex in S. cerevisiae and Drosophila; the latter is thought to facilitate transcriptional activation of specific genes by antagonizing chromatin-mediated transcriptional repression. This subunit may be involved in the regulation of genes by structural modulation of their chromatin, specifically in the brain. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2015]. Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex), as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion, and is required for postmitotic neural development and dendritic outgrowth. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- specific complexes (nBAF). The npBAF complex is essential for the self- renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. ACTL6B/BAF53B is not essential for assembly of the nBAF complex but is required for targeting the complex and CREST to the promoter of genes essential for dendritic growth (By similarity). Essential for neuronal maturation and dendrite development (PubMed:31031012). Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170 and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (PubMed:22952240, PubMed:26601204). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1 and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (PubMed:22952240, PubMed:26601204). Component of neuron- specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A or SMARCD2/BAF60B or SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (ACTB). Note that the nBAF complex is polymorphic in regard to the ATPase, SMARCA2 and SMARCA4 occupying mutually exclusive positions. May be a component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:22952240, PubMed:26601204). Nucleus Developmental and epileptic encephalopathy 76 (DEE76) [MIM:618468]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE76 is an autosomal recessive form that may result in death in childhood. te=The disease is caused by variants affecting the gene represented in this entry. Intellectual developmental disorder with severe speech and ambulation defects (IDDSSAD) [MIM:618470]: An autosomal dominant neurodevelopmental disorder with onset in infancy, and characterized by global developmental delay, intellectual disability, ambulation deficits, severe language impairment, and minor dysmorphic features including a wide mouth, diastema, and bulbous nose. Additional manifestations are spasticity, hypotonia and autistic features including stereotypies. Brain imaging show thin corpus callosum, generalized atrophy, and mild periventricular gliosis. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the actin family. Sequence=AAC78795.1; Type=Erroneous gene model prediction; Evidence=; chromatin binding transcription coactivator activity structural constituent of cytoskeleton nucleus nucleolus chromatin organization chromatin remodeling regulation of transcription from RNA polymerase II promoter cytoskeleton organization nervous system development SWI/SNF complex spinal cord development NuA4 histone acetyltransferase complex ATP-dependent chromatin remodeling histone H4 acetylation nBAF complex positive regulation of nucleic acid-templated transcription uc003uvy.1 uc003uvy.2 uc003uvy.3 uc003uvy.4 uc003uvy.5 
ENST00000160827.9 KIF22 ENST00000160827.9 kinesin family member 22, transcript variant 1 (from RefSeq NM_007317.3) B2R5M0 B7Z265 ENST00000160827.1 ENST00000160827.2 ENST00000160827.3 ENST00000160827.4 ENST00000160827.5 ENST00000160827.6 ENST00000160827.7 ENST00000160827.8 KID KIF22_HUMAN KNSL4 NM_007317 O60845 O94814 Q14807 Q53F58 Q9BT46 uc002dts.1 uc002dts.2 uc002dts.3 uc002dts.4 uc002dts.5 uc002dts.6 The protein encoded by this gene is a member of the kinesin-like protein family. The family members are microtubule-dependent molecular motors that transport organelles within cells and move chromosomes during cell division. The C-terminal half of this protein has been shown to bind DNA. Studies with the Xenopus homolog suggests its essential role in metaphase chromosome alignment and maintenance. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]. Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA (By similarity). Plays a role in congression of laterally attached chromosomes in NDC80-depleted cells (PubMed:25743205). Interacts with FAM83D (PubMed:18485706). Interacts with SIAH1 (PubMed:11146551). Nucleus Cytoplasm, cytoskeleton Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q14807-1; Sequence=Displayed; Name=2; IsoId=Q14807-2; Sequence=VSP_046428; Expressed in bone, cartilage, joint capsule, ligament, skin, and primary cultured chondrocytes. Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. Spondyloepimetaphyseal dysplasia with joint laxity, 2 (SEMDJL2) [MIM:603546]: A bone disease characterized by short stature, distinctive midface retrusion, progressive knee malalignment (genu valgum and/or varum), generalized ligamentous laxity, and mild spinal deformity. Intellectual development is not impaired. Radiographic characteristics include significantly retarded epiphyseal ossification that evolves into epiphyseal dysplasia and precocious osteoarthritis, metaphyseal irregularities and vertical striations, constricted femoral neck, slender metacarpals and metatarsals, and mild thoracolumbar kyphosis or scoliosis with normal or mild platyspondyly. The most distinctive features for differential diagnosis of SEMDJL2 are the slender metacarpals and phalanges and the progressive degeneration of carpal bones; however, these 2 features are evident only in older children and young adults. The soft consistency of cartilage in the airways leads to laryngotracheomalacia with proneness to respiratory obstruction and inspiratory stridor in infancy and childhood. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Sequence=AAC08709.1; Type=Erroneous gene model prediction; Evidence=; Sequence=EAW80007.1; Type=Erroneous gene model prediction; Evidence=; nucleotide binding mitotic cell cycle kinetochore chromatin DNA binding microtubule motor activity protein binding ATP binding nucleus cytoplasm spindle cytosol cytoskeleton kinesin complex microtubule DNA repair retrograde vesicle-mediated transport, Golgi to ER microtubule-based movement sister chromatid cohesion mitotic metaphase plate congression microtubule binding nuclear speck ATPase activity antigen processing and presentation of exogenous peptide antigen via MHC class II metaphase plate congression mitotic spindle uc002dts.1 uc002dts.2 uc002dts.3 uc002dts.4 uc002dts.5 uc002dts.6 
ENST00000161006.8 PRSS22 ENST00000161006.8 serine protease 22 (from RefSeq NM_022119.4) BSSP4 BSSP4_HUMAN ENST00000161006.1 ENST00000161006.2 ENST00000161006.3 ENST00000161006.4 ENST00000161006.5 ENST00000161006.6 ENST00000161006.7 NM_022119 O43342 PRSS26 Q6UXE0 Q9GZN4 SP001LA UNQ302/PRO343 uc002cry.1 uc002cry.2 This gene encodes a member of the trypsin family of serine proteases. The enzyme is expressed in the airways in a developmentally regulated manner. The gene is part of a cluster of serine protease genes on chromosome 16. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AY358396.1, ERR279835.322.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1966682, SAMEA1968189 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000161006.8/ ENSP00000161006.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Preferentially cleaves the synthetic substrate H-D-Leu-Thr- Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. Secreted Expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung. Scarce in adult lung. Expressed at low levels in placenta, pancreas, prostate and thyroid gland. Belongs to the peptidase S1 family. Sequence=AAB93671.1; Type=Erroneous gene model prediction; Evidence=; Sequence=AAQ88762.1; Type=Erroneous initiation; Evidence=; serine-type endopeptidase activity extracellular region proteolysis peptidase activity serine-type peptidase activity hydrolase activity uc002cry.1 uc002cry.2 
ENST00000161559.11 CEACAM1 ENST00000161559.11 CEA cell adhesion molecule 1, transcript variant 1 (from RefSeq NM_001712.5) A6NE38 A8MY49 BGP BGP1 CEACAM1 CEAM1_HUMAN ENST00000161559.1 ENST00000161559.10 ENST00000161559.2 ENST00000161559.3 ENST00000161559.4 ENST00000161559.5 ENST00000161559.6 ENST00000161559.7 ENST00000161559.8 ENST00000161559.9 NM_001712 O60430 P13688 Q069I7 Q13854 Q13857 Q13858 Q13859 Q13860 Q15600 Q15601 Q16170 Q5UB49 Q7KYP5 Q96CA7 Q9UQV9 uc002otv.1 uc002otv.2 uc002otv.3 uc002otv.4 This gene encodes a member of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin superfamily. Two subgroups of the CEA family, the CEA cell adhesion molecules and the pregnancy-specific glycoproteins, are located within a 1.2 Mb cluster on the long arm of chromosome 19. Eleven pseudogenes of the CEA cell adhesion molecule subgroup are also found in the cluster. The encoded protein was originally described in bile ducts of liver as biliary glycoprotein. Subsequently, it was found to be a cell-cell adhesion molecule detected on leukocytes, epithelia, and endothelia. The encoded protein mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. Multiple cellular activities have been attributed to the encoded protein, including roles in the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses. Multiple transcript variants encoding different isoforms have been reported, but the full-length nature of all variants has not been defined. [provided by RefSeq, May 2010]. [Isoform 1]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:18424730, PubMed:23696226, PubMed:25363763). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors. Plays a role in immune response, of T cells, natural killer (NK) and neutrophils (PubMed:18424730, PubMed:23696226). Upon TCR/CD3 complex stimulation, inhibits TCR- mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:18424730). Also inhibits T cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T cell through its interaction with HAVCR2 (PubMed:25363763). Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226). Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome. Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by down-regulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (By similarity). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia. Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (By similarity). Down-regulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1- MAPK1/ERK2 pathway (By similarity). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (By similarity). Inhibits cell migration and cell scattering through interaction with FLNA; interferes with the interaction of FLNA with RALA (PubMed:16291724). Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (By similarity). [Isoform 8]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Promotes populations of T cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (By similarity). Monomer. Oligomer. Heterodimer. Homodimer (PubMed:26483485). Cis-dimer/oligomer (via Ig-like C2-type and/or via cytoplasmic domains); induced by trans-homophilic cell adhesion through an allosteric mechanism transmitted by the Ig-like V-type domain, and is regulated by intracellular calcium and calmodulin. Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces homophilic cell adhesion through dissociation of dimer (By similarity). Isoform 1 interacts (via cytoplasmic domain) with PTPN11 (preferentially) and PTPN6; cis-homodimer form is preferred; this interaction is decreased by formation of Isoform 1 /Isoform 8 cis- heterodimers and is dependent on the monomer/dimer equilibrium; this interaction is phosphorylation-dependent (PubMed:23696226). Isoform 1 interacts with LYN (By similarity). Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (PubMed:7478590). Isoform 1 interacts (via cytoplasmic domain) with LCK; mediates phosphorylation at Tyr-493 and Tyr-520 resulting in PTPN6 association. Isoform 1 interacts with PTPN6; this interaction is phosphorylation-dependent and causes a profound decrease in TCR stimulation-induced CD247 and ZAP70 phosphorylation. Isoform 1 interacts with TCR/CD3 complex through TCR beta chain and CD3E; colocalizes at the cell surface and upon stimulation of the TCR/CD3 complex recruits PTPN6 in the TCR/CD3 complex, resulting in dephosphorylation of CD247 and ZAP70 (PubMed:18424730). Isoform 1 interacts (via cytoplasmic domain) with SHC1 (via SH2 domain); SHC1 mediates interaction with INSR or EGFR in a Ser-508 phosphorylation-dependent manner (By similarity). Isoform 1 interacts with EGFR; the interaction is indirect (PubMed:15467833). Isoform 1 interacts with CSF3R; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Isoform 1 (phosphorylated form) interacts with TLR4 and SYK; recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (By similarity). Isoform 1 interacts with FLNA; inhibits cell migration and cell scattering by interfering with the interaction of FLNA with RALA (PubMed:16291724). Isoform 1 interacts (via cytoplasmic domain) with PXN; the interaction is phosphotyrosyl-dependent (PubMed:11035932). Isoform 1 interacts with KLRK1; recruits PTPN6 that dephosphorylates VAV1 (PubMed:23696226). Isoform 1 interacts with CEACAM8 (PubMed:11994468). Isoform 1 interacts with FASN; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity). Interacts (via Ig-like V-type) with HAVCR2 (via Ig-like V-type); facilitates the maturation and cell surface expression of HAVCR2 thereby regulating T cell tolerance induction (PubMed:25363763). Isoform 8 interacts (via the cytoplasmic domain) with ANXA2; this interaction is regulated by phosphorylation and appears in the AIIt complex (PubMed:14522961). Interacts (via Lewis X moieties) with CD209 (via C-type lectin domain); this interaction is regulated by the glycosylation pattern of CEACAM1 on cell types and regulates contact between dendritic cells and neutrophils (PubMed:16246332). P13688; Q16568: CARTPT; NbExp=3; IntAct=EBI-4314481, EBI-4314526; P13688; P13688: CEACAM1; NbExp=3; IntAct=EBI-4314481, EBI-4314481; P13688; P40199: CEACAM6; NbExp=2; IntAct=EBI-4314481, EBI-4314501; P13688; Q8TDQ0: HAVCR2; NbExp=4; IntAct=EBI-4314481, EBI-11472922; P13688; Q04883: opaD; Xeno; NbExp=2; IntAct=EBI-4314481, EBI-26495131; P13688; Q04884: opaH; Xeno; NbExp=3; IntAct=EBI-4314481, EBI-26495102; P13688; Q8GH87: uspa1; Xeno; NbExp=12; IntAct=EBI-4314481, EBI-7936357; [Isoform 1]: Cell membrane ; Single-pass type I membrane protein Lateral cell membrane Apical cell membrane Basal cell membrane Cell junction Cell junction, adherens junction Note=Canalicular domain of hepatocyte plasma membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions. Found as dimer in the solution. Predominantly localized to the lateral cell membranes. [Isoform 2]: Secreted [Isoform 3]: Secreted [Isoform 4]: Secreted [Isoform 5]: Cell membrane; Single-pass type I membrane protein. [Isoform 6]: Cell membrane; Single-pass type I membrane protein. [Isoform 7]: Cell membrane; Single-pass type I membrane protein. [Isoform 8]: Cell membrane ; Single-pass type I membrane protein Cytoplasmic vesicle, secretory vesicle membrane Lateral cell membrane Apical cell membrane Basal cell membrane Cell junction Cell junction, adherens junction Note=Predominantly localized to the lateral cell membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions (By similarity). Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (PubMed:14522961). Cell projection, microvillus membrane ; Single-pass type I membrane protein Apical cell membrane ; Single-pass type I membrane protein Note=Localized to the apical glycocalyx surface (PubMed:10436421). Colocalizes with CEACAM20 at the apical brush border of intestinal cells. Event=Alternative splicing; Named isoforms=11; Name=1; Synonyms=BGPa, CEACAM1-4L , TM1-CEA; IsoId=P13688-1; Sequence=Displayed; Name=2; Synonyms=BGPg, CEACAM1-4C1 ; IsoId=P13688-2; Sequence=VSP_002482, VSP_002483; Name=3; Synonyms=BGPh, CEACAM1-3 ; IsoId=P13688-3; Sequence=VSP_002478, VSP_002479; Name=4; Synonyms=BGPi, CEACAM1-3C2 ; IsoId=P13688-4; Sequence=VSP_002480, VSP_002481; Name=5; Synonyms=BGPy, CEACAM1-3AL ; IsoId=P13688-5; Sequence=VSP_009227; Name=6; Synonyms=BGPb, CEACAM1-3L , TM2-CEA; IsoId=P13688-6; Sequence=VSP_010938; Name=7; Synonyms=BGPx, CEACAM1-1L ; IsoId=P13688-7; Sequence=VSP_012222; Name=8; Synonyms=BGPc, CEACAM1-4S , TM3-CEA; IsoId=P13688-8; Sequence=VSP_040572, VSP_040574; Name=9; Synonyms=BGPz, CEACAM1-3AS; IsoId=P13688-9; Sequence=VSP_040571, VSP_040572, VSP_040574; Name=10; IsoId=P13688-10; Sequence=VSP_040573, VSP_040575; Name=11; Synonyms=BGPd, CEACAM1-3S; IsoId=P13688-11; Sequence=VSP_010938, VSP_040572, VSP_040574; Expressed in columnar epithelial cells of the colon (at protein level) (PubMed:10436421). The predominant forms expressed by T cells are those containing a long cytoplasmic domain (PubMed:18424730). Expressed in granulocytes and lymphocytes. Leukocytes only express isoforms 6 and isoform 1 (PubMed:11994468). Induced in primary T cells by activation with IL-2. Ig-like V-type domain mediates trans-homophilic cell adhesion through homodimerization and this active process is regulated by tyrosine kinase, PTPN11 and PTPN6. Ig-like C2-type and/or cytoplasmic domains mediate cis-dimer/oligomer. [Isoform 1]: Phosphorylated on serine and tyrosine (By similarity). Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:15467833, PubMed:18424730, PubMed:7478590). Phosphorylated at Ser-508; mediates activity. Phosphorylated at Tyr- 493; regulates activity (By similarity). Phosphorylated at Tyr-493 by EGFR and INSR upon stimulation; this phosphorylation is Ser-508- phosphorylation-dependent; mediates cellular internalization; increases interaction with downstream proteins like SHC1 and FASN (By similarity). Phosphorylated at Tyr-493 and Tyr-520 by LCK; mediates PTPN6 association and is regulated by homophilic ligation of CEACAM1 in the absence of T cell activation (PubMed:18424730). Phosphorylated at Tyr-520; mediates interaction with PTPN11 (By similarity). [Isoform 8]: Phosphorylated on serine and threonine. [Isoform 8]: Pseudophosphorylated double mutant Thr- 457->Asp and Ser-459->Asp. The single mutant Ser-459->Asp mutant highly binds with ANXA2. Belongs to the immunoglobulin superfamily. CEA family. Sequence=AAA57141.1; Type=Erroneous gene model prediction; Evidence=; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ceacam1/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40044/CEACAM1"; angiogenesis regulation of cell growth blood vessel development negative regulation of T cell mediated cytotoxicity negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target molecular_function actin binding protein binding calmodulin binding extracellular region plasma membrane integral component of plasma membrane cell-cell junction adherens junction negative regulation of protein kinase activity cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules integrin-mediated signaling pathway basal plasma membrane cell surface regulation of endothelial cell migration regulation of phosphatidylinositol 3-kinase signaling bile acid transmembrane transporter activity bile acid and bile salt transport membrane integral component of membrane apical plasma membrane lateral plasma membrane cell migration kinase binding protein phosphatase binding cell junction regulation of cell migration transport vesicle membrane negative regulation of granulocyte differentiation filamin binding cytoplasmic vesicle microvillus membrane negative regulation of interleukin-1 production cellular response to insulin stimulus specific granule membrane common myeloid progenitor cell proliferation insulin receptor internalization granulocyte colony-stimulating factor signaling pathway regulation of epidermal growth factor receptor signaling pathway identical protein binding protein homodimerization activity cell projection negative regulation of vascular permeability neutrophil degranulation negative regulation of cytotoxic T cell degranulation wound healing, spreading of cells regulation of endothelial cell differentiation negative regulation of fatty acid biosynthetic process protein dimerization activity negative regulation of T cell receptor signaling pathway leukocyte migration negative regulation of lipid biosynthetic process regulation of blood vessel remodeling extracellular exosome regulation of ERK1 and ERK2 cascade tertiary granule membrane negative regulation of platelet aggregation cell-cell adhesion via plasma-membrane adhesion molecules insulin catabolic process regulation of homophilic cell adhesion regulation of sprouting angiogenesis protein tyrosine kinase binding negative regulation of hepatocyte proliferation positive regulation of vasculogenesis T cell receptor complex uc002otv.1 uc002otv.2 uc002otv.3 uc002otv.4 
ENST00000161863.9 YTHDC2 ENST00000161863.9 YTH N6-methyladenosine RNA binding protein C2, transcript variant 1 (from RefSeq NM_022828.5) B2RP66 ENST00000161863.1 ENST00000161863.2 ENST00000161863.3 ENST00000161863.4 ENST00000161863.5 ENST00000161863.6 ENST00000161863.7 ENST00000161863.8 NM_022828 Q9H6S0 YTDC2_HUMAN YTHDC2 uc003kqn.1 uc003kqn.2 uc003kqn.3 uc003kqn.4 uc003kqn.5 This gene encodes a member of the DEAH (Asp-Glu-Ala-His) subfamily of proteins, part of the DEAD (Asp-Glu-Ala-Asp) box family of RNA helicases. The encoded protein binds to N6-methyladenosine, a common modified RNA nucleotide that is enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. Binding of proteins to this modified nucleotide may regulate mRNA translation and stability. This gene may be associated with susceptibility to pancreatic cancer in human patients, and knockdown of this gene resulted in reduced proliferation in a human liver cancer cell line. [provided by RefSeq, Sep 2016]. 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:26318451, PubMed:29033321, PubMed:29970596). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:26318451, PubMed:29033321). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (By similarity). Acts by binding and promoting degradation of m6A- containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (By similarity). Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence=; Interacts with MEIOC; binds transcripts that regulate the mitotic cell cycle inhibiting progression into metaphase, thereby allowing meiotic prophase to proceed normally (By similarity). Interacts (via ANK repeats) with XRN1 (PubMed:29033321, PubMed:29970596). Interacts with ZCCHC4 (PubMed:31799605). Associates with the small ribosomal subunit (PubMed:29970596). Interacts with RBM46 (By similarity). Q9H6S0; Q15306: IRF4; NbExp=2; IntAct=EBI-1057466, EBI-751345; Q9H6S0; Q99J34: Irak1; Xeno; NbExp=2; IntAct=EBI-1057466, EBI-6117042; Q9H6S0; A2AG06: Meioc; Xeno; NbExp=2; IntAct=EBI-1057466, EBI-11664020; Cytoplasm Cytoplasm, perinuclear region Expressed in testis (PubMed:29087293). Not detected in spermatogonia next to the tubule wall but is strongly expressed in spermatocytes, suggesting that it is up-regulated in germ cells upon entry into meiosis (PubMed:29087293). The YTH domain mediates RNA-binding. It recognizes and binds N6-methyladenosine (m6A)-containing RNAs. Belongs to the DEAD box helicase family. DEAH subfamily. Sequence=BAB15183.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleotide binding nucleic acid binding RNA binding RNA helicase activity helicase activity protein binding ATP binding nucleus cytoplasm endoplasmic reticulum spermatogenesis spermatid development RNA-dependent ATPase activity hydrolase activity cell differentiation 3'-5' RNA helicase activity response to tumor necrosis factor ribonucleoprotein granule positive regulation by host of viral genome replication oogenesis oocyte development meiotic cell cycle germline cell cycle switching, mitotic to meiotic cell cycle RNA polymerase binding response to interleukin-1 N6-methyladenosine-containing RNA binding uc003kqn.1 uc003kqn.2 uc003kqn.3 uc003kqn.4 uc003kqn.5 
ENST00000162044.14 TMEM161A ENST00000162044.14 transmembrane protein 161A, transcript variant 1 (from RefSeq NM_017814.3) B3KUE0 ENST00000162044.1 ENST00000162044.10 ENST00000162044.11 ENST00000162044.12 ENST00000162044.13 ENST00000162044.2 ENST00000162044.3 ENST00000162044.4 ENST00000162044.5 ENST00000162044.6 ENST00000162044.7 ENST00000162044.8 ENST00000162044.9 G5E9M6 NM_017814 Q7L2Y1 Q9NX61 T161A_HUMAN UNQ582/PRO1152 uc002nlg.1 uc002nlg.2 uc002nlg.3 uc002nlg.4 uc002nlg.5 uc002nlg.6 May play a role in protection against oxidative stress. Overexpression leads to reduced levels of oxidant-induced DNA damage and apoptosis. Q9NX61; O15354: GPR37; NbExp=2; IntAct=EBI-6138599, EBI-15639515; Membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NX61-1; Sequence=Displayed; Name=2; IsoId=Q9NX61-2; Sequence=VSP_046042; Up-regulated in cells which display transient adaptation to mild oxidative stress by treatment with diethylmaleate, a glutathione- depleting agent. Also induced by retinoic acid. Belongs to the TMEM161 family. protein binding membrane integral component of membrane response to retinoic acid cellular response to oxidative stress cellular response to UV positive regulation of DNA repair negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage uc002nlg.1 uc002nlg.2 uc002nlg.3 uc002nlg.4 uc002nlg.5 uc002nlg.6 
ENST00000162330.10 BCAR1 ENST00000162330.10 BCAR1 scaffold protein, Cas family member, transcript variant 6 (from RefSeq NM_014567.5) B3KWD7 B4DEV4 B4DGB5 B4DIW5 B7Z7X7 BCAR1_HUMAN CAS CASS1 CRKAS E9PCL5 E9PCV2 ENST00000162330.1 ENST00000162330.2 ENST00000162330.3 ENST00000162330.4 ENST00000162330.5 ENST00000162330.6 ENST00000162330.7 ENST00000162330.8 ENST00000162330.9 F5GXA2 F5GXV6 F5H7Z0 F8WA69 NM_014567 P56945 Q6QEF7 uc002fdv.1 uc002fdv.2 uc002fdv.3 uc002fdv.4 uc002fdv.5 The protein encoded by this gene is a member of the Crk-associated substrate (CAS) family of scaffold proteins, characterized by the presence of multiple protein-protein interaction domains and many serine and tyrosine phosphorylation sites. The encoded protein contains a Src-homology 3 (SH3) domain, a proline-rich domain, a substrate domain which contains 15 repeat of the YxxP consensus phosphorylation motif for Src family kinases, a serine-rich domain, and a bipartite Src-binding domain, which can bind both SH2 and SH3 domains. This adaptor protein functions in multiple cellular pathways, including in cell motility, apoptosis and cell cycle control. Dysregulation of this gene can have a wide range of effects, affecting different pathways, including cardiac development, vascular smooth muscle cells, liver and kidney function, endothelial migration, and cancer. [provided by RefSeq, Sep 2017]. Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (PubMed:12832404, PubMed:12432078). Implicated in induction of cell migration and cell branching (PubMed:12432078, PubMed:12832404, PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB signaling (By similarity). Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase (PubMed:9020138). Heterodimerizes with NEDD9 (PubMed:10502414). Component of a complex comprised of SH2D3C, BCAR1/CAS, and CRK (PubMed:12432078). Within the complex, interacts with SH2D3C (via C-terminus), and CRK (PubMed:12432078, PubMed:17174122). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on intergrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Interacts with BCAR3 (via Ras-GEF domain); the interaction regulates adhesion-dependent serine phosphorylation (PubMed:22081014). Interacts with SMAD2 and SMAD3 (By similarity). Interacts with NPHP1 (By similarity). Interacts with PTK2B/PYK2 (PubMed:9020138, PubMed:19086031). Interacts (via C-terminus) with SH2D3C/CHAT isoform 2 (via C-terminus) (PubMed:17174122, PubMed:22081014). Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1. Part of a collagen-stimulated complex involved in cell migration made of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with TNK2 via SH3 domains. Interacts (when tyrosine-phosphorylated) with tensin TNS1; the interaction is increased by phosphorylation of TNS1 (PubMed:20798394). P56945; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-702093, EBI-11954519; P56945; O75815-1: BCAR3; NbExp=3; IntAct=EBI-702093, EBI-15953103; P56945; P53618: COPB1; NbExp=3; IntAct=EBI-702093, EBI-359063; P56945; P46108: CRK; NbExp=7; IntAct=EBI-702093, EBI-886; P56945; Q5T9C2-3: EEIG1; NbExp=3; IntAct=EBI-702093, EBI-11980989; P56945; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-702093, EBI-6658203; P56945; P06241: FYN; NbExp=4; IntAct=EBI-702093, EBI-515315; P56945; P06241-3: FYN; NbExp=3; IntAct=EBI-702093, EBI-10691738; P56945; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-702093, EBI-7251368; P56945; O15357: INPPL1; NbExp=2; IntAct=EBI-702093, EBI-1384248; P56945; P46940: IQGAP1; NbExp=4; IntAct=EBI-702093, EBI-297509; P56945; P50281: MMP14; NbExp=3; IntAct=EBI-702093, EBI-992788; P56945; O43639: NCK2; NbExp=3; IntAct=EBI-702093, EBI-713635; P56945; Q9H792: PEAK1; NbExp=3; IntAct=EBI-702093, EBI-2609701; P56945; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-702093, EBI-2860740; P56945; Q05397: PTK2; NbExp=2; IntAct=EBI-702093, EBI-702142; P56945; P18031: PTPN1; NbExp=5; IntAct=EBI-702093, EBI-968788; P56945; Q05209: PTPN12; NbExp=5; IntAct=EBI-702093, EBI-2266035; P56945; Q8N5H7-2: SH2D3C; NbExp=8; IntAct=EBI-702093, EBI-15952996; P56945; P12931: SRC; NbExp=3; IntAct=EBI-702093, EBI-621482; P56945; Q9C0H9: SRCIN1; NbExp=3; IntAct=EBI-702093, EBI-1393949; P56945; Q07912: TNK2; NbExp=5; IntAct=EBI-702093, EBI-603457; P56945; Q68CZ2: TNS3; NbExp=8; IntAct=EBI-702093, EBI-1220488; P56945; O75604: USP2; NbExp=3; IntAct=EBI-702093, EBI-743272; P56945; P18206-2: VCL; NbExp=3; IntAct=EBI-702093, EBI-11027067; P56945; P07947: YES1; NbExp=3; IntAct=EBI-702093, EBI-515331; P56945; Q9QWI6: Srcin1; Xeno; NbExp=3; IntAct=EBI-702093, EBI-775592; P56945; Q04205: TNS1; Xeno; NbExp=2; IntAct=EBI-702093, EBI-2607590; Cell junction, focal adhesion Cytoplasm Cell projection, axon Note=Unphosphorylated form localizes in the cytoplasm (By similarity). Localizes to focal adhesion sites following integrin engagement (By similarity). Event=Alternative splicing; Named isoforms=8; Name=1; IsoId=P56945-1; Sequence=Displayed; Name=2; IsoId=P56945-2; Sequence=VSP_043559; Name=3; IsoId=P56945-3; Sequence=VSP_045355; Name=4; IsoId=P56945-4; Sequence=VSP_046127, VSP_046128; Name=5; IsoId=P56945-5; Sequence=VSP_046748; Name=6; IsoId=P56945-6; Sequence=VSP_046749; Name=7; IsoId=P56945-7; Sequence=VSP_046750; Name=8; IsoId=P56945-8; Sequence=VSP_046751; Expressed in B-cells (at protein level) (PubMed:9020138). Widely expressed with an abundant expression in the testis (PubMed:10639512). Low level of expression seen in the liver, thymus, and peripheral blood leukocytes (PubMed:10639512). Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL1 SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9 (By similarity). A serine-rich region promotes activation of the serum response element (SRE). The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK11. PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif; phosphorylation is most likely catalyzed by SRC family members. SRC- family kinases are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Tyrosine phosphorylation is triggered by integrin-mediated adhesion of cells to the extracellular matrix. Dephosphorylated by PTPN14 at Tyr-128. Phosphorylated by SRC kinase in a EDN1- and PTK2B-mediated manner; phosphorylation strengthens its interaction with BCAR3 as part of the PTK2B/BCAR1/BCAR3/RAP1 signaling pathway. Belongs to the CAS family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/761/BCAR1"; regulation of cell growth ruffle protein binding cytoplasm cytosol focal adhesion actin filament organization cell adhesion signal transduction epidermal growth factor receptor signaling pathway G-protein coupled receptor signaling pathway integrin-mediated signaling pathway insulin receptor signaling pathway positive regulation of endothelial cell migration actin cytoskeleton cell migration SH3 domain binding protein kinase binding lamellipodium cell junction positive regulation of cell migration cellular response to hepatocyte growth factor stimulus regulation of apoptotic process platelet-derived growth factor receptor signaling pathway vascular endothelial growth factor receptor signaling pathway neurotrophin TRK receptor signaling pathway hepatocyte growth factor receptor signaling pathway antigen receptor-mediated signaling pathway T cell receptor signaling pathway B cell receptor signaling pathway cell division cell chemotaxis actin filament reorganization plasma membrane uc002fdv.1 uc002fdv.2 uc002fdv.3 uc002fdv.4 uc002fdv.5 
ENST00000162391.8 FOXJ2 ENST00000162391.8 forkhead box J2 (from RefSeq NM_018416.3) A0AVK4 B2RMP3 ENST00000162391.1 ENST00000162391.2 ENST00000162391.3 ENST00000162391.4 ENST00000162391.5 ENST00000162391.6 ENST00000162391.7 FHX FOXJ2_HUMAN NM_018416 Q96PS9 Q9NSN5 Q9P0K8 uc001qtu.1 uc001qtu.2 uc001qtu.3 uc001qtu.4 uc001qtu.5 [Isoform FOXJ2.L]: Transcriptional activator. Able to bind to two different type of DNA binding sites. More effective than isoform FOXJ2.S in transcriptional activation (PubMed:10777590, PubMed:10966786). Plays an important role in spermatogenesis, especially in spermatocyte meiosis (By similarity). [Isoform FOXJ2.S]: Transcriptional activator. Q9P0K8; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-2869608, EBI-747012; Q9P0K8; Q9H6Z9: EGLN3; NbExp=6; IntAct=EBI-2869608, EBI-1175354; Q9P0K8; Q9P0K8: FOXJ2; NbExp=2; IntAct=EBI-2869608, EBI-2869608; Nucleus. Event=Alternative splicing; Named isoforms=2; Name=FOXJ2.L; Synonyms=FHX.L; IsoId=Q9P0K8-1; Sequence=Displayed; Name=FOXJ2.S; Synonyms=FHX.S; IsoId=Q9P0K8-2; Sequence=VSP_001544; Widely expressed. nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding fibrillar center DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated negative regulation of angiogenesis identical protein binding sequence-specific DNA binding positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter positive regulation of vascular smooth muscle cell proliferation uc001qtu.1 uc001qtu.2 uc001qtu.3 uc001qtu.4 uc001qtu.5 
ENST00000162749.7 TNFRSF1A ENST00000162749.7 TNF receptor superfamily member 1A, transcript variant 1 (from RefSeq NM_001065.4) A8K4X3 B2RDE4 B3KPQ1 B4DQB7 B4E309 B5M0B5 D3DUR1 ENST00000162749.1 ENST00000162749.2 ENST00000162749.3 ENST00000162749.4 ENST00000162749.5 ENST00000162749.6 NM_001065 P19438 Q9UCA4 TNFAR TNFR1 TNR1A_HUMAN uc001qnu.1 uc001qnu.2 uc001qnu.3 uc001qnu.4 uc001qnu.5 This gene encodes a member of the TNF receptor superfamily of proteins. The encoded receptor is found in membrane-bound and soluble forms that interact with membrane-bound and soluble forms, respectively, of its ligand, tumor necrosis factor alpha. Binding of membrane-bound tumor necrosis factor alpha to the membrane-bound receptor induces receptor trimerization and activation, which plays a role in cell survival, apoptosis, and inflammation. Proteolytic processing of the encoded receptor results in release of the soluble form of the receptor, which can interact with free tumor necrosis factor alpha to inhibit inflammation. Mutations in this gene underlie tumor necrosis factor receptor-associated periodic syndrome (TRAPS), characterized by fever, abdominal pain and other features. Mutations in this gene may also be associated with multiple sclerosis in human patients. [provided by RefSeq, Sep 2016]. Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BABAM2, FEM1B, GRB2, SQSTM1 and TRPC4AP (PubMed:10356400, PubMed:10359574, PubMed:10542291, PubMed:15465831, PubMed:8387891, PubMed:9915703). Interacts directly with NOL3 (via CARD domain); inhibits TNF-signaling pathway (By similarity). Interacts with SH3RF2, TRADD and RIPK1. SH3RF2 facilitates the recruitment of RIPK1 and TRADD to TNFRSF1A in a TNF- alpha-dependent process (PubMed:24130170). Interacts with PGLYRP1; this interaction is important for cell death induction (PubMed:26183779). Interacts (via death domain) with MADD (via death domain) (PubMed:9115275). (Microbial infection) Interacts with mumps virus protein SH; this interaction inhibits downstream NF-kappa-B pathway activation. (Microbial infection) Interacts with HCV core protein. (Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL138. (Microbial infection) Interacts with host TNFRSF1A; this interaction leads to the stimulation of both surface expression and shedding of TNFRSF1A. P19438; P28799: GRN; NbExp=4; IntAct=EBI-299451, EBI-747754; P19438; Q969G6: RFK; NbExp=4; IntAct=EBI-299451, EBI-716872; P19438; Q13546: RIPK1; NbExp=6; IntAct=EBI-299451, EBI-358507; P19438; P01375: TNF; NbExp=15; IntAct=EBI-299451, EBI-359977; P19438; Q15628: TRADD; NbExp=13; IntAct=EBI-299451, EBI-359215; P19438-1; Q969G6: RFK; NbExp=2; IntAct=EBI-15795644, EBI-716872; Cell membrane ; Single-pass type I membrane protein Golgi apparatus membrane ; Single-pass type I membrane protein Secreted Note=A secreted form is produced through proteolytic processing. [Isoform 4]: Secreted. Note=Lacks a Golgi- retention motif, is not membrane bound and therefore is secreted. Event=Alternative splicing; Named isoforms=5; Name=1; Synonyms=FL-TNFR1; IsoId=P19438-1; Sequence=Displayed; Name=2; IsoId=P19438-2; Sequence=VSP_037153; Name=4; Synonyms=Delta6-TNFR1; IsoId=P19438-4; Sequence=VSP_044949; Name=3; IsoId=P19438-3; Sequence=VSP_037154; Name=5; IsoId=P19438-5; Sequence=VSP_047613, VSP_047614; The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE. Both the cytoplasmic membrane-proximal region and the C- terminal region containing the death domain are involved in the interaction with TRPC4AP. The soluble form is produced from the membrane form by proteolytic processing. (Microbial infection) Glycosylated at Arg-376 by enteropathogenic E.coli protein NleB1 and S.typhimurium protein Ssek3: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions. Periodic fever, familial, autosomal dominant (FPF) [MIM:142680]: A hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases. te=The disease is caused by variants affecting the gene represented in this entry. Multiple sclerosis 5 (MS5) [MIM:614810]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. An intronic mutation affecting alternative splicing and skipping of exon 6 directs increased expression of isoform 4 a transcript encoding a C-terminally truncated protein which is secreted and may function as a TNF antagonist. [Isoform 4]: Disease-associated isoform. Isoform 4 splicing pattern is driven by a variation in the exon 6/intron 6 boundary region that alters exon 6 splicing. Exon 6 skipping introduces a frameshift and the translation of a protein lacking the intracellular, the transmembrane and part of the extracellular domain. Name=INFEVERS; Note=Repertory of FMF and hereditary autoinflammatory disorders mutations; URL="https://infevers.umai-montpellier.fr/web/search.php?n=22"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/tnfrsf1a/"; Golgi membrane tumor necrosis factor receptor superfamily complex aortic valve development pulmonary valve development negative regulation of extracellular matrix constituent secretion tumor necrosis factor-activated receptor activity protein binding extracellular region extracellular space mitochondrion Golgi apparatus plasma membrane integral component of plasma membrane prostaglandin metabolic process apoptotic process defense response inflammatory response signal transduction cell surface receptor signaling pathway I-kappaB kinase/NF-kappaB signaling extrinsic apoptotic signaling pathway via death domain receptors intrinsic apoptotic signaling pathway in response to DNA damage cell surface negative regulation of cardiac muscle hypertrophy regulation of tumor necrosis factor-mediated signaling pathway membrane integral component of membrane viral process cytokine-mediated signaling pathway tumor necrosis factor-mediated signaling pathway positive regulation of tyrosine phosphorylation of STAT protein defense response to bacterium identical protein binding tumor necrosis factor binding positive regulation of I-kappaB kinase/NF-kappaB signaling receptor complex membrane raft positive regulation of transcription from RNA polymerase II promoter negative regulation of inflammatory response positive regulation of inflammatory response cellular response to mechanical stimulus death-inducing signaling complex assembly protein localization to plasma membrane positive regulation of apoptotic process involved in morphogenesis regulation of establishment of endothelial barrier positive regulation of ceramide biosynthetic process uc001qnu.1 uc001qnu.2 uc001qnu.3 uc001qnu.4 uc001qnu.5 
ENST00000163416.7 GOLGA5 ENST00000163416.7 golgin A5 (from RefSeq NM_005113.4) C9JRU1 ENST00000163416.1 ENST00000163416.2 ENST00000163416.3 ENST00000163416.4 ENST00000163416.5 ENST00000163416.6 GOGA5_HUMAN NM_005113 O95287 PIG31 Q03962 Q2TS49 Q8TBA6 Q9UQQ7 RETII RFG5 uc001yaz.1 uc001yaz.2 uc001yaz.3 uc001yaz.4 The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. This gene encodes one of the golgins, a family of proteins localized to the Golgi. This protein is a coiled-coil membrane protein that has been postulated to play a role in vesicle tethering and docking. Translocations involving this gene and the ret proto-oncogene have been found in tumor tissues; the chimeric sequences have been designated RET-II and PTC5. A pseudogene of this gene is located on the short arm of chromosome 5. [provided by RefSeq, Jul 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803616.122087.1, SRR1803611.169184.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000163416.7/ ENSP00000163416.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport. Homodimer. Interacts with RAB1A that has been activated by GTP-binding, and possibly also with OCRL1. Interacts with isoform CASP of CUX1. Golgi apparatus membrane ; Single-pass type IV membrane protein Note=Found throughout the Golgi, both on cisternae and, at higher abundance, on the tubulo-vesicular structures of the cis-Golgi network. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8TBA6-1; Sequence=Displayed; Name=2; IsoId=Q8TBA6-2; Sequence=VSP_007731, VSP_007732; Ubiquitous. Highly expressed in seminiferous tubules and Leydig cells in testis, and detected at much lower levels in the other tissues tested. Expression is very low or not detectable in spermatozoa. Highly phosphorylated during mitosis. Phosphorylation is barely detectable during interphase. Note=A chromosomal aberration involving GOLGA5 is found in papillary thyroid carcinomas (PTCs). Translocation t(10;14)(q11;q32) with RET. The translocation generates the RET/GOLGA5 (PTC5) oncogene. Sequence=CAA33787.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. A chimeric cDNA originating from chromosomes 14 and 10.; Evidence=; Golgi membrane retrograde transport, vesicle recycling within Golgi Golgi apparatus cis-Golgi network Golgi organization membrane integral component of membrane Rab GTPase binding transport vesicle Golgi cisterna protein homodimerization activity Golgi vesicle transport uc001yaz.1 uc001yaz.2 uc001yaz.3 uc001yaz.4 
ENST00000164024.5 CELSR3 ENST00000164024.5 cadherin EGF LAG seven-pass G-type receptor 3 (from RefSeq NM_001407.3) CDHF11 CELR3_HUMAN EGFL1 ENST00000164024.1 ENST00000164024.2 ENST00000164024.3 ENST00000164024.4 FMI1 KIAA0812 MEGF2 NM_001407 O75092 Q9NYQ7 uc003cul.1 uc003cul.2 uc003cul.3 uc003cul.4 uc003cul.5 This gene belongs to the flamingo subfamily, which is included in the cadherin superfamily. The flamingo cadherins consist of nonclassic-type cadherins that do not interact with catenins. They are plasma membrane proteins containing seven epidermal growth factor-like repeats, nine cadherin domains and two laminin A G-type repeats in their ectodomain. They also have seven transmembrane domains, a characteristic feature of their subfamily. The encoded protein may be involved in the regulation of contact-dependent neurite growth and may play a role in tumor formation. [provided by RefSeq, Jun 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF231023.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000164024.5/ ENSP00000164024.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor that may have an important role in cell/cell signaling during nervous system formation. Q9NYQ7; P16333: NCK1; NbExp=2; IntAct=EBI-308417, EBI-389883; Cell membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NYQ7-1; Sequence=Displayed; Name=2; IsoId=Q9NYQ7-2; Sequence=VSP_037125; Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily. neuron migration regulation of protein phosphorylation transmembrane signaling receptor activity G-protein coupled receptor activity calcium ion binding protein binding plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules signal transduction cell surface receptor signaling pathway G-protein coupled receptor signaling pathway multicellular organism development axonal fasciculation membrane integral component of membrane regulation of protein localization dopaminergic neuron axon guidance serotonergic neuron axon guidance Wnt signaling pathway, planar cell polarity pathway cilium assembly cell-cell adhesion planar cell polarity pathway involved in axon guidance uc003cul.1 uc003cul.2 uc003cul.3 uc003cul.4 uc003cul.5 
ENST00000164133.7 PPP2R5B ENST00000164133.7 protein phosphatase 2 regulatory subunit B'beta (from RefSeq NM_006244.4) 2A5B_HUMAN ENST00000164133.1 ENST00000164133.2 ENST00000164133.3 ENST00000164133.4 ENST00000164133.5 ENST00000164133.6 NM_006244 Q13853 Q15173 uc001oby.1 uc001oby.2 uc001oby.3 uc001oby.4 uc001oby.5 The product of this gene belongs to the phosphatase 2A regulatory subunit B family. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes a beta isoform of the regulatory subunit B56 subfamily. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.888844.1, SRR3476690.697029.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000164133.7/ ENSP00000164133.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## As the regulatory component of the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity, subcellular localization, and responsiveness to phosphorylation. The phosphorylated form mediates the interaction between PP2A and AKT1, leading to AKT1 dephosphorylation. Component of the serine/threonine-protein phosphatase 2A complex (PP2A). This complex consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant scaffold subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules (PubMed:23135275). Interacts with SGO1 (PubMed:16541025). Interacts with AKT1 (PubMed:21329884). Interacts with CUL3 and KLHL15; this interaction leads to proteasomal degradation (PubMed:23135275). Q15173; O96017: CHEK2; NbExp=2; IntAct=EBI-1369497, EBI-1180783; Q15173; P46695: IER3; NbExp=4; IntAct=EBI-1369497, EBI-1748945; Q15173; P67775: PPP2CA; NbExp=6; IntAct=EBI-1369497, EBI-712311; Q15173; P30153: PPP2R1A; NbExp=4; IntAct=EBI-1369497, EBI-302388; Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=Beta-1; IsoId=Q15173-1; Sequence=Displayed; Name=Beta-2; IsoId=Q15173-2; Sequence=VSP_005109; Highest expression in brain. By retinoic acid; in neuroblastoma cell lines. Ubiquitinated by E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation. Belongs to the phosphatase 2A regulatory subunit B56 family. protein phosphatase type 2A complex regulation of protein phosphorylation protein binding nucleus cytoplasm cytosol protein dephosphorylation signal transduction regulation of receptor activity positive regulation of neuron projection development regulation of phosphatidylinositol 3-kinase signaling protein phosphatase regulator activity positive regulation of protein complex assembly regulation of protein autophosphorylation IRE1-mediated unfolded protein response regulation of phosphoprotein phosphatase activity positive regulation of transcription from RNA polymerase II promoter regulation of peptidyl-tyrosine phosphorylation positive regulation of sequence-specific DNA binding transcription factor activity positive regulation of neurotrophin TRK receptor signaling pathway negative regulation of protein kinase B signaling negative regulation of G0 to G1 transition positive regulation of cell cycle arrest cellular response to growth factor stimulus protein phosphatase activator activity uc001oby.1 uc001oby.2 uc001oby.3 uc001oby.4 uc001oby.5 
ENST00000164139.4 PYGM ENST00000164139.4 glycogen phosphorylase, muscle associated, transcript variant 1 (from RefSeq NM_005609.4) A0AVK1 A6NDY6 ENST00000164139.1 ENST00000164139.2 ENST00000164139.3 NM_005609 P11217 PYGM PYGM_HUMAN uc001oax.1 uc001oax.2 uc001oax.3 uc001oax.4 uc001oax.5 uc001oax.6 This gene encodes a muscle enzyme involved in glycogenolysis. Highly similar enzymes encoded by different genes are found in liver and brain. Mutations in this gene are associated with McArdle disease (myophosphorylase deficiency), a glycogen storage disease of muscle. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Sep 2009]. Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733; Evidence=; Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence=; Allosterically regulated through the non-covalent binding of metabolites, being activated by AMP and inhibited by ATP, ADP, and glucose-6-phosphate. The activity is also controlled by post- translational modifications including phosphorylation. Homodimer (PubMed:1150650, PubMed:16523484). Homotetramer; to form the enzymatically active phosphorylase A (PubMed:1150650). P11217; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-357469, EBI-741158; P11217; O43741: PRKAB2; NbExp=7; IntAct=EBI-357469, EBI-1053424; P11217; P11216: PYGB; NbExp=3; IntAct=EBI-357469, EBI-1047231; P11217; P06737: PYGL; NbExp=3; IntAct=EBI-357469, EBI-2511865; P11217; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-357469, EBI-25492395; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P11217-1; Sequence=Displayed; Name=2; IsoId=P11217-2; Sequence=VSP_043047; Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycogen phosphorylase family. nucleotide binding catalytic activity phosphorylase activity protein binding cytoplasm cytosol carbohydrate metabolic process glycogen metabolic process glycogen catabolic process metabolic process glycogen phosphorylase activity transferase activity transferase activity, transferring glycosyl groups pyridoxal phosphate binding extracellular exosome uc001oax.1 uc001oax.2 uc001oax.3 uc001oax.4 uc001oax.5 uc001oax.6 
ENST00000164227.10 BCL3 ENST00000164227.10 BCL3 transcription coactivator (from RefSeq NM_005178.5) BCL3_HUMAN BCL4 D19S37 ENST00000164227.1 ENST00000164227.2 ENST00000164227.3 ENST00000164227.4 ENST00000164227.5 ENST00000164227.6 ENST00000164227.7 ENST00000164227.8 ENST00000164227.9 NM_005178 P20749 uc010xxe.1 uc010xxe.2 uc010xxe.3 uc010xxe.4 This gene is a proto-oncogene candidate. It is identified by its translocation into the immunoglobulin alpha-locus in some cases of B-cell leukemia. The protein encoded by this gene contains seven ankyrin repeats, which are most closely related to those found in I kappa B proteins. This protein functions as a transcriptional co-activator that activates through its association with NF-kappa B homodimers. The expression of this gene can be induced by NF-kappa B, which forms a part of the autoregulatory loop that controls the nuclear residence of p50 NF-kappa B. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC064993.1, SRR1163658.355456.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000164227.10/ ENSP00000164227.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit. In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation (By similarity). Component of a complex consisting of the NF-kappa-B p52-p52 homodimer and BCL3. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Interacts with N4BP2, COPS5 and PIR. Interacts with CYLD (By similarity). P20749; O95999: BCL10; NbExp=3; IntAct=EBI-958997, EBI-958922; P20749; P56545: CTBP2; NbExp=2; IntAct=EBI-958997, EBI-741533; P20749; P06239: LCK; NbExp=3; IntAct=EBI-958997, EBI-1348; P20749; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-958997, EBI-2811583; Nucleus. Cytoplasm Cytoplasm, perinuclear region Note=Ubiquitination via 'Lys-63'- linked ubiquitin chains is required for nuclear accumulation. Polyubiquitinated. Ubiquitination via 'Lys-63'-linked ubiquitin chains is required for nuclear accumulation. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains. Deubiquitination by CYLD prevents nuclear accumulation (By similarity). Activated by phosphorylation. Note=A chromosomal aberration involving BCL3 may be a cause of B-cell chronic lymphocytic leukemia (B-CLL). Translocation t(14;19)(q32;q13.1) with immunoglobulin gene regions. It is uncertain whether Met-1 or Met-9 is the initiator. Sequence=AAA51815.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAA51816.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH64993.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; follicular dendritic cell differentiation marginal zone B cell differentiation humoral immune response mediated by circulating immunoglobulin germinal center formation DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm cytoplasm cytosol plasma membrane transcription, DNA-templated cellular response to DNA damage stimulus I-kappaB kinase/NF-kappaB signaling transcription factor binding response to virus response to UV-C antimicrobial humoral response extracellular matrix organization DNA damage response, signal transduction by p53 class mediator midbody protein binding, bridging positive regulation of interferon-gamma production macromolecular complex Bcl3-Bcl10 complex Bcl3/NF-kappaB2 complex T-helper 1 type immune response negative regulation of tumor necrosis factor biosynthetic process defense response to bacterium intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator defense response to protozoan regulation of apoptotic process negative regulation of apoptotic process intracellular membrane-bounded organelle T-helper 2 cell differentiation positive regulation of interleukin-10 biosynthetic process negative regulation of interleukin-8 biosynthetic process positive regulation of translation negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter negative regulation of JAK-STAT cascade perinuclear region of cytoplasm spleen development regulation of DNA binding maintenance of protein location in nucleus regulation of NIK/NF-kappaB signaling uc010xxe.1 uc010xxe.2 uc010xxe.3 uc010xxe.4 
ENST00000164305.10 PIGB ENST00000164305.10 phosphatidylinositol glycan anchor biosynthesis class B (from RefSeq NM_004855.5) ENST00000164305.1 ENST00000164305.2 ENST00000164305.3 ENST00000164305.4 ENST00000164305.5 ENST00000164305.6 ENST00000164305.7 ENST00000164305.8 ENST00000164305.9 NM_004855 PIGB PIGB_HUMAN Q53FF9 Q8WVN7 Q92521 uc002act.1 uc002act.2 uc002act.3 uc002act.4 uc002act.5 This gene encodes a transmembrane protein that is located in the endoplasmic reticulum and is involved in GPI-anchor biosynthesis. The glycosylphosphatidylinositol (GPI) anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This gene is thought to encode a member of a family of dolichol-phosphate-mannose (Dol-P-Man) dependent mannosyltransferases. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: BC017711.1, D42138.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000164305.10/ ENSP00000164305.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2- GlcN-acyl-PI during GPI precursor assembly. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. Endoplasmic reticulum membrane ; Multi-pass membrane protein Developmental and epileptic encephalopathy 80 (DEE80) [MIM:618580]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE80 is an autosomal recessive form characterized by onset of refractory seizures in the first year of life, severe global developmental delay and/or intellectual disability. Additional variable features include polyneuropathy, hearing loss, visual impairment, dysmorphic or coarse facial features, and distal skeletal abnormalities. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyltransferase 22 family. PIGB subfamily. mannosyltransferase activity glycolipid mannosyltransferase activity endoplasmic reticulum endoplasmic reticulum membrane GPI anchor biosynthetic process membrane integral component of membrane preassembly of GPI anchor in ER membrane transferase activity transferase activity, transferring glycosyl groups mannosylation uc002act.1 uc002act.2 uc002act.3 uc002act.4 uc002act.5 
ENST00000165524.1 PRLH ENST00000165524.1 prolactin releasing hormone (from RefSeq NM_015893.1) NM_015893 PRH PRLH Q53QV7 Q53QV7_HUMAN hCG_23020 uc010znl.1 uc010znl.2 tissue homeostasis response to dietary excess reduction of food intake in response to dietary excess hormone activity neuropeptide hormone activity cytoplasm energy reserve metabolic process lipid metabolic process G-protein coupled receptor signaling pathway feeding behavior response to glucose prolactin-releasing peptide receptor binding response to insulin regulation of multicellular organism growth eating behavior response to peptide hormone fat cell differentiation autonomic nervous system development uc010znl.1 uc010znl.2 
ENST00000166139.9 FSTL3 ENST00000166139.9 follistatin like 3 (from RefSeq NM_005860.3) A8K7E3 ENST00000166139.1 ENST00000166139.2 ENST00000166139.3 ENST00000166139.4 ENST00000166139.5 ENST00000166139.6 ENST00000166139.7 ENST00000166139.8 FLRG FSTL3_HUMAN NM_005860 O95633 UNQ674/PRO1308 uc002lpk.1 uc002lpk.2 uc002lpk.3 uc002lpk.4 Follistatin-like 3 is a secreted glycoprotein of the follistatin-module-protein family. It may have a role in leukemogenesis. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC005839.2, AY358917.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000166139.9/ ENSP00000166139.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiationc. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10. Interacts with INHBA and INHBB. Interacts with FN1. Interacts with ADAM12. Isoform 2 interacts with MLLT10; the interaction enhances MLLT10 in vitro transcriptional activity and self-association. Interacts with MSTN. O95633; O43184-2: ADAM12; NbExp=4; IntAct=EBI-2625790, EBI-2625865; [Isoform 1]: Secreted. [Isoform 2]: Nucleus. Note=Although alternative initiation has been demonstrated and resulted in different localization, the major source of nuclear FSTL3 appears not to depend on translation initiation at Met-27 according to. Event=Alternative initiation; Named isoforms=2; Name=1; IsoId=O95633-1; Sequence=Displayed; Name=2; IsoId=O95633-2; Sequence=VSP_038553; Expressed in a wide range of tissues. Note=A chromosomal aberration involving FSTL3 is found in a case of B-cell chronic lymphocytic leukemia. Translocation t(11;19)(q13;p13) with CCDN1. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/111/FSTL3"; ossification kidney development fibronectin binding hematopoietic progenitor cell differentiation protein binding extracellular region extracellular space nucleus nucleoplasm endoplasmic reticulum lumen Golgi apparatus regulation of transcription from RNA polymerase II promoter multicellular organism development spermatogenesis male gonad development positive regulation of cell-cell adhesion secretory granule cell differentiation lung development adrenal gland development regulation of BMP signaling pathway negative regulation of BMP signaling pathway negative regulation of activin receptor signaling pathway post-translational protein modification cellular protein metabolic process neuron projection terminus negative regulation of osteoclast differentiation positive regulation of transcription from RNA polymerase II promoter activin binding cellular response to metal ion negative regulation of transmembrane receptor protein serine/threonine kinase signaling pathway uc002lpk.1 uc002lpk.2 uc002lpk.3 uc002lpk.4 
ENST00000166244.8 EPHA8 ENST00000166244.8 EPH receptor A8, transcript variant 1 (from RefSeq NM_020526.5) EEK ENST00000166244.1 ENST00000166244.2 ENST00000166244.3 ENST00000166244.4 ENST00000166244.5 ENST00000166244.6 ENST00000166244.7 EPHA8_HUMAN HEK3 KIAA1459 NM_020526 P29322 Q6IN80 Q8IUX6 Q9NUA9 Q9P269 uc001bfx.1 uc001bfx.2 uc001bfx.3 This gene encodes a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. The protein encoded by this gene functions as a receptor for ephrin A2, A3 and A5 and plays a role in short-range contact-mediated axonal guidance during development of the mammalian nervous system. [provided by RefSeq, Jul 2008]. Receptor tyrosine kinase which binds promiscuously GPI- anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system also plays a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth (By similarity). Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence=; Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. May also form heterodimers with other ephrin receptors (By similarity). Interacts with FYN; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PIK3CG; regulates integrin-mediated cell adhesion to substrate. Interacts with TIAM1; regulates clathrin- mediated endocytosis of EPHA8. Interacts with ANKS1A and ANKS1B; EPHA8 kinase activity-independent but stimulated by EPHA8 ubiquitination. Cell membrane ; Single-pass type I membrane protein Cell projection Early endosome membrane Note=Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P29322-1; Sequence=Displayed; Name=2; IsoId=P29322-2; Sequence=VSP_041946, VSP_041947; Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr- 616 is critical for association with FYN. Autophosphorylation on Tyr- 839 modulates tyrosine kinase activity (By similarity). Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation (By similarity). Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Sequence=CAA41980.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleotide binding protein kinase activity protein tyrosine kinase activity transmembrane receptor protein tyrosine kinase activity ephrin receptor activity GPI-linked ephrin receptor activity transmembrane-ephrin receptor activity ATP binding endosome plasma membrane integral component of plasma membrane protein phosphorylation substrate-dependent cell migration cell adhesion transmembrane receptor protein tyrosine kinase signaling pathway multicellular organism development nervous system development axon guidance membrane integral component of membrane kinase activity phosphorylation neuron remodeling transferase activity peptidyl-tyrosine phosphorylation regulation of cell adhesion neuron projection development early endosome membrane regulation of cell adhesion mediated by integrin cell projection neuron projection receptor complex positive regulation of MAPK cascade positive regulation of phosphatidylinositol 3-kinase activity protein autophosphorylation ephrin receptor signaling pathway cellular response to follicle-stimulating hormone stimulus uc001bfx.1 uc001bfx.2 uc001bfx.3 
ENST00000166345.8 TRIP13 ENST00000166345.8 thyroid hormone receptor interactor 13, transcript variant 1 (from RefSeq NM_004237.4) C9K0T3 D3DTC0 ENST00000166345.1 ENST00000166345.2 ENST00000166345.3 ENST00000166345.4 ENST00000166345.5 ENST00000166345.6 ENST00000166345.7 NM_004237 O15324 PCH2 PCH2_HUMAN Q15645 uc003jbr.1 uc003jbr.2 uc003jbr.3 uc003jbr.4 uc003jbr.5 This gene encodes a protein that interacts with thyroid hormone receptors, also known as hormone-dependent transcription factors. The gene product interacts specifically with the ligand binding domain. This gene is one of several that may play a role in early-stage non-small cell lung cancer. [provided by RefSeq, Oct 2009]. Plays a key role in chromosome recombination and chromosome structure development during meiosis. Required at early steps in meiotic recombination that leads to non-crossovers pathways. Also needed for efficient completion of homologous synapsis by influencing crossover distribution along the chromosomes affecting both crossovers and non-crossovers pathways. Also required for development of higher- order chromosome structures and is needed for synaptonemal-complex formation. In males, required for efficient synapsis of the sex chromosomes and for sex body formation. Promotes early steps of the DNA double-strand breaks (DSBs) repair process upstream of the assembly of RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from synapsed chromosomes (By similarity). Plays a role in mitotic spindle assembly checkpoint (SAC) activation (PubMed:28553959). Specifically interacts with the ligand binding domain of the thyroid receptor (TR). This interaction does not require the presence of thyroid hormone for its interaction. Interacts with HPV16 E1. Interacts with proteasome subunit PSMA8; to participate in meiosis progression during spermatogenesis (By similarity). Q15645; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-358993, EBI-11976299; Q15645; Q9Y303: AMDHD2; NbExp=3; IntAct=EBI-358993, EBI-2798672; Q15645; Q9Y303-2: AMDHD2; NbExp=3; IntAct=EBI-358993, EBI-12323557; Q15645; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-358993, EBI-12102070; Q15645; Q969Q4: ARL11; NbExp=4; IntAct=EBI-358993, EBI-751892; Q15645; P15289: ARSA; NbExp=13; IntAct=EBI-358993, EBI-2117357; Q15645; Q8WXK3-2: ASB13; NbExp=3; IntAct=EBI-358993, EBI-12015080; Q15645; Q9H0W9: C11orf54; NbExp=3; IntAct=EBI-358993, EBI-740204; Q15645; Q9H0W9-3: C11orf54; NbExp=3; IntAct=EBI-358993, EBI-12108466; Q15645; Q8N1A6: C4orf33; NbExp=7; IntAct=EBI-358993, EBI-10264911; Q15645; Q9Y2V0: CDIN1; NbExp=3; IntAct=EBI-358993, EBI-1047601; Q15645; Q9Y4F5-3: CEP170B; NbExp=3; IntAct=EBI-358993, EBI-12950757; Q15645; A0A0S2Z515: CFP; NbExp=3; IntAct=EBI-358993, EBI-16434710; Q15645; Q8N3C7: CLIP4; NbExp=3; IntAct=EBI-358993, EBI-5655540; Q15645; P21964: COMT; NbExp=3; IntAct=EBI-358993, EBI-372265; Q15645; P21964-2: COMT; NbExp=3; IntAct=EBI-358993, EBI-10200977; Q15645; P53672: CRYBA2; NbExp=5; IntAct=EBI-358993, EBI-750444; Q15645; Q6BCY4: CYB5R2; NbExp=4; IntAct=EBI-358993, EBI-744761; Q15645; Q6BCY4-2: CYB5R2; NbExp=3; IntAct=EBI-358993, EBI-12102608; Q15645; O75935-2: DCTN3; NbExp=3; IntAct=EBI-358993, EBI-12091947; Q15645; O95865: DDAH2; NbExp=6; IntAct=EBI-358993, EBI-749139; Q15645; Q14689: DIP2A; NbExp=3; IntAct=EBI-358993, EBI-2564275; Q15645; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-358993, EBI-10233719; Q15645; O14531: DPYSL4; NbExp=3; IntAct=EBI-358993, EBI-719542; Q15645; Q96G04: EEF2KMT; NbExp=3; IntAct=EBI-358993, EBI-747840; Q15645; Q9UBX5: FBLN5; NbExp=3; IntAct=EBI-358993, EBI-947897; Q15645; A0A0S2Z576: FBXO8; NbExp=3; IntAct=EBI-358993, EBI-16434722; Q15645; Q53EP0-3: FNDC3B; NbExp=6; IntAct=EBI-358993, EBI-10242151; Q15645; A0A0S2Z4I0: GALT; NbExp=3; IntAct=EBI-358993, EBI-16434744; Q15645; P07902: GALT; NbExp=4; IntAct=EBI-358993, EBI-750827; Q15645; Q8IVS8: GLYCTK; NbExp=9; IntAct=EBI-358993, EBI-748515; Q15645; Q9BSH5: HDHD3; NbExp=6; IntAct=EBI-358993, EBI-745201; Q15645; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-358993, EBI-11955401; Q15645; P14784: IL2RB; NbExp=3; IntAct=EBI-358993, EBI-2866779; Q15645; Q0VD86: INCA1; NbExp=3; IntAct=EBI-358993, EBI-6509505; Q15645; P59990: KRTAP12-1; NbExp=6; IntAct=EBI-358993, EBI-10210845; Q15645; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-358993, EBI-10176379; Q15645; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-358993, EBI-10176396; Q15645; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-358993, EBI-3957672; Q15645; Q3LI64: KRTAP6-1; NbExp=4; IntAct=EBI-358993, EBI-12111050; Q15645; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-358993, EBI-11962084; Q15645; Q16773: KYAT1; NbExp=3; IntAct=EBI-358993, EBI-10238309; Q15645; Q14847: LASP1; NbExp=7; IntAct=EBI-358993, EBI-742828; Q15645; Q14847-2: LASP1; NbExp=3; IntAct=EBI-358993, EBI-9088686; Q15645; Q8TBB1: LNX1; NbExp=8; IntAct=EBI-358993, EBI-739832; Q15645; Q96JB6: LOXL4; NbExp=6; IntAct=EBI-358993, EBI-749562; Q15645; Q96L50: LRR1; NbExp=3; IntAct=EBI-358993, EBI-2510106; Q15645; Q8TC57: M1AP; NbExp=3; IntAct=EBI-358993, EBI-748182; Q15645; Q15013: MAD2L1BP; NbExp=9; IntAct=EBI-358993, EBI-712181; Q15645; Q6P9B6: MEAK7; NbExp=4; IntAct=EBI-358993, EBI-746504; Q15645; A6NJ78-4: METTL15; NbExp=6; IntAct=EBI-358993, EBI-10174029; Q15645; Q6PF18: MORN3; NbExp=3; IntAct=EBI-358993, EBI-9675802; Q15645; Q15777: MPPED2; NbExp=8; IntAct=EBI-358993, EBI-2350461; Q15645; Q96EZ4: MYEOV; NbExp=3; IntAct=EBI-358993, EBI-12260130; Q15645; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-358993, EBI-740897; Q15645; O00746: NME4; NbExp=4; IntAct=EBI-358993, EBI-744871; Q15645; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-358993, EBI-741158; Q15645; P55771: PAX9; NbExp=3; IntAct=EBI-358993, EBI-12111000; Q15645; P30039: PBLD; NbExp=4; IntAct=EBI-358993, EBI-750589; Q15645; Q6PIM4: PCMTD2; NbExp=3; IntAct=EBI-358993, EBI-10253759; Q15645; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-358993, EBI-11956269; Q15645; Q96FA3: PELI1; NbExp=3; IntAct=EBI-358993, EBI-448369; Q15645; Q9NRY6: PLSCR3; NbExp=7; IntAct=EBI-358993, EBI-750734; Q15645; Q9NRQ2: PLSCR4; NbExp=5; IntAct=EBI-358993, EBI-769257; Q15645; P62875: POLR2L; NbExp=3; IntAct=EBI-358993, EBI-359527; Q15645; P67775: PPP2CA; NbExp=6; IntAct=EBI-358993, EBI-712311; Q15645; P54646: PRKAA2; NbExp=3; IntAct=EBI-358993, EBI-1383852; Q15645; O60260: PRKN; NbExp=4; IntAct=EBI-358993, EBI-716346; Q15645; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-358993, EBI-740924; Q15645; P28062-2: PSMB8; NbExp=3; IntAct=EBI-358993, EBI-372312; Q15645; P47897: QARS1; NbExp=6; IntAct=EBI-358993, EBI-347462; Q15645; P47897-2: QARS1; NbExp=3; IntAct=EBI-358993, EBI-10209725; Q15645; Q9BQY4: RHOXF2; NbExp=8; IntAct=EBI-358993, EBI-372094; Q15645; P78317: RNF4; NbExp=3; IntAct=EBI-358993, EBI-2340927; Q15645; P22307: SCP2; NbExp=4; IntAct=EBI-358993, EBI-1050999; Q15645; O00560: SDCBP; NbExp=3; IntAct=EBI-358993, EBI-727004; Q15645; Q13228: SELENBP1; NbExp=6; IntAct=EBI-358993, EBI-711619; Q15645; Q13214-2: SEMA3B; NbExp=3; IntAct=EBI-358993, EBI-11017428; Q15645; Q9NTN9: SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-6447340; Q15645; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-9089805; Q15645; Q9H0F6-2: SHARPIN; NbExp=3; IntAct=EBI-358993, EBI-9843813; Q15645; O15389: SIGLEC5; NbExp=4; IntAct=EBI-358993, EBI-750381; Q15645; Q96LM6: SPMIP9; NbExp=7; IntAct=EBI-358993, EBI-743976; Q15645; Q5W111: SPRYD7; NbExp=3; IntAct=EBI-358993, EBI-10248098; Q15645; O95630: STAMBP; NbExp=4; IntAct=EBI-358993, EBI-396676; Q15645; Q96A09: TENT5B; NbExp=3; IntAct=EBI-358993, EBI-752030; Q15645; Q9GZM7: TINAGL1; NbExp=6; IntAct=EBI-358993, EBI-715869; Q15645; Q9GZM7-3: TINAGL1; NbExp=3; IntAct=EBI-358993, EBI-10303636; Q15645; Q8NDV7: TNRC6A; NbExp=3; IntAct=EBI-358993, EBI-2269715; Q15645; P13693: TPT1; NbExp=3; IntAct=EBI-358993, EBI-1783169; Q15645; Q15645: TRIP13; NbExp=8; IntAct=EBI-358993, EBI-358993; Q15645; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-358993, EBI-10180829; Q15645; P11473: VDR; NbExp=3; IntAct=EBI-358993, EBI-286357; Q15645; O95231: VENTX; NbExp=3; IntAct=EBI-358993, EBI-10191303; Q15645; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-358993, EBI-17634549; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q15645-1; Sequence=Displayed; Name=2; IsoId=Q15645-2; Sequence=VSP_016957; Mosaic variegated aneuploidy syndrome 3 (MVA3) [MIM:617598]: A form of mosaic variegated aneuploidy syndrome, a severe disorder characterized by mosaic aneuploidies, predominantly trisomies and monosomies, involving multiple different chromosomes and tissues. Affected individuals typically present with severe intrauterine growth retardation and microcephaly. Eye anomalies, mild dysmorphism, variable developmental delay, and a broad spectrum of additional congenital abnormalities and medical conditions may also occur. The risk of malignancy is high, with rhabdomyosarcoma, Wilms tumor and leukemia reported in several cases. MVA3 inheritance is autosomal recessive. Note=The disease is caused by variants affecting the gene represented in this entry. MVA3 is caused by biallelic mutations in the TRIP13 gene. Oocyte/zygote/embryo maturation arrest 9 (OZEMA9) [MIM:619011]: An autosomal recessive infertility disorder due to oocyte meiotic arrest at metaphase I. Abnormal zygotic cleavage has been observed in some patients. Note=The disease may be caused by variants affecting the gene represented in this entry. Belongs to the AAA ATPase family. PCH2 subfamily. Sequence=AAC41732.1; Type=Frameshift; Evidence=; nucleotide binding oocyte maturation male germ cell nucleus transcription cofactor activity protein binding ATP binding nucleus chromosome double-strand break repair transcription from RNA polymerase II promoter mitotic spindle assembly checkpoint synaptonemal complex assembly reciprocal meiotic recombination male meiosis I female meiosis I spermatogenesis spermatid development cell differentiation identical protein binding oogenesis meiotic cell cycle meiotic recombination checkpoint regulation of nucleic acid-templated transcription uc003jbr.1 uc003jbr.2 uc003jbr.3 uc003jbr.4 uc003jbr.5 
ENST00000167106.9 VASH1 ENST00000167106.9 vasohibin 1 (from RefSeq NM_014909.5) ENST00000167106.1 ENST00000167106.2 ENST00000167106.3 ENST00000167106.4 ENST00000167106.5 ENST00000167106.6 ENST00000167106.7 ENST00000167106.8 KIAA1036 NM_014909 Q7L8A9 Q96H02 Q9UBF4 Q9Y629 VASH VASH1 VASH1_HUMAN uc001xst.1 uc001xst.2 uc001xst.3 uc001xst.4 Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146869, PubMed:31270470, PubMed:31235910, PubMed:31171830, PubMed:31235911). Critical for spindle function and accurate chromosome segregation during mitosis since microtubule detyronisation regulates mitotic spindle length and postioning (PubMed:31171830). Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:15467828, PubMed:16488400, PubMed:16707096, PubMed:19204325). This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (PubMed:15467828, PubMed:16488400, PubMed:16707096). Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl- [tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl- [tubulin] + L-tyrosine; Xref=Rhea:RHEA:57444, Rhea:RHEA-COMP:16434, Rhea:RHEA-COMP:16435, ChEBI:CHEBI:15377, ChEBI:CHEBI:58315, ChEBI:CHEBI:149554, ChEBI:CHEBI:149555; EC=3.4.17.17; Evidence= Kinetic parameters: KM=7.9 uM for alpha-tubulin C-terminal tail ; Note=kcat is 44.5 min(-1) for alpha-tubulin C-terminal tail. ; Interacts with SVBP; interaction enhances VASH1 tyrosine carboxypeptidase activity. Q7L8A9; P49366: DHPS; NbExp=3; IntAct=EBI-10256546, EBI-741925; Q7L8A9-1; Q8N300: SVBP; NbExp=2; IntAct=EBI-21497569, EBI-21497577; Cytoplasm creted te=Mainly localizes in the cytoplasm (PubMed:27879017). Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion (PubMed:27879017). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q7L8A9-1; Sequence=Displayed; Name=2; IsoId=Q7L8A9-2; Sequence=VSP_013324, VSP_013325; Preferentially expressed in endothelial cells (PubMed:15467828, PubMed:16707096). Highly expressed in fetal organs (PubMed:15467828). Expressed in brain and placenta, and at lower level in heart and kidney (PubMed:15467828). Highly detected in microvessels endothelial cells of atherosclerotic lesions (PubMed:16707096). By VEGF. 2 major forms (42 and 36 kDa) and 2 minors (32 and 27 kDa) may be processed by proteolytic cleavage (PubMed:16488400). The largest form (42 kDa) seems to be secreted and the other major form (63 kDa) seems to accumulate within the cells or pericellular milieu (PubMed:16488400). Polypeptide consisting of Met-77 to Arg-318 may correspond to the 27 kDa form and that consisting of Met-77 to Val-365 may correspond to the 36 kDa form (PubMed:16488400). Ubiquitinated in vitro. Belongs to the transglutaminase-like superfamily. Vasohibin family. Sequence=AAD44361.1; Type=Erroneous gene model prediction; Evidence=; Sequence=BAA82988.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; angiogenesis negative regulation of endothelial cell proliferation actin binding carboxypeptidase activity metallocarboxypeptidase activity protein binding extracellular region extracellular space cytoplasm endoplasmic reticulum proteolysis cell cycle cell cycle arrest peptidase activity response to wounding negative regulation of endothelial cell migration negative regulation of angiogenesis hydrolase activity negative regulation of blood vessel endothelial cell migration apical part of cell regulation of angiogenesis placenta blood vessel development labyrinthine layer blood vessel development negative regulation of lymphangiogenesis regulation of cellular senescence uc001xst.1 uc001xst.2 uc001xst.3 uc001xst.4 
ENST00000167586.7 KRT14 ENST00000167586.7 keratin 14 (from RefSeq NM_000526.5) ENST00000167586.1 ENST00000167586.2 ENST00000167586.3 ENST00000167586.4 ENST00000167586.5 ENST00000167586.6 K1C14_HUMAN NM_000526 P02533 Q14715 Q53XY3 Q9BUE3 Q9UBN2 Q9UBN3 Q9UCY4 uc002hxf.1 uc002hxf.2 uc002hxf.3 uc002hxf.4 This gene encodes a member of the keratin family, the most diverse group of intermediate filaments. This gene product, a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC094830.1, BC019097.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145893, SAMEA2147596 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000167586.7/ ENSP00000167586.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## The nonhelical tail domain is involved in promoting KRT5- KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro. Heterotetramer of two type I and two type II keratins (By similarity). Forms a disulfide-linked heterodimer (via 2B domains) with KRT5 (via 2B domains) (PubMed:24940650, PubMed:22705788). Forms a heterodimer with KRT1; the interaction is more abundant in the absence of KRT5 (By similarity). Interacts with PLEC isoform 1C, when in a heterodimer with KRT5 (PubMed:24940650). Interacts with TRADD and with keratin filaments (PubMed:11684708). Associates with other type I keratins (PubMed:11724817). Interacts with EPPK1 (By similarity). Interacts with KLHL24 (PubMed:27798626). Interacts with PKP1 (via N- terminus) and PKP2 (PubMed:10852826). P02533; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-702178, EBI-11096309; P02533; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-702178, EBI-742038; P02533; A2BDD9: AMOT; NbExp=3; IntAct=EBI-702178, EBI-17286414; P02533; Q13515: BFSP2; NbExp=3; IntAct=EBI-702178, EBI-10229433; P02533; Q8WZ74: CTTNBP2; NbExp=3; IntAct=EBI-702178, EBI-1774260; P02533; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-702178, EBI-744099; P02533; O95995: GAS8; NbExp=3; IntAct=EBI-702178, EBI-1052570; P02533; O14964: HGS; NbExp=3; IntAct=EBI-702178, EBI-740220; P02533; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-702178, EBI-14069005; P02533; P04264: KRT1; NbExp=3; IntAct=EBI-702178, EBI-298429; P02533; P12035: KRT3; NbExp=3; IntAct=EBI-702178, EBI-2430095; P02533; P13647: KRT5; NbExp=8; IntAct=EBI-702178, EBI-702187; P02533; P48668: KRT6C; NbExp=3; IntAct=EBI-702178, EBI-2564105; P02533; Q14CN4: KRT72; NbExp=3; IntAct=EBI-702178, EBI-1221280; P02533; Q8N1N4: KRT78; NbExp=3; IntAct=EBI-702178, EBI-1056564; P02533; Q5XKE5: KRT79; NbExp=3; IntAct=EBI-702178, EBI-2514135; P02533; Q6KB66-2: KRT80; NbExp=3; IntAct=EBI-702178, EBI-11999246; P02533; Q14533: KRT81; NbExp=3; IntAct=EBI-702178, EBI-739648; P02533; O43790: KRT86; NbExp=3; IntAct=EBI-702178, EBI-9996498; P02533; O43482: OIP5; NbExp=3; IntAct=EBI-702178, EBI-536879; P02533; Q13835-2: PKP1; NbExp=2; IntAct=EBI-702178, EBI-9087684; P02533; P41219: PRPH; NbExp=3; IntAct=EBI-702178, EBI-752074; P02533; Q3MIT2: PUS10; NbExp=3; IntAct=EBI-702178, EBI-11983583; P02533; O00560: SDCBP; NbExp=3; IntAct=EBI-702178, EBI-727004; P02533; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-702178, EBI-455078; P02533; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-702178, EBI-7353612; P02533; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-702178, EBI-739895; Cytoplasm cleus Note=Expressed in both as a filamentous pattern. Expressed in the corneal epithelium (at protein level) (PubMed:26758872). Detected in the basal layer, lowered within the more apically located layers specifically in the stratum spinosum, stratum granulosum but is not detected in stratum corneum. Strongly expressed in the outer root sheath of anagen follicles but not in the germinative matrix, inner root sheath or hair (PubMed:9457912). Found in keratinocytes surrounding the club hair during telogen (PubMed:9457912). A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus. Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex. Epidermolysis bullosa simplex 1A, generalized severe (EBS1A) [MIM:131760]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1A is an autosomal dominant form characterized by generalized intraepidermal skin blistering that begins and is very prominent at birth. EBS1A may be life-threatening in the first year of life. Tendency to blistering diminishes in adolescence. te=The disease is caused by variants affecting the gene represented in this entry. Epidermolysis bullosa simplex 1C, localized (EBS1C) [MIM:131800]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1C is an autosomal dominant form with intraepidermal blistering mainly restricted to hands and feet beginning in infancy. Nails may be thick and dystrophic. te=The disease is caused by variants affecting the gene represented in this entry. Epidermolysis bullosa simplex 1B, generalized intermediate (EBS1B) [MIM:131900]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1B is an autosomal dominant form characterized by generalized intraepidermal blistering beginning at birth. The tendency to blistering diminishes in adolescence, when it may become localized to hands and feet. te=The disease is caused by variants affecting the gene represented in this entry. Epidermolysis bullosa simplex 1D, generalized, intermediate or severe, autosomal recessive (EBS1D) [MIM:601001]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1D is an autosomal recessive form characterized by blistering beginning at birth or early childhood. In some patients hands and feet are primarily affected, and in others blistering anywhere on the body may occur. In some patients the condition improves with age. te=The disease is caused by variants affecting the gene represented in this entry. Naegeli-Franceschetti-Jadassohn syndrome (NFJS) [MIM:161000]: A rare autosomal dominant form of ectodermal dysplasia. The cardinal features are absence of dermatoglyphics (fingerprints), reticular cutaneous hyperpigmentation (starting at about the age of 2 years without a preceding inflammatory stage), palmoplantar keratoderma, hypohidrosis with diminished sweat gland function and discomfort provoked by heat, nail dystrophy, and tooth enamel defects. Note=The disease is caused by variants affecting the gene represented in this entry. Dermatopathia pigmentosa reticularis (DPR) [MIM:125595]: A rare ectodermal dysplasia characterized by lifelong persistent reticulate hyperpigmentation, non-cicatricial alopecia, and nail dystrophy. Variable features include adermatoglyphia, hypohidrosis or hyperhidrosis, and palmoplantar hyperkeratosis. Note=The disease is caused by variants affecting the gene represented in this entry. There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa). Belongs to the intermediate filament family. structural molecule activity structural constituent of cytoskeleton protein binding nucleus cytoplasm cytosol intermediate filament aging epidermis development response to zinc ion response to ionizing radiation epithelial cell differentiation keratinization hemidesmosome assembly hair cycle keratin filament intermediate filament bundle assembly basal part of cell extracellular exosome cornification cell periphery keratin filament binding uc002hxf.1 uc002hxf.2 uc002hxf.3 uc002hxf.4 
ENST00000167588.4 KRT20 ENST00000167588.4 keratin 20 (from RefSeq NM_019010.3) B2R6W7 ENST00000167588.1 ENST00000167588.2 ENST00000167588.3 K1C20_HUMAN NM_019010 P35900 uc002hvl.1 uc002hvl.2 uc002hvl.3 uc002hvl.4 uc002hvl.5 The protein encoded by this gene is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK312744.1, BC031559.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2152474 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000167588.4/ ENSP00000167588.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine (By similarity). Heterotetramer of two type I and two type II keratins. Associates with KRT8. P35900; Q9NYB9: ABI2; NbExp=3; IntAct=EBI-742094, EBI-743598; P35900; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-742094, EBI-10187270; P35900; Q9BUW7: BBLN; NbExp=9; IntAct=EBI-742094, EBI-752084; P35900; O75934: BCAS2; NbExp=3; IntAct=EBI-742094, EBI-1050106; P35900; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-742094, EBI-10181422; P35900; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-742094, EBI-3867333; P35900; P17661: DES; NbExp=3; IntAct=EBI-742094, EBI-1055572; P35900; P42858: HTT; NbExp=9; IntAct=EBI-742094, EBI-466029; P35900; A1A4E9: KRT13; NbExp=3; IntAct=EBI-742094, EBI-10171552; P35900; P19012: KRT15; NbExp=5; IntAct=EBI-742094, EBI-739566; P35900; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-742094, EBI-2952736; P35900; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-742094, EBI-3044087; P35900; P12035: KRT3; NbExp=3; IntAct=EBI-742094, EBI-2430095; P35900; Q15323: KRT31; NbExp=3; IntAct=EBI-742094, EBI-948001; P35900; O76011: KRT34; NbExp=3; IntAct=EBI-742094, EBI-1047093; P35900; Q6A162: KRT40; NbExp=3; IntAct=EBI-742094, EBI-10171697; P35900; Q14CN4: KRT72; NbExp=3; IntAct=EBI-742094, EBI-1221280; P35900; O95678: KRT75; NbExp=3; IntAct=EBI-742094, EBI-2949715; P35900; Q01546: KRT76; NbExp=3; IntAct=EBI-742094, EBI-2952745; P35900; Q6KB66: KRT80; NbExp=3; IntAct=EBI-742094, EBI-3046635; P35900; Q6KB66-2: KRT80; NbExp=3; IntAct=EBI-742094, EBI-11999246; P35900; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-742094, EBI-11959885; P35900; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-742094, EBI-10172290; P35900; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-742094, EBI-10171774; P35900; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-742094, EBI-10172052; P35900; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-742094, EBI-11953334; P35900; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-742094, EBI-945833; P35900; P37198: NUP62; NbExp=7; IntAct=EBI-742094, EBI-347978; P35900; O00459: PIK3R2; NbExp=3; IntAct=EBI-742094, EBI-346930; P35900; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-742094, EBI-1105153; P35900; P41219: PRPH; NbExp=6; IntAct=EBI-742094, EBI-752074; P35900; O95295: SNAPIN; NbExp=3; IntAct=EBI-742094, EBI-296723; P35900; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-742094, EBI-1105213; P35900; P40222: TXLNA; NbExp=6; IntAct=EBI-742094, EBI-359793; P35900; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-742094, EBI-739895; P35900; P08670: VIM; NbExp=8; IntAct=EBI-742094, EBI-353844; Cytoplasm Expressed predominantly in the intestinal epithelium. Expressed in luminal cells of colonic mucosa. Also expressed in the Merkel cells of keratinized oral mucosa; specifically at the tips of some rete ridges of the gingival mucosa, in the basal layer of the palatal mucosa and in the taste buds of lingual mucosa. First detected at embryonic week 8 in individual 'converted' simple epithelial cells of the developing intestinal mucosa. In later fetal stages, synthesis extends over most goblet cells and a variable number of villus enterocytes. In the developing gastric and intestinal mucosa, expressed in all enterocytes and goblet cells as well as certain 'low-differentiated' columnar cells, whereas the neuroendocrine and Paneth cells are negative. Hyperphosphorylation at Ser-13 occurs during the early stages of apoptosis but becomes less prominent during the later stages. Phosphorylation at Ser-13 also increases in response to stress brought on by cell injury (By similarity). Proteolytically cleaved by caspases during apoptosis. Cleavage occurs at Asp-228. There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa). Belongs to the intermediate filament family. structural molecule activity structural constituent of cytoskeleton protein binding cytoplasm cytosol intermediate filament apoptotic process cellular response to starvation keratinization intermediate filament organization regulation of protein secretion cornification uc002hvl.1 uc002hvl.2 uc002hvl.3 uc002hvl.4 uc002hvl.5 
ENST00000168148.8 SPP2 ENST00000168148.8 secreted phosphoprotein 2 (from RefSeq NM_006944.3) A4QMV3 ENST00000168148.1 ENST00000168148.2 ENST00000168148.3 ENST00000168148.4 ENST00000168148.5 ENST00000168148.6 ENST00000168148.7 NM_006944 Q13103 Q3B892 Q546M5 SPP24 SPP24_HUMAN uc002vvk.1 uc002vvk.2 uc002vvk.3 This gene encodes a secreted phosphoprotein that is a member of the cystatin superfamily. [provided by RefSeq, Oct 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189664.151662.1, SRR5189664.41883.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145122, SAMEA2155590 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000168148.8/ ENSP00000168148.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Could coordinate an aspect of bone turnover. Secreted. Detected in liver and plasma. Found in fetal liver and kidney. Phosphorylation sites are present in the extracellular medium. Belongs to the SPP2 family. skeletal system development platelet degranulation endopeptidase inhibitor activity extracellular region endoplasmic reticulum lumen negative regulation of endopeptidase activity platelet dense granule lumen post-translational protein modification cellular protein metabolic process bone remodeling uc002vvk.1 uc002vvk.2 uc002vvk.3 
ENST00000168216.11 HSD17B10 ENST00000168216.11 hydroxysteroid 17-beta dehydrogenase 10, transcript variant 1 (from RefSeq NM_004493.3) ENST00000168216.1 ENST00000168216.10 ENST00000168216.2 ENST00000168216.3 ENST00000168216.4 ENST00000168216.5 ENST00000168216.6 ENST00000168216.7 ENST00000168216.8 ENST00000168216.9 ERAB HADH2 HCD2_HUMAN MRPP2 NM_004493 Q5H927 Q6IBS9 Q8TCV9 Q96HD5 Q99714 SCHAD SDR5C1 XH98G2 uc004dsl.1 uc004dsl.2 uc004dsl.3 This gene encodes 3-hydroxyacyl-CoA dehydrogenase type II, a member of the short-chain dehydrogenase/reductase superfamily. The gene product is a mitochondrial protein that catalyzes the oxidation of a wide variety of fatty acids and steroids, and is a subunit of mitochondrial ribonuclease P, which is involved in tRNA maturation. The protein has been implicated in the development of Alzheimer disease, and mutations in the gene are the cause of 17beta-hydroxysteroid dehydrogenase type 10 (HSD10) deficiency. Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined. [provided by RefSeq, Aug 2014]. Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (PubMed:9553139, PubMed:10600649, PubMed:12917011, PubMed:20077426, PubMed:18996107, PubMed:19706438, PubMed:25925575, PubMed:26950678, PubMed:28888424). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (PubMed:9553139, PubMed:10600649, PubMed:12917011, PubMed:25925575, PubMed:26950678). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2- methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (PubMed:20077426, PubMed:18996107, PubMed:19706438). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids (PubMed:10600649, PubMed:12917011). Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel (PubMed:19706438, PubMed:28888424). Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (PubMed:26338420). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (PubMed:9338779). Essential for structural and functional integrity of mitochondria (PubMed:20077426). In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:24549042, PubMed:25925575, PubMed:26950678, PubMed:28888424). Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit (PubMed:23042678, PubMed:25925575, PubMed:28888424). The MRPP1- MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'- end cleavage by the mitochondrial ribonuclease P complex, the MRPP1- MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly. Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22434; Evidence= Reaction=(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD(+) = 2-methyl-3- oxobutanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:13281, ChEBI:CHEBI:15378, ChEBI:CHEBI:57312, ChEBI:CHEBI:57335, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.178; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13282; Evidence= Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.239; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930; Evidence=; Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta- hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006; Evidence=; Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613; Evidence=; Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta- cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.159; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410; Evidence=; Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:30799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57316, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30801; Evidence= Reaction=(3S)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31195, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62617, ChEBI:CHEBI:62619; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31196; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31197; Evidence=; Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378, ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62613; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31161; Evidence=; Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha- androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41993; Evidence=; Reaction=5alpha-pregnan-20beta-ol-3-one + NAD(+) = 5alpha-pregnane- 3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:42008, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78594; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42009; Evidence=; Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha- pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981; Evidence=; Reaction=cortisone + NAD(+) = 17alpha-hydroxypregn-4-en-3,11,20-trione- 21-al + H(+) + NADH; Xref=Rhea:RHEA:42016, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78596; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42017; Evidence=; Reaction=11-dehydrocorticosterone + NAD(+) = H(+) + NADH + pregn-4-ene- 3,11,20,21-tetraone; Xref=Rhea:RHEA:42020, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600, ChEBI:CHEBI:78601; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42021; Evidence=; Reaction=cortisol + NAD(+) = 11beta,17alpha-dihydroxypregn-4-ene- 3,20,21-trione + H(+) + NADH; Xref=Rhea:RHEA:42012, ChEBI:CHEBI:15378, ChEBI:CHEBI:17650, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78595; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42013; Evidence=; Reaction=chenodeoxycholate + NAD(+) = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42036, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78605; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037; Evidence=; Reaction=NAD(+) + ursodeoxycholate = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42028, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42029; Evidence=; Reaction=3beta,7beta-dihydroxy-5beta-cholan-24-oate + NAD(+) = 3beta- hydroxy-7-oxo-5beta-cholan-24-oate + H(+) + NADH; Xref=Rhea:RHEA:42024, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78602, ChEBI:CHEBI:78603; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42025; Evidence=; The phospholipase C-like activity toward cardiolipin is inhibited by amyloid-beta peptide. Kinetic parameters: KM=25.7 uM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius) ; KM=85.2 uM for beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) ; KM=41 uM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) ; KM=5 uM for 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) ; KM=219 uM for isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) ; KM=36.4 uM for chenodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) ; KM=1.7 uM for dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) ; KM=30.6 uM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius) ; KM=42.3 uM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius) ; KM=69 uM for DL-3-hydroxybutyryl-CoA ; KM=7.7 uM for 3alpha-hydroxy-5alpha-pregnan-20-one/allopregnanolone ; KM=30 uM for 3alpha-hydroxy-5alpha-pregnan-20-one/allopregnanolone ; KM=140 uM for tetramyristoyl cardiolipin ; KM=148 uM for tetralinoleoyl cardiolipin ; KM=40 uM for oxidized tetralinoleoyl cardiolipin ; KM=7.1 uM for (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA ; Vmax=14.8 umol/min/mg enzyme toward (2S,3S)-3-hydroxy-2- methylbutanoyl-CoA ; Vmax=150 umol/min/mg enzyme 3alpha-hydroxy-5alpha-pregnan-20- one/allopregnanolone ; Note=kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424). ; pH dependence: Optimum pH is 9.3 for the dehydrogenase reaction at 25 degrees Celsius, and 7.0 for the reductase reaction at 25 degrees Celsius. ; Amino-acid degradation; L-isoleucine degradation. Lipid metabolism; fatty acid beta-oxidation. Steroid metabolism. Lipid metabolism; bile acid biosynthesis. Homotetramer (PubMed:15342248, PubMed:20077426, PubMed:25925575). Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3 (PubMed:18984158, PubMed:25925575, PubMed:26950678, PubMed:28888424). Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex (PubMed:23042678, PubMed:29040705). Q99714; P05067: APP; NbExp=7; IntAct=EBI-79964, EBI-77613; Q99714; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-79964, EBI-821758; Q99714; P13639: EEF2; NbExp=3; IntAct=EBI-79964, EBI-352560; Q99714; Q12931: TRAP1; NbExp=3; IntAct=EBI-79964, EBI-1055869; Q99714; Q7L0Y3: TRMT10C; NbExp=22; IntAct=EBI-79964, EBI-2107046; Q99714-2; P05067: APP; NbExp=3; IntAct=EBI-25939412, EBI-77613; Mitochondrion tochondrion matrix, mitochondrion nucleoid Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q99714-1; Sequence=Displayed; Name=2; IsoId=Q99714-2; Sequence=VSP_007830; Ubiquitously expressed in normal tissues but is overexpressed in neurons affected in AD. HSD10 mitochondrial disease (HSD10MD) [MIM:300438]: An X- linked multisystemic disorder with highly variable severity. Age at onset ranges from the neonatal period to early childhood. Features include progressive neurodegeneration, psychomotor retardation, loss of mental and motor skills, seizures, cardiomyopathy, and visual and hearing impairment. Some patients manifest lactic acidosis and metabolic acidosis. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the short-chain dehydrogenases/reductases (SDR) family. tRNA binding RNA binding 3-hydroxyacyl-CoA dehydrogenase activity protein binding cytoplasm mitochondrion mitochondrial matrix plasma membrane lipid metabolic process mitochondrion organization tRNA processing cholate 7-alpha-dehydrogenase activity branched-chain amino acid catabolic process oxidoreductase activity testosterone dehydrogenase [NAD(P)] activity mitochondrial ribonuclease P complex dihydrotestosterone 17-beta-dehydrogenase activity 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity protein homotetramerization oxidation-reduction process mitochondrial tRNA methylation mitochondrial tRNA processing mitochondrial tRNA 5'-end processing mitochondrial tRNA 3'-end processing uc004dsl.1 uc004dsl.2 uc004dsl.3 
ENST00000168712.3 FGF4 ENST00000168712.3 fibroblast growth factor 4 (from RefSeq NM_002007.4) B7U994 ENST00000168712.1 ENST00000168712.2 FGF4 FGF4_HUMAN HST HSTF1 KS3 NM_002007 P08620 uc001opg.1 uc001opg.2 uc001opg.3 The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This gene was identified by its oncogenic transforming activity. This gene and FGF3, another oncogenic growth factor, are located closely on chromosome 11. Co-amplification of both genes was found in various kinds of human tumors. Studies on the mouse homolog suggested a function in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M17446.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968968, SAMEA2148093 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000168712.3/ ENSP00000168712.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal limb and cardiac valve development during embryogenesis. May play a role in embryonic molar tooth bud development via inducing the expression of MSX1, MSX2 and MSX1-mediated expression of SDC1 in dental mesenchyme cells (By similarity). Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P08620-1; Sequence=Displayed; Name=2; Synonyms=FGF4si; IsoId=P08620-2; Sequence=VSP_053541; [Isoform 2]: Antagonist of isoform 1, shutting down FGF4-induced Erk1/2 phosphorylation. Belongs to the heparin-binding growth factors family. MAPK cascade cartilage condensation positive regulation of protein phosphorylation fibroblast growth factor receptor binding extracellular region signal transduction cell-cell signaling multicellular organism development growth factor activity heparin binding positive regulation of cell proliferation fibroblast growth factor receptor signaling pathway mesenchymal cell proliferation regulation of gene expression positive regulation of gene expression stem cell population maintenance cell differentiation embryonic limb morphogenesis embryonic hindlimb morphogenesis odontogenesis of dentin-containing tooth negative regulation of apoptotic process positive regulation of transcription from RNA polymerase II promoter positive regulation of cell division positive regulation of protein kinase B signaling cranial suture morphogenesis apoptotic process involved in morphogenesis chondroblast differentiation positive regulation of ERK1 and ERK2 cascade cellular response to leukemia inhibitory factor regulation of endothelial cell chemotaxis to fibroblast growth factor uc001opg.1 uc001opg.2 uc001opg.3 
ENST00000168977.7 NMRK2 ENST00000168977.7 nicotinamide riboside kinase 2, transcript variant 2 (from RefSeq NM_170678.3) B7ZKR3 ENST00000168977.1 ENST00000168977.2 ENST00000168977.3 ENST00000168977.4 ENST00000168977.5 ENST00000168977.6 ITGB1BP3 NM_170678 NRK2 NRK2_HUMAN Q52M81 Q9NPI5 Q9NZK3 uc002lyz.1 uc002lyz.2 uc002lyz.3 uc002lyz.4 uc002lyz.5 Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. Involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. May play a role in the regulation of terminal myogenesis. Reaction=ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide D-ribonucleotide + H(+); Xref=Rhea:RHEA:14017, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.22; Evidence=; Reaction=ATP + beta-D-ribosylnicotinate = ADP + H(+) + nicotinate beta- D-ribonucleotide; Xref=Rhea:RHEA:25568, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57502, ChEBI:CHEBI:58527, ChEBI:CHEBI:456216; EC=2.7.1.173; Evidence=; Kinetic parameters: KM=0.19 mM for nicotinamide riboside (with ATP as cosubstrate) ; KM=30 mM for nicotinamide riboside (with GTP as cosubstrate) ; KM=0.11 mM for tiazofurin (with ATP as cosubstrate) ; KM=0.063 mM for nicotinic acid riboside (with ATP as cosubstrate) ; KM=1.3 mM for uridine (with ATP as cosubstrate) ; Cofactor biosynthesis; NAD(+) biosynthesis. Monomer (By similarity). Interacts with ITGB1 alone or when associated with alpha-7, but not with alpha-5. Q9NPI5; Q9Y561: LRP12; NbExp=2; IntAct=EBI-514059, EBI-296693; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NPI5-1; Sequence=Displayed; Name=2; IsoId=Q9NPI5-3; Sequence=VSP_054332; Predominantly expressed in skeletal muscle and, at a much lower level, in the heart (at protein level). No expression in brain, kidney, liver, lung, pancreas nor placenta. Down-regulated during myoblast differentiation. Belongs to the uridine kinase family. NRK subfamily. Sequence=AAF26711.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence=; nucleotide binding protein binding ATP binding nucleoplasm cytosol plasma membrane NAD biosynthetic process kinase activity phosphorylation transferase activity pyridine nucleotide biosynthetic process NAD metabolic process intracellular membrane-bounded organelle negative regulation of myoblast differentiation metal ion binding ribosylnicotinamide kinase activity ribosylnicotinate kinase activity uc002lyz.1 uc002lyz.2 uc002lyz.3 uc002lyz.4 uc002lyz.5 
ENST00000169298.8 ST6GAL1 ENST00000169298.8 ST6 beta-galactoside alpha-2,6-sialyltransferase 1, transcript variant 1 (from RefSeq NM_173216.2) A8KA14 B2R513 D3DNV3 ENST00000169298.1 ENST00000169298.2 ENST00000169298.3 ENST00000169298.4 ENST00000169298.5 ENST00000169298.6 ENST00000169298.7 NM_173216 P15907 SIAT1 SIAT1_HUMAN uc003frb.1 uc003frb.2 uc003frb.3 uc003frb.4 uc003frb.5 This gene encodes a member of glycosyltransferase family 29. The encoded protein is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The protein, which is normally found in the Golgi but can be proteolytically processed to a soluble form, is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB-6, CD75, and CD76. This gene has been incorrectly referred to as CD75. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2017]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660807.221866.1, SRR1660805.216305.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000169298.8/ ENSP00000169298.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Transfers sialic acid from CMP-sialic acid to galactose- containing acceptor substrates. Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N- acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP + H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398; EC=2.4.3.1; Evidence=; Inhibited by CTP. Kinetic parameters: KM=530 uM for CMP-NeuAc ; Vmax=1.074 pmol/min/ug enzyme ; Protein modification; protein glycosylation. Monomer and homodimer. Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P15907-1; Sequence=Displayed; Name=2; IsoId=P15907-2; Sequence=VSP_056076; The soluble form derives from the membrane form by proteolytic processing. The HB-6, CDW75, and CD76 differentiation antigens are cell- surface carbohydrate determinants generated by this enzyme. N-glycosylated. Belongs to the glycosyltransferase 29 family. Name=Functional Glycomics Gateway - GTase; Note=ST6Gal I; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_628"; Golgi membrane beta-galactoside alpha-2,6-sialyltransferase activity protein binding extracellular region Golgi apparatus N-acetylneuraminate metabolic process protein glycosylation humoral immune response sialyltransferase activity membrane integral component of membrane O-glycan processing transferase activity transferase activity, transferring glycosyl groups protein N-linked glycosylation via asparagine Golgi cisterna membrane protein homodimerization activity sialylation uc003frb.1 uc003frb.2 uc003frb.3 uc003frb.4 uc003frb.5 
ENST00000169551.11 TIMM21 ENST00000169551.11 translocase of inner mitochondrial membrane 21 (from RefSeq NM_014177.3) C18orf55 ENST00000169551.1 ENST00000169551.10 ENST00000169551.2 ENST00000169551.3 ENST00000169551.4 ENST00000169551.5 ENST00000169551.6 ENST00000169551.7 ENST00000169551.8 ENST00000169551.9 HSPC154 NM_014177 Q9BVV7 Q9P010 TIM21 TIM21_HUMAN uc010dqr.1 uc010dqr.2 uc010dqr.3 Participates in the translocation of transit peptide- containing proteins across the mitochondrial inner membrane. Also required for assembly of mitochondrial respiratory chain complex I and complex IV as component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex. Probably shuttles between the presequence translocase and respiratory-chain assembly intermediates in a process that promotes incorporation of early nuclear-encoded subunits into these complexes. Component of the TIM23 complex. Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, the core components of this complex being COA3/MITRAC12 and COX14 (Probable) (PubMed:23260140). Interacts with COA3 and MT-CO1/COX1 (PubMed:26321642). Q9BVV7; P00395: MT-CO1; NbExp=3; IntAct=EBI-6570759, EBI-2117234; Q9BVV7; O14925: TIMM23; NbExp=3; IntAct=EBI-6570759, EBI-1047996; Q9BVV7; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-6570759, EBI-947187; Mitochondrion membrane ; Single-pass membrane protein Belongs to the TIM21 family. molecular_function protein binding mitochondrion mitochondrial inner membrane presequence translocase complex protein transport membrane integral component of membrane protein import into mitochondrial matrix mitochondrial membrane mitochondrial respiratory chain complex I assembly mitochondrial respiratory chain complex IV assembly uc010dqr.1 uc010dqr.2 uc010dqr.3 
ENST00000170150.4 BPIFB2 ENST00000170150.4 BPI fold containing family B member 2 (from RefSeq NM_025227.3) BPIB2_HUMAN BPIL1 C20orf184 ENST00000170150.1 ENST00000170150.2 ENST00000170150.3 LPLUNC2 NM_025227 Q6UWN3 Q6ZME0 Q8N4F0 Q8NFQ7 UNQ2489/PRO5776 uc002wyj.1 uc002wyj.2 uc002wyj.3 uc002wyj.4 uc002wyj.5 uc002wyj.6 This gene encodes a member of the lipid transfer/lipopolysaccharide binding protein (LT/LBP) gene family. It is highly expressed in hypertrophic tonsils. This gene and three other members of the LT/LBP gene family form a cluster on the long arm of chromosome 20. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK027068.1, AK172819.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968832, SAMEA2150585 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000170150.4/ ENSP00000170150.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Secreted Highly expressed in tonsils, especially in hypertrophic tonsils. Detected at very low levels in fetal liver. Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. extracellular region extracellular space endoplasmic reticulum lumen lipid binding antimicrobial humoral response post-translational protein modification cellular protein metabolic process extracellular exosome uc002wyj.1 uc002wyj.2 uc002wyj.3 uc002wyj.4 uc002wyj.5 uc002wyj.6 
ENST00000170168.9 REXO1 ENST00000170168.9 RNA exonuclease 1 homolog (from RefSeq NM_020695.4) ELOABP1 ENST00000170168.1 ENST00000170168.2 ENST00000170168.3 ENST00000170168.4 ENST00000170168.5 ENST00000170168.6 ENST00000170168.7 ENST00000170168.8 KIAA1138 NM_020695 Q8N1G1 Q9ULT2 REXO1_HUMAN TCEB3BP1 uc002lua.1 uc002lua.2 uc002lua.3 uc002lua.4 uc002lua.5 uc002lua.6 Seems to have no detectable effect on transcription elongation in vitro. Interacts with TCEA2 and ELOA. Nucleus Ubiquitously expressed. Belongs to the REXO1/REXO3 family. Sequence=BAA86452.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleic acid binding nuclease activity exonuclease activity nucleus nucleoplasm nuclear body hydrolase activity nucleic acid phosphodiester bond hydrolysis uc002lua.1 uc002lua.2 uc002lua.3 uc002lua.4 uc002lua.5 uc002lua.6 
ENST00000170447.12 MKRN2 ENST00000170447.12 makorin ring finger protein 2, transcript variant 1 (from RefSeq NM_014160.5) A6NIA2 B3KRC5 B4DPR4 ENST00000170447.1 ENST00000170447.10 ENST00000170447.11 ENST00000170447.2 ENST00000170447.3 ENST00000170447.4 ENST00000170447.5 ENST00000170447.6 ENST00000170447.7 ENST00000170447.8 ENST00000170447.9 HSPC070 MKRN2_HUMAN NM_014160 Q8N391 Q96BD4 Q9BUY2 Q9H000 Q9NRY1 RNF62 uc003bxd.1 uc003bxd.2 uc003bxd.3 uc003bxd.4 uc003bxd.5 uc003bxd.6 This gene encodes a probable E3 ubiquitin ligase containing several zinc finger domains, that is a member of the makorin RING zinc-finger protein family. This gene overlaps the v-raf-1 murine leukemia viral oncogene homolog 1 (RAF1) gene in an antisense orientation and may have a co-regulatory function with RAF1. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2012]. E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Promotes the polyubiquitination and proteasome-dependent degradation of RELA/p65, thereby suppressing RELA-mediated NF-kappaB transactivation and negatively regulating inflammatory responses (By similarity). Plays a role in the regulation of spermiation and in male fertility (By similarity). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence=; Protein modification; protein ubiquitination. Interacts with PDLIM2 (via LIM zinc-binding domain) (By similarity). Interacts with RELA (By similarity). Q9H000; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-2341005, EBI-8643161; Q9H000; Q01658: DR1; NbExp=3; IntAct=EBI-2341005, EBI-750300; Q9H000; O00303: EIF3F; NbExp=3; IntAct=EBI-2341005, EBI-711990; Q9H000; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-2341005, EBI-1054873; Q9H000; P42858: HTT; NbExp=12; IntAct=EBI-2341005, EBI-466029; Q9H000; P63244: RACK1; NbExp=3; IntAct=EBI-2341005, EBI-296739; Q9H000; Q13148: TARDBP; NbExp=6; IntAct=EBI-2341005, EBI-372899; Q9H000; P51668: UBE2D1; NbExp=6; IntAct=EBI-2341005, EBI-743540; Q9H000; Q9Y2X8: UBE2D4; NbExp=6; IntAct=EBI-2341005, EBI-745527; Q9H000; E9KL35; NbExp=3; IntAct=EBI-2341005, EBI-8456500; Q9H000; PRO_0000037311 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-2341005, EBI-25474079; Q9H000; PRO_0000449621 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-2341005, EBI-25492388; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H000-1; Sequence=Displayed; Name=2; IsoId=Q9H000-2; Sequence=VSP_055275; Expressed in sperm, with significantly reduced expression in sperm of patients with oligoasthenoteratozoospermia (at protein level) (PubMed:28008940). Widely expressed with expression in testis, ovary, small intestine, colon, peripheral blood leukocytes, fetal liver, bone marrow, thymus, lymph node and spleen (PubMed:11597136). Partially overlaps and is antisense to the RAF1 proto- oncogene. RNA binding protein binding biological_process protein ubiquitination transferase activity metal ion binding uc003bxd.1 uc003bxd.2 uc003bxd.3 uc003bxd.4 uc003bxd.5 uc003bxd.6 
ENST00000170564.7 GPATCH1 ENST00000170564.7 G-patch domain containing 1, transcript variant 2 (from RefSeq NR_135270.2) ECGP ENST00000170564.1 ENST00000170564.2 ENST00000170564.3 ENST00000170564.4 ENST00000170564.5 ENST00000170564.6 GPATC1 GPTC1_HUMAN NR_135270 Q8IZV6 Q8N3B7 Q9BRR8 Q9NW94 uc002nug.1 uc002nug.2 uc002nug.3 Belongs to the GPATCH1 family. Sequence=BAA91489.1; Type=Erroneous initiation; Evidence=; Sequence=CAD39124.1; Type=Erroneous initiation; Evidence=; mRNA splicing, via spliceosome nucleic acid binding RNA binding nucleus mRNA processing catalytic step 2 spliceosome uc002nug.1 uc002nug.2 uc002nug.3 
ENST00000171111.10 KEAP1 ENST00000171111.10 kelch like ECH associated protein 1, transcript variant 1 (from RefSeq NM_203500.2) B3KPD5 ENST00000171111.1 ENST00000171111.2 ENST00000171111.3 ENST00000171111.4 ENST00000171111.5 ENST00000171111.6 ENST00000171111.7 ENST00000171111.8 ENST00000171111.9 INRF2 KEAP1 KEAP1_HUMAN KIAA0132 KLHL19 NM_203500 Q14145 Q6LEP0 Q8WTX1 Q9BPY9 uc002mor.1 uc002mor.2 uc002mor.3 This gene encodes a protein containing KELCH-1 like domains, as well as a BTB/POZ domain. Kelch-like ECH-associated protein 1 interacts with NF-E2-related factor 2 in a redox-sensitive manner and the dissociation of the proteins in the cytoplasm is followed by transportation of NF-E2-related factor 2 to the nucleus. This interaction results in the expression of the catalytic subunit of gamma-glutamylcysteine synthetase. Two alternatively spliced transcript variants encoding the same isoform have been found for this gene. [provided by RefSeq, Jul 2008]. Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination (PubMed:14585973, PubMed:15379550, PubMed:15572695, PubMed:15983046, PubMed:15601839). KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes (PubMed:15601839, PubMed:16006525). In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes (PubMed:19489739, PubMed:16006525, PubMed:17127771, PubMed:18251510, PubMed:29590092). In response to selective autophagy, KEAP1 is sequestered in inclusion bodies following its interaction with SQSTM1/p62, leading to inactivation of the BCR(KEAP1) complex and activation of NFE2L2/NRF2 (PubMed:20452972). The BCR(KEAP1) complex also mediates ubiquitination of SQSTM1/p62, increasing SQSTM1/p62 sequestering activity and degradation (PubMed:28380357). The BCR(KEAP1) complex also targets BPTF and PGAM5 for ubiquitination and degradation by the proteasome (PubMed:15379550, PubMed:17046835). Ubiquitin ligase activity of the BCR(KEAP1) complex is inhibited by oxidative stress and electrophile metabolites such as sulforaphane (PubMed:15983046, PubMed:17046835, PubMed:29590092, PubMed:30323285). Electrophile metabolites react with reactive cysteine residues in KEAP1 and trigger non-enzymatic covalent modifications of these cysteine residues, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex (PubMed:19489739, PubMed:17127771, PubMed:18251510, PubMed:29590092, PubMed:30323285). Selective autophagy also inactivates the BCR(KEAP1) complex via interaction between KEAP1 and SQSTM1/p62, which sequesters the complex in inclusion bodies and promotes its degradation (PubMed:20495340, PubMed:20452972). Protein modification; protein ubiquitination. Component of the BCR(KEAP1) E3 ubiquitin ligase complex, at least composed of 2 molecules of CUL3, 2 molecules of KEAP1, and RBX1 (PubMed:15572695, PubMed:15983046, PubMed:15601839, PubMed:17127771, PubMed:18251510, PubMed:24896564). Interacts with NFE2L2/NRF2; the interaction is direct (PubMed:15379550, PubMed:15601839, PubMed:16006525, PubMed:18387606, PubMed:16888629). Forms a ternary complex with NFE2L2/NRF2 and PGAM5 (PubMed:17046835). Interacts with (phosphorylated) SQSTM1/p62; the interaction is direct and inactivates the BCR(KEAP1) complex by sequestering it in inclusion bodies, promoting its degradation (PubMed:20495340, PubMed:20452972). Interacts with NFE2L1 (PubMed:16687406). Interacts with BPTF and PTMA (PubMed:15657435). Interacts with MAP1LC3B (PubMed:24089205). Interacts indirectly with ENC1 (PubMed:19424503). Interacts with SESN1 and SESN2 (PubMed:23274085). Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842). (Microbial infection) Interacts with ebolavirus protein VP24; this interaction activates transcription factor NFE2L2/NRF2 by blocking its interaction with KEAP1. Q14145; Q5JTC6: AMER1; NbExp=2; IntAct=EBI-751001, EBI-6169747; Q14145; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-751001, EBI-11954519; Q14145; P45381: ASPA; NbExp=4; IntAct=EBI-751001, EBI-750475; Q14145; O14525-2: ASTN1; NbExp=4; IntAct=EBI-751001, EBI-21977454; Q14145; A9UGY9: ATG5; NbExp=3; IntAct=EBI-751001, EBI-10175276; Q14145; Q9H1Y0: ATG5; NbExp=3; IntAct=EBI-751001, EBI-1047414; Q14145; Q2NKX9: C2orf68; NbExp=3; IntAct=EBI-751001, EBI-11603468; Q14145; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-751001, EBI-3866279; Q14145; Q9NPC3: CCNB1IP1; NbExp=4; IntAct=EBI-751001, EBI-745269; Q14145; P02452: COL1A1; NbExp=3; IntAct=EBI-751001, EBI-982999; Q14145; P02458-1: COL2A1; NbExp=3; IntAct=EBI-751001, EBI-12375799; Q14145; P68400: CSNK2A1; NbExp=3; IntAct=EBI-751001, EBI-347804; Q14145; Q13618: CUL3; NbExp=5; IntAct=EBI-751001, EBI-456129; Q14145; Q9NX09: DDIT4; NbExp=3; IntAct=EBI-751001, EBI-715104; Q14145; Q9NY33: DPP3; NbExp=10; IntAct=EBI-751001, EBI-718333; Q14145; Q96JC9: EAF1; NbExp=3; IntAct=EBI-751001, EBI-769261; Q14145; Q6P6B1: ERICH5; NbExp=3; IntAct=EBI-751001, EBI-11343491; Q14145; P62495: ETF1; NbExp=8; IntAct=EBI-751001, EBI-750990; Q14145; Q6P1L5: FAM117B; NbExp=6; IntAct=EBI-751001, EBI-3893327; Q14145; Q14440: GPErik; NbExp=3; IntAct=EBI-751001, EBI-10232920; Q14145; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-751001, EBI-11955647; Q14145; P28799: GRN; NbExp=3; IntAct=EBI-751001, EBI-747754; Q14145; A0A0C4DFT7: GYPA; NbExp=3; IntAct=EBI-751001, EBI-12044847; Q14145; B8Q183: GYPA; NbExp=4; IntAct=EBI-751001, EBI-10176190; Q14145; P02724: GYPA; NbExp=4; IntAct=EBI-751001, EBI-702665; Q14145; P05362: ICAM1; NbExp=3; IntAct=EBI-751001, EBI-1035358; Q14145; Q9BYX4: IFIH1; NbExp=3; IntAct=EBI-751001, EBI-6115771; Q14145; O14920: IKBKB; NbExp=6; IntAct=EBI-751001, EBI-81266; Q14145; Q4KMZ1: IQCC; NbExp=3; IntAct=EBI-751001, EBI-12206419; Q14145; P05107: ITGB2; NbExp=3; IntAct=EBI-751001, EBI-300173; Q14145; O95198: KLHL2; NbExp=5; IntAct=EBI-751001, EBI-746999; Q14145; Q8N4I8: KLHL3; NbExp=3; IntAct=EBI-751001, EBI-10230467; Q14145; Q9UH77: KLHL3; NbExp=3; IntAct=EBI-751001, EBI-8524663; Q14145; P62310: LSM3; NbExp=6; IntAct=EBI-751001, EBI-348239; Q14145; Q13257: MAD2L1; NbExp=8; IntAct=EBI-751001, EBI-78203; Q14145; O60336: MAPKBP1; NbExp=3; IntAct=EBI-751001, EBI-947402; Q14145; Q9BTE3-2: MCMBP; NbExp=3; IntAct=EBI-751001, EBI-9384556; Q14145; Q14494: NFE2L1; NbExp=28; IntAct=EBI-751001, EBI-2804436; Q14145; Q16236: NFE2L2; NbExp=37; IntAct=EBI-751001, EBI-2007911; Q14145; Q96TA1: NIBAN2; NbExp=9; IntAct=EBI-751001, EBI-2514593; Q14145; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-751001, EBI-741158; Q14145; Q9NZJ9: NUDT4; NbExp=3; IntAct=EBI-751001, EBI-4280066; Q14145; Q9UKX7: NUP50; NbExp=3; IntAct=EBI-751001, EBI-2371082; Q14145; Q8N573-5: OXR1; NbExp=3; IntAct=EBI-751001, EBI-10265887; Q14145; Q86YC2: PALB2; NbExp=5; IntAct=EBI-751001, EBI-1222653; Q14145; Q15149: PLEC; NbExp=3; IntAct=EBI-751001, EBI-297903; Q14145; P54619: PRKAG1; NbExp=6; IntAct=EBI-751001, EBI-1181439; Q14145; P06454-2: PTMA; NbExp=6; IntAct=EBI-751001, EBI-10194874; Q14145; Q6P9E2: RECK; NbExp=6; IntAct=EBI-751001, EBI-10253121; Q14145; Q04206: RELA; NbExp=4; IntAct=EBI-751001, EBI-73886; Q14145; P58004: SESN2; NbExp=3; IntAct=EBI-751001, EBI-3939642; Q14145; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-751001, EBI-358489; Q14145; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-751001, EBI-5235340; Q14145; Q13501: SQSTM1; NbExp=19; IntAct=EBI-751001, EBI-307104; Q14145; Q9UGK3: STAP2; NbExp=3; IntAct=EBI-751001, EBI-1553984; Q14145; Q9P0N9: TBC1D7; NbExp=3; IntAct=EBI-751001, EBI-3258000; Q14145; P54274: TERF1; NbExp=2; IntAct=EBI-751001, EBI-710997; Q14145; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-751001, EBI-739485; Q14145; Q9BRX9: WDR83; NbExp=7; IntAct=EBI-751001, EBI-7705033; Q14145; O76024: WFS1; NbExp=3; IntAct=EBI-751001, EBI-720609; Q14145; Q9P202: WHRN; NbExp=3; IntAct=EBI-751001, EBI-310886; Q14145; P58317: ZNF121; NbExp=3; IntAct=EBI-751001, EBI-1228269; Q14145; Q9NX65: ZSCAN32; NbExp=3; IntAct=EBI-751001, EBI-739949; Q14145; O88351: Ikbkb; Xeno; NbExp=2; IntAct=EBI-751001, EBI-447960; Q14145; P15314: Irf1; Xeno; NbExp=2; IntAct=EBI-751001, EBI-6115486; Q14145; Q64337: Sqstm1; Xeno; NbExp=2; IntAct=EBI-751001, EBI-645025; Cytoplasm cleus Note=Mainly cytoplasmic (PubMed:15601839). In response to selective autophagy, relocalizes to inclusion bodies following interaction with SQSTM1/p62 (PubMed:20452972). Broadly expressed, with highest levels in skeletal muscle. KEAP1 contains reactive cysteine residues that act as sensors for endogenously produced and exogenously encountered small molecules, which react with sulfhydryl groups and modify the cysteine sensors, leading to impair ability of the BCR(KEAP1) complex to ubiquitinate target proteins. The Kelch repeats mediate interaction with NFE2L2/NRF2, BPTF and PGAM5. Non-enzymatic covalent modifications of reactive cysteines by electrophile metabolites inactivate the BCR(KEAP1) complex (PubMed:17127771, PubMed:18251510, PubMed:29590092, PubMed:30323285). Accumulation of fumarate promotes the formation of cysteine S- succination (S-(2-succinyl)cysteine), leading to inactivate the BCR(KEAP1) complex and promote NFE2L2/NRF2 nuclear accumulation and activation (By similarity). Nitric oxide-dependent 8-Nitro-cGMP formation promotes cysteine guanylation (S-cGMP-cysteine), leading to NFE2L2/NRF2 nuclear accumulation and activation (By similarity). Itaconate, an anti-inflammatory metabolite generated in response to lipopolysaccharide, alkylates cysteines, activating NFE2L2/NRF2 (PubMed:29590092). Methylglyoxal, a reactive metabolite that accumulates when the glycolytic enzyme PGK1 is inhibited, promotes formation of a methylimidazole cross-link between proximal Cys-151 and Arg-135 on another KEAP1 molecule, resulting in an inactive dimer that inactivates the BCR(KEAP1) complex (PubMed:30323285). Degraded via a proteasomal-independent process during selective autophagy: interaction with phosphorylated SQSTM1/p62 sequesters KEAP1 in inclusion bodies, leading to its degradation. Auto-ubiquitinated by the BCR(KEAP1) complex (PubMed:15572695, PubMed:15983046). Quinone-induced oxidative stress, but not sulforaphane, increases its ubiquitination (PubMed:15572695, PubMed:15983046). Ubiquitination and subsequent degradation is most pronounced following prolonged exposure of cells to oxidative stress, particularly in glutathione-deficient cells that are highly susceptible to oxidative stress (PubMed:15572695, PubMed:15983046). Belongs to the KEAP1 family. The mechanism of inactivation of the BCR(KEAP1) complex by covalent modifications of reactive cysteines is unclear. Covalent modifications were initially thought to disrupt interaction between KEAP1 and NFE2L2/NRF2 (By similarity). Recent publications suggest that cysteine modifications disrupt the interaction between KEAP1 and CUL3 without affecting the interaction between KEAP1 and NFE2L2/NRF2 (PubMed:16006525, PubMed:17127771, PubMed:18251510, PubMed:24896564). Sequence=BAA09481.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; in utero embryonic development protein binding nucleus nucleoplasm cytoplasm endoplasmic reticulum microtubule organizing center cytosol actin filament regulation of transcription, DNA-templated transcription factor binding proteasomal ubiquitin-independent protein catabolic process viral process protein ubiquitination protein deubiquitination midbody Cul3-RING ubiquitin ligase complex positive regulation of proteasomal ubiquitin-dependent protein catabolic process macromolecular complex identical protein binding protein homodimerization activity cytoplasmic sequestering of transcription factor negative regulation of sequence-specific DNA binding transcription factor activity post-translational protein modification regulation of epidermal cell differentiation cellular response to interleukin-4 disordered domain specific binding uc002mor.1 uc002mor.2 uc002mor.3 
ENST00000171757.3 P2RY10 ENST00000171757.3 P2Y receptor family member 10, transcript variant 1 (from RefSeq NM_014499.4) D3DTE5 ENST00000171757.1 ENST00000171757.2 NM_014499 O00398 P2Y10_HUMAN Q4VBN7 Q86V16 uc004ede.1 uc004ede.2 uc004ede.3 uc004ede.4 uc004ede.5 The protein encoded by this gene belongs to the family of G-protein coupled receptors that are preferentially activated by adenosine and uridine nucleotides. There is a pseudogene for this gene nearby on chromosome X. Multiple alternatively spliced transcripts have been observed. [provided by RefSeq, Apr 2016]. Putative receptor for purines coupled to G-proteins. Cell membrane; Multi-pass membrane protein. Weakly expressed in blood leukocytes. Up-regulated during promyelocytic cell differentiation along the monocytic pathway, but not during granulocytic differentiation. Belongs to the G-protein coupled receptor 1 family. G-protein coupled receptor activity plasma membrane integral component of plasma membrane signal transduction G-protein coupled receptor signaling pathway membrane integral component of membrane positive regulation of Rho protein signal transduction G-protein coupled purinergic nucleotide receptor signaling pathway G-protein coupled purinergic nucleotide receptor activity positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway uc004ede.1 uc004ede.2 uc004ede.3 uc004ede.4 uc004ede.5 
ENST00000172229.8 NGFR ENST00000172229.8 nerve growth factor receptor (from RefSeq NM_002507.4) B2R961 B4E096 ENST00000172229.1 ENST00000172229.2 ENST00000172229.3 ENST00000172229.4 ENST00000172229.5 ENST00000172229.6 ENST00000172229.7 NM_002507 P08138 TNFRSF16 TNR16_HUMAN uc002ioz.1 uc002ioz.2 uc002ioz.3 uc002ioz.4 uc002ioz.5 uc002ioz.6 Nerve growth factor receptor contains an extracellular domain containing four 40-amino acid repeats with 6 cysteine residues at conserved positions followed by a serine/threonine-rich region, a single transmembrane domain, and a 155-amino acid cytoplasmic domain. The cysteine-rich region contains the nerve growth factor binding domain. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC050309.1, M14764.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000172229.8/ ENSP00000172229.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4. Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:24908487). Plays an important role in differentiation and survival of specific neuronal populations during development (By similarity). Can mediate cell survival as well as cell death of neural cells. Plays a role in the inactivation of RHOA (PubMed:26646181). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin- dependent glucose uptake (By similarity). Necessary for the circadian oscillation of the clock genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCmgetaN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (PubMed:23785138). Homodimer; disulfide-linked (By similarity). Heterodimer with SORCS2. The extracellular domains of the heterodimer bind NGF (PubMed:22155786, PubMed:24908487). The cytoplasmic region of the heterodimer binds TRIO. NGF binding mediates dissociation of TRIO from the receptor complex (PubMed:22155786). Interacts with RTN4R (PubMed:19052207). Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and RANBP9 (PubMed:10514511, PubMed:9915784, PubMed:10544233, PubMed:12963025). Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1 (PubMed:11244088). Interacts with BEX1 (By similarity). Interacts with BEX3 (By similarity). Interacts with KIDINS220 and NTRK1. Can form a ternary complex with NTRK1 and KIDINS220 and this complex is affected by the expression levels of KIDINS220. An increase in KIDINS220 expression leads to a decreased association of NGFR and NTRK1. Interacts with NTRK2; may regulate the ligand specificity of the NTRK2 receptor (By similarity). Interacts (via death domain) with RAB31 (By similarity). Interacts with LINGO1 (PubMed:14966521). Interacts with NRADD (By similarity). Interacts with MAGED1; the interaction antagonizes the association NGFR:NTRK1 (By similarity). Interacts (via death domain) with ARHGDIA and RIPK2 (PubMed:26646181). P08138; P05067: APP; NbExp=2; IntAct=EBI-1387782, EBI-77613; P08138; PRO_0000000093 [P05067]: APP; NbExp=2; IntAct=EBI-1387782, EBI-2431589; P08138; P33681: CD80; NbExp=3; IntAct=EBI-1387782, EBI-1031024; P08138; Q96FE5: LINGO1; NbExp=2; IntAct=EBI-1387782, EBI-719955; P08138; P01138: NGF; NbExp=2; IntAct=EBI-1387782, EBI-1028250; P08138; PRO_0000019600 [P01138]: NGF; NbExp=2; IntAct=EBI-1387782, EBI-9249861; P08138; Q9Y467: SALL2; NbExp=3; IntAct=EBI-1387782, EBI-746180; P08138; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1387782, EBI-5235340; P08138; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-1387782, EBI-357085; P08138; O75509: TNFRSF21; NbExp=4; IntAct=EBI-1387782, EBI-2313231; P08138; P25233: Ndn; Xeno; NbExp=3; IntAct=EBI-1387782, EBI-1801080; P08138; Q9CPR8: Nsmce3; Xeno; NbExp=3; IntAct=EBI-1387782, EBI-5529102; Cell membrane ; Single-pass type I membrane protein Perikaryon Cell projection, growth cone Cell projection, dendritic spine Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P08138-1; Sequence=Displayed; Name=2; IsoId=P08138-2; Sequence=VSP_056850; The death domain mediates interaction with RANBP9 (By similarity). It also mediates interaction with ARHGDIA and RIPK2 (PubMed:26646181). The extracellular domain is responsible for interaction with NTRK1. N- and O-glycosylated. O-linked glycans consist of Gal(1-3)GalNAc core elongated by 1 or 2 NeuNAc. Phosphorylated on serine residues. beta-amyloid binding cellular glucose homeostasis transmembrane signaling receptor activity death receptor activity protein binding calmodulin binding extracellular region nucleoplasm endosome cytosol plasma membrane integral component of plasma membrane intracellular protein transport apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process signal transduction Rho protein signal transduction multicellular organism development nervous system development cell surface coreceptor activity membrane integral component of membrane Rab GTPase binding cell differentiation growth cone membrane protein intracellular domain proteolysis ubiquitin protein ligase binding circadian regulation of gene expression signaling receptor activity glucose homeostasis cell projection positive regulation of apoptotic process negative regulation of apoptotic process neurotrophin binding negative regulation of cysteine-type endopeptidase activity involved in apoptotic process dendritic spine perikaryon regulation of cysteine-type endopeptidase activity involved in apoptotic process neurotrophin TRK receptor signaling pathway nerve growth factor binding rhythmic process negative regulation of axonogenesis positive regulation of axonogenesis neuron apoptotic process positive regulation of protein localization to nucleus positive regulation of pri-miRNA transcription from RNA polymerase II promoter negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis cellular response to beta-amyloid uc002ioz.1 uc002ioz.2 uc002ioz.3 uc002ioz.4 uc002ioz.5 uc002ioz.6 
ENST00000173229.7 NTN1 ENST00000173229.7 netrin 1 (from RefSeq NM_004822.3) E9KL51 ENST00000173229.1 ENST00000173229.2 ENST00000173229.3 ENST00000173229.4 ENST00000173229.5 ENST00000173229.6 NET1_HUMAN NM_004822 NTN1L O95631 uc002glw.1 uc002glw.2 uc002glw.3 uc002glw.4 uc002glw.5 Netrin is included in a family of laminin-related secreted proteins. The function of this gene has not yet been defined; however, netrin is thought to be involved in axon guidance and cell migration during development. Mutations and loss of expression of netrin suggest that variation in netrin may be involved in cancer development. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U75586.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142348, SAMEA2154665 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000173229.7/ ENSP00000173229.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Involved in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977). It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in tumorigenesis by regulating apoptosis (PubMed:15343335). Binds to its receptors; DCC, UNC5A, UNC5B, UNC5C and probably UNC5D (PubMed:9950216). Binds to its receptor; DSCAM (PubMed:19196994). Interacts with APP (By similarity). O95631; PRO_0000000089 [P05067]: APP; NbExp=3; IntAct=EBI-2678626, EBI-20829246; O95631; PRO_0000000092 [P05067]: APP; NbExp=6; IntAct=EBI-2678626, EBI-821758; O95631; P43146: DCC; NbExp=4; IntAct=EBI-2678626, EBI-1222919; O95631; Q8NBI3: DRAXIN; NbExp=3; IntAct=EBI-2678626, EBI-10827752; O95631; Q8IZJ1-2: UNC5B; NbExp=2; IntAct=EBI-2678626, EBI-10832046; Secreted Cytoplasm Note=Mainly secreted. Widely expressed in normal adult tissues with highest levels in heart, small intestine, colon, liver and prostate. Reduced expression in brain tumors and neuroblastomas. Expressed in epididymis (at protein level). Mirror movements 4 (MRMV4) [MIM:618264]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities. MRMV4 inheritance is autosomal dominant. Note=The disease is caused by variants affecting the gene represented in this entry. neuron migration protein binding extracellular region basement membrane cytoplasm apoptotic process substrate-dependent cell migration, cell extension nuclear migration Ras protein signal transduction axonogenesis axon guidance motor neuron axon guidance positive regulation of cell proliferation animal organ morphogenesis tissue development dendrite development regulation of cell migration negative regulation of axon extension mammary gland development Cdc42 protein signal transduction anterior/posterior axon guidance inner ear morphogenesis positive regulation of axon extension regulation of synapse assembly mammary gland duct morphogenesis chemorepulsion of axon cell-cell adhesion negative regulation of netrin-activated signaling pathway positive regulation of cell motility uc002glw.1 uc002glw.2 uc002glw.3 uc002glw.4 uc002glw.5 
ENST00000173527.6 ISOC1 ENST00000173527.6 isochorismatase domain containing 1 (from RefSeq NM_016048.2) CGI-111 ENST00000173527.1 ENST00000173527.2 ENST00000173527.3 ENST00000173527.4 ENST00000173527.5 ISOC1_HUMAN NM_016048 Q7Z770 Q96CN7 uc003kva.1 uc003kva.2 uc003kva.3 uc003kva.4 uc003kva.5 Q96CN7; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-2805787, EBI-749920; Belongs to the isochorismatase family. Sequence=AAH08367.1; Type=Erroneous initiation; Evidence=; Sequence=AAH14105.2; Type=Erroneous initiation; Evidence=; molecular_function catalytic activity protein binding cytoplasm peroxisome biological_process uc003kva.1 uc003kva.2 uc003kva.3 uc003kva.4 uc003kva.5 
ENST00000173898.12 TRO ENST00000173898.12 trophinin, transcript variant 6 (from RefSeq NM_001039705.3) B1AKE9 B1AKF1 ENST00000173898.1 ENST00000173898.10 ENST00000173898.11 ENST00000173898.2 ENST00000173898.3 ENST00000173898.4 ENST00000173898.5 ENST00000173898.6 ENST00000173898.7 ENST00000173898.8 ENST00000173898.9 F5GY27 KIAA1114 MAGED3 NM_001039705 Q12816 Q96SX2 Q9NU89 Q9UPN8 TROP_HUMAN uc004dtq.1 uc004dtq.2 uc004dtq.3 uc004dtq.4 uc004dtq.5 uc004dtq.6 uc004dtq.7 This gene encodes a membrane protein that mediates cell adhesion between trophoblastic cells and the epithelial cells of the endometrium. The encoded protein participates in cell signalling during embryo implantation, and may also be involved in cancer formation. This gene is located near several other closely related genes on chromosome X. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2012]. Could be involved with bystin and tastin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation. Directly responsible for homophilic cell adhesion. Directly binds bystin, and indirectly tastin. Q12816; Q13895: BYSL; NbExp=4; IntAct=EBI-950001, EBI-358049; Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q12816-1; Sequence=Displayed; Name=2; IsoId=Q12816-2; Sequence=VSP_043513, VSP_043514; Name=3; IsoId=Q12816-3; Sequence=VSP_053937; Name=4; IsoId=Q12816-4; Sequence=VSP_053938; Name=5; IsoId=Q12816-5; Sequence=VSP_053938, VSP_043513, VSP_043514; Strong expression at implantation sites. Found in the placenta from the sixth week of pregnancy. Was localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the level decreased and then disappeared from placental villi. Also found in macrophages. Sequence=AAA79334.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAA83066.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; protein binding cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules embryo implantation intrinsic component of plasma membrane uc004dtq.1 uc004dtq.2 uc004dtq.3 uc004dtq.4 uc004dtq.5 uc004dtq.6 uc004dtq.7 
ENST00000174618.5 MNT ENST00000174618.5 MAX network transcriptional repressor (from RefSeq NM_020310.3) A8K6D1 BHLHD3 D3DTI7 ENST00000174618.1 ENST00000174618.2 ENST00000174618.3 ENST00000174618.4 MNT_HUMAN NM_020310 Q1ED38 Q99583 ROX uc002fur.1 uc002fur.2 uc002fur.3 uc002fur.4 uc002fur.5 The Myc/Max/Mad network comprises a group of transcription factors that co-interact to regulate gene-specific transcriptional activation or repression. This gene encodes a protein member of the Myc/Max/Mad network. This protein has a basic-Helix-Loop-Helix-zipper domain (bHLHzip) with which it binds the canonical DNA sequence CANNTG, known as the E box, following heterodimerization with Max proteins. This protein is likely a transcriptional repressor and an antagonist of Myc-dependent transcriptional activation and cell growth. This protein represses transcription by binding to DNA binding proteins at its N-terminal Sin3-interaction domain. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC117563.1, X96401.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000174618.5/ ENSP00000174618.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'. Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer with MAX. Q99583; P61244: MAX; NbExp=8; IntAct=EBI-7959025, EBI-751711; Q99583; Q99583: MNT; NbExp=2; IntAct=EBI-7959025, EBI-7959025; Q99583; O43639: NCK2; NbExp=3; IntAct=EBI-7959025, EBI-713635; Q99583; Q60520: Sin3a; Xeno; NbExp=3; IntAct=EBI-7959025, EBI-349034; Nucleus. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding chromatin binding transcription factor activity, sequence-specific DNA binding transcription coactivator activity transcription corepressor activity nucleus nucleoplasm regulation of transcription, DNA-templated transcription from RNA polymerase II promoter multicellular organism development cell aging negative regulation of cell proliferation protein dimerization activity regulation of cell cycle positive regulation of nucleic acid-templated transcription negative regulation of apoptotic signaling pathway uc002fur.1 uc002fur.2 uc002fur.3 uc002fur.4 uc002fur.5 
ENST00000175091.5 LAPTM4A ENST00000175091.5 lysosomal protein transmembrane 4 alpha (from RefSeq NM_014713.5) D6W522 ENST00000175091.1 ENST00000175091.2 ENST00000175091.3 ENST00000175091.4 LAPTM4A NM_014713 Q6IBP4 Q6IBP4_HUMAN hCG_32086 uc002rdm.1 uc002rdm.2 uc002rdm.3 uc002rdm.4 This gene encodes a protein that has four predicted transmembrane domains. The function of this gene has not yet been determined; however, studies in the mouse homolog suggest a role in the transport of small molecules across endosomal and lysosomal membranes. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: ERR279841.1653.1, BC003158.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142853, SAMEA2149178 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000175091.5/ ENSP00000175091.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May function in the transport of nucleosides and/or nucleoside derivatives between the cytosol and the lumen of an intracellular membrane-bound compartment. Endomembrane system ; Multi-pass membrane protein Belongs to the LAPTM4/LAPTM5 transporter family. membrane integral component of membrane uc002rdm.1 uc002rdm.2 uc002rdm.3 uc002rdm.4 
ENST00000175238.10 ADAM7 ENST00000175238.10 ADAM metallopeptidase domain 7 (from RefSeq NM_003817.4) A8K8X7 ADAM7 ADAM7_HUMAN ENST00000175238.1 ENST00000175238.2 ENST00000175238.3 ENST00000175238.4 ENST00000175238.5 ENST00000175238.6 ENST00000175238.7 ENST00000175238.8 ENST00000175238.9 GP83 NM_003817 O75959 Q6PEJ6 Q9H2U9 uc003xeb.1 uc003xeb.2 uc003xeb.3 uc003xeb.4 This gene encodes a member of the ADAMs family of zinc proteases. These transmembrane proteins play roles in multiple processes including cell signaling, adhesion and migration. The encoded protein lacks protease activity and may play roles in protein-protein interactions and cell adhesion processes including sperm-egg fusion. Mutations in this gene may be involved in the progression of melanoma. [provided by RefSeq, Oct 2011]. ##Evidence-Data-START## Transcript exon combination :: AF215824.1, GQ891358.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA2153427, SAMEA2161674 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000175238.10/ ENSP00000175238.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Required for normal male fertility via maintenance of epithelial cell morphology in the caput epididymis and subsequently correct epididymis lumen structure required for sperm development (By similarity). Plays a role in sperm motility, flagella morphology and tyrosine phosphorylation during sperm capacitance (By similarity). Plays a role in normal expression levels of HSPA5, ITM2B and ADAM2 in sperm both prior to and post-capacitation (By similarity). This is a non catalytic metalloprotease-like protein (By similarity). Interacts with ITM2B in sperm; the interaction increases following capacitation (By similarity). Interacts with HSPA5 and CANX (By similarity). Membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H2U9-1; Sequence=Displayed; Name=2; IsoId=Q9H2U9-2; Sequence=VSP_056602, VSP_056603; Note=Has been found to be frequently mutated in melanoma (PubMed:21618342). ADAM7 mutations may play a role in melanoma progression and metastasis (PubMed:21618342). Expressed in melanoma cells but not in healthy melanocytes (PubMed:21618342). endopeptidase activity metalloendopeptidase activity plasma membrane proteolysis metallopeptidase activity membrane integral component of membrane uc003xeb.1 uc003xeb.2 uc003xeb.3 uc003xeb.4 
ENST00000175756.10 PTPN18 ENST00000175756.10 protein tyrosine phosphatase non-receptor type 18, transcript variant 1 (from RefSeq NM_014369.4) B4E1E6 BDP1 ENST00000175756.1 ENST00000175756.2 ENST00000175756.3 ENST00000175756.4 ENST00000175756.5 ENST00000175756.6 ENST00000175756.7 ENST00000175756.8 ENST00000175756.9 NM_014369 PTN18_HUMAN Q53P42 Q99952 uc002trc.1 uc002trc.2 uc002trc.3 uc002trc.4 The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, the mitotic cycle, and oncogenic transformation. This PTP contains a PEST motif, which often serves as a protein-protein interaction domain, and may be related to protein intracellular half-live. This protein can differentially dephosphorylate autophosphorylated tyrosine kinases that are overexpressed in tumor tissues, and it appears to regulate HER2, a member of the epidermal growth factor receptor family of receptor tyrosine kinases. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2008]. Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues. Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence= Interacts with PSTPIP1. Q99952; Q9Y297: BTRC; NbExp=2; IntAct=EBI-1384210, EBI-307461; Q99952; P04626: ERBB2; NbExp=6; IntAct=EBI-1384210, EBI-641062; Q99952; O43586: PSTPIP1; NbExp=5; IntAct=EBI-1384210, EBI-1050964; Q99952-1; Q9Y297: BTRC; NbExp=2; IntAct=EBI-12739708, EBI-307461; Q99952-1; P04626: ERBB2; NbExp=5; IntAct=EBI-12739708, EBI-641062; Nucleus Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q99952-1; Sequence=Displayed; Name=2; IsoId=Q99952-2; Sequence=VSP_043073; Expressed in brain, colon and several tumor-derived cell lines. Belongs to the protein-tyrosine phosphatase family. Non- receptor class 4 subfamily. blastocyst formation phosphoprotein phosphatase activity protein tyrosine phosphatase activity non-membrane spanning protein tyrosine phosphatase activity protein binding nucleus nucleoplasm cytoplasm cytosol protein dephosphorylation dephosphorylation hydrolase activity phosphatase activity peptidyl-tyrosine dephosphorylation ERBB2 signaling pathway cellular response to cytokine stimulus negative regulation of ERBB signaling pathway uc002trc.1 uc002trc.2 uc002trc.3 uc002trc.4 
ENST00000176183.6 DRD4 ENST00000176183.6 dopamine receptor D4 (from RefSeq NM_000797.4) B0M0J7 DRD4_HUMAN ENST00000176183.1 ENST00000176183.2 ENST00000176183.3 ENST00000176183.4 ENST00000176183.5 NM_000797 P21917 Q7Z7Q5 Q8NGM5 uc001lqp.1 uc001lqp.2 uc001lqp.3 uc001lqp.4 This gene encodes the D4 subtype of the dopamine receptor. The D4 subtype is a G-protein coupled receptor which inhibits adenylyl cyclase. It is a target for drugs which treat schizophrenia and Parkinson disease. Mutations in this gene have been associated with various behavioral phenotypes, including autonomic nervous system dysfunction, attention deficit/hyperactivity disorder, and the personality trait of novelty seeking. This gene contains a polymorphic number (2-10 copies) of tandem 48 nt repeats; the sequence shown contains four repeats. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: EU432112.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2152568, SAMEA2159931 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000176183.6/ ENSP00000176183.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Activated by dopamine, but also by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs (PubMed:9003072, PubMed:16423344, PubMed:27659709, PubMed:29051383). Agonist binding triggers signaling via G proteins that inhibit adenylyl cyclase (PubMed:7512953, PubMed:7643093, PubMed:16423344, PubMed:27659709, PubMed:29051383). Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells (By similarity). Signaling in response to agonists such as dopamine, epinephrine and norepinephrine is modulated by Na(+); lower Na(+) levels result in higher receptor activity (in vitro). Forms homo- and heterooligomers with DRD2. D4.7 allele exhibits higher affinity for homodimers compared to DRD2 heterodimers, while alleles D42. and 4.4 have similar affinities for both. The interaction with DRD2 may modulate agonist-induced downstream signaling (PubMed:21184734). Interacts with CLIC6 (By similarity). Interacts with GPRASP1 (PubMed:12142540). May interact with ADORA2A (PubMed:20836733). Interacts with KLHL12 (PubMed:18303015). P21917; P05067: APP; NbExp=6; IntAct=EBI-8592297, EBI-77613; P21917; P21917: DRD4; NbExp=5; IntAct=EBI-8592297, EBI-8592297; P21917; P17677: GAP43; NbExp=3; IntAct=EBI-8592297, EBI-1267511; P21917; P50579: METAP2; NbExp=3; IntAct=EBI-8592297, EBI-2214155; P21917; Q96P71-2: NECAB3; NbExp=3; IntAct=EBI-8592297, EBI-15098952; P21917; P61764: STXBP1; NbExp=3; IntAct=EBI-8592297, EBI-960169; Cell membrane ulti-pass membrane protein Highly expressed in retina. Detected at much lower levels in brain, in amygdala, thalamus, hypothalamus, cerebellum and pituitary. Polyubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex: polyubiquitination does not lead to degradation of DRD4 protein. Palmitoylated. Palmitoylation of the C-terminal Cys is important for normal expression at the cell membrane. The number of repeats of 16 amino acids in the third cytoplasmic loop is highly polymorphic and varies among different alleles. Alleles corresponding in size to a 2 (D4.2), 3 (D4.3), 4 (D4.4), 5 (D4.5), 6 (D4.6), 7 (D4.7) and 9 (D4.9) repeats have been described. The sequence shown is that of allele D4.4. The polymorphic repeat sequence has little influence on DRD4-binding profiles and might not be essential for G protein interaction. Belongs to the G-protein coupled receptor 1 family. Sequence=AAL58637.1; Type=Erroneous gene model prediction; Evidence=; activation of MAPK activity dopamine neurotransmitter receptor activity, coupled via Gi/Go behavioral fear response synaptic transmission, dopaminergic response to amphetamine G-protein coupled receptor activity dopamine neurotransmitter receptor activity G-protein coupled serotonin receptor activity protein binding plasma membrane integral component of plasma membrane cellular calcium ion homeostasis signal transduction G-protein coupled receptor signaling pathway G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger adenylate cyclase-inhibiting dopamine receptor signaling pathway dopamine receptor signaling pathway chemical synaptic transmission drug binding adult locomotory behavior potassium channel regulator activity membrane integral component of membrane SH3 domain binding dendrite neurotransmitter receptor activity positive regulation of sodium:proton antiporter activity positive regulation of kinase activity response to histamine social behavior dopamine binding regulation of dopamine metabolic process dopamine metabolic process fear response regulation of circadian rhythm identical protein binding metal ion binding behavioral response to cocaine behavioral response to ethanol rhythmic process arachidonic acid secretion negative regulation of protein secretion epinephrine binding norepinephrine binding positive regulation of dopamine uptake involved in synaptic transmission inhibitory postsynaptic potential postsynapse glutamatergic synapse negative regulation of voltage-gated calcium channel activity uc001lqp.1 uc001lqp.2 uc001lqp.3 uc001lqp.4 
ENST00000176195.4 SCT ENST00000176195.4 secretin (from RefSeq NM_021920.4) ENST00000176195.1 ENST00000176195.2 ENST00000176195.3 NM_021920 P09683 SCT SECR_HUMAN uc001lqo.1 uc001lqo.2 uc001lqo.3 This gene encodes a member of the glucagon family of peptides. The encoded preproprotein is secreted by endocrine S cells in the proximal small intestinal mucosa as a prohormone, then proteolytically processed to generate the mature peptide hormone. The release of this active peptide hormone is stimulated by either fatty acids or acidic pH in the duodenum. This hormone stimulates the secretion of bile and bicarbonate in the duodenum, pancreatic and biliary ducts. [provided by RefSeq, Feb 2016]. CCDS Note: No human mRNA or EST accessions have been deposited in public databases to support this CCDS, but the gene, transcript and protein have been well-characterized in the literature, e.g., PMIDs:2315322, 12160732, 15706223 and 16888198. Secretin proteins in other species also support this CCDS. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: HY019819.1, HY055530.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142348, SAMEA2144835 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000176195.4/ ENSP00000176195.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Hormone involved in different processes, such as regulation of the pH of the duodenal content, food intake and water homeostasis (PubMed:25332973). Exerts its biological effects by binding to secretin receptor (SCTR), a G-protein coupled receptor expressed in the basolateral domain of several cells (PubMed:25332973). Acts as a key gastrointestinal hormone by regulating the pH of the duodenal content (By similarity). Secreted by S cells of the duodenum in the crypts of Lieberkuehn and regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). Production of bicarbonate is essential to neutralize the pH and ensure no damage is done to the small intestine by the gastric acid (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation (Probable). Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation (By similarity). Also able to stimulate lipolysis in white adipocytes (By similarity). Also plays an important role in cellular osmoregulation: released into the systemic circulation in response to hyperosmolality and acts at different levels in the hypothalamus, pituitary and kidney to regulate water homeostasis (By similarity). Also plays a role in the central nervous system, possibly by acting as a neuropeptide hormone: required for hippocampal synaptic function and neural progenitor cells maintenance (By similarity). P09683; O14964: HGS; NbExp=3; IntAct=EBI-12844598, EBI-740220; P09683; P49639: HOXA1; NbExp=3; IntAct=EBI-12844598, EBI-740785; P09683; O14770-4: MEIS2; NbExp=3; IntAct=EBI-12844598, EBI-8025850; P09683; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12844598, EBI-739895; Secreted Serum secretin levels are increased after single-meal ingestion. Belongs to the glucagon family. Name=Wikipedia; Note=Secretin entry; URL="https://en.wikipedia.org/wiki/Secretin"; G-protein coupled receptor binding diet induced thermogenesis receptor binding hormone activity cellular_component extracellular region extracellular space cell G-protein coupled receptor signaling pathway brain development cellular water homeostasis hippocampus development pancreatic juice secretion response to nutrient levels regulation of appetite positive regulation of cAMP-mediated signaling digestive hormone activity protein N-terminus binding regulation of synaptic plasticity embryonic digestive tract development positive regulation of lipid catabolic process positive regulation of pancreatic juice secretion positive regulation of somatostatin secretion negative regulation of gastrin-induced gastric acid secretion uc001lqo.1 uc001lqo.2 uc001lqo.3 
ENST00000176643.11 ALDH3A2 ENST00000176643.11 aldehyde dehydrogenase 3 family member A2, transcript variant 2 (from RefSeq NM_000382.3) AL3A2_HUMAN ALDH10 ENST00000176643.1 ENST00000176643.10 ENST00000176643.2 ENST00000176643.3 ENST00000176643.4 ENST00000176643.5 ENST00000176643.6 ENST00000176643.7 ENST00000176643.8 ENST00000176643.9 FALDH NM_000382 P51648 Q6I9T3 Q93011 Q96J37 uc002gwb.1 uc002gwb.2 uc002gwb.3 Aldehyde dehydrogenase isozymes are thought to play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. This gene product catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acid. Mutations in the gene cause Sjogren-Larsson syndrome. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Catalyzes the oxidation of medium and long chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length (PubMed:9133646, PubMed:22633490, PubMed:25047030, PubMed:18035827, PubMed:9662422, PubMed:18182499). Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (PubMed:22633490). Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence= Reaction=a fatty aldehyde + H2O + NAD(+) = a fatty acid + 2 H(+) + NADH; Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Reaction=(2E)-hexadecenal + H2O + NAD(+) = (E)-hexadec-2-enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:72745; Evidence=; Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+); Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Reaction=22-oxodocosanoate + H2O + NAD(+) = docosanedioate + 2 H(+) + NADH; Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298, ChEBI:CHEBI:76299; Evidence=; Reaction=2,6,10,14-tetramethylpentadecanal + H2O + NAD(+) = 2,6,10,14- tetramethylpentadecanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44016, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268; Evidence=; Reaction=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate; Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Reaction=dodecanoate + 2 H(+) + NADH = dodecanal + H2O + NAD(+); Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Reaction=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate; Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:84067; Evidence= Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate; Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Reaction=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH; Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; Reaction=(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+) + NADH; Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83276; EC=1.2.1.94; Evidence=; Kinetic parameters: KM=50 uM for hexanal ; KM=32 uM for octanal ; KM=23 uM for decanal ; KM=3.8 uM for decanal ; KM=19 uM for dodecanal ; KM=13.6 uM for dodecanal ; KM=23 uM for tetradecanal ; KM=10.3 uM for tetradecanal ; KM=8.3 uM for hexadecanal ; KM=32 uM for hexadecanal ; KM=21 uM for octadecanal ; KM=20 uM for octadecanal ; KM=23 uM for farnesal ; KM=280 uM for NAD ; KM=180 uM for NAD ; KM=8700 uM for NADP ; Vmax=29 umol/min/mg enzyme with hexanal ; Vmax=63 umol/min/mg enzyme with octanal ; Vmax=73 umol/min/mg enzyme with decanal ; Vmax=2.3 umol/min/mg enzyme with decanal ; Vmax=45 umol/min/mg enzyme with dodecanal ; Vmax=2.3 umol/min/mg enzyme with dodecanal ; Vmax=40 umol/min/mg enzyme with hexadecanal ; Vmax=0.9 umol/min/mg enzyme with hexadecanal ; Vmax=46 umol/min/mg enzyme with octadecanal ; Vmax=1.6 umol/min/mg enzyme with octadecanal ; Vmax=42 umol/min/mg enzyme with tetradecanal ; Vmax=0.9 umol/min/mg enzyme with tetradecanal ; Vmax=0.97 umol/min/mg enzyme with farnesal ; Vmax=1.3 umol/min/mg enzyme with NAD ; Note=kcat is 2.18 sec(-1) for decanal as substrate. kcat is 2.23 sec(-1) for dodecanal as substrate. kcat is 0.86 sec(-1) for tetradecanal as substrate. kcat is 0.95 sec(-1) for hexadecanal as substrate. kcat is 1.52 sec(-1) for octadecanal as substrate. kcat is 0.93 sec(-1) for farnesal as substrate. kcat is 1.28 sec(-1) for NAD as substrate. ; pH dependence: Optimum pH is 9.8. Homodimer. Microsome membrane ; Single-pass membrane protein doplasmic reticulum membrane ; Single-pass membrane protein ; Cytoplasmic side Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P51648-1; Sequence=Displayed; Name=2; IsoId=P51648-2; Sequence=VSP_001283; Detected in liver (at protein level). Sjoegren-Larsson syndrome (SLS) [MIM:270200]: An autosomal recessive neurocutaneous disorder characterized by a combination of severe intellectual disability, spastic di- or tetraplegia and congenital ichthyosis. Ichthyosis is usually evident at birth with varying degrees of erythema and scaling, neurologic symptoms appear in the first or second year of life. Most patients have an IQ of less than 60. Additional clinical features include glistening white spots on the retina, seizures, short stature and speech defects. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the aldehyde dehydrogenase family. fatty acid alpha-oxidation 3-chloroallyl aldehyde dehydrogenase activity aldehyde dehydrogenase (NAD) activity protein binding peroxisome peroxisomal membrane endoplasmic reticulum endoplasmic reticulum membrane cellular aldehyde metabolic process lipid metabolic process fatty acid metabolic process sesquiterpenoid metabolic process central nervous system development peripheral nervous system development epidermis development membrane integral component of membrane oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor sphingolipid biosynthetic process organelle membrane phytol metabolic process protein homodimerization activity intracellular membrane-bounded organelle glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity hexadecanal metabolic process long-chain-alcohol oxidase activity long-chain-aldehyde dehydrogenase activity medium-chain-aldehyde dehydrogenase activity oxidation-reduction process uc002gwb.1 uc002gwb.2 uc002gwb.3 
ENST00000176763.10 STK10 ENST00000176763.10 serine/threonine kinase 10 (from RefSeq NM_005990.4) A6ND35 B2R8F5 B3KMY1 ENST00000176763.1 ENST00000176763.2 ENST00000176763.3 ENST00000176763.4 ENST00000176763.5 ENST00000176763.6 ENST00000176763.7 ENST00000176763.8 ENST00000176763.9 LOK NM_005990 O94804 Q6NSK0 Q9UIW4 STK10_HUMAN uc003mbo.1 uc003mbo.2 uc003mbo.3 This gene encodes a member of the Ste20 family of serine/threonine protein kinases, and is similar to several known polo-like kinase kinases. The protein can associate with and phosphorylate polo-like kinase 1, and overexpression of a kinase-dead version of the protein interferes with normal cell cycle progression. The kinase can also negatively regulate interleukin 2 expression in T-cells via the mitogen activated protein kinase kinase 1 pathway. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803616.134568.1, BC070077.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000176763.10/ ENSP00000176763.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Inhibited by the pyrrole-indolinone inhibitor SU11274 (K00593): intercalates between the ATP-binding Lys-65 and alpha-C glutamate (Glu-81), resulting in a partial disordering of the lysine side chain. Also specifically inhibited by erlotinib. Slightly inhibited by gefitinib. Homodimer; homodimerization is required for activation segment autophosphorylation. O94804; O94804: STK10; NbExp=3; IntAct=EBI-3951541, EBI-3951541; Cell membrane ; Peripheral membrane protein Highly expressed in rapidly proliferating tissues (spleen, placenta, and peripheral blood leukocytes). Also expressed in brain, heart, skeletal muscle, colon, thymus, kidney, liver, small intestine and lung. Autophosphorylates following homodimerization, leading to activation of the protein. Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. Note=The disease may be caused by variants affecting the gene represented in this entry. Inhibition by erlotinib, an orally administered EGFR tyrosine kinase inhibitor used for treatment, enhances STK10-dependent lymphocytic responses, possibly leading to the aggravation of skin inflammation observed upon treatment by erlotinib. Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Sequence=BAG51143.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding cytoplasm plasma membrane protein phosphorylation cell cycle membrane kinase activity phosphorylation transferase activity signal transduction by protein phosphorylation activation of protein kinase activity specific granule membrane identical protein binding protein homodimerization activity neutrophil degranulation protein autophosphorylation extracellular exosome lymphocyte aggregation regulation of lymphocyte migration uc003mbo.1 uc003mbo.2 uc003mbo.3 
ENST00000177694.2 TBX21 ENST00000177694.2 T-box transcription factor 21 (from RefSeq NM_013351.2) ENST00000177694.1 NM_013351 Q9UL17 TBET TBLYM TBX21_HUMAN uc002ilv.1 uc002ilv.2 This gene is a member of a phylogenetically conserved family of genes that share a common DNA-binding domain, the T-box. T-box genes encode transcription factors involved in the regulation of developmental processes. This gene is the human ortholog of mouse Tbx21/Tbet gene. Studies in mouse show that Tbx21 protein is a Th1 cell-specific transcription factor that controls the expression of the hallmark Th1 cytokine, interferon-gamma (IFNG). Expression of the human ortholog also correlates with IFNG expression in Th1 and natural killer cells, suggesting a role for this gene in initiating Th1 lineage development from naive Th precursor cells. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF093098.1, BC039739.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000177694.2/ ENSP00000177694.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Lineage-defining transcription factor which initiates Th1 lineage development from naive Th precursor cells both by activating Th1 genetic programs and by repressing the opposing Th2 and Th17 genetic programs (PubMed:10761931). Activates transcription of a set of genes important for Th1 cell function, including those encoding IFN- gamma and the chemokine receptor CXCR3. Induces permissive chromatin accessibilty and CpG methylation in IFNG (PubMed:33296702). Activates IFNG and CXCR3 genes in part by recruiting chromatin remodeling complexes including KDM6B, a SMARCA4-containing SWI/SNF-complex, and an H3K4me2-methyltransferase complex to their promoters and all of these complexes serve to establish a more permissive chromatin state conducive with transcriptional activation (By similarity). Can activate Th1 genes also via recruitment of Mediator complex and P-TEFb (composed of CDK9 and CCNT1/cyclin-T1) in the form of the super elongation complex (SEC) to super-enhancers and associated genes in activated Th1 cells (PubMed:27292648). Inhibits the Th17 cell lineage commitment by blocking RUNX1-mediated transactivation of Th17 cell-specific transcriptinal regulator RORC. Inhibits the Th2 cell lineage commitment by suppressing the production of Th2 cytokines, such as IL-4, IL-5, and IL- 13, via repression of transcriptional regulators GATA3 and NFATC2. Protects Th1 cells from amplifying aberrant type-I IFN response in an IFN-gamma abundant microenvironment by acting as a repressor of type-I IFN transcription factors and type-I IFN-stimulated genes. Acts as a regulator of antiviral B-cell responses; controls chronic viral infection by promoting the antiviral antibody IgG2a isotype switching and via regulation of a broad antiviral gene expression program (By similarity). Required for the correct development of natural killer (NK) and mucosal-associated invariant T (MAIT) cells (PubMed:33296702). Interacts with RUNX1, RUNX3, ITK, ABL1, RELA, CDK9 and KDM6B. The phosphorylated form (at Thr-303) interacts with NFATC2. Interacts with SMARCA4 in a KDM6B-dependent manner (By similarity). Interacts with CCTN1 (PubMed:27292648). Interacts with USP10 (PubMed:24845384). The phosphorylated form (at Tyr-530) interacts with GATA3 (PubMed:15662016). Q9UL17; Q92793: CREBBP; NbExp=4; IntAct=EBI-3922312, EBI-81215; Q9UL17; Q09472: EP300; NbExp=5; IntAct=EBI-3922312, EBI-447295; Q9UL17; P23771: GATA3; NbExp=6; IntAct=EBI-3922312, EBI-6664760; Q9UL17; P08047: SP1; NbExp=4; IntAct=EBI-3922312, EBI-298336; Nucleus T-cell specific. Phosphorylations at Ser-53, Tyr-77, Ser-225 and Ser-513 are regulated by mTORC1. Phosphorylation at Tyr-530 is essential for its interaction GATA3. Phosphorylation at Tyr-220, Tyr-266 and Tyr-305 enhances its transcriptional activator activity. Phosphorylation at Thr-303 is required for its interaction with NFATC2. Ubiquitinated at Lys-314, leading to its degradation by the proteasome. Ubiquitination is essential for controlling protein stability, binding to the T-box-binding element of the IFN-gamma promoter, and for interaction with NFATC2 through induction of phosphorylation at Thr-303 (By similarity). Deubiquitinated by USP10 leading to its stabilization (PubMed:24845384). Asthma, with nasal polyps and aspirin intolerance (ANPAI) [MIM:208550]: A condition consisting of asthma, aspirin sensitivity and nasal polyposis. Nasal polyposis is due to chronic inflammation of the paranasal sinus mucosa, leading to protrusion of edematous polyps into the nasal cavities. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Immunodeficiency 88 (IMD88) [MIM:619630]: An autosomal recessive disorder characterized by the development of disseminated mycobacterial disease following vaccination with BCG. Clinical features included fever, lymphadenopathy, and cutaneous eruption. Note=The disease is caused by variants affecting the gene represented in this entry. negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding RNA polymerase II activating transcription factor binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding cell fate specification heart looping DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated multicellular organism development response to virus positive regulation of gene expression T cell differentiation negative regulation of interleukin-2 production neuronal cell body proteasome-mediated ubiquitin-dependent protein catabolic process sequence-specific DNA binding transcription regulatory region DNA binding regulation of T cell differentiation negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter positive regulation of isotype switching to IgG isotypes regulation of immune response cellular response to organic substance lymphocyte migration negative regulation of T-helper 17 cell differentiation negative regulation of T-helper 17 cell lineage commitment negative regulation of T-helper 2 cell cytokine production uc002ilv.1 uc002ilv.2 
ENST00000178638.8 CA12 ENST00000178638.8 carbonic anhydrase 12, transcript variant 1 (from RefSeq NM_001218.5) B2RE24 CA12 CAH12_HUMAN ENST00000178638.1 ENST00000178638.2 ENST00000178638.3 ENST00000178638.4 ENST00000178638.5 ENST00000178638.6 ENST00000178638.7 NM_001218 O43570 Q53YE5 Q9BWG2 uc002amc.1 uc002amc.2 uc002amc.3 uc002amc.4 uc002amc.5 Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. This gene product is a type I membrane protein that is highly expressed in normal tissues, such as kidney, colon and pancreas, and has been found to be overexpressed in 10% of clear cell renal carcinomas. Three transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Jun 2014]. Reversible hydration of carbon dioxide. Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA), benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene- sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4- aminoethylbenzene-sulfonamide) and Foscarnet (phosphonoformate trisodium salt). Kinetic parameters: KM=12.0 mM for CO(2) Homodimer. Membrane; Single-pass type I membrane protein. Cell membrane Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43570-1; Sequence=Displayed; Name=2; IsoId=O43570-2; Sequence=VSP_000772; Highly expressed in colon, kidney, prostate, intestine and activated lymphocytes. Expressed at much higher levels in the renal cell cancers than in surrounding normal kidney tissue. Moderately expressed in pancreas, ovary and testis. Expressed in sweat glands and bronchiolar epithelium (PubMed:26911677). Hyperchlorhidrosis, isolated (HYCHL) [MIM:143860]: An autosomal recessive disorder characterized by excessive sweating and increased sweat chloride levels. Affected individuals suffer from episodes of hyponatremic dehydration and report increased amounts of visible salt precipitates in sweat. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the alpha-carbonic anhydrase family. carbonate dehydratase activity plasma membrane zinc ion binding bicarbonate transport membrane integral component of membrane lyase activity metal ion binding chloride ion homeostasis uc002amc.1 uc002amc.2 uc002amc.3 uc002amc.4 uc002amc.5 
ENST00000178640.10 MAP2K5 ENST00000178640.10 mitogen-activated protein kinase kinase 5, transcript variant 1 (from RefSeq NM_145160.3) B4DE43 ENST00000178640.1 ENST00000178640.2 ENST00000178640.3 ENST00000178640.4 ENST00000178640.5 ENST00000178640.6 ENST00000178640.7 ENST00000178640.8 ENST00000178640.9 MEK5 MKK5 MP2K5_HUMAN NM_145160 PRKMK5 Q13163 Q92961 Q92962 uc002aqu.1 uc002aqu.2 uc002aqu.3 uc002aqu.4 uc002aqu.5 The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically interacts with and activates MAPK7/ERK5. This kinase itself can be phosphorylated and activated by MAP3K3/MEKK3, as well as by atypical protein kinase C isoforms (aPKCs). The signal cascade mediated by this kinase is involved in growth factor stimulated cell proliferation and muscle cell differentiation. Three alternatively spliced transcript variants of this gene encoding distinct isoforms have been described. [provided by RefSeq, May 2011]. Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex with SQSTM1 and PRKCZ or PRKCI (By similarity). (Microbial infection) Interacts with Yersinia YopJ. Q13163; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-307294, EBI-18036948; Q13163; Q9H596: DUSP21; NbExp=3; IntAct=EBI-307294, EBI-7357329; Q13163; P62993: GRB2; NbExp=2; IntAct=EBI-307294, EBI-401755; Q13163; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-307294, EBI-11978177; Q13163; P08238: HSP90AB1; NbExp=4; IntAct=EBI-307294, EBI-352572; Q13163; Q8N448: LNX2; NbExp=3; IntAct=EBI-307294, EBI-2340947; Q13163; Q9Y2U5: MAP3K2; NbExp=6; IntAct=EBI-307294, EBI-357393; Q13163; Q99759: MAP3K3; NbExp=4; IntAct=EBI-307294, EBI-307281; Q13163; Q13164: MAPK7; NbExp=7; IntAct=EBI-307294, EBI-1213983; Q13163; Q99471: PFDN5; NbExp=3; IntAct=EBI-307294, EBI-357275; Q13163; Q13501: SQSTM1; NbExp=5; IntAct=EBI-307294, EBI-307104; Q13163; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-307294, EBI-743265; Q13163; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-307294, EBI-4395669; Event=Alternative splicing; Named isoforms=4; Name=B; IsoId=Q13163-1; Sequence=Displayed; Name=A; IsoId=Q13163-2; Sequence=VSP_021825; Name=C; IsoId=Q13163-3; Sequence=VSP_021825, VSP_021826; Name=4; IsoId=Q13163-4; Sequence=VSP_043333; Expressed in many adult tissues. Abundant in heart and skeletal muscle. Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues of the PB1 domain. This domain also mediates interactions with SQSTM1 and PARD6A (By similarity). Activated by phosphorylation on Ser/Thr by MAP kinase kinase kinases. (Microbial infection) Yersinia YopJ may acetylate Ser/Thr residues, preventing phosphorylation and activation, thus blocking the MAPK signaling pathway. [Isoform C]: Incomplete sequence. Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily. negative regulation of transcription from RNA polymerase II promoter MAPK cascade nucleotide binding activation of MAPK activity protein kinase activity protein serine/threonine kinase activity MAP kinase kinase activity protein tyrosine kinase activity protein binding ATP binding nucleus cytoplasm spindle cytosol protein phosphorylation signal transduction heart development kinase activity phosphorylation transferase activity peptidyl-tyrosine phosphorylation signal transduction by protein phosphorylation positive regulation of cell growth negative regulation of NF-kappaB transcription factor activity activation of protein kinase activity negative regulation of heterotypic cell-cell adhesion negative regulation of cysteine-type endopeptidase activity involved in apoptotic process negative regulation of interleukin-8 biosynthetic process positive regulation of transcription from RNA polymerase II promoter metal ion binding positive regulation of epithelial cell proliferation positive regulation of protein metabolic process negative regulation of response to cytokine stimulus ERK5 cascade cellular response to growth factor stimulus cellular response to laminar fluid shear stress negative regulation of cell migration involved in sprouting angiogenesis negative regulation of chemokine (C-X-C motif) ligand 2 production negative regulation of extrinsic apoptotic signaling pathway in absence of ligand uc002aqu.1 uc002aqu.2 uc002aqu.3 uc002aqu.4 uc002aqu.5 
ENST00000179259.6 TIGAR ENST00000179259.6 TP53 induced glycolysis regulatory phosphatase (from RefSeq NM_020375.3) B2R840 C12orf5 ENST00000179259.1 ENST00000179259.2 ENST00000179259.3 ENST00000179259.4 ENST00000179259.5 NM_020375 Q9NQ88 TIGAR TIGAR_HUMAN uc001qmp.1 uc001qmp.2 uc001qmp.3 uc001qmp.4 uc001qmp.5 This gene is regulated as part of the p53 tumor suppressor pathway and encodes a protein with sequence similarity to the bisphosphate domain of the glycolytic enzyme that degrades fructose-2,6-bisphosphate. The protein functions by blocking glycolysis and directing the pathway into the pentose phosphate shunt. Expression of this protein also protects cells from DNA damaging reactive oxygen species and provides some protection from DNA damage-induced apoptosis. The 12p13.32 region that includes this gene is paralogous to the 11q13.3 region. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BP201817.1, SRR1803614.162694.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000179259.6/ ENSP00000179259.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate (PubMed:19015259). Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production (PubMed:16839880, PubMed:22887998). Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death (PubMed:16839880, PubMed:19713938, PubMed:23726973, PubMed:22887998, PubMed:23817040). Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2- dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity (PubMed:23185017). In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3. Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage (By similarity). Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation (PubMed:23726973). Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions (By similarity). Protects glioma cells from hypoxia- and ROS- induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1- dependent and p53/TP53-independent manner (PubMed:22887998). Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses (PubMed:25928429). Involved in intestinal tumor progression (PubMed:23726973). Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6- phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; Evidence=; Interacts with HK2; the interaction increases hexokinase HK2 activity in a hypoxia- and HIF1A-dependent manner, resulting in the regulation of mitochondrial membrane potential, thus increasing NADPH production and decreasing intracellular ROS levels (PubMed:23185017). Q9NQ88; P55212: CASP6; NbExp=3; IntAct=EBI-3920747, EBI-718729; Q9NQ88; O00291: HIP1; NbExp=3; IntAct=EBI-3920747, EBI-473886; Q9NQ88; P52789: HK2; NbExp=3; IntAct=EBI-3920747, EBI-741469; Q9NQ88; P13473-2: LAMP2; NbExp=3; IntAct=EBI-3920747, EBI-21591415; Q9NQ88; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-3920747, EBI-2623095; Cytoplasm cleus Mitochondrion Note=Translocated to the mitochondria during hypoxia in a HIF1A-dependent manner (PubMed:23185017). Colocalizes with HK2 in the mitochondria during hypoxia (PubMed:23185017). Translocated to the nucleus during hypoxia and/or genome stress-induced DNA damage responses in cancer cells (PubMed:25928429). Translocation to the mitochondria is enhanced in ischemic cortex after reperfusion and/or during oxygen and glucose deprivation (OGD)/reoxygenation insult in primary neurons (By similarity). Expressed in the brain (PubMed:22887998). Expressed in breast tumors (PubMed:21820150). Expressed in glioblastomas (PubMed:22887998). Up-regulated by p53/TP53 (at protein level) (PubMed:16839880). Rapidly up-regulated by p53/TP53 (PubMed:16140933, PubMed:16839880, PubMed:19713938). Up-regulated in glioma cell line in a p53/TP53-independent manner (PubMed:22887998). Belongs to the phosphoglycerate mutase family. Not expected to have any kinase activity. response to ischemia catalytic activity bisphosphoglycerate 2-phosphatase activity fructose-2,6-bisphosphate 2-phosphatase activity protein binding intracellular nucleus cytoplasm mitochondrion mitochondrial outer membrane cytosol fructose 2,6-bisphosphate metabolic process autophagy apoptotic process cellular response to DNA damage stimulus response to xenobiotic stimulus response to gamma radiation positive regulation of cardiac muscle cell apoptotic process dephosphorylation hydrolase activity fructose 1,6-bisphosphate metabolic process negative regulation of programmed cell death regulation of pentose-phosphate shunt positive regulation of DNA repair negative regulation of glycolytic process intestinal epithelial cell development cellular response to cobalt ion cellular response to hypoxia negative regulation of neuron death negative regulation of macromitophagy regulation of response to DNA damage checkpoint signaling positive regulation of hexokinase activity negative regulation of glucose catabolic process to lactate via pyruvate negative regulation of reactive oxygen species metabolic process uc001qmp.1 uc001qmp.2 uc001qmp.3 uc001qmp.4 uc001qmp.5 
ENST00000180166.6 FGF20 ENST00000180166.6 fibroblast growth factor 20 (from RefSeq NM_019851.3) B2RPH5 ENST00000180166.1 ENST00000180166.2 ENST00000180166.3 ENST00000180166.4 ENST00000180166.5 FGF20_HUMAN NM_019851 Q9NP95 uc003wxc.1 uc003wxc.2 uc003wxc.3 The protein encoded by this gene is a member of the fibroblast growth factor family. The fibroblast growth factors possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This gene product is a secreted neurotrophic factor but lacks a typical signal peptide. It is expressed in normal brain, particularly the cerebellum, and may regulate central nervous system development and function. Homodimerization of this protein was shown to regulate its receptor binding activity and concentration gradient in the extracellular matrix. Genetic variations of this gene have been associated with Parkinson disease susceptibility. [provided by RefSeq, Oct 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.607830.1, AB044277.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145245, SAMEA2151119 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000180166.6/ ENSP00000180166.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Neurotrophic factor that regulates central nervous development and function. Homodimer. Interacts with FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Secreted Predominantly expressed in the cerebellum. Renal hypodysplasia/aplasia 2 (RHDA2) [MIM:615721]: A perinatally lethal renal disease encompassing a spectrum of kidney development defects, including renal agenesis, bilateral renal aplasia, hypoplasia, (cystic) dysplasia, and severe obstructive uropathy. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the heparin-binding growth factors family. It is uncertain whether variants in this gene are associated with Parkinson disease. Some authors mention association with the disease (PubMed:18252210). In contrast, some others do not observe any association (PubMed:19133659). Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fgf20/"; MAPK cascade receptor binding fibroblast growth factor receptor binding extracellular region signal transduction cell-cell signaling growth factor activity positive regulation of cell proliferation fibroblast growth factor receptor signaling pathway regulation of dopamine secretion cell differentiation heparan sulfate proteoglycan binding negative regulation of neuron apoptotic process regulation of neuron differentiation positive regulation of protein kinase B signaling regulation of cardiac muscle cell proliferation inner ear receptor cell differentiation positive regulation of ERK1 and ERK2 cascade receptor-receptor interaction positive regulation of dopaminergic neuron differentiation uc003wxc.1 uc003wxc.2 uc003wxc.3 
ENST00000180173.10 MTMR7 ENST00000180173.10 myotubularin related protein 7 (from RefSeq NM_004686.5) A1L4K9 B4DG87 ENST00000180173.1 ENST00000180173.2 ENST00000180173.3 ENST00000180173.4 ENST00000180173.5 ENST00000180173.6 ENST00000180173.7 ENST00000180173.8 ENST00000180173.9 MTMR7_HUMAN NM_004686 Q68DX4 Q9Y216 uc003wxm.1 uc003wxm.2 uc003wxm.3 uc003wxm.4 uc003wxm.5 This gene encodes a member of the myotubularin family of tyrosine/dual-specificity phosphatases. The encoded protein is characterized by four distinct domains that are conserved among all members of the myotubularin family: the glucosyltransferase, Rab-like GTPase activator and myotubularins domain, the Rac-induced recruitment domain, the protein tyrosine phosphatases and dual-specificity phosphatases domain and the suppressor of variegation 3-9, enhancer-of-zeste, and trithorax interaction domain. This protein dephosphorylates the target substrates phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate. A pseudogene of this gene is found on chromosome 5. [provided by RefSeq, Mar 2009]. ##Evidence-Data-START## Transcript exon combination :: SRR1660805.71939.1, SRR1660803.76648.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1966682, SAMEA1968189 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000180173.10/ ENSP00000180173.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and inositol 1,3- bisphosphate (Ins(1,3)P2). Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3- phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence=; Reaction=1D-myo-inositol 1,3-bisphosphate + H2O = 1D-myo-inositol 1- phosphate + phosphate; Xref=Rhea:RHEA:57840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58433, ChEBI:CHEBI:83242; Evidence=; Interaction with MTMR9 increases phosphatase activity. Heterodimer (via C-terminus) with MTMR9 (via coiled coil domain); the interaction enhances MTMR7 catalytic activity (By similarity). Does not homodimerize (By similarity). Interacts with RAB1B (in GDP-bound form) (By similarity). Q9Y216; P51946: CCNH; NbExp=6; IntAct=EBI-10293003, EBI-741406; Q9Y216; Q96QG7: MTMR9; NbExp=14; IntAct=EBI-10293003, EBI-744593; Cytoplasm Endomembrane system ; Peripheral membrane protein ; Cytoplasmic side Note=May partially localize to endosomes and/or the Golgi apparatus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y216-1; Sequence=Displayed; Name=2; IsoId=Q9Y216-2; Sequence=VSP_017000, VSP_017001; Expressed specifically in brain. Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily. phosphatidylinositol-3-phosphatase activity protein tyrosine phosphatase activity protein binding cytoplasm cytosol protein dephosphorylation phosphatidylinositol biosynthetic process endomembrane system membrane dephosphorylation hydrolase activity phosphatase activity peptidyl-tyrosine dephosphorylation inositol phosphate dephosphorylation phosphatidylinositol dephosphorylation phosphatidylinositol phosphate phosphatase activity uc003wxm.1 uc003wxm.2 uc003wxm.3 uc003wxm.4 uc003wxm.5 
ENST00000181383.10 CPB2 ENST00000181383.10 carboxypeptidase B2, transcript variant 1 (from RefSeq NM_001872.5) A8K464 CBPB2_HUMAN ENST00000181383.1 ENST00000181383.2 ENST00000181383.3 ENST00000181383.4 ENST00000181383.5 ENST00000181383.6 ENST00000181383.7 ENST00000181383.8 ENST00000181383.9 NM_001872 Q15114 Q5T9K1 Q5T9K2 Q96IY4 Q9P2Y6 uc285kvt.1 uc285kvt.2 Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013]. Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. Reaction=Release of C-terminal Arg and Lys from a polypeptide.; EC=3.4.17.20; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. TAFI/CPB2 is unique among carboxypeptidases in that it spontaneously inactivates with a short half-life, a property that is crucial for its role in controlling blood clot lysis. The zymogen is stabilized by interactions with the activation peptide. Release of the activation peptide increases a dynamic flap mobility and in time this leads to conformational changes that disrupt the catalytic site and expose a cryptic thrombin-cleavage site present at Arg-324. Secreted. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96IY4-1; Sequence=Displayed; Name=2; IsoId=Q96IY4-2; Sequence=VSP_013446, VSP_013447; Plasma; synthesized in the liver. N-glycosylated. N-glycan at Asn-108: Hex5HexNAc4. Belongs to the peptidase M14 family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cpb2/"; positive regulation of extracellular matrix constituent secretion carboxypeptidase activity metallocarboxypeptidase activity extracellular region extracellular space cell proteolysis blood coagulation hemostasis peptidase activity metallopeptidase activity zinc ion binding response to heat negative regulation of plasminogen activation hydrolase activity regulation of complement activation response to drug fibrinolysis metal ion binding negative regulation of fibrinolysis extracellular exosome cellular response to glucose stimulus liver regeneration negative regulation of hepatocyte proliferation uc285kvt.1 uc285kvt.2 
ENST00000181796.7 FAM107B ENST00000181796.7 family with sequence similarity 107 member B, transcript variant 2 (from RefSeq NM_031453.4) A8K1P4 C10orf45 D3DRT2 ENST00000181796.1 ENST00000181796.2 ENST00000181796.3 ENST00000181796.4 ENST00000181796.5 ENST00000181796.6 F107B_HUMAN FAM107B NM_031453 Q5T9K7 Q5T9K8 Q6ZSI4 Q9H098 uc001ina.1 uc001ina.2 uc001ina.3 uc001ina.4 Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H098-1; Sequence=Displayed; Name=2; IsoId=Q9H098-2; Sequence=VSP_037527; Belongs to the FAM107 family. uc001ina.1 uc001ina.2 uc001ina.3 uc001ina.4 
ENST00000181839.10 CDK13 ENST00000181839.10 cyclin dependent kinase 13, transcript variant 1 (from RefSeq NM_003718.5) CDC2L CDC2L5 CDK13_HUMAN CHED ENST00000181839.1 ENST00000181839.2 ENST00000181839.3 ENST00000181839.4 ENST00000181839.5 ENST00000181839.6 ENST00000181839.7 ENST00000181839.8 ENST00000181839.9 KIAA1791 NM_003718 Q14004 Q53G78 Q6DKQ9 Q75MH4 Q75MH5 Q96JN4 Q9H4A0 Q9H4A1 Q9UDR4 uc003thh.1 uc003thh.2 uc003thh.3 uc003thh.4 uc003thh.5 uc003thh.6 uc003thh.7 The protein encoded by this gene is a member of the cyclin-dependent serine/threonine protein kinase family. Members of this family are well known for their essential roles as master switches in cell cycle control. The exact function of this protein has not yet been determined, but it may play a role in mRNA processing and may be involved in regulation of hematopoiesis. Alternatively spliced transcript variants have been described.[provided by RefSeq, Dec 2009]. Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho- [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA- COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence=; Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence=; (Microbial infection) Interacts with human herpes virus 1 (HHV-1) transcriptional regulator ICP22. Interacts with CCNL1 and CCNL2 (By similarity). Interacts with CCNK. Interacts with C1QBP. (Microbial infection) Interacts with HIV-1 Tat. Q14004; O75909: CCNK; NbExp=7; IntAct=EBI-968626, EBI-739806; Q14004; Q16543: CDC37; NbExp=2; IntAct=EBI-968626, EBI-295634; Q14004-2; Q07021: C1QBP; NbExp=6; IntAct=EBI-6375898, EBI-347528; Nucleus speckle Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q14004-1; Sequence=Displayed; Name=2; IsoId=Q14004-2; Sequence=VSP_013579; Expressed in fetal brain, liver, muscle and in adult brain. Also expressed in neuroblastoma and glioblastoma tumors. Modified_positions=103 ; Note=Edited at about 88%.; Congenital heart defects, dysmorphic facial features, and intellectual developmental disorder (CHDFIDD) [MIM:617360]: An autosomal dominant syndrome characterized by atrial and/or ventricular septal congenital heart defects, facial dysmorphism with hypertelorism, upslanted palpebral fissures, epicanthal folds, ptosis, strabismus, posteriorly rotated ears, thin upper lip, and small mouth. Patients manifest global developmental delay, delayed walking and speech acquisition, and intellectual disability. Some patients have mild microcephaly, a small cerebral cortex, and agenesis of corpus callosum. More variable features include clinodactyly and/or camptodactyly of the fingers, hypotonia, and joint hypermobility. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Sequence=AAA58424.1; Type=Frameshift; Evidence=; Sequence=AAS07490.1; Type=Erroneous gene model prediction; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc2l5/"; nucleotide binding cyclin-dependent protein kinase holoenzyme complex alternative mRNA splicing, via spliceosome nuclear chromatin cyclin K-CDK13 complex RNA binding protein kinase activity protein serine/threonine kinase activity cyclin-dependent protein serine/threonine kinase activity protein binding ATP binding extracellular region extracellular space nucleus nucleoplasm chromosome Golgi apparatus cytosol transcription elongation from RNA polymerase II promoter mRNA processing protein phosphorylation regulation of mitotic nuclear division multicellular organism development cyclin/CDK positive transcription elongation factor complex transcription factor binding positive regulation of cell proliferation RNA polymerase II carboxy-terminal domain kinase activity RNA splicing viral process kinase activity phosphorylation nuclear speck transferase activity protein kinase binding nuclear cyclin-dependent protein kinase holoenzyme complex hemopoiesis cyclin binding positive regulation of transcription elongation from RNA polymerase II promoter neutrophil degranulation transcription regulatory region DNA binding positive regulation of transcription from RNA polymerase II promoter phosphorylation of RNA polymerase II C-terminal domain ficolin-1-rich granule lumen negative regulation of stem cell differentiation uc003thh.1 uc003thh.2 uc003thh.3 uc003thh.4 uc003thh.5 uc003thh.6 uc003thh.7 
ENST00000182290.9 TSPAN32 ENST00000182290.9 tetraspanin 32 (from RefSeq NM_139022.3) ENST00000182290.1 ENST00000182290.2 ENST00000182290.3 ENST00000182290.4 ENST00000182290.5 ENST00000182290.6 ENST00000182290.7 ENST00000182290.8 NM_139022 PHEMX Q96KX4 Q96QS1 Q9HC50 Q9HC51 Q9Y5U1 TSN32_HUMAN TSSC6 uc001lvy.1 uc001lvy.2 uc001lvy.3 This gene, which is a member of the tetraspanin superfamily, is one of several tumor-suppressing subtransferable fragments located in the imprinted gene domain of chromosome 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian and breast cancers. This gene is located among several imprinted genes; however, this gene, as well as the tumor-suppressing subchromosomal transferable fragment 4, escapes imprinting. This gene may play a role in malignancies and diseases that involve this region, and it is also involved in hematopoietic cell function. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]. Sequence Note: A downstream start codon is selected for this RefSeq based on better conservation with homologs. The use of an alternative upstream start codon, which is present in primate species, would increase the protein length from 320 aa to 355 aa. The presence of a predicted signal anchor for the shorter, but not the longer, protein suggests that the downstream start codon may be preferentially used. The shorter protein is described in PMID 11718897. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY039001.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## CDS uses downstream in-frame AUG :: lack of evidence for use of upstream AUG MANE Ensembl match :: ENST00000182290.9/ ENSP00000182290.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=5; Comment=Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.; Name=1; IsoId=Q96QS1-1; Sequence=Displayed; Name=2; IsoId=Q96QS1-2; Sequence=VSP_003932; Name=3; IsoId=Q96QS1-3; Sequence=VSP_003937, VSP_003938; Name=4; IsoId=Q96QS1-4; Sequence=VSP_003932, VSP_003933, VSP_003934; Name=5; IsoId=Q96QS1-5; Sequence=VSP_003935, VSP_003936; Expressed ubiquitously at low levels. High levels of expression are confined to hematopoietic tissues including peripheral blood leukocytes, thymus and spleen. Expressed from early embryogenesis through to adulthood. [Isoform 4]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. [Isoform 5]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the tetraspanin (TM4SF) family. molecular_function integral component of plasma membrane cytoskeleton organization integrin-mediated signaling pathway cell-cell signaling blood coagulation hemostasis negative regulation of cell proliferation cell surface membrane integral component of membrane negative regulation of myeloid dendritic cell activation defense response to protozoan regulation of defense response to virus integrin alphaIIb-beta3 complex platelet aggregation uc001lvy.1 uc001lvy.2 uc001lvy.3 
ENST00000182527.4 TRAM2 ENST00000182527.4 translocation associated membrane protein 2 (from RefSeq NM_012288.4) A8K6T6 ENST00000182527.1 ENST00000182527.2 ENST00000182527.3 KIAA0057 NM_012288 Q15035 TRAM2_HUMAN uc003paq.1 uc003paq.2 uc003paq.3 uc003paq.4 uc003paq.5 TRAM2 is a component of the translocon, a gated macromolecular channel that controls the posttranslational processing of nascent secretory and membrane proteins at the endoplasmic reticulum (ER) membrane.[supplied by OMIM, Jul 2004]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: D31762.1, SRR1803614.72826.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000182527.4/ ENSP00000182527.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Necessary for collagen type I synthesis. May couple the activity of the ER Ca(2+) pump SERCA2B with the activity of the translocon. This coupling may increase the local Ca(2+) concentration at the site of collagen synthesis, and a high Ca(2+) concentration may be necessary for the function of molecular chaperones involved in collagen folding. Required for proper insertion of the first transmembrane helix N-terminus of TM4SF20 into the ER lumen, may act as a ceramide sensor for regulated alternative translocation (RAT) (PubMed:27499293). Interacts with SERCA2B and COL1A1. Membrane ; Multi-pass membrane protein Belongs to the TRAM family. Sequence=BAA06540.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; protein binding rough endoplasmic reticulum SRP-dependent cotranslational protein targeting to membrane, translocation protein transport membrane integral component of membrane collagen biosynthetic process protein insertion into ER membrane uc003paq.1 uc003paq.2 uc003paq.3 uc003paq.4 uc003paq.5 
ENST00000183605.10 CLDN18 ENST00000183605.10 claudin 18, transcript variant 1 (from RefSeq NM_016369.4) A5PL21 CLD18_HUMAN ENST00000183605.1 ENST00000183605.2 ENST00000183605.3 ENST00000183605.4 ENST00000183605.5 ENST00000183605.6 ENST00000183605.7 ENST00000183605.8 ENST00000183605.9 NM_016369 P56856 Q96PH4 UNQ778/PRO1572 uc003erp.1 uc003erp.2 uc003erp.3 This gene encodes a member of the claudin family. Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical barrier to prevent solutes and water from passing freely through the paracellular space between epithelial or endothelial cell sheets, and also play critical roles in maintaining cell polarity and signal transductions. This gene is upregulated in patients with ulcerative colitis and highly overexpressed in infiltrating ductal adenocarcinomas. PKC/MAPK/AP-1 (protein kinase C/mitogen-activated protein kinase/activator protein-1) dependent pathway regulates the expression of this gene in gastric cells. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jun 2010]. Involved in alveolar fluid homeostasis via regulation of alveolar epithelial tight junction composition and therefore ion transport and solute permeability, potentially via downstream regulation of the actin cytoskeleton organization and beta-2-adrenergic signaling (By similarity). Required for lung alveolarization and maintenance of the paracellular alveolar epithelial barrier (By similarity). Acts to maintain epithelial progenitor cell proliferation and organ size, via regulation of YAP1 localization away from the nucleus and thereby restriction of YAP1 target gene transcription (By similarity). Acts as a negative regulator of RANKL-induced osteoclast differentiation, potentially via relocation of TJP2/ZO-2 away from the nucleus, subsequently involved in bone resorption in response to calcium deficiency (By similarity). Mediates the osteoprotective effects of estrogen, potentially via acting downstream of estrogen signaling independently of RANKL signaling pathways (By similarity). [Isoform A1]: Involved in the maintenance of homeostasis of the alveolar microenvironment via regulation of pH and subsequent T- cell activation in the alveolar space, is therefore indirectly involved in limiting C. neoformans infection. [Isoform A2]: Required for the formation of the gastric paracellular barrier via its role in tight junction formation, thereby involved in the response to gastric acidification. Interacts with TJP2/ZO-2 (By similarity). Interacts with TJP1/ZO-1 (By similarity). Interacts with YAP1 (phosphorylated); the interaction sequesters YAP1 away from the nucleus and thereby restricts transcription of YAP1 target genes (By similarity). P56856; Q08426: EHHADH; NbExp=3; IntAct=EBI-16354902, EBI-2339219; P56856; Q01453: PMP22; NbExp=3; IntAct=EBI-16354902, EBI-2845982; Cell junction, tight junction Cell membrane ; Multi-pass membrane protein Note=Localizes to tight junctions in epithelial cells. [Isoform A1]: Cell junction, tight junction [Isoform A2]: Cell junction, tight junction Lateral cell membrane Event=Alternative splicing; Named isoforms=2; Name=A1 ; Synonyms=CLDN18.1 ; IsoId=P56856-1; Sequence=Displayed; Name=A2 ; Synonyms=CLDN18.2 ; IsoId=P56856-2; Sequence=VSP_001102; [Isoform A1]: Expression is restricted to the lung. [Isoform A2]: Expression is restricted to the stomach mucosa where it is predominantly observed in the epithelial cells of the pit region and the base of the gastric glands including exocrine and endocrine cells (at protein level). Expressed in the lungs from 23 weeks onwards, expression increases during the third trimester resulting in significantly higher expression at birth. Belongs to the claudin family. structural molecule activity plasma membrane bicellular tight junction membrane integral component of membrane calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules cell junction identical protein binding response to ethanol negative regulation of bone resorption digestive tract development TNFSF11-mediated signaling pathway negative regulation of protein localization to nucleus negative regulation of osteoclast development uc003erp.1 uc003erp.2 uc003erp.3 
ENST00000184266.3 NDUFB4 ENST00000184266.3 NADH:ubiquinone oxidoreductase subunit B4, transcript variant 1 (from RefSeq NM_004547.6) B2RUY3 B9EJC7 ENST00000184266.1 ENST00000184266.2 NDUB4_HUMAN NM_004547 O95168 uc003edu.1 uc003edu.2 uc003edu.3 uc003edu.4 uc003edu.5 This gene encodes a non-catalytic subunit of the multisubunit NADH:ubiquinone oxidoreductase, the first enzyme complex in the mitochondrial electron transport chain (complex I). Mammalian complex I is composed of 45 different subunits and transfers electrons from NADH to ubiquinone. [provided by RefSeq, Dec 2009]. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Complex I is composed of 45 different subunits. Mitochondrion inner membrane ; Single-pass membrane protein ; Matrix side Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95168-1; Sequence=Displayed; Name=2; IsoId=O95168-2; Sequence=VSP_042719; Belongs to the complex I NDUFB4 subunit family. mitochondrion mitochondrial inner membrane mitochondrial respiratory chain complex I mitochondrial electron transport, NADH to ubiquinone response to oxidative stress NADH dehydrogenase (ubiquinone) activity membrane integral component of membrane nuclear membrane mitochondrial respiratory chain complex I assembly oxidation-reduction process respiratory chain uc003edu.1 uc003edu.2 uc003edu.3 uc003edu.4 uc003edu.5 
ENST00000184956.11 HEATR6 ENST00000184956.11 HEAT repeat containing 6 (from RefSeq NM_022070.5) ABC1 B3KXP3 ENST00000184956.1 ENST00000184956.10 ENST00000184956.2 ENST00000184956.3 ENST00000184956.4 ENST00000184956.5 ENST00000184956.6 ENST00000184956.7 ENST00000184956.8 ENST00000184956.9 HEAT6_HUMAN NM_022070 Q6AI08 Q6MZX1 Q6MZY2 Q8TDM9 Q9H6B3 Q9H6M7 uc002iyk.1 uc002iyk.2 uc002iyk.3 Amplification-dependent oncogene. Amplified in breast cancer cell lines MCF-7 and BT- 474. 17q23 region is one of the most commonly amplified regions in breast cancer and therefore may harbor genes important for breast cancer development and progression. Sequence=AAL83912.1; Type=Erroneous initiation; Evidence=; Sequence=BAB15229.1; Type=Erroneous initiation; Evidence=; Sequence=BAB15348.1; Type=Erroneous initiation; Evidence=; RNA binding uc002iyk.1 uc002iyk.2 uc002iyk.3 
ENST00000185150.9 ERLEC1 ENST00000185150.9 endoplasmic reticulum lectin 1, transcript variant 1 (from RefSeq NM_015701.5) ENST00000185150.1 ENST00000185150.2 ENST00000185150.3 ENST00000185150.4 ENST00000185150.5 ENST00000185150.6 ENST00000185150.7 ENST00000185150.8 HEL117 NM_015701 V9HWD3 V9HWD3_HUMAN uc002rxl.1 uc002rxl.2 uc002rxl.3 uc002rxl.4 uc002rxl.5 This gene encodes a resident endoplasmic reticulum (ER) protein that functions in N-glycan recognition. This protein is thought to be involved in ER-associated degradation via its interaction with the membrane-associated ubiquitin ligase complex. It also functions as a regulator of multiple cellular stress-response pathways in a manner that promotes metastatic cell survival. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 21. [provided by RefSeq, Aug 2011]. Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non- glycosylated proteins and glycoproteins. Endoplasmic reticulum lumen Belongs to the OS-9 family. uc002rxl.1 uc002rxl.2 uc002rxl.3 uc002rxl.4 uc002rxl.5 
ENST00000186436.10 TMEM131 ENST00000186436.10 transmembrane protein 131 (from RefSeq NM_015348.2) ENST00000186436.1 ENST00000186436.2 ENST00000186436.3 ENST00000186436.4 ENST00000186436.5 ENST00000186436.6 ENST00000186436.7 ENST00000186436.8 ENST00000186436.9 KIAA0257 NM_015348 Q92545 RW1 TM131_HUMAN uc002syh.1 uc002syh.2 uc002syh.3 uc002syh.4 uc002syh.5 uc002syh.6 May play a role in the immune response to viral infection. Membrane ; Multi-pass membrane protein Belongs to the TMEM131 family. molecular_function cellular_component biological_process membrane integral component of membrane uc002syh.1 uc002syh.2 uc002syh.3 uc002syh.4 uc002syh.5 uc002syh.6 
ENST00000187762.7 TMEM38A ENST00000187762.7 transmembrane protein 38A (from RefSeq NM_024074.4) A8K9P9 ENST00000187762.1 ENST00000187762.2 ENST00000187762.3 ENST00000187762.4 ENST00000187762.5 ENST00000187762.6 NM_024074 Q9H6F2 TM38A_HUMAN uc002nes.1 uc002nes.2 uc002nes.3 uc002nes.4 uc002nes.5 Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. Homotrimer; trimerization probably requires binding to phosphatidylinositol 4,5-bisphosphate (PIP2). Sarcoplasmic reticulum membrane ; Multi-pass membrane protein Nucleus membrane Belongs to the TMEM38 family. cation channel activity potassium channel activity nucleus ion transport potassium ion transport endoplasmic reticulum organization regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion release of sequestered calcium ion into cytosol by sarcoplasmic reticulum monovalent inorganic cation transport membrane integral component of membrane sarcoplasmic reticulum nuclear membrane sarcoplasmic reticulum membrane identical protein binding extracellular exosome cellular response to caffeine potassium ion transmembrane transport uc002nes.1 uc002nes.2 uc002nes.3 uc002nes.4 uc002nes.5 
ENST00000187910.7 PSG6 ENST00000187910.7 pregnancy specific beta-1-glycoprotein 6, transcript variant 2 (from RefSeq NM_001031850.4) CGM3 ENST00000187910.1 ENST00000187910.2 ENST00000187910.3 ENST00000187910.4 ENST00000187910.5 ENST00000187910.6 NM_001031850 O75244 PSG10 PSG12 PSG6_HUMAN PSGGB Q00889 Q15224 Q15235 Q549K1 uc002ovg.1 uc002ovg.2 uc002ovg.3 uc002ovg.4 This gene is a member of the pregnancy-specific glycoprotein (PSG) gene family. The PSG genes are a subgroup of the carcinoembryonic antigen (CEA) family of immunoglobulin-like genes, and are found in a gene cluster at 19q13.1-q13.2 telomeric to another cluster of CEA-related genes. The PSG genes are expressed by placental trophoblasts and released into the maternal circulation during pregnancy, and are thought to be essential for maintenance of normal pregnancy. The protein encoded by this gene contains the Arg-Gly-Asp tripeptide associated with cellular adhesion and recognition. Alternative splicing results in multiple transcript variants and protein isoforms. [provided by RefSeq, Jul 2012]. Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q00889-1; Sequence=Displayed; Name=2; IsoId=Q00889-2; Sequence=VSP_039344; PSBG are produced in high quantity during pregnancy. Belongs to the immunoglobulin superfamily. CEA family. molecular_function extracellular region female pregnancy uc002ovg.1 uc002ovg.2 uc002ovg.3 uc002ovg.4 
ENST00000188312.7 ACTR6 ENST00000188312.7 actin related protein 6, transcript variant 1 (from RefSeq NM_022496.5) ARP6_HUMAN B3KW37 B4DLG9 CDA12 ENST00000188312.1 ENST00000188312.2 ENST00000188312.3 ENST00000188312.4 ENST00000188312.5 ENST00000188312.6 NM_022496 Q53GH2 Q9BY39 Q9GZN1 Q9H8H6 uc001thb.1 uc001thb.2 uc001thb.3 uc001thb.4 Required for formation and/or maintenance of proper nucleolar structure and function (PubMed:26164235). Plays a dual role in the regulation of ribosomal DNA (rDNA) transcription (By similarity). In the presence of high glucose, maintains active rDNA transcription through H2A.Z deposition and under glucose starvation, is required for the repression of rDNA transcription, and this function may be independent of H2A.Z (By similarity). Component of the chromatin-remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1 (PubMed:15647280, PubMed:20473270). Interacts with CBX1, CBX3 and CBX5 (PubMed:16487625). Q9GZN1; P0C0S5: H2AZ1; NbExp=3; IntAct=EBI-769329, EBI-1199859; Q9GZN1; O43257: ZNHIT1; NbExp=5; IntAct=EBI-769329, EBI-347522; Cytoplasm, cytoskeleton Nucleus Nucleus, nucleolus Note=Colocalizes with HP1 family proteins at pericentric heterochromatin. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9GZN1-1; Sequence=Displayed; Name=2; IsoId=Q9GZN1-2; Sequence=VSP_054637, VSP_054638; Belongs to the actin family. ARP6 subfamily. Swr1 complex protein binding nucleus cytoplasm cytoskeleton chromatin remodeling nucleosome binding histone exchange uc001thb.1 uc001thb.2 uc001thb.3 uc001thb.4 
ENST00000188790.9 FAP ENST00000188790.9 fibroblast activation protein alpha, transcript variant 1 (from RefSeq NM_004460.5) ENST00000188790.1 ENST00000188790.2 ENST00000188790.3 ENST00000188790.4 ENST00000188790.5 ENST00000188790.6 ENST00000188790.7 ENST00000188790.8 FAP NM_004460 O00199 Q12884 Q53TP5 Q86Z29 Q99998 Q9UID4 SEPR_HUMAN uc002ucd.1 uc002ucd.2 uc002ucd.3 uc002ucd.4 The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2014]. Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711). Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner. Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence= Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; Evidence= Gelatinase activity is inhibited by serine- protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF), 4- (2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF), 4- amidino phenylsulfonyl fluoride (APSF) and diisopropyl fluorophosphate (DFP), N-ethylmaleimide (NEM) and phenylmethylsulfonyl fluoride (PMSF). Dipeptidyl peptidase activity is inhibited by 2,2'-azino-bis(3- ethylbenzthiazoline-6-sulfonic acid), diisopropylfluorophosphate (DFP). Prolyl endopeptidase activity is inhibited by the boronic acid peptide Ac-Gly-BoroPro, Ac-Gly-Pro-chloromethyl ketone and Thr-Ser-Gly- chloromethyl ketone. Kinetic parameters: KM=0.46 mM for Ala-Pro (Dipeptidyl peptidase activity) ; KM=0.9 mM for Lys-Pro (Dipeptidyl peptidase activity) ; KM=1.15 mM for Gly-Pro (Dipeptidyl peptidase activity) ; KM=0.25 mM for Gly-Pro (Dipeptidyl peptidase activity) ; KM=0.24 mM for Ala-Pro (Dipeptidyl peptidase activity) ; KM=0.10 mM for Ile-Pro (Dipeptidyl peptidase activity) ; KM=0.24 mM for Phe-Pro (Dipeptidyl peptidase activity) ; KM=0.24 mM for Gly-Pro (Dipeptidyl peptidase activity) ; KM=0.33 mM for Ac-Gly-Pro (Prolyl endopeptidase activity) ; KM=1.3 uM for Thr-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity) ; KM=2.2 uM for Ala-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity) ; KM=0.7 uM for Thr-Ala-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity) ; KM=1.9 uM for Thr-Ser-Gly-Pro-Ser-Gln (Prolyl endopeptidase activity) ; KM=2.2 uM for Thr-Ser-Gly-Pro-Asn-Ser (Prolyl endopeptidase activity) ; KM=4.3 uM for Ala-Ser-Gly-Pro-Ser-Ser (Prolyl endopeptidase activity) ; KM=0.101 mM for Gly-Pro (FAP form, prolyl endopeptidase activity) ; KM=0.124 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, prolyl endopeptidase activity) ; KM=0.323 mM for Gly-Pro (FAP form, dipeptidyl peptidase activity) ; KM=0.272 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, dipeptidyl peptidase activity) ; KM=0.029 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (FAP form, prolyl endopeptidase activity) ; KM=0.026 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (Antiplasmin-cleaving enzyme FAP soluble form, prolyl endopeptidase activity) ; pH dependence: Optimum pH is 6-8.4 for gelatinase activity. At pH lower than 5 inhibited gelatinase activity. Temperature dependence: Optimum temperature is 37 degrees Celsius for gelatinase activity. Temperatures above 50 degrees Celsius inhibit gelatinase activity. ; Homodimer; homodimerization is required for activity of both plasma membrane and soluble forms. The monomer is inactive. Heterodimer with DPP4. Interacts with PLAUR; the interaction occurs at the cell surface of invadopodia membranes. Interacts with ITGB1. Interacts with ITGA3. Associates with integrin alpha-3/beta-1; the association occurs in a collagen-dependent manner at the cell surface of invadopodia membranes. Q12884; P01275: GCG; NbExp=4; IntAct=EBI-4319803, EBI-7629173; Q12884; P01282: VIP; NbExp=2; IntAct=EBI-4319803, EBI-751454; [Prolyl endopeptidase FAP]: Cell surface ll membrane ingle-pass type II membrane protein Cell projection, lamellipodium membrane ; Single-pass type II membrane protein Cell projection, invadopodium membrane ingle-pass type II membrane protein Cell projection, ruffle membrane ; Single-pass type II membrane protein Membrane ; Single- pass type II membrane protein Note=Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha- 3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin- dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. [Antiplasmin-cleaving enzyme FAP, soluble form]: Secreted te=Found in blood plasma and serum. [Isoform 2]: Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=L, seprase-I ; IsoId=Q12884-1; Sequence=Displayed; Name=2 ; Synonyms=S, Truncated, seprase-s ; IsoId=Q12884-2; Sequence=VSP_005367; Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from inflamed synovial tissues. Expressed in activated hepatic stellate cells (HSC) and myofibroblasts from cirrhotic liver, but not detected in normal liver. Expressed in glioma cells (at protein level). Expressed in glioblastomas and glioma cells. Isoform 1 and isoform 2 are expressed in melanoma, carcinoma and fibroblast cell lines. In fibroblasts at times and sites of tissue remodeling during development, tissue repair and carcinogenesis. Up-regulated upon tumor stem cell differentiation. Up-regulated by transforming growth factor-beta, 12-O-tetradecanoyl phorbol-13-acetate and retinoids. N-glycosylated. The N-terminus may be blocked. [Isoform 1]: Major isoform. [Isoform 2]: Upstream open reading frames ORF(s)- containing region inhibits the translation of its downstream ORF. Belongs to the peptidase S9B family. angiogenesis protease binding endopeptidase activity metalloendopeptidase activity serine-type endopeptidase activity integrin binding protein binding extracellular region extracellular space cytoplasm plasma membrane focal adhesion proteolysis apoptotic process cell adhesion peptidase activity serine-type peptidase activity dipeptidyl-peptidase activity cell surface regulation of collagen catabolic process negative regulation of extracellular matrix disassembly membrane integral component of membrane hydrolase activity lamellipodium cell junction lamellipodium membrane ruffle membrane protein homodimerization activity cell projection endothelial cell migration apical part of cell basal part of cell protein dimerization activity proteolysis involved in cellular protein catabolic process regulation of fibrinolysis negative regulation of cell proliferation involved in contact inhibition positive regulation of cell cycle arrest invadopodium membrane mitotic cell cycle arrest melanocyte proliferation positive regulation of execution phase of apoptosis melanocyte apoptotic process negative regulation of extracellular matrix organization uc002ucd.1 uc002ucd.2 uc002ucd.3 uc002ucd.4 
ENST00000190165.3 DMRT3 ENST00000190165.3 doublesex and mab-3 related transcription factor 3 (from RefSeq NM_021240.4) DMRT3_HUMAN DMRTA3 ENST00000190165.1 ENST00000190165.2 NM_021240 Q7LA03 Q7LCH8 Q96SC7 Q9NQL9 Q9NRQ9 uc003zgw.1 uc003zgw.2 uc003zgw.3 uc003zgw.4 Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development (By similarity). May homodimerize. Q9NQL9; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-9679045, EBI-357530; Q9NQL9; Q86U10: ASPG; NbExp=3; IntAct=EBI-9679045, EBI-19946665; Q9NQL9; Q86V38: ATN1; NbExp=3; IntAct=EBI-9679045, EBI-11954292; Q9NQL9; P61421: ATP6V0D1; NbExp=3; IntAct=EBI-9679045, EBI-954063; Q9NQL9; O95273: CCNDBP1; NbExp=3; IntAct=EBI-9679045, EBI-748961; Q9NQL9; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-9679045, EBI-718615; Q9NQL9; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9679045, EBI-3867333; Q9NQL9; Q13643: FHL3; NbExp=3; IntAct=EBI-9679045, EBI-741101; Q9NQL9; Q5TD97: FHL5; NbExp=3; IntAct=EBI-9679045, EBI-750641; Q9NQL9; O15353: FOXN1; NbExp=3; IntAct=EBI-9679045, EBI-11319000; Q9NQL9; O43559: FRS3; NbExp=3; IntAct=EBI-9679045, EBI-725515; Q9NQL9; Q86YR5-3: GPSM1; NbExp=3; IntAct=EBI-9679045, EBI-10261098; Q9NQL9; P28799: GRN; NbExp=3; IntAct=EBI-9679045, EBI-747754; Q9NQL9; O75031: HSF2BP; NbExp=3; IntAct=EBI-9679045, EBI-7116203; Q9NQL9; Q0VD86: INCA1; NbExp=6; IntAct=EBI-9679045, EBI-6509505; Q9NQL9; O75525: KHDRBS3; NbExp=3; IntAct=EBI-9679045, EBI-722504; Q9NQL9; Q5T749: KPRP; NbExp=5; IntAct=EBI-9679045, EBI-10981970; Q9NQL9; Q15323: KRT31; NbExp=6; IntAct=EBI-9679045, EBI-948001; Q9NQL9; O76011: KRT34; NbExp=3; IntAct=EBI-9679045, EBI-1047093; Q9NQL9; Q92764: KRT35; NbExp=3; IntAct=EBI-9679045, EBI-1058674; Q9NQL9; O76013-2: KRT36; NbExp=3; IntAct=EBI-9679045, EBI-11958506; Q9NQL9; O76015: KRT38; NbExp=3; IntAct=EBI-9679045, EBI-1047263; Q9NQL9; Q6A162: KRT40; NbExp=6; IntAct=EBI-9679045, EBI-10171697; Q9NQL9; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-9679045, EBI-11959885; Q9NQL9; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-9679045, EBI-11749135; Q9NQL9; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-9679045, EBI-11741292; Q9NQL9; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-9679045, EBI-10172290; Q9NQL9; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-9679045, EBI-10171774; Q9NQL9; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-9679045, EBI-10172052; Q9NQL9; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-9679045, EBI-1048945; Q9NQL9; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-9679045, EBI-14065470; Q9NQL9; Q9BYR8: KRTAP3-1; NbExp=5; IntAct=EBI-9679045, EBI-9996449; Q9NQL9; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-9679045, EBI-3957694; Q9NQL9; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-9679045, EBI-11987425; Q9NQL9; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-9679045, EBI-3958099; Q9NQL9; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-9679045, EBI-11962084; Q9NQL9; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-9679045, EBI-1044640; Q9NQL9; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-9679045, EBI-1043191; Q9NQL9; Q14847-2: LASP1; NbExp=3; IntAct=EBI-9679045, EBI-9088686; Q9NQL9; P25791-3: LMO2; NbExp=3; IntAct=EBI-9679045, EBI-11959475; Q9NQL9; Q99750: MDFI; NbExp=6; IntAct=EBI-9679045, EBI-724076; Q9NQL9; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-9679045, EBI-16439278; Q9NQL9; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-9679045, EBI-10172526; Q9NQL9; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-9679045, EBI-742948; Q9NQL9; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-9679045, EBI-11522433; Q9NQL9; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-9679045, EBI-5662487; Q9NQL9; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-9679045, EBI-10271199; Q9NQL9; P0CG21: NHLRC4; NbExp=3; IntAct=EBI-9679045, EBI-12868744; Q9NQL9; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-9679045, EBI-945833; Q9NQL9; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-9679045, EBI-22310682; Q9NQL9; O43482: OIP5; NbExp=3; IntAct=EBI-9679045, EBI-536879; Q9NQL9; Q99471: PFDN5; NbExp=3; IntAct=EBI-9679045, EBI-357275; Q9NQL9; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-9679045, EBI-742388; Q9NQL9; O15162: PLSCR1; NbExp=3; IntAct=EBI-9679045, EBI-740019; Q9NQL9; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-9679045, EBI-3957793; Q9NQL9; P86480: PRR20D; NbExp=3; IntAct=EBI-9679045, EBI-12754095; Q9NQL9; P25788: PSMA3; NbExp=3; IntAct=EBI-9679045, EBI-348380; Q9NQL9; P61289: PSME3; NbExp=3; IntAct=EBI-9679045, EBI-355546; Q9NQL9; Q93062: RBPMS; NbExp=3; IntAct=EBI-9679045, EBI-740322; Q9NQL9; Q04864: REL; NbExp=3; IntAct=EBI-9679045, EBI-307352; Q9NQL9; Q04864-2: REL; NbExp=3; IntAct=EBI-9679045, EBI-10829018; Q9NQL9; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-9679045, EBI-746118; Q9NQL9; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-9679045, EBI-6257312; Q9NQL9; P21673: SAT1; NbExp=6; IntAct=EBI-9679045, EBI-711613; Q9NQL9; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-9679045, EBI-11959123; Q9NQL9; P15884: TCF4; NbExp=3; IntAct=EBI-9679045, EBI-533224; Q9NQL9; Q08117-2: TLE5; NbExp=3; IntAct=EBI-9679045, EBI-11741437; Q9NQL9; Q13077: TRAF1; NbExp=3; IntAct=EBI-9679045, EBI-359224; Q9NQL9; P36406: TRIM23; NbExp=3; IntAct=EBI-9679045, EBI-740098; Q9NQL9; P14373: TRIM27; NbExp=6; IntAct=EBI-9679045, EBI-719493; Q9NQL9; Q15654: TRIP6; NbExp=3; IntAct=EBI-9679045, EBI-742327; Q9NQL9; Q86WV8: TSC1; NbExp=3; IntAct=EBI-9679045, EBI-12806590; Q9NQL9; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-9679045, EBI-948354; Q9NQL9; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-9679045, EBI-1380492; Q9NQL9; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-9679045, EBI-11975223; Q9NQL9; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-9679045, EBI-12040603; Q9NQL9; P08048: ZFY; NbExp=3; IntAct=EBI-9679045, EBI-12239601; Q9NQL9; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-9679045, EBI-12030590; Q9NQL9; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-9679045, EBI-11962468; Nucleus Expressed in testis. Expressed in 4 to 5 weeks embryos. DMA domain interacts with ubiquitin. DMRT3 is a marker for a subset of spinal cord neurons (dI6). Belongs to the DMRT family. Name=Protein Spotlight; Note=A gait on the wildside - Issue 154 of November 2013; URL="https://web.expasy.org/spotlight/back_issues/154/"; nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development sex differentiation adult walking behavior transmission of nerve impulse ventral spinal cord interneuron specification cell differentiation regulation of odontogenesis of dentin-containing tooth sequence-specific DNA binding male sex differentiation metal ion binding protein heterodimerization activity uc003zgw.1 uc003zgw.2 uc003zgw.3 uc003zgw.4 
ENST00000190611.9 OSBPL6 ENST00000190611.9 oxysterol binding protein like 6, transcript variant 1 (from RefSeq NM_032523.4) B4DTW1 C4AMC0 C4AME4 D3DPF6 D3DPF7 ENST00000190611.1 ENST00000190611.2 ENST00000190611.3 ENST00000190611.4 ENST00000190611.5 ENST00000190611.6 ENST00000190611.7 ENST00000190611.8 NM_032523 ORP6 OSBL6_HUMAN Q4ZG68 Q53T68 Q59H61 Q7Z4Q1 Q86V84 Q8N9T0 Q96SR1 Q9BZF3 uc002ulx.1 uc002ulx.2 uc002ulx.3 uc002ulx.4 uc002ulx.5 This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain. Transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]. Regulates cellular transport and efflux of cholesterol (PubMed:26941018). Plays a role in phosphatidylinositol-4-phophate (PI4P) turnover at the neuronal membrane (By similarity). Binds via its PH domain PI4P, phosphatidylinositol-4,5-diphosphate, phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (By similarity). Weakly binds 25-hydroxycholesterol (PubMed:17428193). Homodimer (By similarity). Interacts with OSBPL3 (By similarity). Q9BZF3; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-2372709, EBI-6248094; Q9BZF3-6; O14901: KLF11; NbExp=3; IntAct=EBI-10698423, EBI-948266; Cytoplasm, cytosol doplasmic reticulum membrane eripheral membrane protein Nucleus envelope Cell membrane ; Peripheral membrane protein Endosome membrane ; Peripheral membrane protein Note=Co-localizes with OSBPL3 at contact sites between the plasma membrane and the endoplasmic reticulum. Event=Alternative splicing; Named isoforms=6; Name=1; IsoId=Q9BZF3-1; Sequence=Displayed; Name=2; IsoId=Q9BZF3-2; Sequence=VSP_010013; Name=3; IsoId=Q9BZF3-3; Sequence=VSP_036559, VSP_036561; Name=4; IsoId=Q9BZF3-4; Sequence=VSP_036560; Name=5; IsoId=Q9BZF3-5; Sequence=VSP_036561; Name=6; IsoId=Q9BZF3-6; Sequence=VSP_036560, VSP_010013, VSP_054430, VSP_054431; Expressed in brain and striated muscle (at protein level) (PubMed:14593528). Widely expressed (PubMed:11735225). Expressed in skeletal muscle (PubMed:14593528). Expressed in fetal brain and lung. By acetylated low-density lipoprotein. Belongs to the OSBP family. Sequence=BAB55223.1; Type=Erroneous initiation; Evidence=; Sequence=BAD92135.1; Type=Erroneous initiation; Evidence=; protein binding nucleus nuclear envelope cytoplasm endoplasmic reticulum endoplasmic reticulum membrane cytosol plasma membrane bile acid biosynthetic process lipid transport lipid binding cholesterol binding membrane nuclear membrane sterol binding intracellular membrane-bounded organelle perinuclear endoplasmic reticulum uc002ulx.1 uc002ulx.2 uc002ulx.3 uc002ulx.4 uc002ulx.5 
ENST00000190983.5 CCN5 ENST00000190983.5 cellular communication network factor 5, transcript variant 3 (from RefSeq NM_003881.4) B2R9N4 CCN5 CCN5_HUMAN CT58 CTGFL E1P612 ENST00000190983.1 ENST00000190983.2 ENST00000190983.3 ENST00000190983.4 NM_003881 O76076 Q6PEG3 UNQ228/PRO261 WISP2 uc002xmp.1 uc002xmp.2 uc002xmp.3 uc002xmp.4 uc002xmp.5 This gene encodes a member of the WNT1 inducible signaling pathway (WISP) protein subfamily, which belongs to the connective tissue growth factor (CTGF) family. WNT1 is a member of a family of cysteine-rich, glycosylated signaling proteins that mediate diverse developmental processes. The CTGF family members are characterized by four conserved cysteine-rich domains: insulin-like growth factor-binding domain, von Willebrand factor type C module, thrombospondin domain and C-terminal cystine knot-like (CT) domain. The encoded protein lacks the CT domain which is implicated in dimerization and heparin binding. It is 72% identical to the mouse protein at the amino acid level. This gene may be downstream in the WNT1 signaling pathway that is relevant to malignant transformation. Its expression in colon tumors is reduced while the other two WISP members are overexpressed in colon tumors. It is expressed at high levels in bone tissue, and may play an important role in modulating bone turnover. [provided by RefSeq, Jul 2008]. May play an important role in modulating bone turnover. Promotes the adhesion of osteoblast cells and inhibits the binding of fibrinogen to integrin receptors. In addition, inhibits osteocalcin production. O76076; P49639: HOXA1; NbExp=3; IntAct=EBI-2850068, EBI-740785; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O76076-1; Sequence=Displayed; Name=2; IsoId=O76076-2; Sequence=VSP_056298, VSP_056299; Expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart. Belongs to the CCN family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42814/WISP2"; integrin binding insulin-like growth factor binding extracellular region extracellular space nucleus cell adhesion signal transduction cell-cell signaling heparin binding extracellular matrix negative regulation of cell death uc002xmp.1 uc002xmp.2 uc002xmp.3 uc002xmp.4 uc002xmp.5 
ENST00000192314.7 GAL3ST2 ENST00000192314.7 galactose-3-O-sulfotransferase 2 (from RefSeq NM_022134.3) ENST00000192314.1 ENST00000192314.2 ENST00000192314.3 ENST00000192314.4 ENST00000192314.5 ENST00000192314.6 G3ST2_HUMAN GP3ST NM_022134 Q17RK0 Q57Z52 Q9H3Q3 uc002wcj.1 uc002wcj.2 uc002wcj.3 This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate group to the hydroxyl at C-3 of nonreducing beta-galactosyl residues, and it can act on both type 1 and type 2 (Galbeta 1-3/1-4GlcNAc-R) oligosaccharides with similar efficiencies, and on core 1 glycans. This enzyme has been implicated in tumor metastasis processes. This gene is different from the GAL3ST3 gene located on chromosome 11, which has also been referred to as GAL3ST2 and encodes a related enzyme with distinct tissue distribution and substrate specificities, compared to galactose-3-O-sulfotransferase 2. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC117295.1, AB040610.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000192314.7/ ENSP00000192314.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transfers a sulfate group to the hydroxyl group at C3 of non- reducing beta-galactosyl residues. Acts both on type 1 (Gal-beta-1,3- GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar efficiency. Strongly inhibited by Cu(2+) and Zn(2+). pH dependence: Optimum pH is 6.0-6.5.; Protein modification; carbohydrate sulfation. Q9H3Q3; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10306373, EBI-742948; Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein Ubiquitous. Detected in heart, stomach, colon, liver and spleen, in epithelial cells lining the lower to middle layer of the crypts in colonic mucosa, hepatocytes surrounding the central vein of the liver, extravillous cytotrophoblasts in the basal plate of the septum of the placenta, renal tubules of the kidney, and neuronal cells of the cerebral cortex. Belongs to the galactose-3-O-sulfotransferase family. galactosylceramide sulfotransferase activity protein binding Golgi apparatus sulfotransferase activity biological_process glycolipid biosynthetic process membrane integral component of membrane transferase activity Golgi cisterna membrane uc002wcj.1 uc002wcj.2 uc002wcj.3 
ENST00000192788.6 BLTP3A ENST00000192788.6 bridge-like lipid transfer protein family member 3A (from RefSeq NM_017754.4) BLT3A_HUMAN BLTP3A C6orf107 ENST00000192788.1 ENST00000192788.2 ENST00000192788.3 ENST00000192788.4 ENST00000192788.5 NM_017754 Q6BDS2 Q9NXE0 UHRF1BP1 uc003oju.1 uc003oju.2 uc003oju.3 uc003oju.4 uc003oju.5 uc003oju.6 Tube-forming lipid transport protein which probably mediates the transfer of lipids between membranes at organelle contact sites (PubMed:35499567). May be involved in the retrograde traffic of vesicle clusters in the endocytic pathway to the Golgi complex (PubMed:35499567). Homodimer (Potential). Interacts with UHRF1. Late endosome Sequence=BAA91074.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence=; protein binding identical protein binding histone deacetylase binding uc003oju.1 uc003oju.2 uc003oju.3 uc003oju.4 uc003oju.5 uc003oju.6 
ENST00000193322.8 OSTM1 ENST00000193322.8 osteoclastogenesis associated transmembrane protein 1 (from RefSeq NM_014028.4) E1P5E3 ENST00000193322.1 ENST00000193322.2 ENST00000193322.3 ENST00000193322.4 ENST00000193322.5 ENST00000193322.6 ENST00000193322.7 GL HSPC019 NM_014028 OSTM1_HUMAN Q5R391 Q6PCA7 Q7RTW6 Q86WC4 Q8NC29 Q8TC82 Q9Y2S9 UNQ6098/PRO21201 uc003psd.1 uc003psd.2 uc003psd.3 uc003psd.4 This gene encodes a protein that may be involved in the degradation of G proteins via the ubiquitin-dependent proteasome pathway. The encoded protein binds to members of subfamily A of the regulator of the G-protein signaling (RGS) family through an N-terminal leucine-rich region. This protein also has a central RING finger-like domain and E3 ubiquitin ligase activity. This protein is highly conserved from flies to humans. Defects in this gene may cause the autosomal recessive, infantile malignant form of osteopetrosis. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803613.213465.1, SRR1803613.136052.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000193322.8/ ENSP00000193322.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Required for osteoclast and melanocyte maturation and function. Chloride channel 7 are heteromers of alpha (CLCN7) and beta (OSTM1) subunits. Q86WC4; P51798: CLCN7; NbExp=3; IntAct=EBI-11037160, EBI-4402346; Lysosome membrane ; Single-pass type I membrane protein Note=Requires CLCN7 to travel to lysosomes. Undergoes proteolytic cleavage in the luminal domain, the cleaved fragments might be linked by disulfide bonds with the remnant of the protein. Highly N-glycosylated. Osteopetrosis, autosomal recessive 5 (OPTB5) [MIM:259720]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB5 patients manifest primary central nervous system involvement in addition to the classical stigmata of severe bone sclerosis, growth failure, anemia, thrombocytopenia and visual impairment with optic atrophy. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the OSTM1 family. Sequence=AAD27000.1; Type=Frameshift; Evidence=; lysosome lysosomal membrane cytosol membrane integral component of membrane osteoclast differentiation ion transmembrane transport uc003psd.1 uc003psd.2 uc003psd.3 uc003psd.4 
ENST00000193391.8 IMPG2 ENST00000193391.8 interphotoreceptor matrix proteoglycan 2 (from RefSeq NM_016247.4) A8MWT5 ENST00000193391.1 ENST00000193391.2 ENST00000193391.3 ENST00000193391.4 ENST00000193391.5 ENST00000193391.6 ENST00000193391.7 IMPG2_HUMAN IPM200 NM_016247 Q9BZV3 Q9UKD4 Q9UKK5 uc003duq.1 uc003duq.2 uc003duq.3 uc003duq.4 The protein encoded by this gene binds chondroitin sulfate and hyaluronan and is a proteoglycan. The encoded protein plays a role in the organization of the interphotoreceptor matrix and may promote the growth and maintenance of the light-sensitive photoreceptor outer segment. Defects in this gene are a cause of retinitis pigmentosa type 56 and maculopathy, IMPG2-related.[provided by RefSeq, Mar 2011]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB593127.1, AF173155.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000193391.8/ ENSP00000193391.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light-sensitive photoreceptor outer segment. Binds heparin. Photoreceptor outer segment membrane ; Single-pass type I membrane protein Photoreceptor inner segment membrane ; Single-pass type I membrane protein Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix Expressed in the retina (at protein level) (PubMed:10702256, PubMed:29777959). Expressed by photoreceptors of the interphotoreceptor matrix (IPM) surrounding both rods and cones (at protein level) (PubMed:10542133, PubMed:29777959). IPM occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina (PubMed:10542133). Expressed in the pineal gland (at protein level) (PubMed:10702256). Expressed in the retina 17 weeks post-conception (at protein level) (PubMed:29777959). Expressed in the outer neuroblastic zone and retinal pigment epithelium (at protein level) (PubMed:29777959). Highly glycosylated (N- and O-linked carbohydrates). Retinitis pigmentosa 56 (RP56) [MIM:613581]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. te=The disease is caused by variants affecting the gene represented in this entry. Macular dystrophy, vitelliform, 5 (VMD5) [MIM:616152]: A form of macular dystrophy, a retinal disease in which various forms of deposits, pigmentary changes, and atrophic lesions are observed in the macula lutea. Vitelliform macular dystrophies are characterized by yellow, lipofuscin-containing deposits, usually localized at the center of the macula. VMD5 features include late-onset moderate visual impairment and preservation of retinal pigment epithelium reflectivity. te=The disease is caused by variants affecting the gene represented in this entry. extracellular matrix structural constituent hyaluronic acid binding visual perception heparin binding membrane integral component of membrane extracellular matrix interphotoreceptor matrix receptor complex uc003duq.1 uc003duq.2 uc003duq.3 uc003duq.4 
ENST00000194130.7 SLC13A1 ENST00000194130.7 solute carrier family 13 member 1, transcript variant 1 (from RefSeq NM_022444.4) ENST00000194130.1 ENST00000194130.2 ENST00000194130.3 ENST00000194130.4 ENST00000194130.5 ENST00000194130.6 NAS1 NASI1 NM_022444 Q9BZW2 Q9H5Z0 S13A1_HUMAN uc003vkm.1 uc003vkm.2 uc003vkm.3 uc003vkm.4 uc003vkm.5 The protein encoded by this gene is an apical membrane Na(+)-sulfate cotransporter involved in sulfate homeostasis in the kidney. Defects in this gene lead to many pathophysiologic problems. [provided by RefSeq, May 2016]. Sodium:sulfate symporter that mediates sulfate reabsorption in the kidney and small intestine (PubMed:11161786). Can also mediate the transport of selenate and thiosulfate (By similarity). Reaction=3 Na(+)(out) + sulfate(out) = 3 Na(+)(in) + sulfate(in); Xref=Rhea:RHEA:71951, ChEBI:CHEBI:16189, ChEBI:CHEBI:29101; Evidence=; Reaction=3 Na(+)(out) + selenate(out) = 3 Na(+)(in) + selenate(in); Xref=Rhea:RHEA:72079, ChEBI:CHEBI:15075, ChEBI:CHEBI:29101; Evidence=; Reaction=3 Na(+)(out) + thiosulfate(out) = 3 Na(+)(in) + thiosulfate(in); Xref=Rhea:RHEA:72323, ChEBI:CHEBI:29101, ChEBI:CHEBI:33542; Evidence=; Inhibited by thiosulfate, selenate, molybdate, tungstate, citrate and succinate. Kinetic parameters: KM=0.31 mM for sulfate ; KM=23.6 mM for sodium ; Apical cell membrane ; Multi-pass membrane protein Highly expressed in kidney; not detectable in the other tissues tested. Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. NADC subfamily. plasma membrane ion transport sodium ion transport dicarboxylic acid transport secondary active sulfate transmembrane transporter activity sulfate transport citrate transmembrane transporter activity succinate transmembrane transporter activity symporter activity sodium:sulfate symporter activity citrate transport membrane integral component of membrane sodium:dicarboxylate symporter activity transmembrane transporter activity transmembrane transport succinate transmembrane transport sulfate transmembrane transport uc003vkm.1 uc003vkm.2 uc003vkm.3 uc003vkm.4 uc003vkm.5 
ENST00000194152.4 PCDHB4 ENST00000194152.4 protocadherin beta 4 (from RefSeq NM_018938.4) ENST00000194152.1 ENST00000194152.2 ENST00000194152.3 NM_018938 PCDB4_HUMAN Q4V761 Q9Y5E5 uc003lip.1 uc003lip.2 uc003lip.3 uc003lip.4 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: SRR1660809.19460.1, SRR1660805.174070.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000194152.4/ ENSP00000194152.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Cell membrane ; Single-pass type I membrane protein calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules chemical synaptic transmission nervous system development synapse assembly membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules uc003lip.1 uc003lip.2 uc003lip.3 uc003lip.4 
ENST00000194155.7 PCDHB2 ENST00000194155.7 protocadherin beta 2 (from RefSeq NM_018936.4) ENST00000194155.1 ENST00000194155.2 ENST00000194155.3 ENST00000194155.4 ENST00000194155.5 ENST00000194155.6 NM_018936 PCDB2_HUMAN Q4KMU1 Q9Y5E7 uc003lil.1 uc003lil.2 uc003lil.3 uc003lil.4 uc003lil.5 uc003lil.6 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: SRR1660805.221139.1, SRR1803615.169890.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000194155.7/ ENSP00000194155.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Cell membrane ; Single-pass type I membrane protein calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules chemical synaptic transmission nervous system development synapse assembly membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules uc003lil.1 uc003lil.2 uc003lil.3 uc003lil.4 uc003lil.5 uc003lil.6 
ENST00000194214.10 IFT25 ENST00000194214.10 intraflagellar transport 25, transcript variant 17 (from RefSeq NR_167995.1) A6NG57 C1orf41 D3DQ45 ENST00000194214.1 ENST00000194214.2 ENST00000194214.3 ENST00000194214.4 ENST00000194214.5 ENST00000194214.6 ENST00000194214.7 ENST00000194214.8 ENST00000194214.9 HSPB11 HSPC034 IFT25 IFT25_HUMAN NR_167995 Q9Y547 Q9Y684 uc001cwh.1 uc001cwh.2 uc001cwh.3 uc001cwh.4 uc001cwh.5 Component of the IFT complex B required for sonic hedgehog/SHH signaling. May mediate transport of SHH components: required for the export of SMO and PTCH1 receptors out of the cilium and the accumulation of GLI2 at the ciliary tip in response to activation of the SHH pathway, suggesting it is involved in the dynamic transport of SHH signaling molecules within the cilium. Not required for ciliary assembly. Its role in intraflagellar transport is mainly seen in tissues rich in ciliated cells such as kidney and testis. Essential for male fertility, spermiogenesis and sperm flagella formation. Plays a role in the early development of the kidney. May be involved in the regulation of ureteric bud initiation (By similarity). Component of the IFT complex B, at least composed of IFT20, IFT22, IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT27. Interacts with IFT88 (By similarity). Q9Y547; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-747101, EBI-739467; Q9Y547; Q9BW83: IFT27; NbExp=20; IntAct=EBI-747101, EBI-747093; Q9Y547; Q9Y6Y8: SEC23IP; NbExp=3; IntAct=EBI-747101, EBI-1767971; Q9Y547; Q13114: TRAF3; NbExp=3; IntAct=EBI-747101, EBI-357631; Cell projection, cilium Detected in placenta. Belongs to the IFT25 family. Was initially classified as a member of the small heat shock family protein. However, it was later shown that it is not the case (PubMed:19921466). Sequence=AAD43011.1; Type=Frameshift; Evidence=; skeletal system development kidney development protein binding centrosome cilium smoothened signaling pathway spermatogenesis heart development protein transport cell differentiation lung development intraciliary transport particle B intraciliary transport involved in cilium assembly intraciliary transport cell projection metal ion binding left/right axis specification ciliary tip cilium assembly uc001cwh.1 uc001cwh.2 uc001cwh.3 uc001cwh.4 uc001cwh.5 
ENST00000194530.8 STRADB ENST00000194530.8 STE20 related adaptor beta, transcript variant 1 (from RefSeq NM_018571.6) ALS2CR2 ENST00000194530.1 ENST00000194530.2 ENST00000194530.3 ENST00000194530.4 ENST00000194530.5 ENST00000194530.6 ENST00000194530.7 ILPIP NM_018571 PRO1038 Q5BKY7 Q9C0K7 Q9P1L0 STRAB_HUMAN uc002uyd.1 uc002uyd.2 uc002uyd.3 uc002uyd.4 uc002uyd.5 uc002uyd.6 This gene encodes a protein that belongs to the serine/threonine protein kinase STE20 subfamily. One of the active site residues in the protein kinase domain of this protein is altered, and it is thus a pseudokinase. This protein is a component of a complex involved in the activation of serine/threonine kinase 11, a master kinase that regulates cell polarity and energy-generating metabolism. This complex regulates the relocation of this kinase from the nucleus to the cytoplasm, and it is essential for G1 cell cycle arrest mediated by this kinase. The protein encoded by this gene can also interact with the X chromosome-linked inhibitor of apoptosis protein, and this interaction enhances the anti-apoptotic activity of this protein via the JNK1 signal transduction pathway. Two pseudogenes, located on chromosomes 1 and 7, have been found for this gene. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2011]. Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity). Component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. Interacts with BIRC4/XIAP. These two proteins are likely to coexist in a complex with TAK1, TRAF6, TAB1 and TAB2. Q9C0K7; Q9Y376: CAB39; NbExp=6; IntAct=EBI-306893, EBI-306905; Q9C0K7; Q15831: STK11; NbExp=9; IntAct=EBI-306893, EBI-306838; Nucleus Cytoplasm Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=ILPIP-alpha; IsoId=Q9C0K7-1; Sequence=Displayed; Name=2; IsoId=Q9C0K7-2; Sequence=VSP_016623, VSP_016624; Name=3; Synonyms=ILPIP-beta; IsoId=Q9C0K7-3; Sequence=VSP_016625; Highly expressed in heart, skeletal muscle, testis, liver and colon. The protein kinase domain is predicted to be catalytically inactive. Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Ser-184 is present instead of the conserved Asp which is expected to be an active site residue. nucleotide binding cell morphogenesis protein serine/threonine kinase activity protein binding ATP binding nucleus cytoplasm cytosol protein export from nucleus cell cycle cell cycle arrest aggresome signal transduction by protein phosphorylation activation of protein kinase activity negative regulation of extrinsic apoptotic signaling pathway in absence of ligand protein kinase activity protein phosphorylation uc002uyd.1 uc002uyd.2 uc002uyd.3 uc002uyd.4 uc002uyd.5 uc002uyd.6 
ENST00000196061.5 PLOD1 ENST00000196061.5 procollagen-lysine,2-oxoglutarate 5-dioxygenase 1, transcript variant 1 (from RefSeq NM_001316320.2) B4DR87 ENST00000196061.1 ENST00000196061.2 ENST00000196061.3 ENST00000196061.4 LLH NM_001316320 PLOD PLOD1_HUMAN Q02809 Q96AV9 Q9H132 uc001atm.1 uc001atm.2 uc001atm.3 uc001atm.4 uc001atm.5 Lysyl hydroxylase is a membrane-bound homodimeric protein localized to the cisternae of the endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VI have deficiencies in lysyl hydroxylase activity. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2015]. Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity). Forms hydroxylysine residues in -Xaa-Lys- Gly- sequences in collagens (PubMed:8621606, PubMed:10686424, PubMed:15854030). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (Probable). Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L- lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA- COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4; Evidence= Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence=; Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence=; Homodimer (By similarity). Identified in a complex with P3H3 and P3H4 (By similarity). Q02809; P55795: HNRNPH2; NbExp=2; IntAct=EBI-357174, EBI-352823; Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q02809-1; Sequence=Displayed; Name=2; IsoId=Q02809-2; Sequence=VSP_056300; Ehlers-Danlos syndrome, kyphoscoliotic type, 1 (EDSKSCL1) [MIM:225400]: A form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. EDSKSCL1 is an autosomal recessive form characterized by severe muscle hypotonia at birth, generalized joint laxity, scoliosis at birth, and scleral fragility and rupture of the ocular globe. te=The disease is caused by variants affecting the gene represented in this entry. response to hypoxia iron ion binding protein binding endoplasmic reticulum endoplasmic reticulum membrane cellular protein modification process procollagen-lysine 5-dioxygenase activity epidermis development membrane oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen peptidyl-lysine hydroxylation collagen fibril organization rough endoplasmic reticulum membrane L-ascorbic acid binding collagen metabolic process protein homodimerization activity metal ion binding hydroxylysine biosynthetic process dioxygenase activity oxidation-reduction process extracellular exosome catalytic complex protein O-linked glycosylation procollagen glucosyltransferase activity uc001atm.1 uc001atm.2 uc001atm.3 uc001atm.4 uc001atm.5 
ENST00000196371.10 OXCT1 ENST00000196371.10 3-oxoacid CoA-transferase 1, transcript variant 7 (from RefSeq NR_157114.2) B2R5V2 B7Z528 ENST00000196371.1 ENST00000196371.2 ENST00000196371.3 ENST00000196371.4 ENST00000196371.5 ENST00000196371.6 ENST00000196371.7 ENST00000196371.8 ENST00000196371.9 NR_157114 OXCT P55809 SCOT SCOT1_HUMAN uc003jmn.1 uc003jmn.2 uc003jmn.3 uc003jmn.4 uc003jmn.5 This gene encodes a member of the 3-oxoacid CoA-transferase gene family. The encoded protein is a homodimeric mitochondrial matrix enzyme that plays a central role in extrahepatic ketone body catabolism by catalyzing the reversible transfer of coenzyme A from succinyl-CoA to acetoacetate. Mutations in this gene are associated with succinyl CoA:3-oxoacid CoA transferase deficiency. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660805.69558.1, SRR5189661.109341.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta ##RefSeq-Attributes-END## Key enzyme for ketone body catabolism. Catalyzes the first, rate-limiting step of ketone body utilization in extrahepatic tissues, by transferring coenzyme A (CoA) from a donor thiolester species (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces acetoacetyl-CoA. Acetoacetyl-CoA is further metabolized by acetoacetyl- CoA thiolase into two acetyl-CoA molecules which enter the citric acid cycle for energy production (PubMed:10964512). Forms a dimeric enzyme where both of the subunits are able to form enzyme-CoA thiolester intermediates, but only one subunit is competent to transfer the CoA moiety to the acceptor carboxylate (3-oxo acid) and produce a new acyl- CoA. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate; Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973, ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24565; Evidence=; Reaction=acetoacetate + succinyl-CoA = acetoacetyl-CoA + succinate; Xref=Rhea:RHEA:25480, ChEBI:CHEBI:13705, ChEBI:CHEBI:30031, ChEBI:CHEBI:57286, ChEBI:CHEBI:57292; EC=2.8.3.5; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25481; Evidence=; Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1. Homodimer (PubMed:10964512, PubMed:23420214). Only one subunit is competent to transfer the CoA moiety to the acceptor carboxylate (3- oxo acid) (By similarity). Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P55809-1; Sequence=Displayed; Name=2; IsoId=P55809-2; Sequence=VSP_056310; Abundant in heart, followed in order by brain, kidney, skeletal muscle, and lung, whereas in liver it is undetectable. Expressed (at protein level) in all tissues (except in liver), most abundant in myocardium, then brain, kidney, adrenal glands, skeletal muscle and lung; also detectable in leukocytes and fibroblasts. Succinyl-CoA:3-oxoacid CoA transferase deficiency (SCOTD) [MIM:245050]: A disorder of ketone body metabolism, characterized by episodic ketoacidosis. Patients are usually asymptomatic between episodes. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the 3-oxoacid CoA-transferase family. nucleoplasm mitochondrion mitochondrial matrix brain development heart development response to nutrient 3-oxoacid CoA-transferase activity CoA-transferase activity response to hormone response to activity transferase activity positive regulation of insulin secretion involved in cellular response to glucose stimulus ketone catabolic process response to drug response to starvation protein homodimerization activity response to ethanol cellular ketone body metabolic process ketone body catabolic process adipose tissue development uc003jmn.1 uc003jmn.2 uc003jmn.3 uc003jmn.4 uc003jmn.5 
ENST00000196482.4 ZNF324 ENST00000196482.4 zinc finger protein 324 (from RefSeq NM_014347.3) B3KRX1 ENST00000196482.1 ENST00000196482.2 ENST00000196482.3 NM_014347 O75467 Z324A_HUMAN ZNF324A uc002qsw.1 uc002qsw.2 uc002qsw.3 uc002qsw.4 May be involved in transcriptional regulation. May be involved in regulation of cell proliferation. Nucleus Expressed at high levels in the spleen, thymus, and PBMC, at low levels in the prostate, ovary, small intestine, colon (mucosal lining), placenta, lung, and pancreas, and very weakly expressed in the liver and kidney. Induced at the early stage of T cell activation. Regulated at the transcriptional level during the cell cycle. Induced at a maximum level in the S phase. Belongs to the krueppel C2H2-type zinc-finger protein family. nucleic acid binding DNA binding nucleus regulation of transcription, DNA-templated metal ion binding uc002qsw.1 uc002qsw.2 uc002qsw.3 uc002qsw.4 
ENST00000196489.4 ZNF416 ENST00000196489.4 zinc finger protein 416, transcript variant 1 (from RefSeq NM_017879.3) ENST00000196489.1 ENST00000196489.2 ENST00000196489.3 NM_017879 Q9BWM5 Q9NWW8 ZN416_HUMAN uc002qpf.1 uc002qpf.2 uc002qpf.3 uc002qpf.4 uc002qpf.5 May be involved in transcriptional regulation. Nucleus Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=BAA91257.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; nucleic acid binding DNA binding nucleus regulation of transcription, DNA-templated metal ion binding uc002qpf.1 uc002qpf.2 uc002qpf.3 uc002qpf.4 uc002qpf.5 
ENST00000196551.8 RPS5 ENST00000196551.8 ribosomal protein S5 (from RefSeq NM_001009.4) B2R4T2 ENST00000196551.1 ENST00000196551.2 ENST00000196551.3 ENST00000196551.4 ENST00000196551.5 ENST00000196551.6 ENST00000196551.7 NM_001009 P46782 Q96BN0 RPS5 RS5_HUMAN uc061dsc.1 uc061dsc.2 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S7P family of ribosomal proteins. It is located in the cytoplasm. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189652.100764.1, SRR5189658.142489.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000196551.8/ ENSP00000196551.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). Component of the small ribosomal subunit. Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). P46782; P54253: ATXN1; NbExp=3; IntAct=EBI-350569, EBI-930964; P46782; P42858: HTT; NbExp=3; IntAct=EBI-350569, EBI-466029; P46782; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-350569, EBI-1055254; Cytoplasm Nucleus, nucleolus Belongs to the universal ribosomal protein uS7 family. ribosomal small subunit assembly nuclear-transcribed mRNA catabolic process, nonsense-mediated decay RNA binding mRNA binding structural constituent of ribosome protein binding nucleoplasm cytosol ribosome focal adhesion translation translational initiation regulation of translational fidelity SRP-dependent cotranslational protein targeting to membrane small ribosomal subunit membrane viral transcription rRNA binding cytosolic small ribosomal subunit extracellular exosome ribonucleoprotein complex uc061dsc.1 uc061dsc.2 
ENST00000197268.13 FAM234B ENST00000197268.13 family with sequence similarity 234 member B (from RefSeq NM_020853.2) A2RU67 ENST00000197268.1 ENST00000197268.10 ENST00000197268.11 ENST00000197268.12 ENST00000197268.2 ENST00000197268.3 ENST00000197268.4 ENST00000197268.5 ENST00000197268.6 ENST00000197268.7 ENST00000197268.8 ENST00000197268.9 F234B_HUMAN FAM234B KIAA1467 NM_020853 Q49AF2 Q5CZ81 Q6ZUV7 Q9P261 uc001rbi.1 uc001rbi.2 uc001rbi.3 uc001rbi.4 uc001rbi.5 Membrane ; Single-pass membrane protein Golgi outpost Cytoplasm, cytoskeleton, microtubule organizing center Note=Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation. Belongs to the FAM234 family. membrane integral component of membrane uc001rbi.1 uc001rbi.2 uc001rbi.3 uc001rbi.4 uc001rbi.5 
ENST00000198536.7 PILRA ENST00000198536.7 paired immunoglobin like type 2 receptor alpha, transcript variant 1 (from RefSeq NM_013439.3) ENST00000198536.1 ENST00000198536.2 ENST00000198536.3 ENST00000198536.4 ENST00000198536.5 ENST00000198536.6 NM_013439 PILRA_HUMAN Q8NHI1 Q9UKJ1 uc003uuo.1 uc003uuo.2 Cell signaling pathways rely on a dynamic interaction between activating and inhibiting processes. SHP-1-mediated dephosphorylation of protein tyrosine residues is central to the regulation of several cell signaling pathways. Two types of inhibitory receptor superfamily members are immunoreceptor tyrosine-based inhibitory motif (ITIM)-bearing receptors and their non-ITIM-bearing, activating counterparts. Control of cell signaling via SHP-1 is thought to occur through a balance between PILRalpha-mediated inhibition and PILRbeta-mediated activation. These paired immunoglobulin-like receptor genes are located in a tandem head-to-tail orientation on chromosome 7. This particular gene encodes the ITIM-bearing member of the receptor pair, which functions in the inhibitory role. Alternative splicing has been observed at this locus and three variants, each encoding a distinct isoform, are described. [provided by RefSeq, Jul 2008]. Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP. (Microbial infection) Acts as an entry co-receptor for herpes simplex virus 1. Monomer. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon tyrosine phosphorylation. (Microbial infection) Interacts with herpes simplex virus 1 glycoprotein B. Q9UKJ1; Q5KU26: COLEC12; NbExp=2; IntAct=EBI-965833, EBI-1104680; Q9UKJ1; Q9NQX5: NPDC1; NbExp=6; IntAct=EBI-965833, EBI-748927; Q9UKJ1; P29350: PTPN6; NbExp=5; IntAct=EBI-965833, EBI-78260; Q9UKJ1; P06436: gB; Xeno; NbExp=3; IntAct=EBI-965833, EBI-1771271; [Isoform 1]: Cell membrane ; Single- pass type I membrane protein [Isoform 2]: Cell membrane ; Single- pass type I membrane protein [Isoform 3]: Secreted [Isoform 4]: Secreted Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9UKJ1-1; Sequence=Displayed; Name=2; IsoId=Q9UKJ1-2; Sequence=VSP_017502; Name=3; Synonyms=FDF03-deltaTM; IsoId=Q9UKJ1-3; Sequence=VSP_017501; Name=4; Synonyms=FDF03-M14; IsoId=Q9UKJ1-4; Sequence=VSP_017500; Predominantly detected in hemopoietic tissues and is expressed by monocytes, macrophages, and granulocytes, but not by lymphocytes. Also strongly expressed by dendritic cells (DC); preferentially by CD14+/CD1a- DC derived from CD34+ progenitors. Also expressed by CD11c+ blood and tonsil DC, but not by CD11c- DC precursors. Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. PTPN6 seems to bind predominantly to the first ITIM motif. According to PubMed:10660620, N- and O-glycosylated. According to PubMed:10903717, only N-glycosylated. Phosphorylated on tyrosine residues. protein binding extracellular region plasma membrane signal transduction membrane integral component of membrane viral process MHC class I protein binding regulation of immune response extracellular exosome uc003uuo.1 uc003uuo.2 
ENST00000198767.11 RRN3 ENST00000198767.11 RRN3 homolog, RNA polymerase I transcription factor, transcript variant 1 (from RefSeq NM_018427.5) A2RTY9 B4E0J7 B4E3T2 ENST00000198767.1 ENST00000198767.10 ENST00000198767.2 ENST00000198767.3 ENST00000198767.4 ENST00000198767.5 ENST00000198767.6 ENST00000198767.7 ENST00000198767.8 ENST00000198767.9 NM_018427 Q3MHU9 Q6IPL4 Q9H4F0 Q9NYV6 RRN3_HUMAN TIFIA uc002dde.1 uc002dde.2 uc002dde.3 uc002dde.4 uc002dde.5 Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction (By similarity). Interacts with POLR1F, EIF3L, TAF1B and TAF1C. Nucleus, nucleolus Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9NYV6-1; Sequence=Displayed; Name=2; IsoId=Q9NYV6-2; Sequence=VSP_056338, VSP_056339; Name=3; IsoId=Q9NYV6-3; Sequence=VSP_056520; Name=4; IsoId=Q9NYV6-4; Sequence=VSP_056519, VSP_056521; Phosphorylation is required for participation in rDNA transcription (By similarity). Phosphorylated at Thr-200 by MAPK9/JNK2, which abrogates initiation complex formation. Belongs to the RRN3 family. RNA polymerase I core binding RNA polymerase I CORE element sequence-specific DNA binding transcription factor activity, core RNA polymerase I binding RNA polymerase I transcriptional preinitiation complex assembly in utero embryonic development nucleus nucleoplasm nucleolus DNA-templated transcription, initiation transcription initiation from RNA polymerase I promoter nucleolus organization cytoplasm organization cell proliferation positive regulation of neuron projection development ribosome biogenesis positive regulation of transcription, DNA-templated homeostasis of number of cells RNA polymerase binding negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator regulation of DNA-templated transcription, initiation uc002dde.1 uc002dde.2 uc002dde.3 uc002dde.4 uc002dde.5 
ENST00000198801.10 MOGAT2 ENST00000198801.10 monoacylglycerol O-acyltransferase 2 (from RefSeq NM_025098.4) A8K7I3 DC5 DGAT2L5 ENST00000198801.1 ENST00000198801.2 ENST00000198801.3 ENST00000198801.4 ENST00000198801.5 ENST00000198801.6 ENST00000198801.7 ENST00000198801.8 ENST00000198801.9 MOGAT2 MOGT2_HUMAN NM_025098 Q3SYC1 Q3SYC2 Q6ZQZ2 Q86UH6 Q9H630 uc010rru.1 uc010rru.2 uc010rru.3 uc010rru.4 The protein encoded by this gene is an enzyme that catalyzes the synthesis of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. The encoded protein is important in the uptake of dietary fat by the small intestine. This protein forms a complex with diacylglycerol O-acyltransferase 2 in the endoplasmic reticulum, and this complex catalyzes the synthesis of triacylglycerol. [provided by RefSeq, Dec 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK291998.1, BC103876.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000198801.10/ ENSP00000198801.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Involved in glycerolipid synthesis and lipid metabolism (PubMed:12621063, PubMed:18768481, PubMed:27184406, PubMed:28420705). Catalyzes the formation of diacylglycerol, the precursor of triacylglycerol, by transferring the acyl chain of a fatty acyl-CoA to a monoacylglycerol (PubMed:12621063, PubMed:27184406). Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes (By similarity). Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0 at sn-2 (PubMed:12621063). Able to use 1-monoalkylglycerol (1-MAkG, 1-O- alkylglycerol) as an acyl acceptor for the synthesis of monoalkyl- monoacylglycerol (MAMAG, 1-O-alkyl-3-acylglycerol or 1-O-alkyl-2- acylglycerol) and subsequently, with lower efficiency, may add another acyl chain producing monoalkyl-diacylglycerol (MADAG, 1-O-alkyl-2,3- diacylglycerol) (PubMed:28420705). Possesses weak but significant activity with diacylglycerol as substrate, producing triacylglycerol (triacyl-sn-glycerol) (PubMed:18768481). Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacylglycerol + CoA; Xref=Rhea:RHEA:16741, ChEBI:CHEBI:17389, ChEBI:CHEBI:49172, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16742; Evidence= Reaction=2-(9Z-octadecenoyl)-glycerol + butanoyl-CoA = 1-butanoyl-2- (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77271, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:73990, ChEBI:CHEBI:197386; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77272; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + octanoyl-CoA = 1-octanoyl-2- (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77539, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:73990, ChEBI:CHEBI:197391; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77540; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + dodecanoyl-CoA = 1-dodecanoyl- 2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77275, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:73990, ChEBI:CHEBI:75579; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77276; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + tetradecanoyl-CoA = 1- tetradecanoyl-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:73990, ChEBI:CHEBI:75582; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77280; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1- hexadecanoyl-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77283, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:73990, ChEBI:CHEBI:75585; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77284; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + octadecanoyl-CoA = 1- octadecanoyl-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77287, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:73990, ChEBI:CHEBI:75590; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77288; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + eicosanoyl-CoA = 1-eicosanoyl- 2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77543, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:73990, ChEBI:CHEBI:197392; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77544; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di- (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:39951, ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73990; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39952; Evidence=; Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1-(9Z,12Z-octadecadienoyl)-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77291, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:73990, ChEBI:CHEBI:75614; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77292; Evidence=; Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2-(9Z-octadecenoyl)- glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-(9Z-octadecenoyl)- glycerol + CoA; Xref=Rhea:RHEA:77547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:73990, ChEBI:CHEBI:75611; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77548; Evidence=; Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32948; Evidence=; Reaction=a 2-acylglycerol + an acyl-CoA = a 2,3-diacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38467, ChEBI:CHEBI:17389, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:75524; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38468; Evidence=; Reaction=a 1-acylglycerol + an acyl-CoA = a 1,2-diacylglycerol + CoA; Xref=Rhea:RHEA:39943, ChEBI:CHEBI:35759, ChEBI:CHEBI:49172, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39944; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-decanoylglycerol = 1-decanoyl-2-(9Z- octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75547, ChEBI:CHEBI:85787; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38020; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-dodecanoylglycerol = 1-dodecanoyl-2- (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38115, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75539, ChEBI:CHEBI:75579; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38116; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoylglycerol = 1- tetradecanoyl-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38119, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75562, ChEBI:CHEBI:75582; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38120; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoylglycerol = 1- hexadecanoyl-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38123, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:69081, ChEBI:CHEBI:75585; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38124; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoylglycerol = 1- octadecanoyl-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38127, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75555, ChEBI:CHEBI:75590; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38128; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di- (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915, ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75342; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z-octadecadienoyl)-glycerol = 1-(9Z,12Z-octadecadienoyl)-2-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75568, ChEBI:CHEBI:75614; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38132; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z-octadecatrienoyl)- glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-2-(9Z-octadecenoyl)- glycerol + CoA; Xref=Rhea:RHEA:38135, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75609, ChEBI:CHEBI:75610; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38136; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)- glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-(9Z-octadecenoyl)- glycerol + CoA; Xref=Rhea:RHEA:38139, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75611, ChEBI:CHEBI:75612; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38140; Evidence=; Reaction=a 1-acylglycerol + an acyl-CoA = a 1,3-diacylglycerol + CoA; Xref=Rhea:RHEA:77571, ChEBI:CHEBI:35759, ChEBI:CHEBI:47777, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77572; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-decanoylglycerol = 1-decanoyl-3-(9Z- octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77615, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75547, ChEBI:CHEBI:197430; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77616; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoylglycerol = 1- tetradecanoyl-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77631, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75562, ChEBI:CHEBI:197427; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77632; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-dodecanoylglycerol = 1-dodecanoyl-3- (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77587, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75539, ChEBI:CHEBI:197406; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77588; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoylglycerol = 1-(9Z- octadecenoyl)-3-hexadecanoylglycerol + CoA; Xref=Rhea:RHEA:77563, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:69081, ChEBI:CHEBI:75869; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77564; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoylglycerol = 1- octadecanoyl-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77583, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75555, ChEBI:CHEBI:197407; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77584; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycerol = 1,3- di-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77267, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75735, ChEBI:CHEBI:75757; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77268; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z-octadecadienoyl)-glycerol = 1-(9Z-octadecenoyl)-3-(9Z,12Z-octadecadienoyl)-glycerol + CoA; Xref=Rhea:RHEA:77591, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75568, ChEBI:CHEBI:133484; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77592; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z-octadecatrienoyl)- glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-3-(9Z-octadecenoyl)- glycerol + CoA; Xref=Rhea:RHEA:77595, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75610, ChEBI:CHEBI:197408; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77596; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)- glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-3-(9Z-octadecenoyl)- glycerol + CoA; Xref=Rhea:RHEA:77635, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75612, ChEBI:CHEBI:197426; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77636; Evidence=; Reaction=1-O-alkylglycerol + an acyl-CoA = 1-O-alkyl-3-acylglycerol + CoA; Xref=Rhea:RHEA:77627, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:76225, ChEBI:CHEBI:77997; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77628; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O- (9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:197429; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341; Evidence=; Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecyl)-3-(9Z- octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z- octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:55344, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:138735, ChEBI:CHEBI:197429; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-octanoylglycerol = 1-octanoyl-3-(9Z- octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:77579, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:85241, ChEBI:CHEBI:197405; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77580; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-O-hexadecylglycerol = 1-O-hexadecyl- 3-(9Z)-octadecenoylglycerol + CoA; Xref=Rhea:RHEA:77575, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:76061, ChEBI:CHEBI:76062; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77576; Evidence=; Inhibited by oleic acid and sphingosine, while it is stimulated by phosphatidylcholine, phosphatidylserine and phosphatidic acid. Kinetic parameters: KM=45 uM for sn-1-monooleoylglycerol ; Glycerolipid metabolism; triacylglycerol biosynthesis. Endoplasmic reticulum membrane ; Multi-pass membrane protein Cytoplasm, perinuclear region Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q3SYC2-1; Sequence=Displayed; Name=2; IsoId=Q3SYC2-2; Sequence=VSP_020358; Name=3; Synonyms=MGAT2V, Trunc; IsoId=Q3SYC2-3; Sequence=VSP_020359, VSP_020360; Highly expressed in liver, small intestine, colon, stomach and kidney. Belongs to the diacylglycerol acyltransferase family. 2-acylglycerol O-acyltransferase activity cytoplasm endoplasmic reticulum endoplasmic reticulum membrane glycerol metabolic process lipid metabolic process diacylglycerol biosynthetic process membrane integral component of membrane acetyltransferase activity transferase activity transferase activity, transferring acyl groups transferase activity, transferring acyl groups other than amino-acyl groups triglyceride biosynthetic process perinuclear region of cytoplasm intestinal absorption perinuclear endoplasmic reticulum membrane uc010rru.1 uc010rru.2 uc010rru.3 uc010rru.4 
ENST00000199280.4 AQP2 ENST00000199280.4 aquaporin 2 (from RefSeq NM_000486.6) AQP2_HUMAN ENST00000199280.1 ENST00000199280.2 ENST00000199280.3 NM_000486 P41181 Q9UD68 uc001rvn.1 uc001rvn.2 uc001rvn.3 uc001rvn.4 uc001rvn.5 This gene encodes a water channel protein located in the kidney collecting tubule. It belongs to the MIP/aquaporin family, some members of which are clustered together on chromosome 12q13. Mutations in this gene have been linked to autosomal dominant and recessive forms of nephrogenic diabetes insipidus. [provided by RefSeq, Oct 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC042496.1, S73196.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient (PubMed:8140421, PubMed:7524315, PubMed:7510718, PubMed:15509592). Plays an essential role in renal water homeostasis (PubMed:8140421, PubMed:7524315, PubMed:15509592). Homotetramer (PubMed:24733887). Interacts with micropeptide MIAC; the interaction leads to a reduction of filamentous actin fibers and inhibition of the EREG/EGFR signaling pathway (PubMed:32176498, PubMed:36117171). P41181; O14735: CDIPT; NbExp=3; IntAct=EBI-12701138, EBI-358858; P41181; O43889-2: CREB3; NbExp=3; IntAct=EBI-12701138, EBI-625022; P41181; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12701138, EBI-6942903; P41181; P52803: EFNA5; NbExp=3; IntAct=EBI-12701138, EBI-1753674; P41181; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12701138, EBI-711490; P41181; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12701138, EBI-781551; P41181; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-12701138, EBI-10976398; P41181; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12701138, EBI-18304435; P41181; Q92520: FAM3C; NbExp=3; IntAct=EBI-12701138, EBI-2876774; P41181; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12701138, EBI-11721746; P41181; P24593: IGFBP5; NbExp=3; IntAct=EBI-12701138, EBI-720480; P41181; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-12701138, EBI-8503746; P41181; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12701138, EBI-17490413; P41181; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12701138, EBI-2820517; P41181; Q6IN84: MRM1; NbExp=3; IntAct=EBI-12701138, EBI-5454865; P41181; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-12701138, EBI-12070086; P41181; P15941-11: MUC1; NbExp=3; IntAct=EBI-12701138, EBI-17263240; P41181; Q8IXM6: NRM; NbExp=3; IntAct=EBI-12701138, EBI-10262547; P41181; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-12701138, EBI-2804156; P41181; Q8NH19: OR10AG1; NbExp=3; IntAct=EBI-12701138, EBI-13339917; P41181; Q96RD7: PANX1; NbExp=3; IntAct=EBI-12701138, EBI-7037612; P41181; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12701138, EBI-716063; P41181; Q01453: PMP22; NbExp=3; IntAct=EBI-12701138, EBI-2845982; P41181; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-12701138, EBI-8652812; P41181; Q59EV6: PPGB; NbExp=3; IntAct=EBI-12701138, EBI-14210385; P41181; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-12701138, EBI-10244780; P41181; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-12701138, EBI-12814225; P41181; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-12701138, EBI-8644112; P41181; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-12701138, EBI-10314552; P41181; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-12701138, EBI-10244848; P41181; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-12701138, EBI-1057733; P41181; A2RU14: TMEM218; NbExp=3; IntAct=EBI-12701138, EBI-10173151; P41181; Q5W0B7: TMEM236; NbExp=3; IntAct=EBI-12701138, EBI-13378608; P41181; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12701138, EBI-2852148; P41181; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-12701138, EBI-12015604; P41181; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12701138, EBI-12111910; P41181; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-12701138, EBI-11988865; P41181; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-12701138, EBI-751210; Apical cell membrane ulti-pass membrane protein Basolateral cell membrane ; Multi-pass membrane protein Cell membrane ulti-pass membrane protein Cytoplasmic vesicle membrane ; Multi-pass membrane protein lgi apparatus, trans-Golgi network membrane ; Multi-pass membrane protein Note=Shuttles from vesicles to the apical membrane (PubMed:15509592). Vasopressin-regulated phosphorylation is required for translocation to the apical cell membrane (PubMed:15509592). PLEKHA8/FAPP2 is required to transport AQP2 from the TGN to sites where AQP2 is phosphorylated (By similarity). Expressed in collecting tubules in kidney medulla (at protein level) (PubMed:7510718). Detected in kidney (PubMed:7510718). Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Ser-256 phosphorylation is necessary and sufficient for expression at the apical membrane. Endocytosis is not phosphorylation-dependent. N-glycosylated. Diabetes insipidus, nephrogenic, 2, autosomal (NDI2) [MIM:125800]: A disorder caused by the inability of the renal collecting ducts to absorb water in response to arginine vasopressin. Characterized by excessive water drinking (polydipsia), excessive urine excretion (polyuria), persistent hypotonic urine, and hypokalemia. Inheritance can be autosomal dominant or recessive. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the MIP/aquaporin (TC 1.A.8) family. renal water homeostasis renal water transport water transmembrane transporter activity protein binding Golgi apparatus plasma membrane integral component of plasma membrane water transport glycerol transmembrane transporter activity water channel activity channel activity glycerol transport membrane integral component of membrane basolateral plasma membrane apical plasma membrane transport vesicle membrane cytoplasmic vesicle membrane cytoplasmic vesicle cellular response to water deprivation protein homotetramerization recycling endosome transmembrane transport extracellular exosome cellular response to copper ion cellular response to mercury ion metanephric collecting duct development lumenal side of membrane uc001rvn.1 uc001rvn.2 uc001rvn.3 uc001rvn.4 uc001rvn.5 
ENST00000199320.9 DIMT1 ENST00000199320.9 DIM1 rRNA methyltransferase and ribosome maturation factor, transcript variant 1 (from RefSeq NM_014473.4) DIM1_HUMAN DIMT1 DIMT1L ENST00000199320.1 ENST00000199320.2 ENST00000199320.3 ENST00000199320.4 ENST00000199320.5 ENST00000199320.6 ENST00000199320.7 ENST00000199320.8 HUSSY-05 NM_014473 O76025 Q9BU77 Q9UES1 Q9UNQ2 uc003jta.1 uc003jta.2 uc003jta.3 uc003jta.4 uc003jta.5 The protein encoded by this gene is a methyltransferase that is responsible for dimethylation of adjacent adenosines near the 18S rRNA decoding site. The encoded protein is essential for ribosome biogenesis, although its catalytic activity is not involved in the process. The yeast ortholog of this protein functions in the cytoplasm while this protein functions in the nucleus. [provided by RefSeq, Jan 2017]. Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle (PubMed:25851604). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity (PubMed:25851604). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). Reaction=adenosine(1779)/adenosine(1780) in 18S rRNA + 4 S-adenosyl-L- methionine = 4 H(+) + N(6)-dimethyladenosine(1779)/N(6)- dimethyladenosine(1780) in 18S rRNA + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42780, Rhea:RHEA-COMP:10234, Rhea:RHEA-COMP:10236, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.183; Evidence=; Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. Nucleus, nucleoplasm Nucleus, nucleolus Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. Sequence=AAC72947.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence=; rRNA modification rRNA (adenine-N6,N6-)-dimethyltransferase activity RNA binding nucleus nucleoplasm nucleolus mitochondrial matrix cytosol rRNA processing methyltransferase activity rRNA methyltransferase activity transferase activity rRNA methylation methylation 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase activity positive regulation of rRNA processing uc003jta.1 uc003jta.2 uc003jta.3 uc003jta.4 uc003jta.5 
ENST00000199389.11 EIF2AK1 ENST00000199389.11 eukaryotic translation initiation factor 2 alpha kinase 1, transcript variant 1 (from RefSeq NM_014413.4) A8K2R2 E2AK1_HUMAN EIF2AK1 ENST00000199389.1 ENST00000199389.10 ENST00000199389.2 ENST00000199389.3 ENST00000199389.4 ENST00000199389.5 ENST00000199389.6 ENST00000199389.7 ENST00000199389.8 ENST00000199389.9 HRI KIAA1369 NM_014413 PRO1362 Q549K6 Q8NBW3 Q9BQI3 Q9HC02 Q9NYE0 Q9P0V6 Q9P1J5 Q9P2H8 Q9UHG4 uc003spp.1 uc003spp.2 uc003spp.3 uc003spp.4 uc003spp.5 The protein encoded by this gene acts at the level of translation initiation to downregulate protein synthesis in response to stress. The encoded protein is a kinase that can be inactivated by hemin. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]. Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions (PubMed:32132706, PubMed:32132707, PubMed:37327776). Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as heme deficiency, oxidative stress, osmotic shock, mitochondrial dysfunction and heat shock (PubMed:32132706, PubMed:32132707, PubMed:37327776). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707, PubMed:37327776). Acts as a key sensor of heme-deficiency: in normal conditions, binds hemin via a cysteine thiolate and histidine nitrogenous coordination, leading to inhibit the protein kinase activity (By similarity). This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell: heme depletion relieves inhibition and stimulates kinase activity, activating the ISR (By similarity). Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions (By similarity). In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties (By similarity). It thereby plays an essential protective role for RBC survival in anemias of iron deficiency (By similarity). Iron deficiency also triggers activation by full-length DELE1 (PubMed:37327776). Also activates the ISR in response to mitochondrial dysfunction: HRI/EIF2AK1 protein kinase activity is activated upon binding to the processed form of DELE1 (S-DELE1), thereby promoting the ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence=; In normal conditions, the protein kinase activity is inhibited; inhibition is relieved by various stress conditions (By similarity). Inhibited by heme: in presence of heme, forms a disulfide- linked inactive homodimer (By similarity). Heme depletion relieves inhibition and stimulates kinase activity by autophosphorylation. Inhibited by the heme metabolites biliverdin and bilirubin (By similarity). Induced by oxidative stress generated by arsenite treatment. Binding of nitric oxide (NO) to the heme iron in the N- terminal heme-binding domain activates the kinase activity, while binding of carbon monoxide (CO) suppresses kinase activity (By similarity). Protein kinase activity is also activated upon binding to DELE1 in response to various stress, triggering the integrated stress response (ISR): activated by full-length DELE1 in response to iron deficiency, while it is activated by the processed form of DELE1 (S- DELE1) in response to mitochondrial stress (PubMed:32132706, PubMed:32132707, PubMed:37327776). Kinetic parameters: KM=3.88 uM for eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) (in absence of DELE1 and in absence of hemin) ; KM=1.13 uM for eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) (in presence of DELE1 and in absence of hemin) ; KM=71.91 uM for eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) (in absence of DELE1 and in presence of hemin) ; KM=6.56 uM for eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) (in presence of DELE1 and in presence of hemin) ; Synthesized in an inactive form that binds to the N-terminal domain of CDC37 (PubMed:11036079). Has to be associated with a multiprotein complex containing Hsp90, CDC37 and PPP5C for maturation and activation by autophosphorylation (PubMed:11036079). The phosphatase PPP5C modulates this activation (PubMed:11036079). Homodimer; homodimerizes in presence of heme, forming a disulfide- linked inactive homodimer (By similarity). Interacts with DELE1; binds both to full-length DELE1 and processed form of DELE1 (S-DELE1) in response to stress, leading to activate its protein kinase activity and trigger the integrated stress response (ISR) (PubMed:32132706, PubMed:32132707, PubMed:37327776). Q9BQI3; P08238: HSP90AB1; NbExp=2; IntAct=EBI-640377, EBI-352572; Q9BQI3; P11142: HSPA8; NbExp=2; IntAct=EBI-640377, EBI-351896; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BQI3-1; Sequence=Displayed; Name=2; IsoId=Q9BQI3-2; Sequence=VSP_007589; Activated by autophosphorylation; phosphorylated predominantly on serine and threonine residues, but also on tyrosine residues. Autophosphorylation at Thr-488 is required for kinase activation. The active autophosphorylated form apparently is largely refractory to cellular heme fluctuations. Leukoencephalopathy, motor delay, spasticity, and dysarthria syndrome (LEMSPAD) [MIM:618878]: A disorder characterized by delayed motor development, speech delay with dysarthria, hypertonia, progressive spasticity, hyperreflexia, and bradykinesia. Cognition is normal. Patients manifest anxiety and attention deficit-hyperactivity disorder. Note=The disease may be caused by variants affecting the gene represented in this entry. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. Was reported to be expressed predominantly in erythroid cells and at much lower levels in hepatocytes. However, this paper has been retracted because there was improper manipulation, reuse and analyses. Sequence=AAF70289.1; Type=Frameshift; Evidence=; Sequence=AAF71057.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAA92607.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleotide binding acute inflammatory response protein kinase activity protein serine/threonine kinase activity eukaryotic translation initiation factor 2alpha kinase activity protein binding ATP binding cytoplasm regulation of translation protein phosphorylation phagocytosis negative regulation of cell proliferation regulation of translational initiation by eIF2 alpha phosphorylation regulation of eIF2 alpha phosphorylation by heme kinase activity phosphorylation transferase activity negative regulation of translation heme binding macrophage differentiation protein homodimerization activity negative regulation of translational initiation by iron protoporphyrinogen IX metabolic process protein autophosphorylation regulation of hemoglobin biosynthetic process negative regulation of hemoglobin biosynthetic process iron ion homeostasis response to iron ion starvation uc003spp.1 uc003spp.2 uc003spp.3 uc003spp.4 uc003spp.5 
ENST00000199447.9 NME8 ENST00000199447.9 NME/NM23 family member 8 (from RefSeq NM_016616.5) ENST00000199447.1 ENST00000199447.2 ENST00000199447.3 ENST00000199447.4 ENST00000199447.5 ENST00000199447.6 ENST00000199447.7 ENST00000199447.8 NM_016616 Q8N427 Q9NZH1 SPTRX2 TXND3_HUMAN TXNDC3 uc003tfn.1 uc003tfn.2 uc003tfn.3 uc003tfn.4 uc003tfn.5 This gene encodes a protein with an N-terminal thioredoxin domain and three C-terminal nucleoside diphosphate kinase (NDK) domains, but the NDK domains are thought to be catalytically inactive. The sea urchin ortholog of this gene encodes a component of sperm outer dynein arms, and the protein is implicated in ciliary function. Mutations in this gene are implicated in primary ciliary dyskinesia type 6.[provided by RefSeq, Nov 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: GQ472221.1, BC036816.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2151119, SAMEA2161674 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000199447.9/ ENSP00000199447.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Probably required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of fibrous sheath (FS) proteins occurs. May be involved in the reduction of disulfide bonds within the sperm FS components. In vitro, it has neither NDP kinase nor reducing activity on disulfide bonds. Monomer. Cytoplasm Testis-specific. Expressed only in primary spermatocytes and round spermatids. Restricted to spermiogenesis, starting at the pachytene spermatocyte level and peaking at the round and elongating spermatid stage. Contains 3 inactive NDK domains that each lack the active His residue, suggesting that they have no NDP kinase activity. Ciliary dyskinesia, primary, 6 (CILD6) [MIM:610852]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. Note=The disease is caused by variants affecting the gene represented in this entry. In the C-terminal section; belongs to the NDK family. cytoplasm multicellular organism development spermatogenesis microtubule binding cell differentiation flagellated sperm motility cellular response to reactive oxygen species outer dynein arm cell redox homeostasis cilium assembly sperm principal piece sperm cytoplasmic droplet uc003tfn.1 uc003tfn.2 uc003tfn.3 uc003tfn.4 uc003tfn.5 
ENST00000199448.9 EPDR1 ENST00000199448.9 ependymin related 1, transcript variant 1 (from RefSeq NM_017549.5) A8K4C0 C9JYS3 ENST00000199448.1 ENST00000199448.2 ENST00000199448.3 ENST00000199448.4 ENST00000199448.5 ENST00000199448.6 ENST00000199448.7 ENST00000199448.8 EPDR1_HUMAN MERP1 NM_017549 Q06BL0 Q99M77 Q9UM22 UCC1 uc003tfp.1 uc003tfp.2 uc003tfp.3 uc003tfp.4 uc003tfp.5 uc003tfp.6 The protein encoded by this gene is a type II transmembrane protein that is similar to two families of cell adhesion molecules, the protocadherins and ependymins. This protein may play a role in calcium-dependent cell adhesion. This protein is glycosylated, and the orthologous mouse protein is localized to the lysosome. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 8. [provided by RefSeq, Aug 2011]. Binds anionic lipids and gangliosides at acidic pH. Homodimer. Q9UM22; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-946972, EBI-10173507; Q9UM22; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-946972, EBI-744366; Q9UM22; P49639: HOXA1; NbExp=3; IntAct=EBI-946972, EBI-740785; Q9UM22; P24592: IGFBP6; NbExp=3; IntAct=EBI-946972, EBI-947015; Q9UM22; Q15323: KRT31; NbExp=3; IntAct=EBI-946972, EBI-948001; Q9UM22; O76011: KRT34; NbExp=3; IntAct=EBI-946972, EBI-1047093; Q9UM22; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-946972, EBI-10171774; Q9UM22; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-946972, EBI-11953846; Q9UM22; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-946972, EBI-10302392; Q9UM22; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-946972, EBI-11339910; Q9UM22; Q63HR2: TNS2; NbExp=3; IntAct=EBI-946972, EBI-949753; Q9UM22; Q15654: TRIP6; NbExp=3; IntAct=EBI-946972, EBI-742327; Lysosome lumen Secreted Note=Lysosomal and also secreted. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9UM22-1; Sequence=Displayed; Name=2; IsoId=Q9UM22-2; Sequence=VSP_031976; Name=3; IsoId=Q9UM22-3; Sequence=VSP_046829; Ubiquitous. Detected in brain, heart, skeletal muscle, kidney, testis, ovary and prostate. N-glycosylated; the glycan contains mannose-6-phosphate moieties. Belongs to the ependymin family. Sequence=AAH00686.2; Type=Erroneous initiation; Evidence=; Sequence=CAB60269.1; Type=Erroneous initiation; Evidence=; calcium ion binding extracellular region lysosome cell-matrix adhesion lipid binding lysosomal lumen uc003tfp.1 uc003tfp.2 uc003tfp.3 uc003tfp.4 uc003tfp.5 uc003tfp.6 
ENST00000199706.13 MRPL28 ENST00000199706.13 mitochondrial ribosomal protein L28 (from RefSeq NM_006428.5) B2RCM4 D3DU46 ENST00000199706.1 ENST00000199706.10 ENST00000199706.11 ENST00000199706.12 ENST00000199706.2 ENST00000199706.3 ENST00000199706.4 ENST00000199706.5 ENST00000199706.6 ENST00000199706.7 ENST00000199706.8 ENST00000199706.9 MAAT1 NM_006428 Q13084 Q4TT39 Q96S26 Q9BQD8 Q9BR04 RM28_HUMAN uc002cgs.1 uc002cgs.2 uc002cgs.3 uc002cgs.4 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein, a part of which was originally isolated by its ability to recognize tyrosinase in an HLA-A24-restricted fashion. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7410570.571234.1, SRR1660803.318866.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2153307, SAMEA2158188 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000199706.13/ ENSP00000199706.7 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the mitochondrial large ribosomal subunit (mt- LSU) (PubMed:28892042, PubMed:25278503, PubMed:11551941). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins (PubMed:11551941, PubMed:25278503). Interacts with OXA1L. Q13084; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-723426, EBI-11096309; Q13084; Q8N9N5: BANP; NbExp=3; IntAct=EBI-723426, EBI-744695; Q13084; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-723426, EBI-5278764; Q13084; Q01850: CDR2; NbExp=3; IntAct=EBI-723426, EBI-1181367; Q13084; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-723426, EBI-744099; Q13084; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-723426, EBI-10175124; Q13084; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-723426, EBI-2549423; Q13084; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-723426, EBI-747204; Q13084; Q659C4-6: LARP1B; NbExp=3; IntAct=EBI-723426, EBI-12036449; Q13084; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-723426, EBI-726510; Q13084; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-723426, EBI-10271199; Q13084; O60437: PPL; NbExp=3; IntAct=EBI-723426, EBI-368321; Q13084; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-723426, EBI-748391; Q13084; Q10587: TEF; NbExp=3; IntAct=EBI-723426, EBI-2796967; Q13084; O43734: TRAF3IP2; NbExp=3; IntAct=EBI-723426, EBI-744798; Q13084; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-723426, EBI-3650647; Q13084; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-723426, EBI-9053916; Q13084; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-723426, EBI-3918381; Q13084; O95045-2: UPP2; NbExp=3; IntAct=EBI-723426, EBI-11528386; Q13084; O75604: USP2; NbExp=3; IntAct=EBI-723426, EBI-743272; Q13084; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-723426, EBI-14096082; Q13084; Q8N720: ZNF655; NbExp=3; IntAct=EBI-723426, EBI-625509; Mitochondrion Found in a variety of normal tissues including spleen, testes, thymus, liver, kidney, brain, adrenal, lung and retinal tissue. Potentially represents an important therapeutic reagent for HLA-A24 patients. This antigen is recognized by tumor-infiltrating lymphocyte (TIL) 1290 in the context of HLA-A24. Belongs to the bacterial ribosomal protein bL28 family. Sequence=AAC50181.1; Type=Erroneous initiation; Evidence=; Sequence=AAK61226.1; Type=Erroneous gene model prediction; Evidence=; RNA binding structural constituent of ribosome protein binding mitochondrion mitochondrial inner membrane mitochondrial ribosome mitochondrial large ribosomal subunit cytosol ribosome translation mitochondrial translational elongation mitochondrial translational termination uc002cgs.1 uc002cgs.2 uc002cgs.3 uc002cgs.4 
ENST00000199708.3 HBQ1 ENST00000199708.3 hemoglobin subunit theta 1 (from RefSeq NM_005331.5) ENST00000199708.1 ENST00000199708.2 HBAT_HUMAN NM_005331 P09105 Q13723 Q1W6G5 uc002cfz.1 uc002cfz.2 uc002cfz.3 uc002cfz.4 uc002cfz.5 Theta-globin mRNA is found in human fetal erythroid tissue but not in adult erythroid or other nonerythroid tissue. The theta-1 gene may be expressed very early in embryonic life, perhaps sometime before 5 weeks. Theta-1 is a member of the human alpha-globin gene cluster that involves five functional genes and two pseudogenes. The order of genes is: 5' - zeta - pseudozeta - mu - pseudoalpha-2 -pseudoalpha-1 - alpha-2 - alpha-1 - theta-1 - 3'. Research supports a transcriptionally active role for the gene and a functional role for the peptide in specific cells, possibly those of early erythroid tissue. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC056686.1, CD580449.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145743, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000199708.3/ ENSP00000199708.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## P09105; O43865: AHCYL1; NbExp=6; IntAct=EBI-10193656, EBI-2371423; P09105; P69905: HBA2; NbExp=3; IntAct=EBI-10193656, EBI-714680; P09105; P68871: HBB; NbExp=3; IntAct=EBI-10193656, EBI-715554; P09105; P02042: HBD; NbExp=6; IntAct=EBI-10193656, EBI-6152722; P09105; P02100: HBE1; NbExp=3; IntAct=EBI-10193656, EBI-6190240; P09105; P69892: HBG2; NbExp=3; IntAct=EBI-10193656, EBI-3910089; P09105; P02008: HBZ; NbExp=3; IntAct=EBI-10193656, EBI-719843; P09105; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10193656, EBI-741158; P09105; Q8TAC1: RFESD; NbExp=9; IntAct=EBI-10193656, EBI-10271664; Belongs to the globin family. oxygen transporter activity iron ion binding protein binding hemoglobin complex oxygen transport oxygen binding heme binding haptoglobin-hemoglobin complex hydrogen peroxide catabolic process organic acid binding metal ion binding cellular oxidant detoxification peroxidase activity haptoglobin binding uc002cfz.1 uc002cfz.2 uc002cfz.3 uc002cfz.4 uc002cfz.5 
ENST00000199764.7 CEACAM6 ENST00000199764.7 CEA cell adhesion molecule 6 (from RefSeq NM_002483.7) CEAM6_HUMAN ENST00000199764.1 ENST00000199764.2 ENST00000199764.3 ENST00000199764.4 ENST00000199764.5 ENST00000199764.6 NCA NM_002483 P40199 Q13774 Q14920 Q53XP7 uc032hyc.1 uc032hyc.2 uc032hyc.3 This gene encodes a protein that belongs to the carcinoembryonic antigen (CEA) family whose members are glycosyl phosphatidyl inositol (GPI) anchored cell surface glycoproteins. Members of this family play a role in cell adhesion and are widely used as tumor markers in serum immunoassay determinations of carcinoma. This gene affects the sensitivity of tumor cells to adenovirus infection. The protein encoded by this gene acts as a receptor for adherent-invasive E. coli adhesion to the surface of ileal epithelial cells in patients with Crohn's disease. This gene is clustered with genes and pseudogenes of the cell adhesion molecules subgroup of the CEA family on chromosome 19. [provided by RefSeq, Apr 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M18728.1, M18216.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000199764.7/ ENSP00000199764.6 RefSeq Select criteria :: based on expression, longest protein ##RefSeq-Attributes-END## Cell surface glycoprotein that plays a role in cell adhesion and tumor progression (PubMed:2803308, PubMed:2022629, PubMed:1378450, PubMed:8776764, PubMed:11590190, PubMed:10910050, PubMed:14724575, PubMed:16204051). Intercellular adhesion occurs in a calcium- and fibronectin-independent manner (PubMed:2022629, PubMed:16204051). Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM5 and CEACAM8 (PubMed:2803308, PubMed:2022629, PubMed:8776764, PubMed:11590190, PubMed:16204051). Heterophilic interaction with CEACAM8 occurs in activated neutrophils (PubMed:8776764). Plays a role in neutrophil adhesion to cytokine-activated endothelial cells (PubMed:1378450). Plays a role as an oncogene by promoting tumor progression; positively regulates cell migration, cell adhesion to endothelial cells and cell invasion (PubMed:16204051). Also involved in the metastatic cascade process by inducing gain resistance to anoikis of pancreatic adenocarcinoma and colorectal carcinoma cells (PubMed:10910050, PubMed:14724575). Homodimer; homodimerizes via its Ig-like V-type domain. Heterodimer with CEACAM8; heterodimerizes via its Ig-like V-type domain. P40199; Q86U10: ASPG; NbExp=3; IntAct=EBI-4314501, EBI-19946665; P40199; Q16568: CARTPT; NbExp=3; IntAct=EBI-4314501, EBI-4314526; P40199; P13688: CEACAM1; NbExp=2; IntAct=EBI-4314501, EBI-4314481; P40199; P40199: CEACAM6; NbExp=6; IntAct=EBI-4314501, EBI-4314501; P40199; P31997: CEACAM8; NbExp=5; IntAct=EBI-4314501, EBI-4314540; P40199; Q99828: CIB1; NbExp=3; IntAct=EBI-4314501, EBI-372594; P40199; P33240: CSTF2; NbExp=3; IntAct=EBI-4314501, EBI-711360; P40199; Q86VI1: EXOC3L1; NbExp=3; IntAct=EBI-4314501, EBI-2813180; P40199; O75593: FOXH1; NbExp=3; IntAct=EBI-4314501, EBI-1759806; P40199; O75603: GCM2; NbExp=3; IntAct=EBI-4314501, EBI-10188645; P40199; O95872: GPANK1; NbExp=3; IntAct=EBI-4314501, EBI-751540; P40199; O14964: HGS; NbExp=3; IntAct=EBI-4314501, EBI-740220; P40199; Q9UM19: HPCAL4; NbExp=3; IntAct=EBI-4314501, EBI-744820; P40199; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-4314501, EBI-2556193; P40199; Q4VC12: MSS51; NbExp=5; IntAct=EBI-4314501, EBI-11599933; P40199; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-4314501, EBI-744402; P40199; P78337: PITX1; NbExp=3; IntAct=EBI-4314501, EBI-748265; P40199; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-4314501, EBI-11956563; P40199; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-4314501, EBI-2798044; P40199; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-4314501, EBI-372094; P40199; Q92529: SHC3; NbExp=3; IntAct=EBI-4314501, EBI-79084; P40199; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-4314501, EBI-358489; P40199; O43711: TLX3; NbExp=3; IntAct=EBI-4314501, EBI-3939165; P40199; P22105-1: TNXB; NbExp=3; IntAct=EBI-4314501, EBI-20753895; P40199; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-4314501, EBI-947187; P40199; O95231: VENTX; NbExp=3; IntAct=EBI-4314501, EBI-10191303; P40199; Q14119: VEZF1; NbExp=3; IntAct=EBI-4314501, EBI-11980193; P40199; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-4314501, EBI-12040603; P40199; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-4314501, EBI-746595; P40199; P36508: ZNF76; NbExp=3; IntAct=EBI-4314501, EBI-7254550; Cell membrane; Lipid-anchor, GPI-anchor Apical cell membrane Cell surface te=Localized to the apical glycocalyx surface. Expressed in neutrophils (PubMed:1378450). Expressed in columnar epithelial and goblet cells of the colon (PubMed:10436421). Expressed in numerous tumor cell lines (at protein level) (PubMed:16204051). Up-regulated in anoikis-resistant pancreatic adenocarcinoma cells (at protein level). The extracellular N-terminus Ig-like V-type domain is necessary for homophilic and heterophilic intercellular adhesion. Glycosylated. Belongs to the immunoglobulin superfamily. CEA family. protein binding extracellular space plasma membrane apoptotic process cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules signal transduction positive regulation of cell proliferation cell surface membrane apical plasma membrane positive regulation of cell migration anchored component of membrane positive regulation of heterotypic cell-cell adhesion azurophil granule membrane identical protein binding neutrophil degranulation protein heterodimerization activity leukocyte migration positive regulation of endothelial cell-matrix adhesion via fibronectin negative regulation of anoikis uc032hyc.1 uc032hyc.2 uc032hyc.3 
ENST00000199814.9 RBM22 ENST00000199814.9 RNA binding motif protein 22 (from RefSeq NM_018047.3) 199G4 A6NDM5 B4DLI9 ENST00000199814.1 ENST00000199814.2 ENST00000199814.3 ENST00000199814.4 ENST00000199814.5 ENST00000199814.6 ENST00000199814.7 ENST00000199814.8 NM_018047 O95607 Q9NW64 RBM22_HUMAN ZC3H16 uc003lst.1 uc003lst.2 uc003lst.3 uc003lst.4 uc003lst.5 This gene encodes an RNA binding protein. The encoded protein may play a role in cell division and may be involved in pre-mRNA splicing. Related pseudogenes exist on chromosomes 6, 7, 9, 13, 16, 18, and X. [provided by RefSeq, Mar 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK001152.1, SRR3476690.115598.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000199814.9/ ENSP00000199814.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:28502770, PubMed:28076346, PubMed:29361316, PubMed:29360106, PubMed:29301961, PubMed:30705154). Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem- loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses. Component of the pre-catalytic and catalytic spliceosome complexes (PubMed:11991638, PubMed:28502770, PubMed:28076346, PubMed:29361316, PubMed:29360106, PubMed:29301961). Component of the postcatalytic spliceosome P complex (PubMed:30705154). Interacts with PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm. Interacts with PPIL1 (PubMed:33220177). Q9NW64; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-2602260, EBI-747776; Q9NW64; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2602260, EBI-3867333; Q9NW64; O75420: GIGYF1; NbExp=3; IntAct=EBI-2602260, EBI-947774; Q9NW64; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2602260, EBI-618309; Q9NW64; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-2602260, EBI-748420; Q9NW64; Q9NZQ3-3: NCKIPSD; NbExp=5; IntAct=EBI-2602260, EBI-10963850; Nucleus toplasm Note=Nearly exclusively nuclear. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NW64-1; Sequence=Displayed; Name=2; IsoId=Q9NW64-2; Sequence=VSP_036832; The C-terminal RRM domain and the zinc finger motif are necessary for RNA-binding. Belongs to the SLT11 family. Sequence=AAC99998.1; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence=; mRNA splicing, via spliceosome Prp19 complex nucleic acid binding RNA binding protein binding nucleus nucleoplasm spliceosomal complex cytoplasm mRNA processing RNA splicing U6 snRNA binding positive regulation of RNA splicing cellular response to drug pre-mRNA binding positive regulation of protein import into nucleus mRNA cis splicing, via spliceosome positive regulation of protein export from nucleus metal ion binding calcium-dependent protein binding U2-type catalytic step 1 spliceosome U2-type catalytic step 2 spliceosome catalytic step 2 spliceosome uc003lst.1 uc003lst.2 uc003lst.3 uc003lst.4 uc003lst.5 
ENST00000199936.9 HSD17B2 ENST00000199936.9 hydroxysteroid 17-beta dehydrogenase 2 (from RefSeq NM_002153.3) B2R7T4 DHB2_HUMAN EDH17B2 ENST00000199936.1 ENST00000199936.2 ENST00000199936.3 ENST00000199936.4 ENST00000199936.5 ENST00000199936.6 ENST00000199936.7 ENST00000199936.8 HSD17B2 NM_002153 P37059 SDR9C2 uc002fgv.1 uc002fgv.2 uc002fgv.3 uc002fgv.4 uc002fgv.5 Catalyzes the NAD-dependent oxidation of the highly active 17beta-hydroxysteroids, such as estradiol (E2), testosterone (T), and dihydrotestosterone (DHT), to their less active forms and thus regulates the biological potency of these steroids. Oxidizes estradiol to estrone, testosterone to androstenedione, and dihydrotestosterone to 5alpha-androstan-3,17-dione. Also has 20-alpha-HSD activity. Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613; Evidence=; Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.239; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930; Evidence=; Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha- androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Reaction=(20S)-hydroxypregn-4-en-3-one + NAD(+) = H(+) + NADH + progesterone; Xref=Rhea:RHEA:42108, ChEBI:CHEBI:15378, ChEBI:CHEBI:17026, ChEBI:CHEBI:28453, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= Kinetic parameters: KM=0.21 uM for estradiol ; KM=0.39 uM for testosterone ; KM=0.31 uM for dihydrotestosterone ; KM=0.71 uM for 20-alpha-dihydroprogesterone ; KM=2.63 uM for androstenedione ; KM=0.78 uM for estrone ; KM=110 uM for NAD ; KM=9600 uM for NADP ; KM=0.35 uM for estradiol ; KM=0.61 uM for testosterone ; KM=0.25 uM for dihydrotestosterone ; KM=0.53 uM for 20-alpha-dihydroprogesterone ; Vmax=38 nmol/min/mg enzyme with estradiol as substrate ; Vmax=45 nmol/min/mg enzyme with testosterone as substrate ; Vmax=38 nmol/min/mg enzyme with dihydrotestosterone as substrate ; Vmax=5.6 nmol/min/mg enzyme with 20-alpha-dihydroprogesterone as substrate ; Vmax=6.6 nmol/min/mg enzyme with estrone as substrate ; Vmax=11.5 nmol/min/mg enzyme with androstenedione as substrate ; pH dependence: Optimum pH is 9 with testosterone and estradiol as substrates and 5.5 with androstenedione and estrone as substrates. ; Homodimer. Endoplasmic reticulum membrane ; Single-pass type II membrane protein Expressed in placenta. Belongs to the short-chain dehydrogenases/reductases (SDR) family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/hsd17b2/"; in utero embryonic development placenta development estradiol 17-beta-dehydrogenase activity endoplasmic reticulum membrane lipid metabolic process steroid biosynthetic process estrogen biosynthetic process membrane integral component of membrane oxidoreductase activity response to retinoic acid 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity testosterone dehydrogenase (NAD+) activity oxidation-reduction process uc002fgv.1 uc002fgv.2 uc002fgv.3 uc002fgv.4 uc002fgv.5 
ENST00000200135.8 ZW10 ENST00000200135.8 zw10 kinetochore protein (from RefSeq NM_004724.4) A1A528 ENST00000200135.1 ENST00000200135.2 ENST00000200135.3 ENST00000200135.4 ENST00000200135.5 ENST00000200135.6 ENST00000200135.7 NM_004724 O43264 ZW10_HUMAN uc001poe.1 uc001poe.2 uc001poe.3 uc001poe.4 uc001poe.5 This gene encodes a protein that is one of many involved in mechanisms to ensure proper chromosome segregation during cell division. This protein is an essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. [provided by RefSeq, Aug 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U54996.1, SRR1660809.133900.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000200135.8/ ENSP00000200135.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:11590237, PubMed:15485811, PubMed:15824131). Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:15029241). Interacts with NBAS and KNTC1/ROD; the interactions are mutually exclusive and indicative for its association in two different vesicle tethering complexes (PubMed:11590237, PubMed:15824131, PubMed:20462495). Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH (PubMed:12686595, PubMed:20462495). Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L; NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the assembly has been described as syntaxin 18 complex). Interacts directly with RINT1/TIP20L bound to BNIP1/SEC20L (PubMed:15029241, PubMed:15272311, PubMed:20462495, PubMed:19369418). Interacts with C19orf25 and ZWINT (PubMed:15485811, PubMed:15824131, PubMed:16732327). Interacts with ZFYVE1 (PubMed:30970241). Interacts with RAB18 and this interaction is enhanced in the presence of ZFYVE1 (PubMed:30970241). O43264; Q6NUQ1: RINT1; NbExp=16; IntAct=EBI-1001217, EBI-726876; O43264; O95229: ZWINT; NbExp=6; IntAct=EBI-1001217, EBI-1001132; Cytoplasm Endoplasmic reticulum membrane ; Peripheral membrane protein Chromosome, centromere, kinetochore toplasm, cytoskeleton, spindle Lipid droplet Note=Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely in the cytoplasm (PubMed:15029241). In prometaphase, associated with the kinetochore. At metaphase, detected both at the kinetochores and, most prominently, at the spindle, particularly at the spindle poles. In very early anaphase, detected on segregating kinetochores. In late anaphase and telophase, accumulates at the spindle midzone (PubMed:11590237). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43264-1; Sequence=Displayed; Name=2; IsoId=O43264-2; Sequence=VSP_056006; Widely expressed. No significant variation in expression during cell cycle. Overexpression as well as silencing of ZW10 disrupts the morphology of the ER-Golgi intermediate compartment as well as the Golgi apparatus and slows down ER-Golgi transport. Belongs to the ZW10 family. mitotic sister chromatid segregation establishment of mitotic spindle orientation mitotic cell cycle chromosome, centromeric region kinetochore condensed chromosome kinetochore spindle pole protein binding nucleus chromosome cytoplasm endoplasmic reticulum endoplasmic reticulum membrane spindle kinetochore microtubule cytosol cytoskeleton ER to Golgi vesicle-mediated transport retrograde vesicle-mediated transport, Golgi to ER Golgi organization cell cycle mitotic metaphase plate congression mitotic cell cycle checkpoint mitotic spindle assembly checkpoint regulation of exit from mitosis protein transport membrane vesicle-mediated transport centromeric DNA binding protein localization to kinetochore cell division meiotic cell cycle macromolecular complex assembly Dsl1/NZR complex RZZ complex uc001poe.1 uc001poe.2 uc001poe.3 uc001poe.4 uc001poe.5 
ENST00000200181.8 ITGB4 ENST00000200181.8 integrin subunit beta 4, transcript variant 1 (from RefSeq NM_000213.5) A0AVL6 ENST00000200181.1 ENST00000200181.2 ENST00000200181.3 ENST00000200181.4 ENST00000200181.5 ENST00000200181.6 ENST00000200181.7 ITB4_HUMAN NM_000213 O14690 O14691 O15339 O15340 O15341 P16144 Q0VF97 Q9UIQ4 uc002jpg.1 uc002jpg.2 uc002jpg.3 uc002jpg.4 Integrins are heterodimers comprised of alpha and beta subunits, that are noncovalently associated transmembrane glycoprotein receptors. Different combinations of alpha and beta polypeptides form complexes that vary in their ligand-binding specificities. Integrins mediate cell-matrix or cell-cell adhesion, and transduced signals that regulate gene expression and cell growth. This gene encodes the integrin beta 4 subunit, a receptor for the laminins. This subunit tends to associate with alpha 6 subunit and is likely to play a pivotal role in the biology of invasive carcinoma. Mutations in this gene are associated with epidermolysis bullosa with pyloric atresia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). Heterodimer of an alpha and a beta subunit. Beta-4 associates with alpha-6. Interacts (via cytoplasmic region) with COL17A1 (via cytoplasmic region). Interacts (via cytoplasmic region) with DST isoform 3 (via N-terminus). Isoform beta-4a interacts (via cytoplasmic domain) with DST (via N-terminus). Interacts with RAC1. ITGA6:ITGB4 is found in a ternary complex with NRG1 and ERBB3 (PubMed:20682778). ITGA6:ITGB4 is found in a ternary complex with IGF1 and IGF1R (PubMed:22351760). ITGA6:ITGB4 interacts with IGF2 (PubMed:28873464). P16144; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-948678, EBI-2875665; P16144; P23229: ITGA6; NbExp=5; IntAct=EBI-948678, EBI-2436548; P16144; Q15149: PLEC; NbExp=7; IntAct=EBI-948678, EBI-297903; P16144; Q05397: PTK2; NbExp=7; IntAct=EBI-948678, EBI-702142; P16144; O95136: S1PR2; NbExp=2; IntAct=EBI-948678, EBI-10634606; P16144; Q99500: S1PR3; NbExp=3; IntAct=EBI-948678, EBI-10634734; P16144; Q8R5M8-2: Cadm1; Xeno; NbExp=3; IntAct=EBI-948678, EBI-5651941; P16144; Q9QXS1-3: Plec; Xeno; NbExp=4; IntAct=EBI-948678, EBI-16145475; P16144-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-11051601, EBI-10173507; P16144-2; Q92624: APPBP2; NbExp=3; IntAct=EBI-11051601, EBI-743771; P16144-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11051601, EBI-3867333; P16144-2; Q16610: ECM1; NbExp=3; IntAct=EBI-11051601, EBI-947964; P16144-2; P49639: HOXA1; NbExp=3; IntAct=EBI-11051601, EBI-740785; P16144-2; Q5T749: KPRP; NbExp=3; IntAct=EBI-11051601, EBI-10981970; P16144-2; Q15323: KRT31; NbExp=3; IntAct=EBI-11051601, EBI-948001; P16144-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-11051601, EBI-10171697; P16144-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11051601, EBI-11959885; P16144-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-11051601, EBI-11749135; P16144-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-11051601, EBI-10172290; P16144-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11051601, EBI-10171774; P16144-2; P60411: KRTAP10-9; NbExp=5; IntAct=EBI-11051601, EBI-10172052; P16144-2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11051601, EBI-11953334; P16144-2; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-11051601, EBI-11992140; P16144-2; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-11051601, EBI-11988175; P16144-2; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-11051601, EBI-14065470; P16144-2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-11051601, EBI-9996449; P16144-2; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-11051601, EBI-10172511; P16144-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11051601, EBI-11962084; P16144-2; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-11051601, EBI-1044640; P16144-2; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-11051601, EBI-1043191; P16144-2; Q99750: MDFI; NbExp=3; IntAct=EBI-11051601, EBI-724076; P16144-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-11051601, EBI-10172526; P16144-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11051601, EBI-11522433; P16144-2; P13349: MYF5; NbExp=3; IntAct=EBI-11051601, EBI-17491620; P16144-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11051601, EBI-22310682; P16144-2; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-11051601, EBI-769257; P16144-2; Q16633: POU2AF1; NbExp=3; IntAct=EBI-11051601, EBI-943588; P16144-2; P22735: TGM1; NbExp=3; IntAct=EBI-11051601, EBI-2562368; P16144-2; Q15654: TRIP6; NbExp=3; IntAct=EBI-11051601, EBI-742327; Cell membrane; Single-pass type I membrane protein. Cell membrane; Lipid-anchor. Cell junction, hemidesmosome. Note=Colocalizes with DST at the leading edge of migrating keratinocytes. Event=Alternative splicing; Named isoforms=5; Name=Beta-4C; IsoId=P16144-1; Sequence=Displayed; Name=Beta-4A; IsoId=P16144-2; Sequence=VSP_002749; Name=Beta-4B; IsoId=P16144-3; Sequence=VSP_002749, VSP_002750; Name=Beta-4D; IsoId=P16144-4; Sequence=VSP_002749, VSP_002751; Name=Beta-4E; IsoId=P16144-5; Sequence=VSP_002747, VSP_002748; Integrin alpha-6/beta-4 is predominantly expressed by epithelia. Isoform beta-4D is also expressed in colon and placenta. Isoform beta-4E is also expressed in epidermis, lung, duodenum, heart, spleen and stomach. The VWFA domain (or beta I domain) contains three cation- binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent MIDAS site (ADMIDAS). This domain is also part of the ligand-binding site. The fibronectin type-III-like domains bind BPAG1 and plectin and probably also recruit BP230. Palmitoylated by DHHC3 at several cysteines of the membrane- proximal region, enhancing stability and cell surface expression. Palmitoylation also promotes secondary association with tertaspanins. Epidermolysis bullosa, junctional 5A, intermediate (JEB5A) [MIM:619816]: A form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB5A is an autosomal recessive, intermediate form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. In intermediate forms of junctional epidermolysis bullosa, blistering does not lead to the formation of chronic granulation tissue and does not affect the lifespan of affected individuals. Nail dystrophy and dental enamel defects are present. Scarring or non-scarring alopecia and diffuse hair loss may occur. te=The disease is caused by variants affecting the gene represented in this entry. Epidermolysis bullosa, junctional 5B, with pyloric atresia (JEB5B) [MIM:226730]: A form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. Junctional epidermolysis bullosa is characterized by blistering that occurs at the level of the lamina lucida in the skin basement membrane. JEB5B is an autosomal recessive, severe, frequently lethal form with variable involvement of skin, nails, mucosa, and with variable effects on the digestive system. It is characterized by mucocutaneous fragility, aplasia cutis congenita, and gastrointestinal atresia, which most commonly affects the pylorus. Pyloric atresia is a primary manifestation rather than a scarring process secondary to epidermolysis bullosa. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the integrin beta chain family. Sequence=CAA37656.1; Type=Frameshift; Evidence=; G-protein coupled receptor binding integrin binding protein binding plasma membrane autophagy cell communication cell adhesion cell-matrix adhesion integrin-mediated signaling pathway integrin complex response to wounding cell surface membrane integral component of membrane cell migration cell junction hemidesmosome extracellular matrix organization cell leading edge hemidesmosome assembly cell adhesion mediated by integrin nail development receptor complex skin development mesodermal cell differentiation digestive tract development cell motility extracellular exosome renal system development amelogenesis insulin-like growth factor I binding neuregulin binding uc002jpg.1 uc002jpg.2 uc002jpg.3 uc002jpg.4 
ENST00000200453.6 PPP1R15A ENST00000200453.6 protein phosphatase 1 regulatory subunit 15A (from RefSeq NM_014330.5) B4DKQ3 ENST00000200453.1 ENST00000200453.2 ENST00000200453.3 ENST00000200453.4 ENST00000200453.5 GADD34 NM_014330 O75807 PR15A_HUMAN Q6IA96 Q9NVU6 uc002pky.1 uc002pky.2 uc002pky.3 uc002pky.4 uc002pky.5 uc002pky.6 This gene is a member of a group of genes whose transcript levels are increased following stressful growth arrest conditions and treatment with DNA-damaging agents. The induction of this gene by ionizing radiation occurs in certain cell lines regardless of p53 status, and its protein response is correlated with apoptosis following ionizing radiation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK225632.1, SRR1803612.227044.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript regulatory uORF :: PMID: 19131336 ##RefSeq-Attributes-END## Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress (PubMed:26742780, PubMed:26095357). Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1 (PubMed:14718519). May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15' (PubMed:14635196). Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux (PubMed:32978159). Acts also a viral restriction factor by attenuating HIV-1 replication (PubMed:31778897). Mechanistically, mediates the inhibition of HIV-1 TAR RNA-mediated translation (PubMed:31778897). (Microbial infection) Promotes enterovirus 71 replication by mediating the internal ribosome entry site (IRES) activity of viral 5'- UTR. Interacts with PPP1CA (PubMed:15705855, PubMed:26095357). Interacts with EIF2S1 (PubMed:26095357). Interacts with PCNA (By similarity). Interacts with LYN and KMT2A/MLL1 (PubMed:11517336). Interacts with PPP1R1A and SMARCB1 (PubMed:12016208). Interacts with SMAD7 (PubMed:14718519). Interacts with BAG1 (PubMed:12724406). Interacts with NOX4 (PubMed:26742780). (Microbial infection) Interacts with enterovirus 71/EV71 non- structural protein precursor 3CD; this interaction promotes EV71 replication. O75807; P56545: CTBP2; NbExp=2; IntAct=EBI-714746, EBI-741533; O75807; P62136: PPP1CA; NbExp=12; IntAct=EBI-714746, EBI-357253; O75807; Q13522: PPP1R1A; NbExp=4; IntAct=EBI-714746, EBI-1568511; O75807; Q13148: TARDBP; NbExp=10; IntAct=EBI-714746, EBI-372899; Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Note=Associates with membranes via an N-terminal amphipathic intramembrane region. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75807-1; Sequence=Displayed; Name=2; IsoId=O75807-2; Sequence=VSP_057083, VSP_057084; Specifically produced in response to stress: in absence of stress, some upstream open reading frame (uORF) of this transcript is translated, thereby preventing its translation (PubMed:19131336). By methyl methanesulfonate and ionizing irradiation (PubMed:9153226). By IL24/interleukin-24 in melanoma cells; which induces apoptosis (PubMed:10490642, PubMed:12114539). By viral infection including enterovirus 71/EV71 or HIV-1 (PubMed:34985336, PubMed:31778897). Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-262 enhances proteasomal degradation, this position is dephosphorylated by PTPN2. Polyubiquitinated. Exhibits a rapid proteasomal degradation with a half-life under 1 hour, ubiquitination depends on endoplasmic reticulum association. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress. Belongs to the PPP1R15 family. protein phosphatase type 1 complex protein binding cytoplasm mitochondrion mitochondrial outer membrane endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus cytosol regulation of translation apoptotic process cellular response to DNA damage stimulus cell cycle arrest protein phosphatase 1 binding membrane protein phosphatase regulator activity protein kinase binding positive regulation of translational initiation in response to stress negative regulation of phosphoprotein phosphatase activity positive regulation of phosphoprotein phosphatase activity response to endoplasmic reticulum stress negative regulation of protein dephosphorylation regulation of translational initiation by eIF2 alpha dephosphorylation intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress protein localization to endoplasmic reticulum protein phosphatase activator activity positive regulation of peptidyl-serine dephosphorylation negative regulation of PERK-mediated unfolded protein response positive regulation of endoplasmic reticulum stress-induced eIF2 alpha dephosphorylation uc002pky.1 uc002pky.2 uc002pky.3 uc002pky.4 uc002pky.5 uc002pky.6 
ENST00000200457.9 TRIP6 ENST00000200457.9 thyroid hormone receptor interactor 6 (from RefSeq NM_003302.3) A4D2E7 ENST00000200457.1 ENST00000200457.2 ENST00000200457.3 ENST00000200457.4 ENST00000200457.5 ENST00000200457.6 ENST00000200457.7 ENST00000200457.8 F2ZC07 F2ZC08 NM_003302 O15170 O15275 OIP1 Q15654 Q9BTB2 Q9BUE5 Q9BXP3 Q9UNT4 TRIP6_HUMAN uc003uww.1 uc003uww.2 uc003uww.3 uc003uww.4 uc003uww.5 This gene is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.193113.1, SRR3476690.676481.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000200457.9/ ENSP00000200457.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF- kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor. Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone (PubMed:14688263). Interacts (via the third LIM domain and C-terminus) with PTPN13 (via the second PDZ domain) (PubMed:10400701, PubMed:17591779, PubMed:19017743, PubMed:10826496). Interacts (via the second LIM domain or via the third LIM domain plus C-terminus) with PDLIM4 (via PDZ domain) (PubMed:10826496). Found in a complex with PTPN13 and PDLIM4 (By similarity). Interacts with SVIL isoform 2 (PubMed:16880273). Interacts with LPAR2 but not other LPA receptors (PubMed:14688263). Interacts with PRKAA2 (PubMed:16624523). Interacts with MAGI1 (PubMed:19017743). Interacts with SCRIB (PubMed:16137684). In case of infection, interacts with S.typhimurium protein sseI (PubMed:17095609). Q15654; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-742327, EBI-743598; Q15654; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-742327, EBI-10173507; Q15654; P29972: AQP1; NbExp=7; IntAct=EBI-742327, EBI-745213; Q15654; P54259: ATN1; NbExp=2; IntAct=EBI-742327, EBI-945980; Q15654; P48047: ATP5PO; NbExp=3; IntAct=EBI-742327, EBI-355815; Q15654; P54253: ATXN1; NbExp=7; IntAct=EBI-742327, EBI-930964; Q15654; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-742327, EBI-16429430; Q15654; O15169: AXIN1; NbExp=6; IntAct=EBI-742327, EBI-710484; Q15654; O95817: BAG3; NbExp=3; IntAct=EBI-742327, EBI-747185; Q15654; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-742327, EBI-745073; Q15654; Q13895: BYSL; NbExp=6; IntAct=EBI-742327, EBI-358049; Q15654; Q6NUJ2: C11orf87; NbExp=3; IntAct=EBI-742327, EBI-6660291; Q15654; Q8NEC5: CATSPER1; NbExp=7; IntAct=EBI-742327, EBI-744545; Q15654; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-742327, EBI-744556; Q15654; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-742327, EBI-1104933; Q15654; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-742327, EBI-10181988; Q15654; P26441: CNTF; NbExp=3; IntAct=EBI-742327, EBI-1050897; Q15654; Q02930-3: CREB5; NbExp=3; IntAct=EBI-742327, EBI-10192698; Q15654; P53673: CRYBA4; NbExp=3; IntAct=EBI-742327, EBI-7519711; Q15654; O75638: CTAG2; NbExp=4; IntAct=EBI-742327, EBI-10188927; Q15654; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-742327, EBI-9679045; Q15654; Q86UW9: DTX2; NbExp=3; IntAct=EBI-742327, EBI-740376; Q15654; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-742327, EBI-743105; Q15654; Q9UM22: EPDR1; NbExp=3; IntAct=EBI-742327, EBI-946972; Q15654; Q8N2X6: EXOC3-AS1; NbExp=4; IntAct=EBI-742327, EBI-749333; Q15654; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-742327, EBI-2807642; Q15654; O95363: FARS2; NbExp=3; IntAct=EBI-742327, EBI-2513774; Q15654; P48023: FASLG; NbExp=3; IntAct=EBI-742327, EBI-495538; Q15654; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-742327, EBI-11320806; Q15654; O43559: FRS3; NbExp=6; IntAct=EBI-742327, EBI-725515; Q15654; A0A0S2Z4D9: GAD1; NbExp=3; IntAct=EBI-742327, EBI-16430771; Q15654; P15976-2: GATA1; NbExp=4; IntAct=EBI-742327, EBI-9090198; Q15654; Q9HBR3: GDPD5; NbExp=3; IntAct=EBI-742327, EBI-10310206; Q15654; Q8NEA6-2: GLIS3; NbExp=3; IntAct=EBI-742327, EBI-12232117; Q15654; P04899: GNAI2; NbExp=3; IntAct=EBI-742327, EBI-353997; Q15654; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-742327, EBI-11975289; Q15654; Q13227: GPS2; NbExp=3; IntAct=EBI-742327, EBI-713355; Q15654; Q14687: GSE1; NbExp=5; IntAct=EBI-742327, EBI-372619; Q15654; P08631-2: HCK; NbExp=3; IntAct=EBI-742327, EBI-9834454; Q15654; V9HWD0: HEL-S-42; NbExp=3; IntAct=EBI-742327, EBI-10330219; Q15654; P31269: HOXA9; NbExp=4; IntAct=EBI-742327, EBI-742314; Q15654; P17482: HOXB9; NbExp=3; IntAct=EBI-742327, EBI-745290; Q15654; P31273: HOXC8; NbExp=3; IntAct=EBI-742327, EBI-1752118; Q15654; P42858: HTT; NbExp=3; IntAct=EBI-742327, EBI-466029; Q15654; A0A0C4DGM4: HYKK; NbExp=3; IntAct=EBI-742327, EBI-10236738; Q15654; Q0VD86: INCA1; NbExp=3; IntAct=EBI-742327, EBI-6509505; Q15654; Q96PC2: IP6K3; NbExp=3; IntAct=EBI-742327, EBI-10990676; Q15654; P16144-2: ITGB4; NbExp=3; IntAct=EBI-742327, EBI-11051601; Q15654; Q7L273: KCTD9; NbExp=3; IntAct=EBI-742327, EBI-4397613; Q15654; Q99706: KIR2DL4; NbExp=3; IntAct=EBI-742327, EBI-10294579; Q15654; Q9H2R5: KLK15; NbExp=3; IntAct=EBI-742327, EBI-8645371; Q15654; Q5T749: KPRP; NbExp=3; IntAct=EBI-742327, EBI-10981970; Q15654; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-742327, EBI-3957672; Q15654; P25791: LMO2; NbExp=3; IntAct=EBI-742327, EBI-739696; Q15654; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-742327, EBI-739832; Q15654; O60336: MAPKBP1; NbExp=3; IntAct=EBI-742327, EBI-947402; Q15654; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-742327, EBI-1104564; Q15654; Q9H7H0: METTL17; NbExp=5; IntAct=EBI-742327, EBI-749353; Q15654; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-742327, EBI-14086479; Q15654; Q9BRT3: MIEN1; NbExp=3; IntAct=EBI-742327, EBI-6137472; Q15654; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-742327, EBI-2801965; Q15654; Q8IVT2: MISP; NbExp=3; IntAct=EBI-742327, EBI-2555085; Q15654; Q8IXL7: MSRB3; NbExp=3; IntAct=EBI-742327, EBI-8634060; Q15654; O43639: NCK2; NbExp=8; IntAct=EBI-742327, EBI-713635; Q15654; Q14511: NEDD9; NbExp=3; IntAct=EBI-742327, EBI-2108053; Q15654; Q8WWR8-2: NEU4; NbExp=3; IntAct=EBI-742327, EBI-10277551; Q15654; Q6NSM0: NR1D2; NbExp=3; IntAct=EBI-742327, EBI-10250949; Q15654; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-742327, EBI-12028784; Q15654; O43482: OIP5; NbExp=4; IntAct=EBI-742327, EBI-536879; Q15654; Q9BWI9: OTUB2; NbExp=3; IntAct=EBI-742327, EBI-10300896; Q15654; P32242: OTX1; NbExp=3; IntAct=EBI-742327, EBI-740446; Q15654; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-742327, EBI-11022007; Q15654; P09619: PDGFRB; NbExp=3; IntAct=EBI-742327, EBI-641237; Q15654; J3QSH9: PER1; NbExp=3; IntAct=EBI-742327, EBI-10178671; Q15654; Q96S52: PIGS; NbExp=3; IntAct=EBI-742327, EBI-2908273; Q15654; Q13526: PIN1; NbExp=3; IntAct=EBI-742327, EBI-714158; Q15654; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-742327, EBI-12014286; Q15654; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-742327, EBI-11956563; Q15654; Q3SYA9: POM121L1P; NbExp=3; IntAct=EBI-742327, EBI-10241319; Q15654; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-742327, EBI-710402; Q15654; Q13131: PRKAA1; NbExp=3; IntAct=EBI-742327, EBI-1181405; Q15654; P54646: PRKAA2; NbExp=3; IntAct=EBI-742327, EBI-1383852; Q15654; Q15678: PTPN14; NbExp=3; IntAct=EBI-742327, EBI-1237156; Q15654; P54725: RAD23A; NbExp=3; IntAct=EBI-742327, EBI-746453; Q15654; Q86VV4: RANBP3L; NbExp=3; IntAct=EBI-742327, EBI-12028066; Q15654; P48380: RFX3; NbExp=3; IntAct=EBI-742327, EBI-742557; Q15654; P61586: RHOA; NbExp=3; IntAct=EBI-742327, EBI-446668; Q15654; Q63HN8-6: RNF213; NbExp=3; IntAct=EBI-742327, EBI-10248548; Q15654; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-742327, EBI-3957636; Q15654; P57086: SCAND1; NbExp=3; IntAct=EBI-742327, EBI-745846; Q15654; Q15047-3: SETDB1; NbExp=3; IntAct=EBI-742327, EBI-11149962; Q15654; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-742327, EBI-12037847; Q15654; Q9Y2K2-7: SIK3; NbExp=3; IntAct=EBI-742327, EBI-17172855; Q15654; Q05CH4: SLC15A3; NbExp=3; IntAct=EBI-742327, EBI-10223741; Q15654; P12236: SLC25A6; NbExp=3; IntAct=EBI-742327, EBI-356254; Q15654; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-742327, EBI-2872322; Q15654; O95863: SNAI1; NbExp=4; IntAct=EBI-742327, EBI-1045459; Q15654; O75716: STK16; NbExp=3; IntAct=EBI-742327, EBI-749295; Q15654; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-742327, EBI-8787464; Q15654; Q9Y4C2: TCAF1; NbExp=3; IntAct=EBI-742327, EBI-750484; Q15654; Q8WW24: TEKT4; NbExp=4; IntAct=EBI-742327, EBI-750487; Q15654; P35590: TIE1; NbExp=3; IntAct=EBI-742327, EBI-2256865; Q15654; Q08117-2: TLE5; NbExp=3; IntAct=EBI-742327, EBI-11741437; Q15654; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-742327, EBI-10226570; Q15654; Q5VU62: TPM3; NbExp=3; IntAct=EBI-742327, EBI-10184033; Q15654; O43734: TRAF3IP2; NbExp=3; IntAct=EBI-742327, EBI-744798; Q15654; Q9UL33: TRAPPC2L; NbExp=3; IntAct=EBI-742327, EBI-747601; Q15654; Q14134: TRIM29; NbExp=3; IntAct=EBI-742327, EBI-702370; Q15654; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-742327, EBI-10241197; Q15654; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-742327, EBI-3918381; Q15654; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-742327, EBI-9090990; Q15654; Q6ZVT0: TTLL10; NbExp=3; IntAct=EBI-742327, EBI-7844656; Q15654; Q99757: TXN2; NbExp=3; IntAct=EBI-742327, EBI-2932492; Q15654; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-742327, EBI-2825190; Q15654; O75604: USP2; NbExp=3; IntAct=EBI-742327, EBI-743272; Q15654; Q6EMK4: VASN; NbExp=3; IntAct=EBI-742327, EBI-10249550; Q15654; Q06250: WT1-AS; NbExp=3; IntAct=EBI-742327, EBI-10223946; Q15654; Q8N4L5: XRCC6BP1; NbExp=3; IntAct=EBI-742327, EBI-10265517; Q15654; A2RRL9: ZBP1; NbExp=3; IntAct=EBI-742327, EBI-10173066; Q15654; Q15915: ZIC1; NbExp=3; IntAct=EBI-742327, EBI-11963196; Q15654; Q9H0D2: ZNF541; NbExp=3; IntAct=EBI-742327, EBI-3957075; Q15654; Q9UK33: ZNF580; NbExp=3; IntAct=EBI-742327, EBI-746277; Q15654; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-742327, EBI-745520; Q15654; A0A0S2Z5X4: ZNF688; NbExp=6; IntAct=EBI-742327, EBI-16429014; Q15654; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-742327, EBI-3925400; Q15654; Q5W150; NbExp=3; IntAct=EBI-742327, EBI-10248148; Q15654; Q95HA4; NbExp=3; IntAct=EBI-742327, EBI-10236795; Q15654; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-742327, EBI-3957603; Q15654; O46385: SVIL; Xeno; NbExp=5; IntAct=EBI-742327, EBI-6995105; Cytoplasm, cytoskeleton Cell junction, focal adhesion Nucleus toplasm Note=Shuttles between nucleus and cytoplasm (PubMed:16624523). Colocalizes with actin (PubMed:10826496). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q15654-1; Sequence=Displayed; Name=2; IsoId=Q15654-2; Sequence=VSP_047621, VSP_047624; Name=3; IsoId=Q15654-3; Sequence=VSP_047622, VSP_047623; Abundantly expressed in kidney, liver and lung. Lower levels in heart, placenta and pancreas. Expressed in colonic epithelial cells. Up-regulated in colonic tumors. The LIM zinc-binding domains mediate interaction with LPAR2 and with S.typhimurium protein sseI. Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13. Belongs to the zyxin/ajuba family. Sequence=AAC41740.1; Type=Frameshift; Evidence=; stress fiber RNA binding interleukin-1 receptor binding protein binding nucleus cytoplasm cytosol cytoskeleton plasma membrane focal adhesion cell adhesion signal transduction kinase binding cell junction positive regulation of cell migration metal ion binding thyroid hormone receptor binding focal adhesion assembly positive regulation of NIK/NF-kappaB signaling uc003uww.1 uc003uww.2 uc003uww.3 uc003uww.4 uc003uww.5 
ENST00000200557.11 ADAM11 ENST00000200557.11 ADAM metallopeptidase domain 11, transcript variant 1 (from RefSeq NM_002390.6) ADA11_HUMAN ENST00000200557.1 ENST00000200557.10 ENST00000200557.2 ENST00000200557.3 ENST00000200557.4 ENST00000200557.5 ENST00000200557.6 ENST00000200557.7 ENST00000200557.8 ENST00000200557.9 MDC NM_002390 O75078 Q14808 Q14809 Q14810 uc002ihh.1 uc002ihh.2 uc002ihh.3 uc002ihh.4 uc002ihh.5 This gene encodes a member of the ADAM (a disintegrin and metalloprotease) protein family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The encoded preproprotein is proteolytically processed to generate the mature protease. This gene represents a candidate tumor suppressor gene for human breast cancer based on its location within a minimal region of chromosome 17q21 previously defined by tumor deletion mapping. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Jan 2016]. Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Required for localization of the potassium channel subunit proteins KCNA1/KV1.1 and KCNA2/KV1.2 at cerebellar cortex basket cell distal terminals, is thereby involved in ephaptic inhibitory synchronization of Purkinje cell firing and response to stress (By similarity). Plays a role in spatial learning and motor coordination (By similarity). Involved in the nociceptive pain response to chemical-derived stimulation (By similarity). Interacts with LGI1 and LGI4 (By similarity). Interacts with KCNA1/KV1.1, KCNA2/KV1.2, DLG4/PSD-95 and ADAM22 (By similarity). Presynaptic cell membrane ; Single-pass type I membrane protein. Perikaryon Cell projection, axon Note=Localizes to basket cell terminals and pinceaux. Event=Alternative splicing; Named isoforms=2; Name=Long; Synonyms=MDC-769; IsoId=O75078-1; Sequence=Displayed; Name=Short; Synonyms=MDC-524; IsoId=O75078-2; Sequence=VSP_005472, VSP_005473, VSP_005474, VSP_005475; Expressed predominantly in brain. Slightly detected or not at all in other tissues. A conserved motif [AVN[ED]CD] within the disintegrin-like domain could be involved in the binding to the integrin receptor. The precursor is cleaved by a furin endopeptidase. [Isoform Short]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. metalloendopeptidase activity integrin binding plasma membrane proteolysis integrin-mediated signaling pathway metallopeptidase activity membrane integral component of membrane uc002ihh.1 uc002ihh.2 uc002ihh.3 uc002ihh.4 uc002ihh.5 
ENST00000200639.9 LAMP2 ENST00000200639.9 lysosomal associated membrane protein 2, transcript variant A (from RefSeq NM_002294.3) A8K4X5 D3DTF0 ENST00000200639.1 ENST00000200639.2 ENST00000200639.3 ENST00000200639.4 ENST00000200639.5 ENST00000200639.6 ENST00000200639.7 ENST00000200639.8 LAMP2_HUMAN NM_002294 P13473 Q16641 Q6Q3G8 Q96J30 Q99534 Q9UD93 uc004est.1 uc004est.2 uc004est.3 uc004est.4 uc004est.5 uc004est.6 The protein encoded by this gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may play a role in tumor cell metastasis. It may also function in the protection, maintenance, and adhesion of the lysosome. Alternative splicing of this gene results in multiple transcript variants encoding distinct proteins. [provided by RefSeq, Jul 2008]. Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation and autophagy (PubMed:8662539, PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:27628032, PubMed:36586411, PubMed:37390818). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (PubMed:37390818). Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live (PubMed:8662539, PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:27628032, PubMed:36586411). Functions by binding target proteins, such as GAPDH, NLRP3 and MLLT11, and targeting them for lysosomal degradation (PubMed:8662539, PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:36586411). In the chaperone- mediated autophagy, acts downstream of chaperones, such as HSPA8/HSC70, which recognize and bind substrate proteins and mediate their recruitment to lysosomes, where target proteins bind LAMP2 (PubMed:36586411). Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed:27628032). Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes (PubMed:27628032). Required for normal degradation of the contents of autophagosomes (PubMed:27628032). Required for efficient MHC class II-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHC II subunits (PubMed:20518820, PubMed:15894275). Is not required for efficient MHC class II-mediated presentation of endogenous antigens (PubMed:20518820). [Isoform LAMP-2C]: Modulates chaperone-mediated autophagy. Decreases presentation of endogenous antigens by MHCII. Does not play a role in the presentation of exogenous and membrane-derived antigens by MHCII. (Microbial infection) Supports the FURIN-mediated cleavage of mumps virus fusion protein F by interacting with both FURIN and the unprocessed form but not the processed form of the viral protein F. Monomer (PubMed:18644871, PubMed:25342746). Homodimer (PubMed:25342746). Homotrimer (PubMed:25342746). Forms large homooligomers (PubMed:18644871). Interacts (via its cytoplasmic region) with HSPA8; HSPA8 mediates recruitment of proteins with a KFERQ motif to the surface of the lysosome for chaperone-mediated autophagy (PubMed:36586411, PubMed:25342746). Interacts with HSP90 in the lysosome lumen; this enhances LAMP2 stability (By similarity). Interacts with MLLT11 (PubMed:24880125). Interacts with ABCB9 (PubMed:22641697). Interacts with FURIN (PubMed:32295904). Interacts with CT55; this interaction may be important for LAMP2 protein stability (PubMed:36481789). Interacts with TMEM175; inhibiting the proton channel activity of TMEM175 (PubMed:37390818). (Microbial infection) Interacts with mumps virus protein F; this interaction promotes protein F cleavage by FURIN. P13473-2; P45844-6: ABCG1; NbExp=3; IntAct=EBI-21591415, EBI-25873349; P13473-2; Q7Z5M8-2: ABHD12B; NbExp=3; IntAct=EBI-21591415, EBI-21854797; P13473-2; Q9Y614: ACTL7B; NbExp=3; IntAct=EBI-21591415, EBI-25835070; P13473-2; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-21591415, EBI-18899653; P13473-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-21591415, EBI-10173507; P13473-2; Q96MA6: AK8; NbExp=3; IntAct=EBI-21591415, EBI-8466265; P13473-2; Q5T2L2: AKR1C8; NbExp=3; IntAct=EBI-21591415, EBI-22006248; P13473-2; Q96Q83-2: ALKBH3; NbExp=3; IntAct=EBI-21591415, EBI-9089544; P13473-2; Q9Y303-2: AMDHD2; NbExp=3; IntAct=EBI-21591415, EBI-12323557; P13473-2; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-21591415, EBI-8464238; P13473-2; P09525: ANXA4; NbExp=3; IntAct=EBI-21591415, EBI-2556852; P13473-2; P02647: APOA1; NbExp=3; IntAct=EBI-21591415, EBI-701692; P13473-2; P02749: APOH; NbExp=3; IntAct=EBI-21591415, EBI-2114682; P13473-2; P53365: ARFIP2; NbExp=3; IntAct=EBI-21591415, EBI-638194; P13473-2; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-21591415, EBI-5280499; P13473-2; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-21591415, EBI-10254793; P13473-2; P18848: ATF4; NbExp=3; IntAct=EBI-21591415, EBI-492498; P13473-2; Q9H0Y0: ATG10; NbExp=3; IntAct=EBI-21591415, EBI-1048913; P13473-2; C1IDX9: ATG12; NbExp=3; IntAct=EBI-21591415, EBI-25836940; P13473-2; O75964: ATP5MG; NbExp=3; IntAct=EBI-21591415, EBI-1044001; P13473-2; Q14032: BAAT; NbExp=3; IntAct=EBI-21591415, EBI-8994378; P13473-2; P54687-4: BCAT1; NbExp=3; IntAct=EBI-21591415, EBI-25834445; P13473-2; P06276: BCHE; NbExp=3; IntAct=EBI-21591415, EBI-7936069; P13473-2; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-21591415, EBI-10693038; P13473-2; Q8WZ55: BSND; NbExp=3; IntAct=EBI-21591415, EBI-7996695; P13473-2; Q96Q07-2: BTBD9; NbExp=3; IntAct=EBI-21591415, EBI-22006737; P13473-2; Q9H0W9-3: C11orf54; NbExp=3; IntAct=EBI-21591415, EBI-12108466; P13473-2; Q9NQ89: C12orf4; NbExp=3; IntAct=EBI-21591415, EBI-11090973; P13473-2; Q13901: C1D; NbExp=3; IntAct=EBI-21591415, EBI-3844053; P13473-2; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-21591415, EBI-18036948; P13473-2; Q8N1A6: C4orf33; NbExp=3; IntAct=EBI-21591415, EBI-10264911; P13473-2; P17655: CAPN2; NbExp=3; IntAct=EBI-21591415, EBI-1028956; P13473-2; P20807-4: CAPN3; NbExp=3; IntAct=EBI-21591415, EBI-11532021; P13473-2; P55212: CASP6; NbExp=3; IntAct=EBI-21591415, EBI-718729; P13473-2; O00257-3: CBX4; NbExp=3; IntAct=EBI-21591415, EBI-4392727; P13473-2; P24863: CCNC; NbExp=3; IntAct=EBI-21591415, EBI-395261; P13473-2; Q9UK58-5: CCNL1; NbExp=3; IntAct=EBI-21591415, EBI-25873837; P13473-2; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-21591415, EBI-12300031; P13473-2; P01730: CD4; NbExp=3; IntAct=EBI-21591415, EBI-353826; P13473-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-21591415, EBI-396137; P13473-2; P42773: CDKN2C; NbExp=3; IntAct=EBI-21591415, EBI-711290; P13473-2; O95674: CDS2; NbExp=3; IntAct=EBI-21591415, EBI-3913685; P13473-2; O15182: CETN3; NbExp=3; IntAct=EBI-21591415, EBI-712959; P13473-2; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-21591415, EBI-749253; P13473-2; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-21591415, EBI-744045; P13473-2; Q8N365: CIART; NbExp=3; IntAct=EBI-21591415, EBI-10265133; P13473-2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-21591415, EBI-7062247; P13473-2; Q99966: CITED1; NbExp=3; IntAct=EBI-21591415, EBI-2624951; P13473-2; P09496-2: CLTA; NbExp=3; IntAct=EBI-21591415, EBI-4401010; P13473-2; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-21591415, EBI-25836090; P13473-2; Q96BR5: COA7; NbExp=3; IntAct=EBI-21591415, EBI-6269632; P13473-2; P02458-1: COL2A1; NbExp=3; IntAct=EBI-21591415, EBI-12375799; P13473-2; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-21591415, EBI-745535; P13473-2; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-21591415, EBI-713677; P13473-2; P26998: CRYBB3; NbExp=3; IntAct=EBI-21591415, EBI-1965681; P13473-2; P35222: CTNNB1; NbExp=3; IntAct=EBI-21591415, EBI-491549; P13473-2; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-21591415, EBI-8637742; P13473-2; P10632: CYP2C8; NbExp=3; IntAct=EBI-21591415, EBI-2951522; P13473-2; P61962: DCAF7; NbExp=3; IntAct=EBI-21591415, EBI-359808; P13473-2; Q96LJ7: DHRS1; NbExp=3; IntAct=EBI-21591415, EBI-746300; P13473-2; O60479: DLX3; NbExp=3; IntAct=EBI-21591415, EBI-3908248; P13473-2; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-21591415, EBI-11526226; P13473-2; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-21591415, EBI-296550; P13473-2; Q92782-2: DPF1; NbExp=3; IntAct=EBI-21591415, EBI-23669343; P13473-2; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-21591415, EBI-724653; P13473-2; Q658K8: EEF1DP3; NbExp=3; IntAct=EBI-21591415, EBI-10248874; P13473-2; O00303: EIF3F; NbExp=3; IntAct=EBI-21591415, EBI-711990; P13473-2; Q13347: EIF3I; NbExp=3; IntAct=EBI-21591415, EBI-354047; P13473-2; O00472: ELL2; NbExp=3; IntAct=EBI-21591415, EBI-395274; P13473-2; O00423: EML1; NbExp=3; IntAct=EBI-21591415, EBI-751327; P13473-2; O95278-6: EPM2A; NbExp=3; IntAct=EBI-21591415, EBI-25836908; P13473-2; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-21591415, EBI-21567429; P13473-2; P00748: F12; NbExp=3; IntAct=EBI-21591415, EBI-6378830; P13473-2; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-21591415, EBI-25835236; P13473-2; Q96KS9: FAM167A; NbExp=3; IntAct=EBI-21591415, EBI-10290462; P13473-2; Q8N128-2: FAM177A1; NbExp=3; IntAct=EBI-21591415, EBI-12201693; P13473-2; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-21591415, EBI-8468186; P13473-2; Q9NYY8: FASTKD2; NbExp=3; IntAct=EBI-21591415, EBI-1055752; P13473-2; P02671-2: FGA; NbExp=3; IntAct=EBI-21591415, EBI-9640259; P13473-2; Q6ZNL6: FGD5; NbExp=3; IntAct=EBI-21591415, EBI-7962481; P13473-2; Q9NSA1: FGF21; NbExp=3; IntAct=EBI-21591415, EBI-3909329; P13473-2; P49771-3: FLT3LG; NbExp=3; IntAct=EBI-21591415, EBI-25872794; P13473-2; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-21591415, EBI-6425864; P13473-2; Q6P7E6: FUT6; NbExp=3; IntAct=EBI-21591415, EBI-25872807; P13473-2; P06241: FYN; NbExp=3; IntAct=EBI-21591415, EBI-515315; P13473-2; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-21591415, EBI-9088619; P13473-2; Q9H3K2: GHITM; NbExp=3; IntAct=EBI-21591415, EBI-2868909; P13473-2; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-21591415, EBI-11991950; P13473-2; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-21591415, EBI-12143817; P13473-2; Q9HAV0: GNB4; NbExp=3; IntAct=EBI-21591415, EBI-358539; P13473-2; P32780: GTF2H1; NbExp=3; IntAct=EBI-21591415, EBI-715539; P13473-2; O75409: H2AP; NbExp=3; IntAct=EBI-21591415, EBI-6447217; P13473-2; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-21591415, EBI-2868501; P13473-2; P68431: H3C12; NbExp=3; IntAct=EBI-21591415, EBI-79722; P13473-2; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-21591415, EBI-2558143; P13473-2; Q9NRZ9-6: HELLS; NbExp=3; IntAct=EBI-21591415, EBI-12003732; P13473-2; Q96EW2-2: HSPBAP1; NbExp=3; IntAct=EBI-21591415, EBI-25835621; P13473-2; Q8N6M8-2: IQCF1; NbExp=3; IntAct=EBI-21591415, EBI-21771049; P13473-2; Q92613: JADE3; NbExp=3; IntAct=EBI-21591415, EBI-10278909; P13473-2; P0C870: JMJD7; NbExp=3; IntAct=EBI-21591415, EBI-9090173; P13473-2; Q9UK76: JPT1; NbExp=3; IntAct=EBI-21591415, EBI-720411; P13473-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-21591415, EBI-743960; P13473-2; Q8TBB5-2: KLHDC4; NbExp=3; IntAct=EBI-21591415, EBI-21838933; P13473-2; Q9UH77: KLHL3; NbExp=3; IntAct=EBI-21591415, EBI-8524663; P13473-2; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-21591415, EBI-10973851; P13473-2; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-21591415, EBI-8473062; P13473-2; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-21591415, EBI-9088829; P13473-2; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-21591415, EBI-25835523; P13473-2; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-21591415, EBI-10264791; P13473-2; Q9Y234: LIPT1; NbExp=3; IntAct=EBI-21591415, EBI-727376; P13473-2; Q99732: LITAF; NbExp=3; IntAct=EBI-21591415, EBI-725647; P13473-2; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-21591415, EBI-2510853; P13473-2; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-21591415, EBI-749562; P13473-2; Q8IYG6: LRRC56; NbExp=3; IntAct=EBI-21591415, EBI-14752528; P13473-2; Q5VYH9: LY9; NbExp=3; IntAct=EBI-21591415, EBI-25872860; P13473-2; P0DP58-2: LYNX1; NbExp=3; IntAct=EBI-21591415, EBI-21916939; P13473-2; P43361: MAGEA8; NbExp=3; IntAct=EBI-21591415, EBI-10182930; P13473-2; Q96M61: MAGEB18; NbExp=3; IntAct=EBI-21591415, EBI-741835; P13473-2; Q969L2: MAL2; NbExp=3; IntAct=EBI-21591415, EBI-944295; P13473-2; P27338: MAOB; NbExp=3; IntAct=EBI-21591415, EBI-3911344; P13473-2; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-21591415, EBI-2689785; P13473-2; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-21591415, EBI-10174029; P13473-2; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-21591415, EBI-25835557; P13473-2; P34949-2: MPI; NbExp=3; IntAct=EBI-21591415, EBI-21823432; P13473-2; Q9BV20: MRI1; NbExp=3; IntAct=EBI-21591415, EBI-747381; P13473-2; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-21591415, EBI-25835707; P13473-2; Q8N387: MUC15; NbExp=3; IntAct=EBI-21591415, EBI-17937277; P13473-2; A2RUH7: MYBPHL; NbExp=3; IntAct=EBI-21591415, EBI-9088235; P13473-2; P01106: MYC; NbExp=3; IntAct=EBI-21591415, EBI-447544; P13473-2; Q9H7X0: NAA60; NbExp=3; IntAct=EBI-21591415, EBI-12260336; P13473-2; Q15742-2: NAB2; NbExp=3; IntAct=EBI-21591415, EBI-25834665; P13473-2; Q9UJ70-2: NAGK; NbExp=3; IntAct=EBI-21591415, EBI-11526455; P13473-2; Q69YL0: NCBP2AS2; NbExp=3; IntAct=EBI-21591415, EBI-10986258; P13473-2; P25208: NFYB; NbExp=3; IntAct=EBI-21591415, EBI-389728; P13473-2; Q8NDH3-5: NPEPL1; NbExp=3; IntAct=EBI-21591415, EBI-12329915; P13473-2; O15130-2: NPFF; NbExp=3; IntAct=EBI-21591415, EBI-25840002; P13473-2; P36639-4: NUDT1; NbExp=3; IntAct=EBI-21591415, EBI-25834643; P13473-2; Q8NFH4: NUP37; NbExp=3; IntAct=EBI-21591415, EBI-2563158; P13473-2; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-21591415, EBI-1059321; P13473-2; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-21591415, EBI-741048; P13473-2; Q6N063-2: OGFOD2; NbExp=3; IntAct=EBI-21591415, EBI-22006224; P13473-2; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-21591415, EBI-25830200; P13473-2; Q99447: PCYT2; NbExp=3; IntAct=EBI-21591415, EBI-750317; P13473-2; P27815-4: PDE4A; NbExp=3; IntAct=EBI-21591415, EBI-12080840; P13473-2; A5PLL7: PEDS1; NbExp=3; IntAct=EBI-21591415, EBI-11337896; P13473-2; Q9BUL5: PHF23; NbExp=3; IntAct=EBI-21591415, EBI-722852; P13473-2; Q00169: PITPNA; NbExp=3; IntAct=EBI-21591415, EBI-1042490; P13473-2; P48739: PITPNB; NbExp=3; IntAct=EBI-21591415, EBI-1047143; P13473-2; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-21591415, EBI-21503705; P13473-2; O60664: PLIN3; NbExp=3; IntAct=EBI-21591415, EBI-725795; P13473-2; Q14181: POLA2; NbExp=3; IntAct=EBI-21591415, EBI-712752; P13473-2; P0DPB6: POLR1D; NbExp=3; IntAct=EBI-21591415, EBI-359498; P13473-2; P36954: POLR2I; NbExp=3; IntAct=EBI-21591415, EBI-395202; P13473-2; Q07869: PPARA; NbExp=3; IntAct=EBI-21591415, EBI-78615; P13473-2; O60927: PPP1R11; NbExp=3; IntAct=EBI-21591415, EBI-1048104; P13473-2; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-21591415, EBI-25835994; P13473-2; Q8NCQ7-2: PROCA1; NbExp=3; IntAct=EBI-21591415, EBI-25836043; P13473-2; P23942: PRPH2; NbExp=3; IntAct=EBI-21591415, EBI-25836834; P13473-2; P41222: PTGDS; NbExp=3; IntAct=EBI-21591415, EBI-948821; P13473-2; P29074: PTPN4; NbExp=3; IntAct=EBI-21591415, EBI-710431; P13473-2; Q8WUD1-2: RAB2B; NbExp=3; IntAct=EBI-21591415, EBI-25835884; P13473-2; Q5R372-9: RABGAP1L; NbExp=3; IntAct=EBI-21591415, EBI-10699389; P13473-2; Q9HD47-3: RANGRF; NbExp=3; IntAct=EBI-21591415, EBI-9089733; P13473-2; Q09028: RBBP4; NbExp=3; IntAct=EBI-21591415, EBI-620823; P13473-2; Q14498: RBM39; NbExp=3; IntAct=EBI-21591415, EBI-395290; P13473-2; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-21591415, EBI-14065960; P13473-2; Q04206: RELA; NbExp=3; IntAct=EBI-21591415, EBI-73886; P13473-2; P47804-3: RGR; NbExp=3; IntAct=EBI-21591415, EBI-25834767; P13473-2; Q15382: RHEB; NbExp=4; IntAct=EBI-21591415, EBI-1055287; P13473-2; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-21591415, EBI-9091816; P13473-2; Q06587: RING1; NbExp=3; IntAct=EBI-21591415, EBI-752313; P13473-2; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-21591415, EBI-714023; P13473-2; Q96IZ7: RSRC1; NbExp=3; IntAct=EBI-21591415, EBI-712189; P13473-2; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-21591415, EBI-10248967; P13473-2; O15126: SCAMP1; NbExp=3; IntAct=EBI-21591415, EBI-954338; P13473-2; P22307-3: SCP2; NbExp=3; IntAct=EBI-21591415, EBI-25834804; P13473-2; Q9BRK5: SDF4; NbExp=3; IntAct=EBI-21591415, EBI-1389808; P13473-2; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-21591415, EBI-9089805; P13473-2; P01011: SERPINA3; NbExp=3; IntAct=EBI-21591415, EBI-296557; P13473-2; Q9BWM7: SFXN3; NbExp=4; IntAct=EBI-21591415, EBI-1171999; P13473-2; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-21591415, EBI-749607; P13473-2; Q9BZQ2: SHCBP1L; NbExp=3; IntAct=EBI-21591415, EBI-10818532; P13473-2; O60902-3: SHOX2; NbExp=3; IntAct=EBI-21591415, EBI-9092164; P13473-2; O43772: SLC25A20; NbExp=3; IntAct=EBI-21591415, EBI-727085; P13473-2; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-21591415, EBI-2822550; P13473-2; Q86US8: SMG6; NbExp=3; IntAct=EBI-21591415, EBI-3232100; P13473-2; Q96EX1: SMIM12; NbExp=3; IntAct=EBI-21591415, EBI-2874543; P13473-2; P37840: SNCA; NbExp=3; IntAct=EBI-21591415, EBI-985879; P13473-2; Q96H20: SNF8; NbExp=3; IntAct=EBI-21591415, EBI-747719; P13473-2; Q8N0X7: SPART; NbExp=3; IntAct=EBI-21591415, EBI-2643803; P13473-2; Q496A3: SPATS1; NbExp=3; IntAct=EBI-21591415, EBI-3923692; P13473-2; Q9NYA1-2: SPHK1; NbExp=3; IntAct=EBI-21591415, EBI-12512419; P13473-2; Q9BPZ2: SPIN2B; NbExp=3; IntAct=EBI-21591415, EBI-21726245; P13473-2; Q9P2T0: SPMAP2; NbExp=3; IntAct=EBI-21591415, EBI-751020; P13473-2; Q9C004: SPRY4; NbExp=3; IntAct=EBI-21591415, EBI-354861; P13473-2; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-21591415, EBI-2659201; P13473-2; Q9BXA5: SUCNR1; NbExp=3; IntAct=EBI-21591415, EBI-17962797; P13473-2; Q92797-2: SYMPK; NbExp=3; IntAct=EBI-21591415, EBI-21560407; P13473-2; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-21591415, EBI-11123832; P13473-2; P08247: SYP; NbExp=3; IntAct=EBI-21591415, EBI-9071725; P13473-2; Q17RD7: SYT16; NbExp=3; IntAct=EBI-21591415, EBI-10238936; P13473-2; O95947: TBX6; NbExp=3; IntAct=EBI-21591415, EBI-2824328; P13473-2; O15273: TCAP; NbExp=3; IntAct=EBI-21591415, EBI-954089; P13473-2; Q86WV5: TEN1; NbExp=3; IntAct=EBI-21591415, EBI-2562799; P13473-2; P54274-2: TERF1; NbExp=3; IntAct=EBI-21591415, EBI-711018; P13473-2; P22735: TGM1; NbExp=3; IntAct=EBI-21591415, EBI-2562368; P13473-2; O43548: TGM5; NbExp=3; IntAct=EBI-21591415, EBI-12027348; P13473-2; Q9NQ88: TIGAR; NbExp=3; IntAct=EBI-21591415, EBI-3920747; P13473-2; O14925: TIMM23; NbExp=3; IntAct=EBI-21591415, EBI-1047996; P13473-2; Q12893: TMEM115; NbExp=3; IntAct=EBI-21591415, EBI-8633987; P13473-2; Q8WVE6-2: TMEM171; NbExp=3; IntAct=EBI-21591415, EBI-25874374; P13473-2; Q3YBM2: TMEM176B; NbExp=3; IntAct=EBI-21591415, EBI-2821479; P13473-2; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-21591415, EBI-10242677; P13473-2; Q9NS69: TOMM22; NbExp=3; IntAct=EBI-21591415, EBI-1047508; P13473-2; P04637: TP53; NbExp=3; IntAct=EBI-21591415, EBI-366083; P13473-2; Q12888: TP53BP1; NbExp=3; IntAct=EBI-21591415, EBI-396540; P13473-2; O00463: TRAF5; NbExp=3; IntAct=EBI-21591415, EBI-523498; P13473-2; P36406: TRIM23; NbExp=3; IntAct=EBI-21591415, EBI-740098; P13473-2; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-21591415, EBI-12840050; P13473-2; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-21591415, EBI-11525489; P13473-2; Q9H313-4: TTYH1; NbExp=3; IntAct=EBI-21591415, EBI-17671298; P13473-2; Q9BQE3: TUBA1C; NbExp=3; IntAct=EBI-21591415, EBI-1103245; P13473-2; P49459: UBE2A; NbExp=3; IntAct=EBI-21591415, EBI-2339348; P13473-2; P62253: UBE2G1; NbExp=3; IntAct=EBI-21591415, EBI-2340619; P13473-2; P09936: UCHL1; NbExp=3; IntAct=EBI-21591415, EBI-714860; P13473-2; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-21591415, EBI-25835297; P13473-2; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-21591415, EBI-10316321; P13473-2; Q6ICG8: WBP2NL; NbExp=3; IntAct=EBI-21591415, EBI-17769315; P13473-2; Q8NA23-2: WDR31; NbExp=3; IntAct=EBI-21591415, EBI-25835937; P13473-2; Q9BQA1: WDR77; NbExp=3; IntAct=EBI-21591415, EBI-1237307; P13473-2; O00755: WNT7A; NbExp=3; IntAct=EBI-21591415, EBI-727198; P13473-2; O95070: YIF1A; NbExp=3; IntAct=EBI-21591415, EBI-2799703; P13473-2; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-21591415, EBI-12956041; P13473-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-21591415, EBI-14104088; P13473-2; Q05CR2: ZNF248; NbExp=3; IntAct=EBI-21591415, EBI-25835471; P13473-2; Q96JL9-2: ZNF333; NbExp=3; IntAct=EBI-21591415, EBI-25835852; P13473-2; Q96LX8: ZNF597; NbExp=3; IntAct=EBI-21591415, EBI-9091553; P13473-2; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-21591415, EBI-18036029; P13473-2; Q5JTY5: ZNG1C; NbExp=3; IntAct=EBI-21591415, EBI-723434; P13473-2; A0A384MDV8; NbExp=3; IntAct=EBI-21591415, EBI-25834468; P13473-2; B7Z3E8; NbExp=3; IntAct=EBI-21591415, EBI-25831617; P13473-2; Q86V28; NbExp=3; IntAct=EBI-21591415, EBI-10259496; Lysosome membrane ingle-pass type I membrane protein Endosome membrane ; Single-pass type I membrane protein ll membrane ; Single-pass type I membrane protein toplasmic vesicle, autophagosome membrane Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane. Event=Alternative splicing; Named isoforms=3; Name=LAMP-2A; IsoId=P13473-1; Sequence=Displayed; Name=LAMP-2B; IsoId=P13473-2; Sequence=VSP_003044; Name=LAMP-2C; IsoId=P13473-3; Sequence=VSP_042519; Isoform LAMP-2A is highly expressed in placenta, lung and liver, less in kidney and pancreas, low in brain and skeletal muscle (PubMed:7488019, PubMed:26856698). Isoform LAMP-2B is detected in spleen, thymus, prostate, testis, small intestine, colon, skeletal muscle, brain, placenta, lung, kidney, ovary and pancreas and liver (PubMed:7488019, PubMed:26856698). Isoform LAMP-2C is detected in small intestine, colon, heart, brain, skeletal muscle, and at lower levels in kidney and placenta (PubMed:26856698). In peripheral blood B cells isoform LAMP-2A, LAMP-2B and LAMP-2C are up-regulated in response to treatments that stimulate immune responses via the Toll-like receptors TLR7 or TLR9. O- and N-glycosylated; some of the 16 N-linked glycans are polylactosaminoglycans. Danon disease (DAND) [MIM:300257]: DAND is a lysosomal glycogen storage disease characterized by the clinical triad of cardiomyopathy, vacuolar myopathy and intellectual disability. It is often associated with an accumulation of glycogen in muscle and lysosomes. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the LAMP family. autophagosome membrane platelet degranulation protein binding extracellular space lysosome lysosomal membrane endosome late endosome trans-Golgi network plasma membrane protein targeting autophagy cellular response to starvation endosome membrane membrane integral component of membrane protein import enzyme binding protein domain specific binding phagocytic vesicle membrane platelet dense granule membrane negative regulation of protein complex assembly cytoplasmic vesicle regulation of protein stability late endosome membrane azurophil granule membrane lysosomal lumen neutrophil degranulation autolysosome membrane raft muscle cell cellular homeostasis perinuclear region of cytoplasm protein stabilization chaperone-mediated autophagy protein targeting to lysosome involved in chaperone-mediated autophagy chaperone-mediated autophagy translocation complex extracellular exosome establishment of protein localization to organelle autophagosome maturation integral component of autophagosome membrane ficolin-1-rich granule membrane lysosomal protein catabolic process lysosomal matrix membrane microdomain uc004est.1 uc004est.2 uc004est.3 uc004est.4 uc004est.5 uc004est.6 
ENST00000200652.4 SLC22A4 ENST00000200652.4 solute carrier family 22 member 4 (from RefSeq NM_003059.3) ENST00000200652.1 ENST00000200652.2 ENST00000200652.3 ETT NM_003059 O14546 OCTN1 Q9H015 S22A4_HUMAN SLC22A4 UT2H uc003kwq.1 uc003kwq.2 uc003kwq.3 uc003kwq.4 uc003kwq.5 Polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. The encoded protein is an organic cation transporter and plasma integral membrane protein containing eleven putative transmembrane domains as well as a nucleotide-binding site motif. Transport by this protein is at least partially ATP-dependent. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803613.246404.1, SRR3476690.258062.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000200652.4/ ENSP00000200652.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Transporter that mediates the transport of endogenous and microbial zwitterions and organic cations (PubMed:15795384, PubMed:10215651, PubMed:16729965, PubMed:20601551, PubMed:22569296, PubMed:29530864, PubMed:15107849, PubMed:22206629). Functions as a Na(+)-dependent and pH-dependent high affinity microbial symporter of potent food-derived antioxidant ergothioeine (PubMed:15795384, PubMed:29530864, PubMed:33124720). Transports one sodium ion with one ergothioeine molecule (By similarity). Involved in the absorption of ergothioneine from the luminal/apical side of the small intestine and renal tubular cells, and into non-parenchymal liver cells, thereby contributing to maintain steady-state ergothioneine level in the body (PubMed:20601551). Also mediates the bidirectional transport of acetycholine, although the exact transport mechanism has not been fully identified yet (PubMed:22206629). Most likely exports anti-inflammatory acetylcholine in non-neuronal tissues, thereby contributing to the non- neuronal cholinergic system (PubMed:22569296, PubMed:22206629). Displays a general physiological role linked to better survival by controlling inflammation and oxidative stress, which may be related to ergothioneine and acetycholine transports (PubMed:15795384, PubMed:22206629). May also function as a low-affinity Na(+)-dependent transporter of L-carnitine through the mitochondrial membrane, thereby maintaining intracellular carnitine homeostasis (PubMed:10215651, PubMed:16729965, PubMed:15107849). May contribute to regulate the transport of cationic compounds in testis across the blood-testis- barrier (PubMed:35307651). Reaction=ergothioneine(out) + Na(+)(out) = ergothioneine(in) + Na(+)(in); Xref=Rhea:RHEA:75843, ChEBI:CHEBI:29101, ChEBI:CHEBI:134344; Evidence= Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74664; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:74665; Evidence=; Reaction=(R)-carnitine(out) + Na(+)(out) = (R)-carnitine(in) + Na(+)(in); Xref=Rhea:RHEA:72091, ChEBI:CHEBI:16347, ChEBI:CHEBI:29101; Evidence= Reaction=glycine betaine(out) + Na(+)(out) = glycine betaine(in) + Na(+)(in); Xref=Rhea:RHEA:72115, ChEBI:CHEBI:17750, ChEBI:CHEBI:29101; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72116; Evidence=; Allosterically activated by intracellular ATP. Kinetic parameters: KM=21 uM for ergothioneine (at pH 7.4) ; KM=1000 uM for acetylcholine(in) (at pH 8.0) ; KM=780 uM for acetylcholine(out) (at pH 8.0) ; KM=422.5 uM for (R)-carnitine (at pH 7.5) ; KM=571 uM for (R)-carnitine ; Vmax=42000 pmol/min/mg enzyme for ergothioneine uptake (at pH 7.4) ; Vmax=160000 pmol/min/mg enzyme for acetylcholine uptake (at pH 8.0) ; Vmax=14000 pmol/min/mg enzyme for acetylcholine export (at pH 8.0) ; Vmax=22.61 pmol/min/mg enzyme for (R)-carnitine uptake (at pH 7.5) ; Vmax=883 pmol/min/mg enzyme for (R)-carnitine uptake ; pH dependence: Optimum pH is 6.5-7.0 for ergothioneine uptake and transport efficiency decreased at more alkaline pHs. ; Interacts with PDZK1. Apical cell membrane ; Multi-pass membrane protein Basal cell membrane ; Multi-pass membrane protein Mitochondrion membrane ; Multi-pass membrane protein Note=Localized to the apical membrane of small intestines (PubMed:20601551). Localized to the basal membrane of Sertoli cells (PubMed:35307651). Widely expressed (PubMed:9426230). Highly expressed in kidney, trachea, ileum, bone marrow and whole blood (PubMed:9426230, PubMed:15795384). Expressed in small intestines (PubMed:20601551). Weakly expressed in skeletal muscle, prostate, lung, pancreas, placenta, heart, uterus, spleen and spinal cord (PubMed:9426230, PubMed:15795384, PubMed:16729965). Expressed in testis, primarily to the basal membrane of Sertoli cells (PubMed:35307651, PubMed:16729965). Expressed in brain (PubMed:16729965). Expressed in liver (PubMed:16729965). Highly expressed in intestinal cell types affected by Crohn disease, including epithelial cells. Expressed in CD68 macrophage and CD43 T-cells but not in CD20 B-cells (PubMed:15107849). Predominantly expressed in CD14 cells in peripheral blood mononuclear cells (PubMed:14608356). Expressed in fetal liver, kidney and lung (PubMed:9426230, PubMed:15795384). Overexpressed upon TNF treatment. Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mediates the Na(+)-independent and pH-dependent bidirectional transport of exogenous prototype organic cation tetraethylammonium (TEA). Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family. Despite a previous report demonstrating SLC22A4/OCTN1-mediated transport of nucleosides such as the endogenous 2'deoxycytidine or the anticancer drug cytarabine, another study was unable to verify these findings. nucleotide binding protein binding ATP binding mitochondrion plasma membrane integral component of plasma membrane triglyceride metabolic process ion transport sodium ion transport body fluid secretion secondary active organic cation transmembrane transporter activity carnitine metabolic process carnitine transmembrane transporter activity symporter activity cation:cation antiporter activity quaternary ammonium group transmembrane transporter activity organic cation transport quaternary ammonium group transport carnitine transport membrane integral component of membrane apical plasma membrane transmembrane transporter activity PDZ domain binding transmembrane transport cation transmembrane transport carnitine transmembrane transport uc003kwq.1 uc003kwq.2 uc003kwq.3 uc003kwq.4 uc003kwq.5 
ENST00000200676.8 CETP ENST00000200676.8 cholesteryl ester transfer protein, transcript variant 1 (from RefSeq NM_000078.3) CETP CETP_HUMAN ENST00000200676.1 ENST00000200676.2 ENST00000200676.3 ENST00000200676.4 ENST00000200676.5 ENST00000200676.6 ENST00000200676.7 NM_000078 P11597 Q13987 Q13988 Q53YZ1 uc002eki.1 uc002eki.2 uc002eki.3 uc002eki.4 The protein encoded by this gene is found in plasma, where it is involved in the transfer of cholesteryl ester from high density lipoprotein (HDL) to other lipoproteins. Defects in this gene are a cause of hyperalphalipoproteinemia 1 (HALP1). Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2013]. Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL (PubMed:3600759, PubMed:24293641, PubMed:3281933). Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (PubMed:17237796). Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z- octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898; Evidence=; Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol(in) = 1,2,3-tri-(9Z- octadecenoyl)-glycerol(out); Xref=Rhea:RHEA:43352, ChEBI:CHEBI:53753; Evidence=; Reaction=cholesteryl (9Z,12Z)-octadecadienoate(in) = cholesteryl (9Z,12Z)-octadecadienoate(out); Xref=Rhea:RHEA:43356, ChEBI:CHEBI:41509; Evidence=; Secreted te=Secreted in plasma. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P11597-1; Sequence=Displayed; Name=2; IsoId=P11597-2; Sequence=VSP_023645; Expressed by the liver and secreted in plasma. Genetic variations in CETP define the high density lipoprotein cholesterol level quantitative trait locus 10 (HDLCQ10) [MIM:143470]. Hyperalphalipoproteinemia 1 (HALP1) [MIM:143470]: A condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. Name=Wikipedia; Note=Cholesterylester transfer protein entry; URL="https://en.wikipedia.org/wiki/Cholesterylester_transfer_protein"; lipid transporter activity phospholipid transporter activity extracellular region extracellular space lipid metabolic process triglyceride metabolic process lipid transport steroid metabolic process cholesterol metabolic process lipid binding negative regulation of macrophage derived foam cell differentiation regulation of cholesterol efflux cholesterol binding phospholipid transport triglyceride binding cholesterol transport phosphatidylcholine binding vesicle triglyceride transport high-density lipoprotein particle very-low-density lipoprotein particle remodeling low-density lipoprotein particle remodeling high-density lipoprotein particle remodeling cholesterol homeostasis reverse cholesterol transport phosphatidylcholine metabolic process lipid homeostasis phospholipid homeostasis extracellular exosome triglyceride homeostasis uc002eki.1 uc002eki.2 uc002eki.3 uc002eki.4 
ENST00000200691.5 MT3 ENST00000200691.5 metallothionein 3 (from RefSeq NM_005954.4) ENST00000200691.1 ENST00000200691.2 ENST00000200691.3 ENST00000200691.4 MT3_HUMAN NM_005954 P25713 Q2V574 uc002ejf.1 uc002ejf.2 uc002ejf.3 uc002ejf.4 uc002ejf.5 This gene is a member of the metallothionein family of genes. Proteins encoded by this gene family are low in molecular weight, are cysteine-rich, lack aromatic residues, and bind divalent heavy metal ions. This gene family member displays tissue-specific expression, and contains a threonine insert near its N-terminus and a glutamate-rich hexapeptide insert near its C-terminus relative to the proteins encoded by other gene family members. It plays an important role in zinc and copper homeostasis, and is induced under hypoxic conditions. The encoded protein is a growth inhibitory factor, and reduced levels of the protein are observed in the brains of individuals with some metal-linked neurodegenerative disorders such as Alzheimer's disease. [provided by RefSeq, Sep 2017]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BP211991.1, CK001163.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000200691.5/ ENSP00000200691.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro. P25713; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-8084264, EBI-750109; P25713; P02766: TTR; NbExp=3; IntAct=EBI-8084264, EBI-711909; Abundant in a subset of astrocytes in the normal human brain, but greatly reduced in the Alzheimer disease (AD) brain. Belongs to the metallothionein superfamily. Type 1 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mt3/"; response to hypoxia positive regulation of protein phosphorylation copper ion binding protein binding extracellular space nucleus cytoplasm mitochondrial outer membrane rough endoplasmic reticulum cytosol ribosome microtubule plasma membrane energy reserve metabolic process cholesterol catabolic process zinc II ion transport cellular metal ion homeostasis cellular zinc ion homeostasis apoptotic process response to oxidative stress brain development synaptic vesicle drug binding zinc ion binding response to metal ion detoxification of copper ion negative regulation of autophagy positive regulation of gene expression positive regulation of necrotic cell death positive regulation of cell death negative regulation of neuron projection development astrocyte development postsynaptic density antioxidant activity inclusion body histone modification removal of superoxide radicals protein kinase activator activity negative regulation of cell growth axon negative regulation of axon extension positive regulation of vascular endothelial growth factor receptor signaling pathway regulation of response to food activation of protein kinase B activity leptin-mediated signaling pathway cellular response to oxidative stress cellular response to drug positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress cysteine-type endopeptidase inhibitor activity involved in apoptotic process negative regulation of apoptotic process positive regulation of catalytic activity negative regulation of cysteine-type endopeptidase activity involved in apoptotic process dendritic spine protein kinase B signaling negative regulation of neuron apoptotic process cellular lipid catabolic process negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated cadmium ion binding metal ion binding perinuclear region of cytoplasm negative regulation of neurogenesis protein stabilization negative regulation of oxidoreductase activity zinc ion homeostasis cadmium ion homeostasis regulation of protein glycosylation negative regulation of necrotic cell death ERK1 and ERK2 cascade positive regulation of ERK1 and ERK2 cascade cellular response to cadmium ion cellular response to copper ion cellular response to zinc ion cellular response to hypoxia cellular response to nitric oxide positive regulation of lysosomal membrane permeability astrocyte projection astrocyte end-foot negative regulation of neuron death negative regulation of cysteine-type endopeptidase activity negative regulation of hydrogen peroxide catabolic process positive regulation of oxygen metabolic process negative regulation of reactive oxygen species metabolic process uc002ejf.1 uc002ejf.2 uc002ejf.3 uc002ejf.4 uc002ejf.5 
ENST00000201031.3 TFAP2C ENST00000201031.3 transcription factor AP-2 gamma (from RefSeq NM_003222.4) AP2C_HUMAN B4DWK3 ENST00000201031.1 ENST00000201031.2 NM_003222 O00685 O00730 Q86V30 Q8IVB6 Q92754 Q9P1X2 uc002xya.1 uc002xya.2 uc002xya.3 uc002xya.4 uc002xya.5 The protein encoded by this gene is a sequence-specific DNA-binding transcription factor involved in the activation of several developmental genes. The encoded protein can act as either a homodimer or heterodimer with other family members and is induced during retinoic acid-mediated differentiation. It plays a role in the development of the eyes, face, body wall, limbs, and neural tube. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC051829.1, U85658.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968832, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000201031.3/ ENSP00000201031.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members (By similarity). Interacts with WWOX. Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity. Interacts with MTA1. Q92754; Q99967: CITED2; NbExp=2; IntAct=EBI-937309, EBI-937732; Q92754; P63279: UBE2I; NbExp=5; IntAct=EBI-937309, EBI-80168; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q92754-1; Sequence=Displayed; Name=2; IsoId=Q92754-2; Sequence=VSP_056501; During retinoic acid-mediated differentiation. The PPxY motif mediates interaction with WWOX. Sumoylated on Lys-10; which inhibits transcriptional activity. Belongs to the AP-2 family. Name=Wikipedia; Note=Activating protein 2 entry; URL="https://en.wikipedia.org/wiki/Activating_protein_2"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm mitochondrion cytosol regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter cell-cell signaling male gonad development regulation of gene expression, epigenetic positive regulation of transcription from RNA polymerase II promoter protein dimerization activity uc002xya.1 uc002xya.2 uc002xya.3 uc002xya.4 uc002xya.5 
ENST00000201586.7 SULT2B1 ENST00000201586.7 sulfotransferase family 2B member 1, transcript variant 2 (from RefSeq NM_177973.2) ENST00000201586.1 ENST00000201586.2 ENST00000201586.3 ENST00000201586.4 ENST00000201586.5 ENST00000201586.6 HSST2 NM_177973 O00204 O00205 O75814 ST2B1_HUMAN uc002pjl.1 uc002pjl.2 uc002pjl.3 uc002pjl.4 uc002pjl.5 Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene sulfates dehydroepiandrosterone but not 4-nitrophenol, a typical substrate for the phenol and estrogen sulfotransferase subfamilies. Two alternatively spliced variants that encode different isoforms have been described. [provided by RefSeq, Jul 2008]. Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol (PubMed:19589875, PubMed:12145317). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA) (PubMed:9799594, PubMed:12145317, PubMed:21855633, PubMed:16855051). Preferentially sulfonates cholesterol, while it has also significant activity with pregnenolone and DHEA (PubMed:12145317, PubMed:21855633). Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (PubMed:28575648). [Isoform 2]: Sulfonates pregnenolone but not cholesterol. Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'- bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; Evidence= Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate + H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217; Evidence=; Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)- hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349; Evidence=; Reaction=3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'- bisphosphate + cholesterol sulfate + H(+); Xref=Rhea:RHEA:52368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136579; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52369; Evidence=; Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'- bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356, ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133000; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357; Evidence=; Kinetic parameters: KM=23.5 uM for (24S)-hydroxycholesterol ; KM=10.9 uM for DHEA (at 37 degrees Celsius, in the presence of 1 mM MgCl2) ; KM=3.8 uM for DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2) ; KM=11.8 uM for pregnenolone (at 37 degrees Celsius, in the presence of 1 mM MgCl2) ; KM=0.6 uM for PAPS (at 37 degrees Celsius, in the presence of 1 mM MgCl2) ; Vmax=1752 pmol/min/mg enzyme toward DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2) ; Temperature dependence: Optimum temperature is 37 degrees Celsius. Retains 70% and 20% of activity when incubated at 42 degrees Celsius for 45 and 120 minutes, respectively. Activity is lost after 200 minutes incubation at 42 degrees Celsius. O00204; P14621: ACYP2; NbExp=3; IntAct=EBI-749441, EBI-10198377; O00204; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-749441, EBI-742054; O00204; Q96Q35: FLACC1; NbExp=8; IntAct=EBI-749441, EBI-750451; O00204; Q96Q35-2: FLACC1; NbExp=8; IntAct=EBI-749441, EBI-11533409; O00204; Q9P2G9-2: KLHL8; NbExp=3; IntAct=EBI-749441, EBI-11959635; O00204; O43900: PRICKLE3; NbExp=3; IntAct=EBI-749441, EBI-1751761; O00204; Q04864-2: REL; NbExp=3; IntAct=EBI-749441, EBI-10829018; O00204; O76094: SRP72; NbExp=3; IntAct=EBI-749441, EBI-1058850; O00204; P50225: SULT1A1; NbExp=7; IntAct=EBI-749441, EBI-2814403; O00204; O43704: SULT1B1; NbExp=9; IntAct=EBI-749441, EBI-10179062; O00204; Q6IMI6: SULT1C3; NbExp=3; IntAct=EBI-749441, EBI-12837366; O00204; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-749441, EBI-10486136; Cytoplasm, cytosol crosome cleus te=Phosphorylation of Ser-348 is required for translocation to the nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=SULT2B1b, B; IsoId=O00204-1; Sequence=Displayed; Name=2; Synonyms=SULT2B1a, A; IsoId=O00204-2; Sequence=VSP_012510; Expressed in the stratum granulosum-stratum corneum junction in the skin (at protein level) (PubMed:28575648). Expressed highly in placenta, prostate and trachea and lower expression in the small intestine and lung (PubMed:9799594). The C-terminus, which contains a proline/serine-rich region is involved in nuclear translocation and enzymatic thermostability. Phosphorylated. Ichthyosis, congenital, autosomal recessive 14 (ARCI14) [MIM:617571]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non- bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the sulfotransferase 1 family. sulfate assimilation nucleic acid binding alcohol sulfotransferase activity protein binding nucleus cytoplasm endoplasmic reticulum cytosol lipid metabolic process sulfotransferase activity steroid metabolic process cholesterol metabolic process negative regulation of cell proliferation cholesterol binding transferase activity intracellular membrane-bounded organelle positive regulation of epidermal cell differentiation steroid sulfotransferase activity 3'-phosphoadenosine 5'-phosphosulfate metabolic process extracellular exosome steroid hormone binding uc002pjl.1 uc002pjl.2 uc002pjl.3 uc002pjl.4 uc002pjl.5 
ENST00000201647.11 EPS8L1 ENST00000201647.11 EPS8 like 1, transcript variant 1 (from RefSeq NM_133180.3) DRC3 ENST00000201647.1 ENST00000201647.10 ENST00000201647.2 ENST00000201647.3 ENST00000201647.4 ENST00000201647.5 ENST00000201647.6 ENST00000201647.7 ENST00000201647.8 ENST00000201647.9 EPS8R1 ES8L1_HUMAN NM_133180 PP10566 Q71RE2 Q8NC10 Q8TE68 Q96BB7 Q9BSQ2 Q9GZQ2 Q9NXH0 uc002qis.1 uc002qis.2 uc002qis.3 uc002qis.4 uc002qis.5 uc002qis.6 This gene encodes a protein that is related to epidermal growth factor receptor pathway substrate 8 (EPS8), a substrate for the epidermal growth factor receptor. The function of this protein is unknown. At least two alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. Interacts with ABI1. Part of a complex that contains SOS1, ABI1 and EPS8L2. Associates with F-actin. Q8TE68; Q9H013: ADAM19; NbExp=2; IntAct=EBI-7487998, EBI-8567699; Q8TE68; P07766: CD3E; NbExp=6; IntAct=EBI-7487998, EBI-1211297; Q8TE68; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-7487998, EBI-750109; Q8TE68-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12003490, EBI-11096309; Q8TE68-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12003490, EBI-3867333; Q8TE68-3; P28799: GRN; NbExp=3; IntAct=EBI-21574901, EBI-747754; Q8TE68-3; P42858: HTT; NbExp=3; IntAct=EBI-21574901, EBI-466029; Q8TE68-3; O43933: PEX1; NbExp=3; IntAct=EBI-21574901, EBI-988601; Q8TE68-3; O76024: WFS1; NbExp=3; IntAct=EBI-21574901, EBI-720609; Cytoplasm Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=A; IsoId=Q8TE68-1; Sequence=Displayed; Name=2; Synonyms=B; IsoId=Q8TE68-2; Sequence=VSP_019083, VSP_019085; Name=3; Synonyms=C; IsoId=Q8TE68-3; Sequence=VSP_019084, VSP_019088, VSP_019089; Name=4; IsoId=Q8TE68-4; Sequence=VSP_019082, VSP_019086, VSP_019087, VSP_019088; Detected in placenta. Belongs to the EPS8 family. Sequence=AAG03038.1; Type=Frameshift; Evidence=; Sequence=AAG03039.1; Type=Erroneous gene model prediction; Evidence=; actin binding protein binding cytoplasm cytosol plasma membrane Rho protein signal transduction ruffle membrane macromolecular complex regulation of Rho protein signal transduction T cell receptor binding cadherin binding extracellular exosome positive regulation of ruffle assembly Rho guanyl-nucleotide exchange factor activity Rac guanyl-nucleotide exchange factor activity uc002qis.1 uc002qis.2 uc002qis.3 uc002qis.4 uc002qis.5 uc002qis.6 
ENST00000201979.3 REM1 ENST00000201979.3 RRAD and GEM like GTPase 1 (from RefSeq NM_014012.6) E1P5L1 ENST00000201979.1 ENST00000201979.2 GES NM_014012 O75628 Q5TZR7 Q5TZR8 Q9NP57 REM REM1_HUMAN uc002wwa.1 uc002wwa.2 uc002wwa.3 uc002wwa.4 uc002wwa.5 uc002wwa.6 The protein encoded by this gene is a GTPase and member of the RAS-like GTP-binding protein family. The encoded protein is expressed in endothelial cells, where it promotes reorganization of the actin cytoskeleton and morphological changes in the cells. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.462911.1, AF152863.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000201979.3/ ENSP00000201979.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Promotes endothelial cell sprouting and actin cytoskeletal reorganization. May be involved in angiogenesis. May function in Ca(2+) signaling. In vitro, interacts with calmodulin in a calcium-dependent manner. Most highly expressed in the endothelial lining of the blood vessels in uterus and heart. Lower levels found in spleen, lymph node, kidney and testis. Also found in cells with secretory function such as the islets of Langerhans, lobule/duct epithelium in the breast, bile duct epithelium in the liver, surface epithelium in the endometrial glands of the uterus, colon mucosa and acinar cells in the pancreas and the prostate. Belongs to the small GTPase superfamily. RGK family. nucleotide binding GTPase activity calcium channel regulator activity calmodulin binding GTP binding plasma membrane signal transduction membrane negative regulation of high voltage-gated calcium channel activity uc002wwa.1 uc002wwa.2 uc002wwa.3 uc002wwa.4 uc002wwa.5 uc002wwa.6 
ENST00000202017.6 PDRG1 ENST00000202017.6 p53 and DNA damage regulated 1 (from RefSeq NM_030815.3) B2R511 C20orf126 ENST00000202017.1 ENST00000202017.2 ENST00000202017.3 ENST00000202017.4 ENST00000202017.5 NM_030815 PDRG PDRG1_HUMAN Q96GP3 Q9BUW8 Q9NUG6 uc002wxd.1 uc002wxd.2 uc002wxd.3 uc002wxd.4 uc002wxd.5 May play a role in chaperone-mediated protein folding. Component of the PAQosome complex which is responsible for the biogenesis of several protein complexes and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92. Q9NUG6; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-307050, EBI-742887; Q9NUG6; Q9UHV9: PFDN2; NbExp=2; IntAct=EBI-307050, EBI-359873; Cytoplasm Predominantly expressed in normal testis and exhibits reduced but detectable expression in other organs. By UV irradiation and repressed by p53/TP53. Belongs to the prefoldin subunit beta family. protein binding cytoplasm protein folding prefoldin complex unfolded protein binding uc002wxd.1 uc002wxd.2 uc002wxd.3 uc002wxd.4 uc002wxd.5 
ENST00000202556.14 PPP1R13B ENST00000202556.14 protein phosphatase 1 regulatory subunit 13B (from RefSeq NM_015316.3) ASPP1 ASPP1_HUMAN B2RMX5 ENST00000202556.1 ENST00000202556.10 ENST00000202556.11 ENST00000202556.12 ENST00000202556.13 ENST00000202556.2 ENST00000202556.3 ENST00000202556.4 ENST00000202556.5 ENST00000202556.6 ENST00000202556.7 ENST00000202556.8 ENST00000202556.9 KIAA0771 NM_015316 O94870 Q96KQ4 uc001yof.1 uc001yof.2 uc001yof.3 This gene encodes a member of the ASPP (apoptosis-stimulating protein of p53) family of p53 interacting proteins. The protein contains four ankyrin repeats and an SH3 domain involved in protein-protein interactions. ASPP proteins are required for the induction of apoptosis by p53-family proteins. They promote DNA binding and transactivation of p53-family proteins on the promoters of proapoptotic genes. Expression of this gene is regulated by the E2F transcription factor. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC035446.1, AJ318887.2 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000202556.14/ ENSP00000202556.9 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Regulator that plays a central role in regulation of apoptosis via its interaction with p53/TP53 (PubMed:11684014, PubMed:12524540). Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Interacts with P53/TP53; the interaction promotes pro- apoptotic activity. Q96KQ4; Q4G176: ACSF3; NbExp=3; IntAct=EBI-1105153, EBI-10714818; Q96KQ4; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-1105153, EBI-2825900; Q96KQ4; Q13515: BFSP2; NbExp=3; IntAct=EBI-1105153, EBI-10229433; Q96KQ4; Q9NWW7: C2orf42; NbExp=3; IntAct=EBI-1105153, EBI-2812028; Q96KQ4; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-1105153, EBI-1765641; Q96KQ4; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-1105153, EBI-11524851; Q96KQ4; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-1105153, EBI-10171570; Q96KQ4; Q52MB2: CCDC184; NbExp=3; IntAct=EBI-1105153, EBI-10179526; Q96KQ4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-1105153, EBI-10175300; Q96KQ4; Q99459: CDC5L; NbExp=5; IntAct=EBI-1105153, EBI-374880; Q96KQ4; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-1105153, EBI-11752486; Q96KQ4; B9EK46: CGN; NbExp=3; IntAct=EBI-1105153, EBI-14314072; Q96KQ4; P61024: CKS1B; NbExp=3; IntAct=EBI-1105153, EBI-456371; Q96KQ4; Q05D60: DEUP1; NbExp=3; IntAct=EBI-1105153, EBI-748597; Q96KQ4; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-1105153, EBI-742953; Q96KQ4; O95057: DIRAS1; NbExp=3; IntAct=EBI-1105153, EBI-11993172; Q96KQ4; O60941-5: DTNB; NbExp=3; IntAct=EBI-1105153, EBI-11984733; Q96KQ4; Q09472: EP300; NbExp=2; IntAct=EBI-1105153, EBI-447295; Q96KQ4; Q8NB25: FAM184A; NbExp=3; IntAct=EBI-1105153, EBI-9917523; Q96KQ4; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-1105153, EBI-6658203; Q96KQ4; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-1105153, EBI-7960826; Q96KQ4; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-1105153, EBI-747500; Q96KQ4; Q92805: GOLGA1; NbExp=3; IntAct=EBI-1105153, EBI-6164177; Q96KQ4; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-1105153, EBI-713401; Q96KQ4; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-1105153, EBI-1018153; Q96KQ4; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-1105153, EBI-8472129; Q96KQ4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-1105153, EBI-14069005; Q96KQ4; P35900: KRT20; NbExp=3; IntAct=EBI-1105153, EBI-742094; Q96KQ4; P19013: KRT4; NbExp=3; IntAct=EBI-1105153, EBI-2371606; Q96KQ4; P20700: LMNB1; NbExp=3; IntAct=EBI-1105153, EBI-968218; Q96KQ4; Q03252: LMNB2; NbExp=3; IntAct=EBI-1105153, EBI-2830427; Q96KQ4; P25800: LMO1; NbExp=3; IntAct=EBI-1105153, EBI-8639312; Q96KQ4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1105153, EBI-11742507; Q96KQ4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1105153, EBI-739832; Q96KQ4; O95460-2: MATN4; NbExp=3; IntAct=EBI-1105153, EBI-12072296; Q96KQ4; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1105153, EBI-348259; Q96KQ4; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-1105153, EBI-2548751; Q96KQ4; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-1105153, EBI-1104552; Q96KQ4; P40692: MLH1; NbExp=3; IntAct=EBI-1105153, EBI-744248; Q96KQ4; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-1105153, EBI-3911716; Q96KQ4; O14777: NDC80; NbExp=3; IntAct=EBI-1105153, EBI-715849; Q96KQ4; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-1105153, EBI-2859639; Q96KQ4; O75145: PPFIA3; NbExp=3; IntAct=EBI-1105153, EBI-1763225; Q96KQ4; P62136: PPP1CA; NbExp=11; IntAct=EBI-1105153, EBI-357253; Q96KQ4; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-1105153, EBI-2557469; Q96KQ4; O43741: PRKAB2; NbExp=3; IntAct=EBI-1105153, EBI-1053424; Q96KQ4; P41219: PRPH; NbExp=3; IntAct=EBI-1105153, EBI-752074; Q96KQ4; P0CG20: PRR35; NbExp=3; IntAct=EBI-1105153, EBI-11986293; Q96KQ4; Q15311: RALBP1; NbExp=3; IntAct=EBI-1105153, EBI-749285; Q96KQ4; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-1105153, EBI-3437896; Q96KQ4; Q8NHQ8-2: RASSF8; NbExp=6; IntAct=EBI-1105153, EBI-10976415; Q96KQ4; Q9NSC2: SALL1; NbExp=3; IntAct=EBI-1105153, EBI-11317266; Q96KQ4; O94964-4: SOGA1; NbExp=3; IntAct=EBI-1105153, EBI-14083835; Q96KQ4; P56279: TCL1A; NbExp=3; IntAct=EBI-1105153, EBI-749995; Q96KQ4; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-1105153, EBI-750487; Q96KQ4; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-1105153, EBI-12090309; Q96KQ4; Q8N6V9: TEX9; NbExp=3; IntAct=EBI-1105153, EBI-746341; Q96KQ4; Q13077: TRAF1; NbExp=3; IntAct=EBI-1105153, EBI-359224; Q96KQ4; Q99816: TSG101; NbExp=3; IntAct=EBI-1105153, EBI-346882; Q96KQ4; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-1105153, EBI-744794; Q96KQ4; P40222: TXLNA; NbExp=3; IntAct=EBI-1105153, EBI-359793; Q96KQ4; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-1105153, EBI-10183064; Q96KQ4; Q8IYH5: ZZZ3; NbExp=3; IntAct=EBI-1105153, EBI-2795524; Cytoplasm Nucleus Note=Predominantly cytoplasmic. Some fraction is nuclear. Reduced expression in breast carcinomas expressing a wild-type TP53 protein. The ankyrin repeats and the SH3 domain are required for specific interactions with TP53. In contrast to its official gene name, it is not a regulatory subunit of protein phosphatase 1. This name was given due to its similarity with a protein that binds to protein phosphatase 1. Belongs to the ASPP family. p53 binding protein binding nucleus nucleoplasm cytoplasm mitochondrion cytosol plasma membrane apoptotic process transcription factor binding regulation of apoptotic process negative regulation of cell cycle perinuclear region of cytoplasm intrinsic apoptotic signaling pathway by p53 class mediator positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway positive regulation of neuron death regulation of signal transduction by p53 class mediator uc001yof.1 uc001yof.2 uc001yof.3 
ENST00000202625.7 TGM6 ENST00000202625.7 transglutaminase 6, transcript variant 1 (from RefSeq NM_198994.3) ENST00000202625.1 ENST00000202625.2 ENST00000202625.3 ENST00000202625.4 ENST00000202625.5 ENST00000202625.6 NM_198994 O95932 Q5JXU4 Q5JXU5 Q719M2 Q719M3 Q9Y4U8 TGM3L TGM3L_HUMAN uc002wfy.1 uc002wfy.2 The protein encoded by this gene belongs to the transglutaminase superfamily. It catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Mutations in this gene are associated with spinocerebellar ataxia type 35 (SCA35). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011]. Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L- lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence= Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Note=Binds up to 3 Ca(2+) cations per subunit. ; Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Long; IsoId=O95932-1; Sequence=Displayed; Name=2; Synonyms=Short; IsoId=O95932-2; Sequence=VSP_015103, VSP_015104; Spinocerebellar ataxia 35 (SCA35) [MIM:613908]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA35 patients commonly show upper limb involvement and torticollis. There is no cognitive impairment. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the transglutaminase superfamily. Transglutaminase family. protein-glutamine gamma-glutamyltransferase activity cytoplasm transferase activity transferase activity, transferring acyl groups peptide cross-linking metal ion binding uc002wfy.1 uc002wfy.2 
ENST00000202677.12 RALGAPA2 ENST00000202677.12 Ral GTPase activating protein catalytic subunit alpha 2 (from RefSeq NM_020343.4) C20orf74 ENST00000202677.1 ENST00000202677.10 ENST00000202677.11 ENST00000202677.2 ENST00000202677.3 ENST00000202677.4 ENST00000202677.5 ENST00000202677.6 ENST00000202677.7 ENST00000202677.8 ENST00000202677.9 KIAA1272 NM_020343 Q2PPJ7 Q4VXU6 Q5JUA3 Q5JUA4 Q5T9K3 Q96CX9 Q9BQT7 Q9H9D9 Q9ULE8 RGPA2_HUMAN uc002wrz.1 uc002wrz.2 uc002wrz.3 uc002wrz.4 uc002wrz.5 Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB. Component of the heterodimeric RalGAP2 complex with RALGAPB. Heterodimerization is required for activity (By similarity). Q2PPJ7; Q8WTU0: DDI1; NbExp=3; IntAct=EBI-9519763, EBI-748248; Cytoplasm Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q2PPJ7-1; Sequence=Displayed; Name=2; IsoId=Q2PPJ7-2; Sequence=VSP_025247; Name=3; IsoId=Q2PPJ7-3; Sequence=VSP_025248; Sequence=AAH13749.1; Type=Frameshift; Evidence=; Sequence=BAB14290.1; Type=Erroneous initiation; Evidence=; GTPase activator activity extracellular space nucleus cytoplasm cytosol plasma membrane positive regulation of GTPase activity protein heterodimerization activity regulation of small GTPase mediated signal transduction activation of GTPase activity uc002wrz.1 uc002wrz.2 uc002wrz.3 uc002wrz.4 uc002wrz.5 
ENST00000202773.14 RPL6 ENST00000202773.14 ribosomal protein L6, transcript variant 8 (from RefSeq NM_001320142.1) ENST00000202773.1 ENST00000202773.10 ENST00000202773.11 ENST00000202773.12 ENST00000202773.13 ENST00000202773.2 ENST00000202773.3 ENST00000202773.4 ENST00000202773.5 ENST00000202773.6 ENST00000202773.7 ENST00000202773.8 ENST00000202773.9 NM_001320142 Q02878 Q2M3Q3 Q8WW97 RL6_HUMAN TXREB1 uc001ttv.1 uc001ttv.2 uc001ttv.3 uc001ttv.4 uc001ttv.5 This gene encodes a protein component of the 60S ribosomal subunit. This protein can bind specifically to domain C of the tax-responsive enhancer element of human T-cell leukemia virus type 1, and may participate in tax-mediated transactivation of transcription. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed throughout the genome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]. Component of the large ribosomal subunit (PubMed:12962325, PubMed:25957688, PubMed:25901680, PubMed:32669547, PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:25957688, PubMed:25901680, PubMed:32669547, PubMed:23636399). (Microbial infection) Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I (PubMed:8457378). Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547). May bind IPO9 with low affinity (By similarity). Q02878; Q99558: MAP3K14; NbExp=3; IntAct=EBI-359655, EBI-358011; Cytoplasm, cytosol Cytoplasm Rough endoplasmic reticulum Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). Belongs to the eukaryotic ribosomal protein eL6 family. ribosomal large subunit assembly nuclear-transcribed mRNA catabolic process, nonsense-mediated decay cytoplasmic translation DNA binding RNA binding structural constituent of ribosome nucleus cytoplasm endoplasmic reticulum rough endoplasmic reticulum cytosol ribosome focal adhesion regulation of transcription, DNA-templated translation translational initiation SRP-dependent cotranslational protein targeting to membrane postsynaptic density membrane viral transcription cytosolic large ribosomal subunit cytoplasmic ribonucleoprotein granule polysomal ribosome synapse cadherin binding uc001ttv.1 uc001ttv.2 uc001ttv.3 uc001ttv.4 uc001ttv.5 
ENST00000202834.12 TMEM230 ENST00000202834.12 transmembrane protein 230, transcript variant 4 (from RefSeq NM_001009925.2) B2RDM8 C20orf30 D3DVZ9 ENST00000202834.1 ENST00000202834.10 ENST00000202834.11 ENST00000202834.2 ENST00000202834.3 ENST00000202834.4 ENST00000202834.5 ENST00000202834.6 ENST00000202834.7 ENST00000202834.8 ENST00000202834.9 HSPC274 NM_001009925 Q0VGC8 Q5TDS5 Q96A57 Q96ES2 Q9P0A7 TM230_HUMAN UNQ2432/PRO4992 uc002wlm.1 uc002wlm.2 uc002wlm.3 uc002wlm.4 uc002wlm.5 This gene encodes a multi-pass transmembrane protein that belongs to the TMEM134/TMEM230 protein family. The encoded protein localizes to secretory and recycling vesicle in the neuron and may be involved in synaptic vesicles trafficking and recycling. Mutations in this gene may be linked to familial Parkinson's disease. [provided by RefSeq, Mar 2017]. Involved in trafficking and recycling of synaptic vesicles. Q96A57-2; O43765: SGTA; NbExp=3; IntAct=EBI-17546822, EBI-347996; Membrane ; Multi-pass membrane protein Golgi apparatus, trans-Golgi network Cytoplasmic vesicle, secretory vesicle, synaptic vesicle Early endosome Recycling endosome Late endosome Cytoplasmic vesicle, autophagosome Event=Alternative splicing; Named isoforms=2; Name=2; IsoId=Q96A57-1; Sequence=Displayed; Name=1; IsoId=Q96A57-2; Sequence=VSP_018155; Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. Note=The gene represented in this entry may be involved in disease pathogenesis. Genetic variants in TMEM230 and DNAJC13 have been found in the same large multigenerational family with adult-onset Parkinson disease. The pathological role of each gene and therefore the exact molecular basis of the disease is unclear. Belongs to the TMEM134/TMEM230 family. [Isoform 1]: Sequence=AAF28952.1; Type=Frameshift; Evidence=; endosome early endosome late endosome autophagosome endoplasmic reticulum Golgi apparatus trans-Golgi network synaptic vesicle membrane integral component of membrane cell junction cytoplasmic vesicle synapse synaptic vesicle transport recycling endosome uc002wlm.1 uc002wlm.2 uc002wlm.3 uc002wlm.4 uc002wlm.5 
ENST00000202917.10 OAS1 ENST00000202917.10 2'-5'-oligoadenylate synthetase 1, transcript variant 22 (from RefSeq NR_175992.1) A8K4N8 ENST00000202917.1 ENST00000202917.2 ENST00000202917.3 ENST00000202917.4 ENST00000202917.5 ENST00000202917.6 ENST00000202917.7 ENST00000202917.8 ENST00000202917.9 F8VXY3 NR_175992 OAS1_HUMAN OIAS P00973 P04820 P29080 P29081 P78485 P78486 Q16700 Q16701 Q1PG42 Q3ZM01 Q53GC5 Q53YA4 Q6A1Z3 Q6IPC6 Q6P7N9 Q96J61 uc001tud.1 uc001tud.2 uc001tud.3 uc001tud.4 uc001tud.5 Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:34581622). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:34581622, PubMed:34145065). Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L. [Isoform p46]: When prenylated at C-terminal, acts as a double-stranded RNA (dsRNA) sensor specifically targeted to membranous replicative organelles in SARS coronavirus-2/SARS-CoV-2 infected cells where it binds to dsRNA structures in the SARS-CoV-2 5'-UTR and initiates a potent block to SARS-CoV-2 replication. Recognizes short stretches of dsRNA and activates RNase L. The binding is remarkably specific, with two conserved stem loops in the SARS-CoV-2 5'- untranslated region (UTR) constituting the principal viral target (PubMed:34581622). The same mechanism is necessary to initiate a block to cardiovirus EMCV (PubMed:34581622). [Isoform p42]: Not prenylated at C-terminal, is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication. Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')- adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Produced as a latent enzyme which is activated by dsRNA generated during the course of viral infection. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated (PubMed:34581622). ssRNA or dsDNA do not act as activators. Kinetic parameters: KM=0.31 mM for ATP ; Monomer (PubMed:9407111). Homotetramer (PubMed:9407111, PubMed:23319625). P00973; P12814: ACTN1; NbExp=4; IntAct=EBI-3932815, EBI-351710; P00973; O00471: EXOC5; NbExp=3; IntAct=EBI-3932815, EBI-949824; P00973; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-3932815, EBI-912440; P00973; P14373: TRIM27; NbExp=5; IntAct=EBI-3932815, EBI-719493; P00973-2; P12814: ACTN1; NbExp=3; IntAct=EBI-12081862, EBI-351710; P00973-2; Q96RK4: BBS4; NbExp=5; IntAct=EBI-12081862, EBI-1805814; P00973-2; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-12081862, EBI-3866319; P00973-2; O00471: EXOC5; NbExp=6; IntAct=EBI-12081862, EBI-949824; P00973-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12081862, EBI-618309; P00973-2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-12081862, EBI-10961706; P00973-2; Q96T51-2: RUFY1; NbExp=3; IntAct=EBI-12081862, EBI-12192715; P00973-2; P14373: TRIM27; NbExp=6; IntAct=EBI-12081862, EBI-719493; Cytoplasm tochondrion Nucleus crosome Endoplasmic reticulum Secreted Note=Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. [Isoform p46]: Note=(Microbial infection) In SARS coronavirus-2/SARS-CoV-2 infected cells, prenylated form localizes to membranous perinuclear structures reminiscent of the endoplasmic reticulum rich in viral dsRNA which are SARS-CoV-2 replicative organelles. [Isoform p42]: Note=(Microbial infection) In SARS coronavirus-2/SARS-CoV-2 infected cells, since its not prenylated, is diffusely localized and unable to initiate a detectable block to SARS- CoV-2 replication. Event=Alternative splicing; Named isoforms=4; Name=p46 ; Synonyms=46 kDa, E18; IsoId=P00973-1; Sequence=Displayed; Name=p42 ; Synonyms=41 kDa, E16, 3-9, p41; IsoId=P00973-2; Sequence=VSP_003738, VSP_003739; Name=p48; Synonyms=9-2; IsoId=P00973-3; Sequence=VSP_003740; Name=p44; IsoId=P00973-4; Sequence=VSP_060747, VSP_060748; Expressed in lungs. By type I interferon (IFN) and viruses. [Isoform p46]: Prenylated at C-terminal. C-terminal prenylation is necessary to initiate a block to SARS-CoV-2 and is associated with protection from severe COVID-1. The prenylated form is targeted to perinuclear structures rich in viral dsRNA, whereas the non-prenylated form is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication (Probable). C-terminal prenylation is also necessary to initiate a block to cardiovirus EMCV (Probable). [Isoform p42]: Not prenylated at C-terminal. The non-prenylated form is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication. Polymorphism dbSNP:rs10774671 is associated with protection against severe COVID-19 disease (PubMed:34581622, PubMed:33633408). In humans, the OAS1 protein is expressed as two major forms designated p46 and p42. The longer p46 isoform is generated by alternative splicing to an exon downstream of the terminal exon used by the p42 isoform. Although all human genotypes contain the exon that completes the transcript encoding p46, an intronic SNP (rs10774671) determines OAS1 exon usage. Alleles with a G at this SNP (G alleles) specify expression of the p46 isoform and some p42, whereas alleles with A at this position predominantly encode the p42 isoform and cannot express the p46 isoform (PubMed:34581622). The p42 isoform, which is the most common isoform in humans (~61% of alleles), has no detectable anti-SARS-CoV-2 activity. The p46 isoform has anti-SARS-CoV-2 activity (PubMed:34581622). Immunodeficiency 100 with pulmonary alveolar proteinosis and hypogammaglobulinemia (IMD100) [MIM:618042]: An autosomal dominant disorder characterized by onset of respiratory insufficiency due to pulmonary alveolar proteinosis in the first months of life. Disease development appears to be influenced or triggered by viral infection. Patients also have hypogammaglobulinemia, leukocytosis, and splenomegaly. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the 2-5A synthase family. PubMed:1651324 sequence was originally thought to originate from mouse. Sequence=AAA39857.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAA39858.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAA59955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAD96726.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=CAA26497.1; Type=Erroneous gene model prediction; Evidence=; Sequence=CAA30164.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=CAF33358.1; Type=Frameshift; Evidence=; Name=Protein Spotlight; Note=Luck of the draw - Issue 246 of April 2022; URL="https://web.expasy.org/spotlight/back_issues/246/"; nucleotide binding 2'-5'-oligoadenylate synthetase activity immune system process RNA binding double-stranded RNA binding protein binding ATP binding extracellular region nucleus nucleoplasm cytoplasm mitochondrion endoplasmic reticulum cytosol glucose metabolic process purine nucleotide biosynthetic process immune response response to virus transferase activity nucleotidyltransferase activity cellular response to interferon-alpha glucose homeostasis intracellular membrane-bounded organelle negative regulation of viral genome replication innate immune response metal ion binding protein oligomerization defense response to virus interferon-gamma-mediated signaling pathway type I interferon signaling pathway regulation of ribonuclease activity uc001tud.1 uc001tud.2 uc001tud.3 uc001tud.4 uc001tud.5 
ENST00000202967.4 SIRT4 ENST00000202967.4 sirtuin 4, transcript variant 1 (from RefSeq NM_012240.3) ENST00000202967.1 ENST00000202967.2 ENST00000202967.3 NM_012240 O43346 Q32M33 Q9Y6E7 SIR2L4 SIR4_HUMAN SIRT4 uc001tyc.1 uc001tyc.2 uc001tyc.3 uc001tyc.4 This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class IV of the sirtuin family. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF083109.1, BC034736.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Acts as a NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase (PubMed:16959573, PubMed:17715127, PubMed:24052263, PubMed:25525879). Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications (PubMed:24052263, PubMed:25525879). Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity (PubMed:16959573, PubMed:17715127). Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed:16959573, PubMed:17715127). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation (PubMed:23663782). Acts as a tumor suppressor (PubMed:23562301, PubMed:23663782). Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (By similarity). Does not seem to deacetylate PC (PubMed:23438705). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation (PubMed:24043310). Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels (PubMed:24043310). Down-regulates insulin secretion (PubMed:17715127). Reaction=H2O + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NAD(+) = 2''-O- lipoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:63640, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10474, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:83099, ChEBI:CHEBI:189572; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63641; Evidence= Reaction=H2O + N(6)-biotinyl-L-lysyl-[protein] + NAD(+) = 2''-O- biotinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70479, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:83144, ChEBI:CHEBI:189573; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70480; Evidence= Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl- ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637; Evidence=; Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP- D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA- COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540, ChEBI:CHEBI:140607; Evidence= Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Kinetic parameters: KM=719 uM for a peptide of H3 biotinylated at 'Lys-9' ; KM=814 uM for a peptide of H3 lipoylated at 'Lys-9' ; KM=239 uM for a peptide of DLAT lipoylated at 'Lys-259' ; Note=kcat is 0.0019 sec(-1) for the delipoylation of H3 'Lys-9'. kcat is 0.0005 sec(-1) for the debiotinylation of H3 'Lys-9'. kcat is 0.0018 sec(-1) for the delipoylation of DLAT 'Lys-259'. ; Interacts with GLUD1, IDE and SLC25A5 (PubMed:16959573, PubMed:17715127). Interacts with DLAT and PDHX (PubMed:25525879). Interacts with MCCC1 (via the biotin carboxylation domain) (PubMed:23438705). Interacts with PCCA and PC (PubMed:23438705). Q9Y6E7; P10515: DLAT; NbExp=6; IntAct=EBI-2606540, EBI-2959723; Q9Y6E7; O00330: PDHX; NbExp=4; IntAct=EBI-2606540, EBI-751566; Q9Y6E7; P05141: SLC25A5; NbExp=2; IntAct=EBI-2606540, EBI-355133; Mitochondrion matrix Detected in vascular smooth muscle and striated muscle. Detected in insulin-producing beta-cells in pancreas islets of Langerhans (at protein level). Widely expressed. Weakly expressed in leukocytes and fetal thymus. Induced by glutamine (at protein level). Expression is down-regulated in a number of cancers, while overexpression reduces cell proliferation, transformation, and tumor development (PubMed:23562301, PubMed:23663782). According to some authors, ADP-ribosyltransferase activity of sirtuins may be an inefficient side reaction of the deacetylase activity and may not be physiologically relevant. Belongs to the sirtuin family. Class II subfamily. Sequence=AAB95634.1; Type=Erroneous gene model prediction; Evidence=; regulation of glutamine family amino acid metabolic process NAD+ ADP-ribosyltransferase activity protein binding mitochondrion mitochondrial inner membrane mitochondrial matrix protein ADP-ribosylation protein deacetylation glutamine metabolic process cellular response to DNA damage stimulus mitochondrion organization zinc ion binding negative regulation of cardiac muscle cell apoptotic process transferase activity hydrolase activity peptidyl-lysine deacetylation negative regulation of fatty acid oxidation negative regulation of insulin secretion metal ion binding positive regulation of lipid biosynthetic process biotinidase activity lipoamidase activity NAD+ binding cellular response to hypoxia tricarboxylic acid metabolic process negative regulation of protein processing involved in protein targeting to mitochondrion regulation of pyruvate dehydrogenase activity NAD-dependent protein deacetylase activity uc001tyc.1 uc001tyc.2 uc001tyc.3 uc001tyc.4 
ENST00000203001.7 TRMT6 ENST00000203001.7 tRNA methyltransferase 6 non-catalytic subunit, transcript variant 1 (from RefSeq NM_015939.5) B4DUV6 CGI-09 ENST00000203001.1 ENST00000203001.2 ENST00000203001.3 ENST00000203001.4 ENST00000203001.5 ENST00000203001.6 KIAA1153 NM_015939 Q76P92 Q9BQV5 Q9UJA5 Q9ULR7 Q9Y2Z8 TRM6 TRM6_HUMAN uc002wmh.1 uc002wmh.2 uc002wmh.3 uc002wmh.4 This gene encodes a member of the tRNA methyltransferase 6 protein family. A similar protein in yeast is part of a two component methyltransferase, which is involved in the posttranslational modification that produces the modified nucleoside 1-methyladenosine in tRNAs. Modified 1-methyladenosine influences initiator methionine stability and may be involved in the replication of human immunodeficiency virus type 1. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]. Substrate-binding subunit of tRNA (adenine-N(1)-)- methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA (PubMed:16043508). Together with the TRMT61A catalytic subunit, part of a mRNA N(1)- methyltransferase complex that mediates methylation of adenosine residues at the N(1) position of a small subset of mRNAs: N(1) methylation takes place in tRNA T-loop-like structures of mRNAs and is only present at low stoichiometries (PubMed:29107537, PubMed:29072297). Heterotetramer; composed of two copies of TRMT6 and two copies of TRMT61A. Q9UJA5; Q92993: KAT5; NbExp=3; IntAct=EBI-934061, EBI-399080; Q9UJA5; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-934061, EBI-11742507; Q9UJA5; P62937-2: PPIA; NbExp=3; IntAct=EBI-934061, EBI-25884072; Q9UJA5; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-934061, EBI-9090795; Q9UJA5; Q96FX7: TRMT61A; NbExp=2; IntAct=EBI-934061, EBI-934042; Q9UJA5; P61981: YWHAG; NbExp=3; IntAct=EBI-934061, EBI-359832; Nucleus Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9UJA5-1; Sequence=Displayed; Name=2; IsoId=Q9UJA5-2; Sequence=VSP_018025; Name=3; IsoId=Q9UJA5-3; Sequence=VSP_031100, VSP_031101; Name=4; IsoId=Q9UJA5-4; Sequence=VSP_054740; Expressed in brain, liver, testis and ovary. Belongs to the TRM6/GCD10 family. Sequence=BAA86467.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=BAA86467.1; Type=Frameshift; Evidence=; RNA binding protein binding nucleus nucleoplasm tRNA modification tRNA processing tRNA methylation tRNA (m1A) methyltransferase complex mRNA methylation tRNA (adenine-N1-)-methyltransferase activity uc002wmh.1 uc002wmh.2 uc002wmh.3 uc002wmh.4 
ENST00000203166.10 HAUS5 ENST00000203166.10 HAUS augmin like complex subunit 5 (from RefSeq NM_015302.2) B2RXK1 ENST00000203166.1 ENST00000203166.2 ENST00000203166.3 ENST00000203166.4 ENST00000203166.5 ENST00000203166.6 ENST00000203166.7 ENST00000203166.8 ENST00000203166.9 HAUS5_HUMAN KIAA0841 NM_015302 O94927 Q6P2P7 Q7L3D5 Q96CT8 uc002oam.1 uc002oam.2 uc002oam.3 HAUS5 is 1 of 8 subunits of the 390-kD human augmin complex, or HAUS complex. The augmin complex was first identified in Drosophila, and its name comes from the Latin verb 'augmentare,' meaning 'to increase.' The augmin complex is a microtubule-binding complex involved in microtubule generation within the mitotic spindle and is vital to mitotic spindle assembly (Goshima et al., 2008 [PubMed 18443220]; Uehara et al., 2009 [PubMed 19369198]).[supplied by OMIM, Jun 2010]. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.78718.1, AB020648.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000203166.10/ ENSP00000439056.1 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly. Interacts with EML3 (phosphorylated at 'Thr-881') (PubMed:30723163). O94927; Q7Z4H7: HAUS6; NbExp=3; IntAct=EBI-2558224, EBI-2558196; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome toplasm, cytoskeleton, spindle te=Localizes to interphase centrosomes and to mitotic spindle microtubules. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O94927-1; Sequence=Displayed; Name=2; IsoId=O94927-2; Sequence=VSP_013927, VSP_013928; Belongs to the HAUS5 family. Sequence=AAH13947.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=BAA74864.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; G2/M transition of mitotic cell cycle molecular_function protein binding cytoplasm centrosome microtubule organizing center spindle cytosol cytoskeleton microtubule cell cycle centrosome cycle regulation of G2/M transition of mitotic cell cycle spindle assembly cell division HAUS complex ciliary basal body docking uc002oam.1 uc002oam.2 uc002oam.3 
ENST00000203407.6 UQCRC1 ENST00000203407.6 ubiquinol-cytochrome c reductase core protein 1 (from RefSeq NM_003365.3) B2R7R8 ENST00000203407.1 ENST00000203407.2 ENST00000203407.3 ENST00000203407.4 ENST00000203407.5 NM_003365 P31930 Q96DD2 QCR1_HUMAN uc003cub.1 uc003cub.2 uc003cub.3 Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (By similarity). The 2 core subunits UQCRC1/QCR1 and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they seem to have preserved their MPP processing properties (By similarity). May be involved in the in situ processing of UQCRFS1 into the mature Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated into complex III (Probable). Seems to play an important role in the maintenance of proper mitochondrial function in nigral dopaminergic neurons (PubMed:33141179). Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 11 subunits. The complex is composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske protein UQCRFS1 (By similarity). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase (complex IV, CIV), resulting in different assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:28844695). Interacts with UQCC6 (PubMed:32161263). Interacts with STMP1 (By similarity). P31930; P52566: ARHGDIB; NbExp=3; IntAct=EBI-1052596, EBI-2806617; P31930; Q14457: BECN1; NbExp=3; IntAct=EBI-1052596, EBI-949378; P31930; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-1052596, EBI-741214; P31930; Q8WU43: C2orf15; NbExp=3; IntAct=EBI-1052596, EBI-12904676; P31930; A0A024R9H7: CCDC26; NbExp=3; IntAct=EBI-1052596, EBI-10271580; P31930; Q8IV13: CCNJL; NbExp=3; IntAct=EBI-1052596, EBI-21668062; P31930; Q9Y6G5: COMMD10; NbExp=3; IntAct=EBI-1052596, EBI-1550310; P31930; P26641: EEF1G; NbExp=3; IntAct=EBI-1052596, EBI-351467; P31930; Q9UI10: EIF2B4; NbExp=3; IntAct=EBI-1052596, EBI-2340132; P31930; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-1052596, EBI-618189; P31930; Q9HC44: GPBP1L1; NbExp=3; IntAct=EBI-1052596, EBI-746674; P31930; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-1052596, EBI-743960; P31930; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-1052596, EBI-11985629; P31930; Q8N108-16: MIER1; NbExp=3; IntAct=EBI-1052596, EBI-25830642; P31930; C9J082: NPHP1; NbExp=3; IntAct=EBI-1052596, EBI-25830675; P31930; Q9UHV9: PFDN2; NbExp=3; IntAct=EBI-1052596, EBI-359873; P31930; Q00169: PITPNA; NbExp=3; IntAct=EBI-1052596, EBI-1042490; P31930; O14744: PRMT5; NbExp=3; IntAct=EBI-1052596, EBI-351098; P31930; O95416: SOX14; NbExp=3; IntAct=EBI-1052596, EBI-9087806; P31930; Q9BUA3: SPINDOC; NbExp=3; IntAct=EBI-1052596, EBI-1773488; P31930; O43704: SULT1B1; NbExp=3; IntAct=EBI-1052596, EBI-10179062; P31930; O95947: TBX6; NbExp=3; IntAct=EBI-1052596, EBI-2824328; P31930; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-1052596, EBI-17438286; P31930; Q9BZM4: ULBP3; NbExp=3; IntAct=EBI-1052596, EBI-1032551; P31930; Q6ZMY6-2: WDR88; NbExp=3; IntAct=EBI-1052596, EBI-25857007; P31930; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-1052596, EBI-749023; P31930; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-1052596, EBI-25831733; P31930; Q8N8E2: ZNF513; NbExp=3; IntAct=EBI-1052596, EBI-10279993; P31930; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-1052596, EBI-745520; P31930; Q9BRT8: ZNG1A; NbExp=3; IntAct=EBI-1052596, EBI-1054417; Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side Expressed in brain, including substantia nigra, striatum, cortex and cerebellum, and in spinal cord, heart, kidney, liver and muscle. Parkinsonism with polyneuropathy (PKNPY) [MIM:619279]: An autosomal dominant disorder characterized by late-onset, levodopa- responsive parkinsonism with asymmetric tremor, rigidity and bradykinesia. Patients also manifest a sensorimotor polyneuropathy with variable degrees of distal legs and hands muscle atrophy and weakness, and absent deep tendon reflexes. Note=The protein represented in this entry is involved in disease pathogenesis. Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily. catalytic activity mitochondrion mitochondrial inner membrane mitochondrial respiratory chain mitochondrial respiratory chain complex III cytosol oxidative phosphorylation mitochondrial electron transport, ubiquinol to cytochrome c ubiquinol-cytochrome-c reductase activity aerobic respiration response to activity membrane ubiquitin protein ligase binding response to alkaloid macromolecular complex binding metal ion binding oxidation-reduction process respiratory chain uc003cub.1 uc003cub.2 uc003cub.3 
ENST00000203556.9 GMIP ENST00000203556.9 GEM interacting protein, transcript variant 1 (from RefSeq NM_016573.4) A0AVN9 B7ZLZ0 ENST00000203556.1 ENST00000203556.2 ENST00000203556.3 ENST00000203556.4 ENST00000203556.5 ENST00000203556.6 ENST00000203556.7 ENST00000203556.8 GMIP_HUMAN NM_016573 Q9P107 uc002nnd.1 uc002nnd.2 uc002nnd.3 uc002nnd.4 uc002nnd.5 uc002nnd.6 This gene encodes a member of the ARHGAP family of Rho/Rac/Cdc42-like GTPase activating proteins. The encoded protein interacts with the Ras-related protein Gem through its N-terminal domain. Separately, it interacts with RhoA through a RhoGAP domain, and stimulates RhoA-dependent GTPase activity. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]. Stimulates, in vitro and in vivo, the GTPase activity of RhoA. Interacts with GEM through its N-terminal. Q9P107; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-11603420, EBI-2825900; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9P107-1; Sequence=Displayed; Name=2; IsoId=Q9P107-2; Sequence=VSP_056142; GTPase activator activity protein binding nucleoplasm cytosol plasma membrane signal transduction negative regulation of GTPase activity intracellular signal transduction positive regulation of GTPase activity metal ion binding regulation of small GTPase mediated signal transduction uc002nnd.1 uc002nnd.2 uc002nnd.3 uc002nnd.4 uc002nnd.5 uc002nnd.6 
ENST00000203629.3 LAG3 ENST00000203629.3 lymphocyte activating 3, transcript variant 1 (from RefSeq NM_002286.6) A8K7T9 ENST00000203629.1 ENST00000203629.2 FDC LAG3 LAG3_HUMAN NM_002286 P18627 Q7Z643 uc001qqt.1 uc001qqt.2 uc001qqt.3 uc001qqt.4 uc001qqt.5 uc001qqt.6 Lymphocyte-activation protein 3 belongs to Ig superfamily and contains 4 extracellular Ig-like domains. The LAG3 gene contains 8 exons. The sequence data, exon/intron organization, and chromosomal localization all indicate a close relationship of LAG3 to CD4. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by published experimental evidence. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.544442.1, AK292104.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000203629.3/ ENSP00000203629.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Lymphocyte activation gene 3 protein: Inhibitory receptor on antigen activated T-cells (PubMed:7805750, PubMed:8647185, PubMed:20421648). Delivers inhibitory signals upon binding to ligands, such as FGL1 (By similarity). FGL1 constitutes a major ligand of LAG3 and is responsible for LAG3 T-cell inhibitory function (By similarity). Following TCR engagement, LAG3 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation (By similarity). May inhibit antigen-specific T-cell activation in synergy with PDCD1/PD-1, possibly by acting as a coreceptor for PDCD1/PD-1 (By similarity). Negatively regulates the proliferation, activation, effector function and homeostasis of both CD8(+) and CD4(+) T-cells (PubMed:7805750, PubMed:8647185, PubMed:20421648). Also mediates immune tolerance: constitutively expressed on a subset of regulatory T-cells (Tregs) and contributes to their suppressive function (By similarity). Also acts as a negative regulator of plasmacytoid dendritic cell (pDCs) activation (By similarity). Binds MHC class II (MHC-II); the precise role of MHC-II-binding is however unclear (PubMed:8647185). [Secreted lymphocyte activation gene 3 protein]: May function as a ligand for MHC class II (MHC-II) on antigen-presenting cells (APC), promoting APC activation/maturation and driving Th1 immune response. Interacts with MHC class II (MHC-II); selectively recognizes stable complexes of peptide and MHC-II (PubMed:1692078, PubMed:7589152, PubMed:8647185, PubMed:9159144). Interacts with FGL1 (via the Fibrinogen C-terminal domain) (PubMed:30580966). P18627; Q08830: FGL1; NbExp=3; IntAct=EBI-2830752, EBI-3934830; P18627; Q71KU9: Fgl1; Xeno; NbExp=2; IntAct=EBI-2830752, EBI-34579174; [Lymphocyte activation gene 3 protein]: Cell membrane ingle-pass type I membrane protein [Secreted lymphocyte activation gene 3 protein]: Secreted Note=Produced following cleavage of the main chain. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P18627-1; Sequence=Displayed; Name=2; IsoId=P18627-2; Sequence=VSP_056311, VSP_056312; Primarily expressed in activated T-cells and a subset of natural killer (NK) cells. Expression is induced by interleukin-2 (IL2), interleukin-7 (IL7) and interleukin-12 (IL12A and IL12B) on activated T-cells. [Lymphocyte activation gene 3 protein]: The KIEELE motif is required for interaction with downstream signaling molecules. [Lymphocyte activation gene 3 protein]: Proteolytically cleaved by ADAM10 and ADAM17 within the connecting peptide region, leading to release of Secreted lymphocyte activation gene 3 protein (sLAG-3). ADAM10 mediates constitutive cleavage, but cleavage increases following T-cell activation, whereas shedding by ADAM17 is induced by TCR signaling in a PRKCQ-dependent manner. Belongs to the LAG3 family. adaptive immune response plasmacytoid dendritic cell activation immune system process antigen binding transmembrane signaling receptor activity protein binding extracellular region plasma membrane cell surface receptor signaling pathway external side of plasma membrane membrane integral component of membrane antigen processing and presentation of exogenous peptide antigen via MHC class II MHC class II protein binding negative regulation of interleukin-2 biosynthetic process negative regulation of regulatory T cell differentiation positive regulation of natural killer cell mediated cytotoxicity regulation of immune response negative regulation of T cell activation uc001qqt.1 uc001qqt.2 uc001qqt.3 uc001qqt.4 uc001qqt.5 uc001qqt.6 
ENST00000203630.10 MLF2 ENST00000203630.10 myeloid leukemia factor 2, transcript variant 2 (from RefSeq NM_001382226.1) ENST00000203630.1 ENST00000203630.2 ENST00000203630.3 ENST00000203630.4 ENST00000203630.5 ENST00000203630.6 ENST00000203630.7 ENST00000203630.8 ENST00000203630.9 MLF2 NM_001382226 Q5U0N1 Q5U0N1_HUMAN hCG_25928 uc001qqp.1 uc001qqp.2 uc001qqp.3 uc001qqp.4 uc001qqp.5 Cytoplasm Belongs to the MLF family. nucleus uc001qqp.1 uc001qqp.2 uc001qqp.3 uc001qqp.4 uc001qqp.5 
ENST00000203664.10 OTUB2 ENST00000203664.10 OTU deubiquitinase, ubiquitin aldehyde binding 2 (from RefSeq NM_023112.4) C14orf137 ENST00000203664.1 ENST00000203664.2 ENST00000203664.3 ENST00000203664.4 ENST00000203664.5 ENST00000203664.6 ENST00000203664.7 ENST00000203664.8 ENST00000203664.9 NM_023112 OTB2 OTU2 OTUB2_HUMAN Q6IA10 Q96DC9 Q9H6T1 uc001yci.1 uc001yci.2 uc001yci.3 uc001yci.4 uc001yci.5 This gene encodes one of several deubiquitylating enzymes. Ubiquitin modification of proteins is needed for their stability and function; to reverse the process, deubiquityling enzymes remove ubiquitin. This protein contains an OTU domain and binds Ubal (ubiquitin aldehyde); an active cysteine protease site is present in the OTU domain. [provided by RefSeq, Aug 2011]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK025569.1, SRR1803612.175176.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000203664.10/ ENSP00000203664.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence=; Q96DC9; Q96B67: ARRDC3; NbExp=8; IntAct=EBI-746259, EBI-2875665; Q96DC9; P54252: ATXN3; NbExp=9; IntAct=EBI-746259, EBI-946046; Q96DC9; Q9H305: CDIP1; NbExp=3; IntAct=EBI-746259, EBI-2876678; Q96DC9; Q16630: CPSF6; NbExp=3; IntAct=EBI-746259, EBI-358410; Q96DC9; Q15038: DAZAP2; NbExp=5; IntAct=EBI-746259, EBI-724310; Q96DC9; Q92567: FAM168A; NbExp=5; IntAct=EBI-746259, EBI-7957930; Q96DC9; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-746259, EBI-11978259; Q96DC9; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-746259, EBI-741037; Q96DC9; O15344: MID1; NbExp=3; IntAct=EBI-746259, EBI-2340316; Q96DC9; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-746259, EBI-10172526; Q96DC9; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-746259, EBI-373524; Q96DC9; Q53GA4: PHLDA2; NbExp=3; IntAct=EBI-746259, EBI-4402464; Q96DC9; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-746259, EBI-373552; Q96DC9; Q969W9-2: PMEPA1; NbExp=3; IntAct=EBI-746259, EBI-13318883; Q96DC9; Q04864: REL; NbExp=3; IntAct=EBI-746259, EBI-307352; Q96DC9; Q04864-2: REL; NbExp=3; IntAct=EBI-746259, EBI-10829018; Q96DC9; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-746259, EBI-747107; Q96DC9; Q8N0X7: SPART; NbExp=3; IntAct=EBI-746259, EBI-2643803; Q96DC9; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-746259, EBI-11952721; Q96DC9; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-746259, EBI-10175039; Q96DC9; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-746259, EBI-359276; Q96DC9; Q9BYV2: TRIM54; NbExp=4; IntAct=EBI-746259, EBI-2130429; Q96DC9; Q9BZR9: TRIM8; NbExp=7; IntAct=EBI-746259, EBI-2340370; Q96DC9-2; P54252: ATXN3; NbExp=9; IntAct=EBI-25973449, EBI-946046; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96DC9-1; Sequence=Displayed; Name=2; IsoId=Q96DC9-2; Sequence=VSP_009465; Widely expressed. Expressed at higher level in brain. In the structure described by PubMed:15258613, the Asp- 48 active site of the catalytic triad is located too far to interact directly with the active site His-224. A possible explanation is that OTUB2 is in inactive conformation in absence of ubiquitin and a conformation change may move Asp-48 in the proximity of His-224 in presence of ubiquitin substrate. Belongs to the peptidase C65 family. thiol-dependent ubiquitin-specific protease activity protein binding nucleus proteolysis peptidase activity cysteine-type peptidase activity protein deubiquitination hydrolase activity NEDD8-specific protease activity protein K11-linked deubiquitination thiol-dependent ubiquitinyl hydrolase activity ubiquitin binding protein K63-linked deubiquitination protein K48-linked deubiquitination uc001yci.1 uc001yci.2 uc001yci.3 uc001yci.4 uc001yci.5 
ENST00000204517.11 TFAP4 ENST00000204517.11 transcription factor AP-4 (from RefSeq NM_003223.3) BHLHC41 ENST00000204517.1 ENST00000204517.10 ENST00000204517.2 ENST00000204517.3 ENST00000204517.4 ENST00000204517.5 ENST00000204517.6 ENST00000204517.7 ENST00000204517.8 ENST00000204517.9 NM_003223 O60409 Q01664 TFAP4_HUMAN uc010uxg.1 uc010uxg.2 uc010uxg.3 uc010uxg.4 Transcription factors of the basic helix-loop-helix-zipper (bHLH-ZIP) family contain a basic domain, which is used for DNA binding, and HLH and ZIP domains, which are used for oligomerization. Transcription factor AP4 activates both viral and cellular genes by binding to the symmetrical DNA sequence CAGCTG (Mermod et al., 1988 [PubMed 2833704]; Hu et al., 1990 [PubMed 2123466]).[supplied by OMIM, Jul 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: S73885.1, SRR3476690.494405.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145245, SAMEA2467147 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000204517.11/ ENSP00000204517.6 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Transcription factor that activates both viral and cellular genes by binding to the symmetrical DNA sequence 5'-CAGCTG-3'. Efficient DNA binding requires dimerization with another bHLH protein. Homodimer. Q01664; Q96IF1: AJUBA; NbExp=3; IntAct=EBI-2514218, EBI-949782; Q01664; Q96B26: EXOSC8; NbExp=6; IntAct=EBI-2514218, EBI-371922; Q01664; P55040: GEM; NbExp=2; IntAct=EBI-2514218, EBI-744104; Q01664; Q08379: GOLGA2; NbExp=6; IntAct=EBI-2514218, EBI-618309; Q01664; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2514218, EBI-6509505; Q01664; Q92876: KLK6; NbExp=3; IntAct=EBI-2514218, EBI-2432309; Q01664; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-2514218, EBI-348259; Q01664; P17568: NDUFB7; NbExp=3; IntAct=EBI-2514218, EBI-1246238; Q01664; P26045: PTPN3; NbExp=3; IntAct=EBI-2514218, EBI-1047946; Q01664; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-2514218, EBI-12025260; Q01664; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-2514218, EBI-750487; Q01664; Q13077: TRAF1; NbExp=6; IntAct=EBI-2514218, EBI-359224; Q01664; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-2514218, EBI-3650647; Q01664; Q2NL98: VMAC; NbExp=3; IntAct=EBI-2514218, EBI-2803134; Nucleus. nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus mitochondrion regulation of transcription from RNA polymerase II promoter DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator negative regulation of cell proliferation negative regulation of gene expression transcriptional repressor complex protein homodimerization activity histone deacetylase binding positive regulation of apoptotic process negative regulation of DNA binding sequence-specific DNA binding negative regulation by host of viral transcription positive regulation by host of viral transcription transcription regulatory region DNA binding negative regulation of cyclin-dependent protein serine/threonine kinase activity negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein dimerization activity macromolecular complex assembly E-box binding negative regulation of cell cycle arrest cellular response to dexamethasone stimulus regulation of mitotic cell cycle phase transition positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway transcription coactivator activity protein heterodimerization activity uc010uxg.1 uc010uxg.2 uc010uxg.3 uc010uxg.4 
ENST00000204549.9 PDCD7 ENST00000204549.9 programmed cell death 7 (from RefSeq NM_005707.2) ENST00000204549.1 ENST00000204549.2 ENST00000204549.3 ENST00000204549.4 ENST00000204549.5 ENST00000204549.6 ENST00000204549.7 ENST00000204549.8 NM_005707 PDCD7_HUMAN Q8N8D1 Q96AK8 Q9Y6D7 uc002aol.1 uc002aol.2 uc002aol.3 uc002aol.4 This gene encodes a 59 kDa protein that is associated with the U11 small nuclear ribonucleoprotein (snRNP), which is a component of the minor U12-type spliceosome responsible for catalyzing pre-mRNA splicing of U12-type introns. [provided by RefSeq, Dec 2010]. ##Evidence-Data-START## Transcript exon combination :: AK096970.1, SRR1803613.51790.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2159764, SAMN03267755 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000204549.9/ ENSP00000204549.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Promotes apoptosis when overexpressed. Interacts with RBM40. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Nucleus mRNA splicing, via spliceosome nucleus nucleoplasm U12-type spliceosomal complex apoptotic process RNA splicing response to glucocorticoid uc002aol.1 uc002aol.2 uc002aol.3 uc002aol.4 
ENST00000204566.7 SPG21 ENST00000204566.7 SPG21 abhydrolase domain containing, maspardin, transcript variant 1 (from RefSeq NM_016630.7) ACP33 B4DW44 BM-019 ENST00000204566.1 ENST00000204566.2 ENST00000204566.3 ENST00000204566.4 ENST00000204566.5 ENST00000204566.6 GL010 NM_016630 Q6ZMB6 Q9NZD8 SPG21_HUMAN uc002aoe.1 uc002aoe.2 uc002aoe.3 uc002aoe.4 uc002aoe.5 uc002aoe.6 The protein encoded by this gene binds to the hydrophobic C-terminal amino acids of CD4 which are involved in repression of T cell activation. The interaction with CD4 is mediated by the noncatalytic alpha/beta hydrolase fold domain of this protein. It is thus proposed that this gene product modulates the stimulatory activity of CD4. Mutations in this gene are associated with autosomal recessive spastic paraplegia 21 (SPG21), also known as mast syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2014]. May play a role as a negative regulatory factor in CD4- dependent T-cell activation. Interacts with CD4. Interacts with ALDH16A1. Q9NZD8; Q9NPJ3: ACOT13; NbExp=3; IntAct=EBI-742688, EBI-1045357; Q9NZD8; Q6RW13: AGTRAP; NbExp=5; IntAct=EBI-742688, EBI-741181; Q9NZD8; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-742688, EBI-11522760; Q9NZD8; Q53H80: AKIRIN2; NbExp=11; IntAct=EBI-742688, EBI-742928; Q9NZD8; P02654: APOC1; NbExp=3; IntAct=EBI-742688, EBI-1220105; Q9NZD8; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-742688, EBI-714543; Q9NZD8; Q96BM9: ARL8A; NbExp=3; IntAct=EBI-742688, EBI-4401082; Q9NZD8; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-742688, EBI-36513937; Q9NZD8; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-742688, EBI-742909; Q9NZD8; P56385: ATP5ME; NbExp=3; IntAct=EBI-742688, EBI-2270000; Q9NZD8; Q8N5M1: ATPAF2; NbExp=18; IntAct=EBI-742688, EBI-1166928; Q9NZD8; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-742688, EBI-10193358; Q9NZD8; Q8WZ55: BSND; NbExp=3; IntAct=EBI-742688, EBI-7996695; Q9NZD8; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-742688, EBI-10171570; Q9NZD8; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-742688, EBI-11974185; Q9NZD8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-742688, EBI-10175300; Q9NZD8; O14519: CDK2AP1; NbExp=3; IntAct=EBI-742688, EBI-1052532; Q9NZD8; P42772: CDKN2B; NbExp=6; IntAct=EBI-742688, EBI-711280; Q9NZD8; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-742688, EBI-742887; Q9NZD8; Q9Y6K0: CEPT1; NbExp=3; IntAct=EBI-742688, EBI-1237183; Q9NZD8; O43822-4: CFAP410; NbExp=3; IntAct=EBI-742688, EBI-11943144; Q9NZD8; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-742688, EBI-7062247; Q9NZD8; Q8N7P3: CLDN22; NbExp=3; IntAct=EBI-742688, EBI-17766761; Q9NZD8; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-742688, EBI-17278014; Q9NZD8; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-742688, EBI-2548702; Q9NZD8; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-742688, EBI-11522780; Q9NZD8; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-742688, EBI-1054315; Q9NZD8; Q96JB2-2: COG3; NbExp=3; IntAct=EBI-742688, EBI-9091495; Q9NZD8; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-742688, EBI-3866319; Q9NZD8; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-742688, EBI-11523759; Q9NZD8; O43186: CRX; NbExp=3; IntAct=EBI-742688, EBI-748171; Q9NZD8; P02489: CRYAA; NbExp=7; IntAct=EBI-742688, EBI-6875961; Q9NZD8; Q8WUE5: CT55; NbExp=3; IntAct=EBI-742688, EBI-6873363; Q9NZD8; O43310-2: CTIF; NbExp=3; IntAct=EBI-742688, EBI-12180013; Q9NZD8; Q9NRF8: CTPS2; NbExp=4; IntAct=EBI-742688, EBI-740874; Q9NZD8; Q9NTM9: CUTC; NbExp=8; IntAct=EBI-742688, EBI-714918; Q9NZD8; Q9H773: DCTPP1; NbExp=3; IntAct=EBI-742688, EBI-723569; Q9NZD8; Q86UW9: DTX2; NbExp=7; IntAct=EBI-742688, EBI-740376; Q9NZD8; Q8TDB6: DTX3L; NbExp=10; IntAct=EBI-742688, EBI-2340392; Q9NZD8; Q5JST6: EFHC2; NbExp=6; IntAct=EBI-742688, EBI-2349927; Q9NZD8; O60739: EIF1B; NbExp=3; IntAct=EBI-742688, EBI-1043343; Q9NZD8; Q15056-2: EIF4H; NbExp=6; IntAct=EBI-742688, EBI-12222405; Q9NZD8; O00167-2: EYA2; NbExp=3; IntAct=EBI-742688, EBI-12807776; Q9NZD8; Q8IWE2: FAM114A1; NbExp=7; IntAct=EBI-742688, EBI-2686288; Q9NZD8; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-742688, EBI-12845222; Q9NZD8; Q9H4M3-2: FBXO44; NbExp=3; IntAct=EBI-742688, EBI-12104696; Q9NZD8; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-742688, EBI-11533409; Q9NZD8; Q05329: GAD2; NbExp=3; IntAct=EBI-742688, EBI-9304251; Q9NZD8; O95995: GAS8; NbExp=3; IntAct=EBI-742688, EBI-1052570; Q9NZD8; O14893: GEMIN2; NbExp=3; IntAct=EBI-742688, EBI-443648; Q9NZD8; P57678: GEMIN4; NbExp=3; IntAct=EBI-742688, EBI-356700; Q9NZD8; Q9UJY4: GGA2; NbExp=4; IntAct=EBI-742688, EBI-447646; Q9NZD8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-742688, EBI-618309; Q9NZD8; Q9Y3E0: GOLT1B; NbExp=3; IntAct=EBI-742688, EBI-4402607; Q9NZD8; Q9HAV7: GRPEL1; NbExp=3; IntAct=EBI-742688, EBI-1043499; Q9NZD8; P31943: HNRNPH1; NbExp=3; IntAct=EBI-742688, EBI-351590; Q9NZD8; P00492: HPRT1; NbExp=3; IntAct=EBI-742688, EBI-748210; Q9NZD8; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-742688, EBI-18053395; Q9NZD8; Q9UKT9: IKZF3; NbExp=6; IntAct=EBI-742688, EBI-747204; Q9NZD8; Q0VD86: INCA1; NbExp=6; IntAct=EBI-742688, EBI-6509505; Q9NZD8; Q15051-2: IQCB1; NbExp=3; IntAct=EBI-742688, EBI-11944935; Q9NZD8; Q7L273: KCTD9; NbExp=3; IntAct=EBI-742688, EBI-4397613; Q9NZD8; P13646: KRT13; NbExp=3; IntAct=EBI-742688, EBI-1223876; Q9NZD8; P19012: KRT15; NbExp=3; IntAct=EBI-742688, EBI-739566; Q9NZD8; P08727: KRT19; NbExp=3; IntAct=EBI-742688, EBI-742756; Q9NZD8; Q15323: KRT31; NbExp=3; IntAct=EBI-742688, EBI-948001; Q9NZD8; O95214: LEPROTL1; NbExp=3; IntAct=EBI-742688, EBI-750776; Q9NZD8; P25800: LMO1; NbExp=3; IntAct=EBI-742688, EBI-8639312; Q9NZD8; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-742688, EBI-739832; Q9NZD8; Q8N112: LSMEM2; NbExp=3; IntAct=EBI-742688, EBI-10264855; Q9NZD8; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-742688, EBI-10268010; Q9NZD8; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-742688, EBI-10172526; Q9NZD8; O95563: MPC2; NbExp=3; IntAct=EBI-742688, EBI-719403; Q9NZD8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-742688, EBI-11522433; Q9NZD8; Q9HB07: MYG1; NbExp=3; IntAct=EBI-742688, EBI-709754; Q9NZD8; P15173: MYOG; NbExp=3; IntAct=EBI-742688, EBI-3906629; Q9NZD8; O15049: N4BP3; NbExp=3; IntAct=EBI-742688, EBI-2512055; Q9NZD8; Q15742: NAB2; NbExp=3; IntAct=EBI-742688, EBI-8641936; Q9NZD8; Q8N183: NDUFAF2; NbExp=3; IntAct=EBI-742688, EBI-2682365; Q9NZD8; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-742688, EBI-740897; Q9NZD8; O00746: NME4; NbExp=3; IntAct=EBI-742688, EBI-744871; Q9NZD8; P16083: NQO2; NbExp=3; IntAct=EBI-742688, EBI-358466; Q9NZD8; P20393: NR1D1; NbExp=3; IntAct=EBI-742688, EBI-2811738; Q9NZD8; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-742688, EBI-1042642; Q9NZD8; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-742688, EBI-741048; Q9NZD8; P26367: PAX6; NbExp=3; IntAct=EBI-742688, EBI-747278; Q9NZD8; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-742688, EBI-10302990; Q9NZD8; Q9H0N5: PCBD2; NbExp=3; IntAct=EBI-742688, EBI-634289; Q9NZD8; P12004: PCNA; NbExp=3; IntAct=EBI-742688, EBI-358311; Q9NZD8; O76074: PDE5A; NbExp=3; IntAct=EBI-742688, EBI-9023531; Q9NZD8; Q9UBV8: PEF1; NbExp=6; IntAct=EBI-742688, EBI-724639; Q9NZD8; Q99471: PFDN5; NbExp=3; IntAct=EBI-742688, EBI-357275; Q9NZD8; Q04941: PLP2; NbExp=3; IntAct=EBI-742688, EBI-608347; Q9NZD8; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-742688, EBI-10171633; Q9NZD8; Q5JR12: PPM1J; NbExp=3; IntAct=EBI-742688, EBI-13292717; Q9NZD8; P60891: PRPS1; NbExp=8; IntAct=EBI-742688, EBI-749195; Q9NZD8; Q9NRG1: PRTFDC1; NbExp=3; IntAct=EBI-742688, EBI-739759; Q9NZD8; P28070: PSMB4; NbExp=3; IntAct=EBI-742688, EBI-603350; Q9NZD8; Q15257-2: PTPA; NbExp=5; IntAct=EBI-742688, EBI-12164121; Q9NZD8; Q9UI14: RABAC1; NbExp=7; IntAct=EBI-742688, EBI-712367; Q9NZD8; O43502-2: RAD51C; NbExp=3; IntAct=EBI-742688, EBI-14233893; Q9NZD8; Q96HR9: REEP6; NbExp=4; IntAct=EBI-742688, EBI-750345; Q9NZD8; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-742688, EBI-14065960; Q9NZD8; Q04864-2: REL; NbExp=3; IntAct=EBI-742688, EBI-10829018; Q9NZD8; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-742688, EBI-1378139; Q9NZD8; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-742688, EBI-747925; Q9NZD8; P39019: RPS19; NbExp=3; IntAct=EBI-742688, EBI-354451; Q9NZD8; Q17RB0: RTL8B; NbExp=3; IntAct=EBI-742688, EBI-10238588; Q9NZD8; P04271: S100B; NbExp=7; IntAct=EBI-742688, EBI-458391; Q9NZD8; Q01826: SATB1; NbExp=3; IntAct=EBI-742688, EBI-743747; Q9NZD8; O15126: SCAMP1; NbExp=3; IntAct=EBI-742688, EBI-954338; Q9NZD8; Q99719: SEPTIN5; NbExp=3; IntAct=EBI-742688, EBI-373345; Q9NZD8; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-742688, EBI-2854842; Q9NZD8; Q99961: SH3GL1; NbExp=3; IntAct=EBI-742688, EBI-697911; Q9NZD8; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-742688, EBI-13389236; Q9NZD8; O60504: SORBS3; NbExp=3; IntAct=EBI-742688, EBI-741237; Q9NZD8; Q8WW14-2: SPMIP5; NbExp=3; IntAct=EBI-742688, EBI-12831628; Q9NZD8; Q8NCR6: SPMIP6; NbExp=3; IntAct=EBI-742688, EBI-10269322; Q9NZD8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-742688, EBI-5235340; Q9NZD8; Q7Z698: SPRED2; NbExp=10; IntAct=EBI-742688, EBI-7082156; Q9NZD8; A0A286YEY3: SRGAP2B; NbExp=3; IntAct=EBI-742688, EBI-17766455; Q9NZD8; Q9BWG4: SSBP4; NbExp=3; IntAct=EBI-742688, EBI-744719; Q9NZD8; Q6NVH7: SWSAP1; NbExp=6; IntAct=EBI-742688, EBI-5281637; Q9NZD8; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-742688, EBI-12187159; Q9NZD8; O43761: SYNGR3; NbExp=5; IntAct=EBI-742688, EBI-11321949; Q9NZD8; P08247: SYP; NbExp=3; IntAct=EBI-742688, EBI-9071725; Q9NZD8; Q99081: TCF12; NbExp=4; IntAct=EBI-742688, EBI-722877; Q9NZD8; P15884: TCF4; NbExp=3; IntAct=EBI-742688, EBI-533224; Q9NZD8; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-742688, EBI-750487; Q9NZD8; Q92734: TFG; NbExp=6; IntAct=EBI-742688, EBI-357061; Q9NZD8; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-742688, EBI-1105213; Q9NZD8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-742688, EBI-11741437; Q9NZD8; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-742688, EBI-12876824; Q9NZD8; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-742688, EBI-11528917; Q9NZD8; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-742688, EBI-12815137; Q9NZD8; P55327-2: TPD52; NbExp=3; IntAct=EBI-742688, EBI-12124194; Q9NZD8; Q13077: TRAF1; NbExp=6; IntAct=EBI-742688, EBI-359224; Q9NZD8; Q12933: TRAF2; NbExp=8; IntAct=EBI-742688, EBI-355744; Q9NZD8; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-742688, EBI-492476; Q9NZD8; Q14142: TRIM14; NbExp=3; IntAct=EBI-742688, EBI-2820256; Q9NZD8; P36406: TRIM23; NbExp=3; IntAct=EBI-742688, EBI-740098; Q9NZD8; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-742688, EBI-9867283; Q9NZD8; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-742688, EBI-2130429; Q9NZD8; Q9C026: TRIM9; NbExp=6; IntAct=EBI-742688, EBI-720828; Q9NZD8; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-742688, EBI-10241197; Q9NZD8; Q2TAA8: TSNAXIP1; NbExp=3; IntAct=EBI-742688, EBI-6872498; Q9NZD8; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-742688, EBI-8656864; Q9NZD8; P10599: TXN; NbExp=6; IntAct=EBI-742688, EBI-594644; Q9NZD8; Q9NX01: TXNL4B; NbExp=6; IntAct=EBI-742688, EBI-10309345; Q9NZD8; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-742688, EBI-12068150; Q9NZD8; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-742688, EBI-739895; Q9NZD8; Q2NL98: VMAC; NbExp=3; IntAct=EBI-742688, EBI-2803134; Q9NZD8; Q9BRG1: VPS25; NbExp=3; IntAct=EBI-742688, EBI-741945; Q9NZD8; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-742688, EBI-12287587; Q9NZD8; Q9H0C1: ZMYND12; NbExp=5; IntAct=EBI-742688, EBI-12030590; Q9NZD8; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-742688, EBI-745520; Q9NZD8; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-742688, EBI-9977294; Q9NZD8; P03410: tax; Xeno; NbExp=3; IntAct=EBI-742688, EBI-9676218; Cytoplasm, cytosol Membrane ; Peripheral membrane protein Endosome membrane ; Peripheral membrane protein Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein Note=Partially localized in the cytosol but also accumulated on an intracellular vesicular compartment. Colocalizes with CD4 on endosomal/trans-Golgi network. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NZD8-1; Sequence=Displayed; Name=2; IsoId=Q9NZD8-2; Sequence=VSP_041512; Expressed in all tissues tested, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed in J.CaM1.6, HuT 78 and HeLa cell lines (at protein level). Spastic paraplegia 21, autosomal recessive (SPG21) [MIM:248900]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG21 is associated with dementia and other central nervous system abnormalities. Subtle childhood abnormalities may be present, but the main features develop in early adulthood. The disease is slowly progressive, and cerebellar and extrapyramidal signs are also found in patients with advanced disease. Patients have a thin corpus callosum and white-matter abnormalities. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the AB hydrolase superfamily. protein binding cytoplasm endosome Golgi apparatus cytosol endosome membrane membrane trans-Golgi network transport vesicle CD4 receptor binding intracellular membrane-bounded organelle antigen receptor-mediated signaling pathway uc002aoe.1 uc002aoe.2 uc002aoe.3 uc002aoe.4 uc002aoe.5 uc002aoe.6 
ENST00000204604.6 CHRD ENST00000204604.6 chordin, transcript variant 1 (from RefSeq NM_003741.4) CHRD_HUMAN ENST00000204604.1 ENST00000204604.2 ENST00000204604.3 ENST00000204604.4 ENST00000204604.5 NM_003741 O95254 Q2M1I8 Q6UW83 Q9H2D3 Q9H2W8 Q9H2W9 Q9H2X0 Q9P0Z2 Q9P0Z3 Q9P0Z4 Q9P0Z5 UNQ217/PRO243 uc003fov.1 uc003fov.2 uc003fov.3 uc003fov.4 This gene encodes a secreted protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta-like bone morphogenetic proteins and sequestering them in latent complexes. The encoded protein may also have roles in organogenesis and during adulthood. It has been suggested that this gene could be a candidate gene for Cornelia de Lange syndrome. Reduced expression of this gene results in enhanced bone regeneration. Alternative splicing results in multiple transcript variants. Other alternative splice variants have been described but their full length sequence has not been determined. [provided by RefSeq, Jan 2015]. Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes (By similarity). Interacts with TWSG1 and/or BMP4. Q9H2X0; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-947551, EBI-10173507; Q9H2X0; P13497: BMP1; NbExp=2; IntAct=EBI-947551, EBI-489827; Q9H2X0; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-947551, EBI-744545; Q9H2X0; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-947551, EBI-12593838; Q9H2X0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-947551, EBI-3867333; Q9H2X0; P15976-2: GATA1; NbExp=3; IntAct=EBI-947551, EBI-9090198; Q9H2X0; P49639: HOXA1; NbExp=4; IntAct=EBI-947551, EBI-740785; Q9H2X0; Q0VD86: INCA1; NbExp=3; IntAct=EBI-947551, EBI-6509505; Q9H2X0; O76011: KRT34; NbExp=3; IntAct=EBI-947551, EBI-1047093; Q9H2X0; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-947551, EBI-11959885; Q9H2X0; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-947551, EBI-11749135; Q9H2X0; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-947551, EBI-10172150; Q9H2X0; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-947551, EBI-10172290; Q9H2X0; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-947551, EBI-10171774; Q9H2X0; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-947551, EBI-10172052; Q9H2X0; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-947551, EBI-10210845; Q9H2X0; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-947551, EBI-10176379; Q9H2X0; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-947551, EBI-11953334; Q9H2X0; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-947551, EBI-12196745; Q9H2X0; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-947551, EBI-1048945; Q9H2X0; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-947551, EBI-739863; Q9H2X0; Q9BYR5: KRTAP4-2; NbExp=6; IntAct=EBI-947551, EBI-10172511; Q9H2X0; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-947551, EBI-3958099; Q9H2X0; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-947551, EBI-1044640; Q9H2X0; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-947551, EBI-1043191; Q9H2X0; Q5T751: LCE1C; NbExp=3; IntAct=EBI-947551, EBI-12224199; Q9H2X0; Q5T754: LCE1F; NbExp=3; IntAct=EBI-947551, EBI-11958008; Q9H2X0; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-947551, EBI-11955689; Q9H2X0; O14910: LIN7A; NbExp=3; IntAct=EBI-947551, EBI-2513988; Q9H2X0; P50222: MEOX2; NbExp=3; IntAct=EBI-947551, EBI-748397; Q9H2X0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-947551, EBI-16439278; Q9H2X0; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-947551, EBI-945833; Q9H2X0; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-947551, EBI-22310682; Q9H2X0; Q92570: NR4A3; NbExp=3; IntAct=EBI-947551, EBI-13644623; Q9H2X0; P32242: OTX1; NbExp=3; IntAct=EBI-947551, EBI-740446; Q9H2X0; O15162: PLSCR1; NbExp=3; IntAct=EBI-947551, EBI-740019; Q9H2X0; Q12837: POU4F2; NbExp=3; IntAct=EBI-947551, EBI-17236143; Q9H2X0; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-947551, EBI-3918154; Q9H2X0; Q16348: SLC15A2; NbExp=3; IntAct=EBI-947551, EBI-12806032; Q9H2X0; P84022: SMAD3; NbExp=2; IntAct=EBI-947551, EBI-347161; Q9H2X0; O43609: SPRY1; NbExp=3; IntAct=EBI-947551, EBI-3866665; Q9H2X0; O43597: SPRY2; NbExp=3; IntAct=EBI-947551, EBI-742487; Q9H2X0; O43610: SPRY3; NbExp=3; IntAct=EBI-947551, EBI-12290641; Q9H2X0; Q8IWZ5: TRIM42; NbExp=5; IntAct=EBI-947551, EBI-5235829; Q9H2X0; O14817: TSPAN4; NbExp=3; IntAct=EBI-947551, EBI-8652667; Secreted Event=Alternative splicing; Named isoforms=5; Comment=Experimental confirmation may be lacking for some isoforms.; Name=1; IsoId=Q9H2X0-1; Sequence=Displayed; Name=2; IsoId=Q9H2X0-2; Sequence=VSP_001069, VSP_001070; Name=3; IsoId=Q9H2X0-3; Sequence=VSP_001071, VSP_001072; Name=4; IsoId=Q9H2X0-4; Sequence=VSP_001073, VSP_001074; Name=5; IsoId=Q9H2X0-5; Sequence=VSP_001075; Expressed at the highest level in liver. Cleaved by tolloid proteases; cleavage participates in dorsoventral patterning during early development. [Isoform 2]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. [Isoform 3]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. [Isoform 4]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the chordin family. skeletal system development osteoblast differentiation gastrulation with mouth forming second mesoderm formation positive regulation of mesenchymal cell proliferation protein binding extracellular region extracellular space multicellular organism development pattern specification process central nervous system development heparin binding dorsal/ventral pattern formation cytokine binding BMP signaling pathway involved in spinal cord dorsal/ventral patterning negative regulation of cell migration negative regulation of BMP signaling pathway forebrain development floor plate development syndecan binding negative regulation of osteoblast differentiation positive regulation of cell adhesion uc003fov.1 uc003fov.2 uc003fov.3 uc003fov.4 
ENST00000204679.9 GNPTG ENST00000204679.9 N-acetylglucosamine-1-phosphate transferase subunit gamma (from RefSeq NM_032520.5) B2R556 C16orf27 CAB56184 ENST00000204679.1 ENST00000204679.2 ENST00000204679.3 ENST00000204679.4 ENST00000204679.5 ENST00000204679.6 ENST00000204679.7 ENST00000204679.8 GNPTAG GNPTG_HUMAN LP2537 NM_032520 Q6XYD7 Q96L13 Q9UJJ9 uc002clm.1 uc002clm.2 uc002clm.3 uc002clm.4 uc002clm.5 This gene encodes the gamma sunbunit of the N-acetylglucosamine-1-phosphotransferase complex. This hexameric complex, composed of alpha, beta and gamma subunits, catalyzes the first step in synthesis of a mannose 6-phosphate lysosomal recognition marker. This enzyme complex is necessary for targeting of lysosomal hydrolases to the lysosome. Mutations in the gene encoding the gamma subunit have been associated with mucolipidosis IIIC, also known as mucolipidosis III gamma.[provided by RefSeq, Feb 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK312067.1, SRR1660803.200444.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000204679.9/ ENSP00000204679.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Non-catalytic subunit of the N-acetylglucosamine-1- phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. Binds and presents the high mannose glycans of the acceptor to the catalytic alpha and beta subunits (GNPTAB). Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the oligosaccharides of acid hydrolase acceptors. Homodimer; disulfide-linked. Hexamer of two alpha (GNPTAB), two beta (GNPTAB) and two gamma (GNPTG) subunits; disulfide-linked. The alpha and/or the beta subunits of the enzyme constitute the catalytic subunits. Q9UJJ9; Q3T906: GNPTAB; NbExp=6; IntAct=EBI-372067, EBI-1104907; Secreted Golgi apparatus Widely expressed. Cys-245 mediates the formation of the interchain disulfide bond for formation of the homodimer. Cys-142, Cys-157 and Cys-169 are involved in intramolecular disulfide bonds formation (By similarity). Mucolipidosis type III complementation group C (MLIIIC) [MIM:252605]: Autosomal recessive disease of lysosomal hydrolase trafficking. Unlike the related diseases, mucolipidosis II and IIIA, the enzyme affected in mucolipidosis IIIC (GlcNAc-phosphotransferase) retains full transferase activity on synthetic substrates but lacks activity on lysosomal hydrolases. Typical clinical findings include stiffness of the hands and shoulders, claw-hand deformity, scoliosis, short stature, coarse facies, and mild intellectual disability. Radiographically, severe dysostosis multiplex of the hip is characteristic and frequently disabling. The clinical diagnosis can be confirmed by finding elevated serum lysosomal enzyme levels and/or decreased lysosomal enzyme levels in cultured fibroblasts. te=The disease is caused by variants affecting the gene represented in this entry. Note=Defects in GNPTG have been suggested to play a role in susceptibility to persistent stuttering. Stuttering is a common speech disorder characterized by repetitions, prolongations, and interruptions in the flow of speech. Sequence=AAP34456.1; Type=Erroneous initiation; Evidence=; Golgi membrane UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity extracellular region Golgi apparatus membrane protein homodimerization activity intracellular membrane-bounded organelle carbohydrate phosphorylation extracellular exosome uc002clm.1 uc002clm.2 uc002clm.3 uc002clm.4 uc002clm.5 
ENST00000204961.5 EFNB1 ENST00000204961.5 ephrin B1 (from RefSeq NM_004429.5) D3DVU0 EFL3 EFNB1_HUMAN ENST00000204961.1 ENST00000204961.2 ENST00000204961.3 ENST00000204961.4 EPLG2 LERK2 NM_004429 P98172 uc004dxd.1 uc004dxd.2 uc004dxd.3 uc004dxd.4 uc004dxd.5 uc004dxd.6 The protein encoded by this gene is a type I membrane protein and a ligand of Eph-related receptor tyrosine kinases. It may play a role in cell adhesion and function in the development or maintenance of the nervous system. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC016649.1, U09303.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000204961.5/ ENSP00000204961.4 RefSeq Select criteria :: based on single protein-coding transcript regulatory uORF :: PMID: 23335590 ##RefSeq-Attributes-END## Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development (PubMed:8070404, PubMed:7973638). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:8070404, PubMed:7973638). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:8070404, PubMed:7973638). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity). Interacts (via PDZ-binding motif) with GRIP1 and GRIP2 (via PDZ domain 6) (PubMed:10197531). Interacts with TLE1 (PubMed:21429299). The intracellular domain peptide interacts with ZHX2; the interaction enhances ZHX2 transcriptional repression activity (By similarity). P98172; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-538287, EBI-12109402; P98172; P04626: ERBB2; NbExp=11; IntAct=EBI-538287, EBI-641062; Cell membrane ingle-pass type I membrane protein Membrane raft Note=May recruit GRIP1 and GRIP2 to membrane raft domains. [Ephrin-B1 C-terminal fragment]: Cell membrane ; Single-pass type I membrane protein [Ephrin-B1 intracellular domain]: Nucleus Note=Colocalizes with ZHX2 in the nucleus. Widely expressed (PubMed:8070404, PubMed:7973638). Detected in both neuronal and non-neuronal tissues (PubMed:8070404, PubMed:7973638). Seems to have particularly strong expression in retina, sciatic nerve, heart and spinal cord (PubMed:7973638). Up-regulated in response to TNF. Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. Proteolytically processed. The ectodomain is cleaved, probably by a metalloprotease, to produce a membrane-tethered C-terminal fragment. This fragment is then further processed by the gamma-secretase complex to yield a soluble intracellular domain peptide which can translocate to the nucleus. The intracellular domain peptide is highly labile suggesting that it is targeted for degradation by the proteasome. Craniofrontonasal syndrome (CFNS) [MIM:304110]: X-linked inherited syndrome characterized by hypertelorism, coronal synostosis with brachycephaly, downslanting palpebral fissures, clefting of the nasal tip, joint anomalies, longitudinally grooved fingernails and other digital anomalies. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the ephrin family. neural crest cell migration protein binding nucleus cytoplasm plasma membrane integral component of plasma membrane cell adhesion cell-cell signaling multicellular organism development nervous system development axon guidance embryonic pattern specification membrane integral component of membrane cell differentiation T cell costimulation positive regulation of T cell proliferation membrane raft synapse ephrin receptor binding ephrin receptor signaling pathway extracellular exosome uc004dxd.1 uc004dxd.2 uc004dxd.3 uc004dxd.4 uc004dxd.5 uc004dxd.6 
ENST00000205194.5 NAT14 ENST00000205194.5 N-acetyltransferase 14 (putative) (from RefSeq NM_020378.4) ENST00000205194.1 ENST00000205194.2 ENST00000205194.3 ENST00000205194.4 KLP1 NAT14_HUMAN NM_020378 Q8TDY7 Q8WUY8 Q9NS72 uc002qle.1 uc002qle.2 uc002qle.3 uc002qle.4 Probable acetyltransferase. May act as a transcription factor that regulates the expression of coproporphyrinogen oxidase by binding to a promoter regulatory element. Membrane ; Single-pass membrane protein Expressed in K-562 and HeLa cell lines and in brain. Belongs to the camello family. DNA binding nucleus DNA-templated transcription, initiation N-acetyltransferase activity membrane integral component of membrane transferase activity transferase activity, transferring acyl groups positive regulation of transcription, DNA-templated uc002qle.1 uc002qle.2 uc002qle.3 uc002qle.4 
ENST00000205214.11 AASDH ENST00000205214.11 aminoadipate-semialdehyde dehydrogenase, transcript variant 1 (from RefSeq NM_181806.4) A5D8V3 A5PL22 ACSF4 ACSF4_HUMAN ENST00000205214.1 ENST00000205214.10 ENST00000205214.2 ENST00000205214.3 ENST00000205214.4 ENST00000205214.5 ENST00000205214.6 ENST00000205214.7 ENST00000205214.8 ENST00000205214.9 HSPC318 NM_181806 Q4L235 Q63HK2 Q63HR7 Q6IPP8 Q6TFZ6 Q7Z5Y3 Q96BW4 Q9P064 U26 uc003hbn.1 uc003hbn.2 uc003hbn.3 uc003hbn.4 uc003hbn.5 uc003hbn.6 This gene encodes a member of the non-ribosome peptide syntesase (NRPS) enzyme family. The encoded protein contains an AMP-binding domain, PP-binding (phosphopantetheine, or pantetheine 4'phosphate-binding) domain and the Pyrrolo-quinoline quinon (PQQ) binding domain. The protein is expressed in several adult tissues. [provided by RefSeq, Apr 2016]. ##Evidence-Data-START## Transcript exon combination :: AY422212.1, AK316296.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000205214.11/ ENSP00000205214.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Covalently binds beta-alanine in an ATP-dependent manner to form a thioester bond with its phosphopantetheine group and transfers it to an, as yet, unknown acceptor. May be required for a post- translational protein modification or for post-transcriptional modification of an RNA. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q4L235-1; Sequence=Displayed; Name=2; IsoId=Q4L235-2; Sequence=VSP_030707; Name=3; IsoId=Q4L235-3; Sequence=VSP_030711, VSP_030712; Name=4; IsoId=Q4L235-4; Sequence=VSP_030710, VSP_030713; Ubiquitously expressed in adult tissues. Belongs to the ATP-dependent AMP-binding enzyme family. Sequence=CAH56482.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleotide binding catalytic activity ATP binding lipid metabolic process fatty acid metabolic process ligase activity acid-thiol ligase activity beta-alanine metabolic process amino acid activation for nonribosomal peptide biosynthetic process uc003hbn.1 uc003hbn.2 uc003hbn.3 uc003hbn.4 uc003hbn.5 uc003hbn.6 
ENST00000205402.10 DLD ENST00000205402.10 dihydrolipoamide dehydrogenase, transcript variant 1 (from RefSeq NM_000108.5) B2R5X0 B4DHG0 B4DT69 DLDH_HUMAN ENST00000205402.1 ENST00000205402.2 ENST00000205402.3 ENST00000205402.4 ENST00000205402.5 ENST00000205402.6 ENST00000205402.7 ENST00000205402.8 ENST00000205402.9 GCSL LAD NM_000108 P09622 PHE3 Q14131 Q14167 Q59EV8 Q8WTS4 uc003vet.1 uc003vet.2 uc003vet.3 uc003vet.4 uc003vet.5 uc003vet.6 This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. However, as a monomer, this protein can function as a protease. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]. Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched- chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2- oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence= Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence=; Note=Binds 1 FAD per subunit. Disruption of native heterodimer state inhibits primary dihydrolipoamide dehydrogenase activity and induces serine protease activity. Homodimer (PubMed:15946682). Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDHA (PDHA1 or PDHA2) and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (PubMed:14638692). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds) (PubMed:14638692, PubMed:20361979). The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2), DLD (dihydrolipoamide dehydrogenase; E3) and the assembly factor KGD4 (By similarity). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A (PubMed:29211711). Interacts with PDHX (PubMed:20385101, PubMed:16442803, PubMed:20160912, PubMed:20361979). P09622; P42858: HTT; NbExp=3; IntAct=EBI-353366, EBI-466029; P09622; O14713: ITGB1BP1; NbExp=3; IntAct=EBI-353366, EBI-2127319; P09622; O00330: PDHX; NbExp=7; IntAct=EBI-353366, EBI-751566; P09622; P30041: PRDX6; NbExp=3; IntAct=EBI-353366, EBI-2255129; P09622; P62258: YWHAE; NbExp=5; IntAct=EBI-353366, EBI-356498; Mitochondrion matrix Nucleus Cell projection, cilium, flagellum Cytoplasmic vesicle, secretory vesicle, acrosome Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2- oxoglutarate dehydrogenase complex is required for histone succinylation. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P09622-1; Sequence=Displayed; Name=2; IsoId=P09622-2; Sequence=VSP_055855; Name=3; IsoId=P09622-3; Sequence=VSP_055856; Tyrosine phosphorylated. Dihydrolipoamide dehydrogenase deficiency (DLDD) [MIM:246900]: An autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism. te=The disease is caused by variants affecting the gene represented in this entry. The active site is a redox-active disulfide bond. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. Sequence=BAD92940.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; acrosomal vesicle dihydrolipoyl dehydrogenase activity protein binding nucleus nucleoplasm mitochondrion mitochondrial matrix cilium acetyl-CoA biosynthetic process from pyruvate pyruvate metabolic process tricarboxylic acid cycle 2-oxoglutarate metabolic process mitochondrial electron transport, NADH to ubiquinone proteolysis lysine catabolic process gastrulation aging electron carrier activity branched-chain amino acid catabolic process lipoate metabolic process oxidoreductase activity oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor cytoplasmic vesicle motile cilium regulation of membrane potential cell projection acrosomal matrix lipoamide binding oxoglutarate dehydrogenase complex pyruvate dehydrogenase complex cell redox homeostasis sperm capacitation flavin adenine dinucleotide binding dihydrolipoamide metabolic process NAD binding oxidation-reduction process mitochondrial acetyl-CoA biosynthetic process from pyruvate pyruvate dehydrogenase (NAD+) activity uc003vet.1 uc003vet.2 uc003vet.3 uc003vet.4 uc003vet.5 uc003vet.6 
ENST00000205557.12 ABCC6 ENST00000205557.12 ATP binding cassette subfamily C member 6, transcript variant 3 (from RefSeq NM_001351800.1) A2RRN8 A8KIG6 A8Y988 ARA E7ESW8 ENST00000205557.1 ENST00000205557.10 ENST00000205557.11 ENST00000205557.2 ENST00000205557.3 ENST00000205557.4 ENST00000205557.5 ENST00000205557.6 ENST00000205557.7 ENST00000205557.8 ENST00000205557.9 MRP6 MRP6_HUMAN NM_001351800 O95255 P78420 Q8TCY8 Q9UMZ7 uc002den.1 uc002den.2 uc002den.3 uc002den.4 uc002den.5 uc002den.6 The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). The encoded protein, a member of the MRP subfamily, is involved in multi-drug resistance. Mutations in this gene cause pseudoxanthoma elasticum. Alternatively spliced transcript variants that encode different proteins have been described for this gene. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.96299.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## [Isoform 1]: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of glutathione conjugates such as leukotriene-c4 (LTC4) and N- ethylmaleimide S-glutathione (NEM-GS) (in vitro), and an anionic cyclopentapeptide endothelin antagonist, BQ-123 (PubMed:11880368, PubMed:12414644). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Does not appear to actively transport drugs outside the cell. Confers low levels of cellular resistance to etoposide, teniposide, anthracyclines and cisplatin (PubMed:12414644). [Isoform 1]: Mediates the release of nucleoside triphosphates, predominantly ATP, into the circulation, where it is rapidly converted into AMP and the mineralization inhibitor inorganic pyrophosphate (PPi) by the ecto-enzyme ectonucleotide pyrophosphatase phosphodiesterase 1 (ENPP1), therefore playing a role in PPi homeostasis. [Isoform 2]: Inhibits TNF-alpha-mediated apoptosis through blocking one or more caspases. [Isoform 1]: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S- substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence=; [Isoform 1]: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; LTC4 transport is completely inhibited by 1 mM orthovanadate. Kinetic parameters: KM=600 nM for LTC4 ; KM=282 uM for N-ethylmaleimide S-glutathione ; Vmax=106 pmol/min/mg enzyme for N-ethylmaleimide S-glutathione transport ; Vmax=50 pmol/min/mg enzyme for LTC4 transport ; Basal cell membrane ; Multi-pass membrane protein Note=Localized to the basal membrane of Sertoli cells. [Isoform 1]: Basolateral cell membrane ; Multi-pass membrane protein [Isoform 2]: Endoplasmic reticulum membrane ; Single-pass membrane protein Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O95255-1; Sequence=Displayed; Name=2; Synonyms=URG7 ; IsoId=O95255-2; Sequence=VSP_047315, VSP_047316; Name=3; Synonyms=Delta19Delta24; IsoId=O95255-3; Sequence=VSP_057077, VSP_057078; Expressed in kidney and liver. Very low expression in other tissues. In testis, localized to peritubular myoid cells, Leydig cells, along the basal membrane of Sertoli cells and moderately in the adluminal compartment of the seminiferous tubules (PubMed:35307651). [Isoform 2]: Induced by HBV x antigen upon hepatitis B viral infection. Glycosylated. Pseudoxanthoma elasticum (PXE) [MIM:264800]: A multisystem disorder characterized by accumulation of mineralized and fragmented elastic fibers in the skin, vascular walls, and Burch membrane in the eye. Clinically, patients exhibit characteristic lesions of the posterior segment of the eye including peau d'orange, angioid streaks, and choroidal neovascularizations, of the skin including soft, ivory colored papules in a reticular pattern that predominantly affect the neck and large flexor surfaces, and of the cardiovascular system with peripheral and coronary arterial occlusive disease as well as gastrointestinal bleedings. te=The disease is caused by variants affecting the gene represented in this entry. Homozygous or compound heterozygous ABCC6 mutations have been found in the overwhelming majority of cases. Individuals carrying heterozygous mutations express limited manifestations of the pseudoxanthoma elasticum phenotype. Arterial calcification of infancy, generalized, 2 (GACI2) [MIM:614473]: A severe autosomal recessive disorder characterized by calcification of the internal elastic lamina of muscular arteries and stenosis due to myointimal proliferation. The disorder is often fatal within the first 6 months of life because of myocardial ischemia resulting in refractory heart failure. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 3]: May function as a half transporter. Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. Sequence=AAC15785.1; Type=Erroneous gene model prediction; Evidence=; Name=Mutations of the ABCC6 gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/abcc6mut.htm"; Name=ABCMdb; Note=Database for mutations in ABC proteins; URL="http://abcm2.hegelab.org/search"; nucleotide binding transporter activity ATP binding nucleus endoplasmic reticulum endoplasmic reticulum membrane plasma membrane visual perception membrane integral component of membrane basolateral plasma membrane apical plasma membrane lateral plasma membrane ATPase activity transmembrane transporter activity response to drug ATPase activity, coupled to transmembrane movement of substances response to stimulus transmembrane transport uc002den.1 uc002den.2 uc002den.3 uc002den.4 uc002den.5 uc002den.6 
ENST00000205636.4 CMTM6 ENST00000205636.4 CKLF like MARVEL transmembrane domain containing 6 (from RefSeq NM_017801.3) CKLF6_HUMAN CKLFSF6 CMTM6 ENST00000205636.1 ENST00000205636.2 ENST00000205636.3 NM_017801 Q6IAC4 Q9NX76 uc003cfa.1 uc003cfa.2 uc003cfa.3 This gene belongs to the chemokine-like factor gene superfamily, a novel family that is similar to the chemokine and transmembrane 4 superfamilies. This gene is one of several chemokine-like factor genes located in a cluster on chromosome 3. This gene is widely expressed in many tissues, but the exact function of the encoded protein is unknown. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AF479261.1, SRR1660809.9855.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2467146 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000205636.4/ ENSP00000205636.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Master regulator of recycling and plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Associates with both constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where it protects PD-L1/CD274 from being targeted for lysosomal degradation, likely by preventing its STUB1-mediated ubiquitination. May stabilize PD-L1/CD274 expression on antigen presenting cells and potentiates inhibitory signaling by PDCD1/CD279, its receptor on T-cells, ultimately triggering T-cell anergy. Interacts with PD-L1/CD274 (via transmembrane domain); the interaction is direct (PubMed:28813417, PubMed:28813410). Interacts with CMTM4 (PubMed:28813410). Interacts with CD58, ARG1, ENO1 and TMPO (PubMed:28813417). Q9NX76; Q6Q788: APOA5; NbExp=3; IntAct=EBI-1054315, EBI-3936819; Q9NX76; Q96DR5: BPIFA2; NbExp=3; IntAct=EBI-1054315, EBI-10284754; Q9NX76; O95971: CD160; NbExp=3; IntAct=EBI-1054315, EBI-4314390; Q9NX76; Q9NZQ7: CD274; NbExp=14; IntAct=EBI-1054315, EBI-4314282; Q9NX76; P25942: CD40; NbExp=3; IntAct=EBI-1054315, EBI-525714; Q9NX76; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-1054315, EBI-752069; Q9NX76; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-1054315, EBI-745535; Q9NX76; Q5VYK3: ECPAS; NbExp=3; IntAct=EBI-1054315, EBI-521451; Q9NX76; Q08426: EHHADH; NbExp=3; IntAct=EBI-1054315, EBI-2339219; Q9NX76; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-1054315, EBI-740987; Q9NX76; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-1054315, EBI-3232108; Q9NX76; P38159: RBMX; NbExp=3; IntAct=EBI-1054315, EBI-743526; Q9NX76; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-1054315, EBI-6257312; Q9NX76; P08579: SNRPB2; NbExp=3; IntAct=EBI-1054315, EBI-1053651; Q9NX76; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-1054315, EBI-742688; Q9NX76; Q15560: TCEA2; NbExp=3; IntAct=EBI-1054315, EBI-710310; Q9NX76; Q6PL24: TMED8; NbExp=3; IntAct=EBI-1054315, EBI-11603430; Cell membrane ulti-pass membrane protein Early endosome membrane ; Multi-pass membrane protein Recycling endosome membrane ; Multi-pass membrane protein Note=Co-localizes with PD-L1/CD274 in the plasma membrane and in recycling endosomes. Expressed in the leukocytes, placenta and testis. Belongs to the chemokine-like factor family. protein binding endosome plasma membrane protein transport membrane integral component of membrane regulation of protein stability early endosome membrane endocytic recycling azurophil granule membrane specific granule membrane neutrophil degranulation recycling endosome membrane uc003cfa.1 uc003cfa.2 uc003cfa.3 
ENST00000205948.11 APOH ENST00000205948.11 apolipoprotein H (from RefSeq NM_000042.3) APOH_HUMAN B2G1 B2R9M3 ENST00000205948.1 ENST00000205948.10 ENST00000205948.2 ENST00000205948.3 ENST00000205948.4 ENST00000205948.5 ENST00000205948.6 ENST00000205948.7 ENST00000205948.8 ENST00000205948.9 NM_000042 P02749 Q9UCN7 uc002jfn.1 uc002jfn.2 uc002jfn.3 uc002jfn.4 uc002jfn.5 uc002jfn.6 Apolipoprotein H, also known as beta-2-glycoprotein I, is a component of circulating plasma lipoproteins. It has been implicated in a variety of physiologic pathways including lipoprotein metabolism, coagulation, hemostasis, and the production of antiphospholipid autoantibodies. APOH may be a required cofactor for anionic phospholipid binding by the antiphospholipid autoantibodies found in sera of many patients with lupus and primary antiphospholipid syndrome (APS). The anti-beta (2) glycoprotein I antibodies from APS patients, mediate inhibition of activated protein C which has anticoagulant properties. Because beta-2-GPI is the main autoantigen in patients with APS, the disruption of this pathway by autoantibodies may be an important mechanism for thrombosis in patients with APS.[provided by RefSeq, Dec 2019]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M62839.1, SRR5189664.103267.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145122, SAMEA2162895 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000205948.11/ ENSP00000205948.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. P02749; P02749: APOH; NbExp=2; IntAct=EBI-2114682, EBI-2114682; P02749; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2114682, EBI-21591415; P02749; P01130: LDLR; NbExp=3; IntAct=EBI-2114682, EBI-988319; P02749; P08519: LPA; NbExp=4; IntAct=EBI-2114682, EBI-9232288; P02749; P11226: MBL2; NbExp=3; IntAct=EBI-2114682, EBI-5325353; P02749; P02776: PF4; NbExp=2; IntAct=EBI-2114682, EBI-2565740; P02749; P00747: PLG; NbExp=2; IntAct=EBI-2114682, EBI-999394; P02749; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2114682, EBI-2623095; P02749; Q924X6: Lrp8; Xeno; NbExp=2; IntAct=EBI-2114682, EBI-432319; PRO_0000002059; PRO_0000002059 [P02749]: APOH; NbExp=2; IntAct=EBI-11809989, EBI-11809989; PRO_0000002059; PRO_0000005068 [P02776]: PF4; NbExp=4; IntAct=EBI-11809989, EBI-11809981; Secreted. Expressed by the liver and secreted in plasma. N- and O-glycosylated. PubMed:6587378 also reports glycosylation on 'Asn-188' for their allele. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/apoh/"; negative regulation of endothelial cell proliferation platelet degranulation protein binding phospholipid binding extracellular region extracellular space triglyceride metabolic process blood coagulation, intrinsic pathway heparin binding lipid binding cell surface negative regulation of endothelial cell migration negative regulation of angiogenesis regulation of blood coagulation positive regulation of blood coagulation negative regulation of blood coagulation platelet dense granule lumen plasminogen activation negative regulation of myeloid cell apoptotic process triglyceride transport very-low-density lipoprotein particle high-density lipoprotein particle negative regulation of smooth muscle cell apoptotic process chylomicron identical protein binding positive regulation of lipoprotein lipase activity regulation of fibrinolysis negative regulation of fibrinolysis lipoprotein lipase activator activity extracellular exosome uc002jfn.1 uc002jfn.2 uc002jfn.3 uc002jfn.4 uc002jfn.5 uc002jfn.6 
ENST00000206020.8 SPAG7 ENST00000206020.8 sperm associated antigen 7 (from RefSeq NM_004890.3) ENST00000206020.1 ENST00000206020.2 ENST00000206020.3 ENST00000206020.4 ENST00000206020.5 ENST00000206020.6 ENST00000206020.7 NM_004890 O75391 Q96EU5 SPAG7_HUMAN uc002gae.1 uc002gae.2 uc002gae.3 uc002gae.4 uc002gae.5 O75391; Q9BS40: LXN; NbExp=3; IntAct=EBI-348464, EBI-1044504; Nucleus Detected in fetal brain. Sequence=AAC39888.1; Type=Frameshift; Evidence=; nucleic acid binding nucleus uc002gae.1 uc002gae.2 uc002gae.3 uc002gae.4 uc002gae.5 
ENST00000206249.8 ESR1 ENST00000206249.8 estrogen receptor 1, transcript variant 12 (from RefSeq NM_001385572.1) ENST00000206249.1 ENST00000206249.2 ENST00000206249.3 ENST00000206249.4 ENST00000206249.5 ENST00000206249.6 ENST00000206249.7 ESR ESR1_HUMAN NM_001385572 NR3A1 P03372 Q13511 Q14276 Q5T5H7 Q6MZQ9 Q9NU51 Q9UDZ7 Q9UIS7 uc003qoo.1 uc003qoo.2 uc003qoo.3 uc003qoo.4 uc003qoo.5 uc003qoo.6 This gene encodes an estrogen receptor and ligand-activated transcription factor. The canonical protein contains an N-terminal ligand-independent transactivation domain, a central DNA binding domain, a hinge domain, and a C-terminal ligand-dependent transactivation domain. The protein localizes to the nucleus where it may form either a homodimer or a heterodimer with estrogen receptor 2. The protein encoded by this gene regulates the transcription of many estrogen-inducible genes that play a role in growth, metabolism, sexual development, gestation, and other reproductive functions and is expressed in many non-reproductive tissues. The receptor encoded by this gene plays a key role in breast cancer, endometrial cancer, and osteoporosis. This gene is reported to have dozens of transcript variants due to the use of alternate promoters and alternative splicing, however, the full-length nature of many of these variants remain uncertain. [provided by RefSeq, Jul 2020]. Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE- independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa- B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (PubMed:17922032). [Isoform 3]: Involved in activation of NOS3 and endothelial nitric oxide production (PubMed:21937726). Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full-length receptor (PubMed:10970861). Binds to ERE and inhibits isoform 1 (PubMed:10970861). Binds DNA as a homodimer. Can form a heterodimer with ESR2. Interacts with FOXC2, MAP1S, SLC30A9, UBE1C and NCOA3 coactivator (By similarity). Interacts with PELP1, the interaction is enhanced by 17- beta-estradiol, the interaction increases ESR1 transcriptional activity (PubMed:11481323, PubMed:14963108). Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with CITED1; the interaction is estrogen-dependent. Interacts with NCOA5 and NCOA6 coactivators. Interacts with NCOA7; the interaction is a ligand-inducible. Interacts with PHB2, and UBE1C. Interacts with AKAP13. Interacts with CUEDC2. Interacts with KDM5A. Interacts with SMARD1. Interacts with HEXIM1. Interacts with PBXIP1. Interaction with MUC1 is stimulated by 7 beta-estradiol (E2) and enhances ESR1-mediated transcription. Interacts with DNTTIP2, FAM120B and UIMC1. Interacts with isoform 4 of TXNRD1. Interacts with KMT2D/MLL2. Interacts with ATAD2 and this interaction is enhanced by estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG. Interaction with SH2D4A blocks binding to PLCG and inhibits estrogen-induced cell proliferation. Interacts with DYNLL1. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes. Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth. Interacts with DNAAF4. Interacts with PRMT2. Interacts with RBFOX2. Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Binds to CSNK1D. Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy. Interacts with DDX5 (PubMed:11682626). Interacts with NCOA1; the interaction seems to require a self- association of N-terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3. Interacts with NRIP1 (By similarity). Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts with CLOCK and the interaction is stimulated by estrogen. Interacts with BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent. Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. Interacts with CCAR2 (via N-terminus) in a ligand- independent manner. Interacts with ZFHX3. Interacts with SFR1 in a ligand-dependent and -independent manner (PubMed:23874500). Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (PubMed:28068668). Interacts (via DNA-binding domain) with POU4F2 (C-terminus); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (By similarity). Interacts with ESRRB isoform 1 (PubMed:19755138). Interacts with UBE3A and WBP2 (PubMed:16772533). Interacts with GTF2B (PubMed:1517211). Interacts with RBM39 (By similarity). In the absence of hormonal ligand, interacts with TACC1 (PubMed:20078863). Interacts with PI3KR1 or PI3KR2 and PTK2/FAK1 (PubMed:18657504). Interacts with SRC (PubMed:14963108, PubMed:18657504). [Isoform 3]: Probably homodimerizes or heterodimerizes with isoform 1 and ESR2. P03372; Q12802: AKAP13; NbExp=3; IntAct=EBI-78473, EBI-1373806; P03372; Q03989: ARID5A; NbExp=9; IntAct=EBI-78473, EBI-948603; P03372; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-78473, EBI-10254793; P03372; Q9Y294: ASF1A; NbExp=4; IntAct=EBI-78473, EBI-749553; P03372; Q8IXJ9: ASXL1; NbExp=2; IntAct=EBI-78473, EBI-1646500; P03372; Q6PL18: ATAD2; NbExp=5; IntAct=EBI-78473, EBI-6598454; P03372; P18846: ATF1; NbExp=3; IntAct=EBI-78473, EBI-852794; P03372; P62952: BLCAP; NbExp=2; IntAct=EBI-78473, EBI-3895726; P03372; P38398: BRCA1; NbExp=14; IntAct=EBI-78473, EBI-349905; P03372; P20290-2: BTF3; NbExp=5; IntAct=EBI-78473, EBI-1054703; P03372; Q86Y37: CACUL1; NbExp=5; IntAct=EBI-78473, EBI-8168227; P03372; P29279: CCN2; NbExp=7; IntAct=EBI-78473, EBI-2835375; P03372; P17676: CEBPB; NbExp=2; IntAct=EBI-78473, EBI-969696; P03372; Q99966: CITED1; NbExp=3; IntAct=EBI-78473, EBI-2624951; P03372; Q9H467: CUEDC2; NbExp=2; IntAct=EBI-78473, EBI-1248228; P03372; Q9NV06: DCAF13; NbExp=2; IntAct=EBI-78473, EBI-7402939; P03372; O00429: DNM1L; NbExp=2; IntAct=EBI-78473, EBI-724571; P03372; O60869: EDF1; NbExp=3; IntAct=EBI-78473, EBI-781301; P03372; P00533: EGFR; NbExp=2; IntAct=EBI-78473, EBI-297353; P03372; P03372: ESR1; NbExp=11; IntAct=EBI-78473, EBI-78473; P03372; Q12778: FOXO1; NbExp=2; IntAct=EBI-78473, EBI-1108782; P03372; O43524: FOXO3; NbExp=7; IntAct=EBI-78473, EBI-1644164; P03372; Q9Y3R0: GRIP1; NbExp=2; IntAct=EBI-78473, EBI-5349621; P03372; O00165: HAX1; NbExp=2; IntAct=EBI-78473, EBI-357001; P03372; Q6NYC1: JMJD6; NbExp=8; IntAct=EBI-78473, EBI-8464037; P03372; O15054: KDM6B; NbExp=2; IntAct=EBI-78473, EBI-2831260; P03372; O14686: KMT2D; NbExp=3; IntAct=EBI-78473, EBI-996065; P03372; O95835: LATS1; NbExp=2; IntAct=EBI-78473, EBI-444209; P03372; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-78473, EBI-25830459; P03372; Q96Q04: LMTK3; NbExp=3; IntAct=EBI-78473, EBI-720814; P03372; Q9BQ69: MACROD1; NbExp=6; IntAct=EBI-78473, EBI-5324932; P03372; Q00987: MDM2; NbExp=2; IntAct=EBI-78473, EBI-389668; P03372; Q15648: MED1; NbExp=3; IntAct=EBI-78473, EBI-394459; P03372; P60660: MYL6; NbExp=3; IntAct=EBI-78473, EBI-300817; P03372; Q15788: NCOA1; NbExp=8; IntAct=EBI-78473, EBI-455189; P03372; Q15596: NCOA2; NbExp=5; IntAct=EBI-78473, EBI-81236; P03372; Q9Y6Q9: NCOA3; NbExp=4; IntAct=EBI-78473, EBI-81196; P03372; Q9UN36: NDRG2; NbExp=2; IntAct=EBI-78473, EBI-3895741; P03372; PRO_0000030311 [P19838]: NFKB1; NbExp=3; IntAct=EBI-78473, EBI-697771; P03372; Q96RI1-3: NR1H4; NbExp=2; IntAct=EBI-78473, EBI-10921781; P03372; Q9BZ95: NSD3; NbExp=3; IntAct=EBI-78473, EBI-3390132; P03372; Q9BTK6: PAGR1; NbExp=5; IntAct=EBI-78473, EBI-2372223; P03372; Q96AQ6-1: PBXIP1; NbExp=3; IntAct=EBI-78473, EBI-15606280; P03372; P06401: PGR; NbExp=20; IntAct=EBI-78473, EBI-78539; P03372; P06401-1: PGR; NbExp=4; IntAct=EBI-78473, EBI-12590474; P03372; Q99623: PHB2; NbExp=4; IntAct=EBI-78473, EBI-358348; P03372; P36873: PPP1CC; NbExp=3; IntAct=EBI-78473, EBI-356283; P03372; P53041: PPP5C; NbExp=4; IntAct=EBI-78473, EBI-716663; P03372; P55345: PRMT2; NbExp=9; IntAct=EBI-78473, EBI-78458; P03372; P60763: RAC3; NbExp=5; IntAct=EBI-78473, EBI-767084; P03372; O43251: RBFOX2; NbExp=4; IntAct=EBI-78473, EBI-746056; P03372; Q04206: RELA; NbExp=9; IntAct=EBI-78473, EBI-73886; P03372; Q14151: SAFB2; NbExp=2; IntAct=EBI-78473, EBI-352869; P03372; Q96HI0: SENP5; NbExp=2; IntAct=EBI-78473, EBI-3895753; P03372; P08047: SP1; NbExp=2; IntAct=EBI-78473, EBI-298336; P03372; Q02447: SP3; NbExp=4; IntAct=EBI-78473, EBI-348158; P03372; P12931: SRC; NbExp=12; IntAct=EBI-78473, EBI-621482; P03372; O15164: TRIM24; NbExp=3; IntAct=EBI-78473, EBI-2130378; P03372; Q16881-4: TXNRD1; NbExp=4; IntAct=EBI-78473, EBI-9080335; P03372; Q9UBK9: UXT; NbExp=2; IntAct=EBI-78473, EBI-357355; P03372; O76024: WFS1; NbExp=3; IntAct=EBI-78473, EBI-720609; P03372; Q8N895: ZNF366; NbExp=6; IntAct=EBI-78473, EBI-2813661; P03372; P59598: Asxl1; Xeno; NbExp=2; IntAct=EBI-78473, EBI-5743705; P03372; P05627: Jun; Xeno; NbExp=6; IntAct=EBI-78473, EBI-764369; P03372; Q9JLI4: Ncoa6; Xeno; NbExp=2; IntAct=EBI-78473, EBI-286271; P03372; Q60974: Ncor1; Xeno; NbExp=2; IntAct=EBI-78473, EBI-349004; P03372; P62962: Pfn1; Xeno; NbExp=3; IntAct=EBI-78473, EBI-647096; P03372; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-78473, EBI-848039; P03372-1; P03372-1: ESR1; NbExp=4; IntAct=EBI-15606245, EBI-15606245; P03372-1; Q92731: ESR2; NbExp=5; IntAct=EBI-15606245, EBI-78505; P03372-1; Q92993: KAT5; NbExp=3; IntAct=EBI-15606245, EBI-399080; P03372-1; Q96AQ6-1: PBXIP1; NbExp=5; IntAct=EBI-15606245, EBI-15606280; P03372-4; P00533: EGFR; NbExp=4; IntAct=EBI-4309277, EBI-297353; P03372-4; P29353: SHC1; NbExp=2; IntAct=EBI-4309277, EBI-78835; P03372-4; P12931: SRC; NbExp=2; IntAct=EBI-4309277, EBI-621482; [Isoform 1]: Nucleus toplasm ll membrane ; Peripheral membrane protein ; Cytoplasmic side Note=A minor fraction is associated with the inner membrane. [Isoform 3]: Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Single- pass type I membrane protein. Note=Associated with the inner membrane via palmitoylation (Probable). At least a subset exists as a transmembrane protein with a N-terminal extracellular domain. Nucleus. Golgi apparatus. Cell membrane. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated. Event=Alternative promoter usage, Alternative splicing; Named isoforms=4; Name=1; Synonyms=Long, hER-alpha66, ER66; IsoId=P03372-1; Sequence=Displayed; Name=2; Synonyms=Short; IsoId=P03372-2; Sequence=VSP_003680; Name=3; Synonyms=hER-alpha46, ER46; IsoId=P03372-3; Sequence=VSP_042460; Name=4; Synonyms=hER-alpha36, ER36; IsoId=P03372-4; Sequence=VSP_042460, VSP_042461; Widely expressed (PubMed:10970861). Not expressed in the pituitary gland (PubMed:10970861). [Isoform 3]: Widely expressed, however not expressed in the pituitary gland. Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand- independent transactivation function. The C-terminus contains a ligand- dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner. AF-1 seems to provide the major transactivation function in differentiated cells. Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Self-association induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity. Phosphorylated by LMTK3 in vitro. Glycosylated; contains N-acetylglucosamine, probably O-linked. Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation (PubMed:21602804, PubMed:28068668). Deubiquitinated by OTUB1 (PubMed:19383985). Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization (PubMed:18657504, PubMed:24498420). Demethylated by JMJD6 at Arg-260 (PubMed:24498420). Palmitoylated (isoform 3). Not biotinylated (isoform 3). Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor. Genetic variations in ESR1 are correlated with bone mineral density (BMD). Low BMD is a risk factor for osteoporotic fracture. Osteoporosis is characterized by reduced bone mineral density, disruption of bone microarchitecture, and the alteration of the amount and variety of non-collagenous proteins in bone. Osteoporotic bones are more at risk of fracture. Estrogen resistance (ESTRR) [MIM:615363]: A disorder characterized by partial or complete resistance to estrogens, in the presence of elevated estrogen serum levels. Clinical features include absence of the pubertal growth spurt, delayed bone maturation, unfused epiphyses, reduced bone mineral density, osteoporosis, continued growth into adulthood and very tall adult stature. Glucose intolerance, hyperinsulinemia and lipid abnormalities may also be present. Note=The disease is caused by variants affecting the gene represented in this entry. Selective estrogen receptor modulators (SERMs), such as tamoxifen, raloxifene, toremifene, lasofoxifene, clomifene, femarelle and ormeloxifene, have tissue selective agonistic and antagonistic effects on the estrogen receptor (ER). They interfere with the ER association with coactivators or corepressors, mainly involving the AF- 2 domain. [Isoform 3]: Produced by alternative promoter usage. [Isoform 4]: Produced by alternative splicing of isoform 3. Belongs to the nuclear hormone receptor family. NR3 subfamily. Was reported to be activated by DDX5. However, this study has been retracted due to concerns of image manipulation. Sequence=AAB00115.1; Type=Miscellaneous discrepancy; Note=contains an in-frame duplication of exons 6 and 7.; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/esr1/"; Name=Wikipedia; Note=Estrogen receptor entry; URL="https://en.wikipedia.org/wiki/Estrogen_receptor"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding TFIIB-class transcription factor binding transcription coactivator binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding antral ovarian follicle growth epithelial cell development DNA binding chromatin binding transcription factor activity, sequence-specific DNA binding steroid hormone receptor activity RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding steroid binding protein binding nucleus nucleoplasm cytoplasm Golgi apparatus cytosol plasma membrane chromatin remodeling transcription, DNA-templated regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter transcription from RNA polymerase II promoter transcription initiation from RNA polymerase II promoter signal transduction phospholipase C-activating G-protein coupled receptor signaling pathway positive regulation of cytosolic calcium ion concentration beta-catenin binding transcription factor binding androgen metabolic process zinc ion binding lipid binding male gonad development negative regulation of gene expression positive regulation of phospholipase C activity membrane integral component of membrane protein deubiquitination TBP-class protein binding enzyme binding protein kinase binding regulation of Wnt signaling pathway nitric-oxide synthase regulator activity estrogen receptor activity estrogen receptor binding intracellular steroid hormone receptor signaling pathway intracellular estrogen receptor signaling pathway response to estradiol macromolecular complex regulation of intracellular estrogen receptor signaling pathway estrogen response element binding regulation of toll-like receptor signaling pathway transcriptionally active chromatin identical protein binding regulation of apoptotic process negative regulation of I-kappaB kinase/NF-kappaB signaling steroid hormone mediated signaling pathway negative regulation of sequence-specific DNA binding transcription factor activity sequence-specific DNA binding response to estrogen positive regulation of nitric oxide biosynthetic process positive regulation of transcription, DNA-templated positive regulation of RNA polymerase II transcriptional preinitiation complex assembly positive regulation of transcription from RNA polymerase II promoter metal ion binding positive regulation of fibroblast proliferation stem cell differentiation regulation of inflammatory response positive regulation of nitric-oxide synthase activity positive regulation of sequence-specific DNA binding transcription factor activity ATPase binding positive regulation of protein kinase B signaling uterus development vagina development prostate epithelial cord elongation prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis regulation of branching involved in prostate gland morphogenesis mammary gland branching involved in pregnancy mammary gland alveolus development epithelial cell proliferation involved in mammary gland duct elongation protein localization to chromatin cellular response to estrogen stimulus cellular response to estradiol stimulus transcriptional preinitiation complex negative regulation of production of miRNAs involved in gene silencing by miRNA uc003qoo.1 uc003qoo.2 uc003qoo.3 uc003qoo.4 uc003qoo.5 uc003qoo.6 
ENST00000206262.2 RGS17 ENST00000206262.2 regulator of G protein signaling 17 (from RefSeq NM_012419.5) ENST00000206262.1 NM_012419 Q5TF49 Q8TD61 Q9UGC6 Q9UJS8 RGS17_HUMAN RGSZ2 uc003qpm.1 uc003qpm.2 uc003qpm.3 uc003qpm.4 uc003qpm.5 This gene encodes a member of the regulator of G-protein signaling family. This protein contains a conserved, 120 amino acid motif called the RGS domain and a cysteine-rich region. The protein attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC013117.1, SRR3476690.1148404.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1968540 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000206262.2/ ENSP00000206262.1 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:15096504). Binds selectively to GNAZ and GNAI2 subunits, accelerates their GTPase activity and regulates their signaling activities. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity). Interacts with GNAI1 and GNAQ (PubMed:18434541). Interacts with GNAZ and GNAI2. Interacts with OPRM1. Forms a complex with mu- opioid receptors and G(alpha)z/i2 subunits, including GNAZ and GNAI2; the formation of this complex results in mu-opioid receptor desensitization (By similarity). Interacts with HINT1 (By similarity). Q9UGC6; P29972: AQP1; NbExp=6; IntAct=EBI-3918154, EBI-745213; Q9UGC6; A0A087WZT3: BOLA2-SMG1P6; NbExp=3; IntAct=EBI-3918154, EBI-12006120; Q9UGC6; Q9H2X0: CHRD; NbExp=3; IntAct=EBI-3918154, EBI-947551; Q9UGC6; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-3918154, EBI-713677; Q9UGC6; Q02930-3: CREB5; NbExp=3; IntAct=EBI-3918154, EBI-10192698; Q9UGC6; G5E9A7: DMWD; NbExp=3; IntAct=EBI-3918154, EBI-10976677; Q9UGC6; Q53GS7: GLE1; NbExp=3; IntAct=EBI-3918154, EBI-1955541; Q9UGC6; P63096: GNAI1; NbExp=3; IntAct=EBI-3918154, EBI-618639; Q9UGC6; P08754: GNAI3; NbExp=3; IntAct=EBI-3918154, EBI-357563; Q9UGC6; P49639: HOXA1; NbExp=6; IntAct=EBI-3918154, EBI-740785; Q9UGC6; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-3918154, EBI-3918847; Q9UGC6; O14901: KLF11; NbExp=3; IntAct=EBI-3918154, EBI-948266; Q9UGC6; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-3918154, EBI-10302392; Q9UGC6; Q6L8G4: KRTAP5-11; NbExp=5; IntAct=EBI-3918154, EBI-11993296; Q9UGC6; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-3918154, EBI-11974251; Q9UGC6; Q6L8H1: KRTAP5-4; NbExp=3; IntAct=EBI-3918154, EBI-11963072; Q9UGC6; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-3918154, EBI-10250562; Q9UGC6; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-3918154, EBI-11962058; Q9UGC6; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-3918154, EBI-10245913; Q9UGC6; Q5T752: LCE1D; NbExp=5; IntAct=EBI-3918154, EBI-11741311; Q9UGC6; Q5T753: LCE1E; NbExp=3; IntAct=EBI-3918154, EBI-11955335; Q9UGC6; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-3918154, EBI-10246607; Q9UGC6; O14633: LCE2B; NbExp=3; IntAct=EBI-3918154, EBI-11478468; Q9UGC6; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-3918154, EBI-11973993; Q9UGC6; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-3918154, EBI-9394625; Q9UGC6; Q5TA77: LCE3B; NbExp=5; IntAct=EBI-3918154, EBI-11974495; Q9UGC6; Q5T5A8: LCE3C; NbExp=3; IntAct=EBI-3918154, EBI-10245291; Q9UGC6; Q9BYE3: LCE3D; NbExp=3; IntAct=EBI-3918154, EBI-6658837; Q9UGC6; Q5T5B0: LCE3E; NbExp=3; IntAct=EBI-3918154, EBI-10245456; Q9UGC6; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-3918154, EBI-10246358; Q9UGC6; Q5TCM9: LCE5A; NbExp=5; IntAct=EBI-3918154, EBI-11955689; Q9UGC6; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-3918154, EBI-1210753; Q9UGC6; P32242: OTX1; NbExp=6; IntAct=EBI-3918154, EBI-740446; Q9UGC6; P43115-12: PTGER3; NbExp=3; IntAct=EBI-3918154, EBI-10234038; Q9UGC6; P62906: RPL10A; NbExp=6; IntAct=EBI-3918154, EBI-356860; Q9UGC6; Q92504: SLC39A7; NbExp=3; IntAct=EBI-3918154, EBI-1051105; Q9UGC6; P49901: SMCP; NbExp=3; IntAct=EBI-3918154, EBI-750494; Q9UGC6; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3918154, EBI-5235340; Q9UGC6; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-3918154, EBI-357085; Q9UGC6; Q6EMK4: VASN; NbExp=3; IntAct=EBI-3918154, EBI-10249550; Q9UGC6; Q9NWL9; NbExp=3; IntAct=EBI-3918154, EBI-10315054; Membrane Synapse, synaptosome Nucleus Cytoplasm Predominantly expressed in the cerebellum. Also expressed in the cortex and medulla. Weakly expressed in a number of peripheral tissues notably spleen, lung and leukocytes. N- and O-glycosylated in synapsomal membranes. Serine phosphorylated in synapsomal membranes. Sumoylated with SUMO1 and SUM02 in synaptosomes. The sumoylated forms act as a scaffold for sequestering mu-opioid receptor-activated G(alpha) subunits (By similarity). Desumoylated by HINT1 (By similarity). Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/47522/RGS17"; response to amphetamine GTPase activity GTPase activator activity protein binding nucleus cytoplasm plasma membrane G-protein coupled receptor signaling pathway negative regulation of signal transduction membrane cell junction neuron projection positive regulation of GTPase activity synapse uc003qpm.1 uc003qpm.2 uc003qpm.3 uc003qpm.4 uc003qpm.5 
ENST00000206380.8 TMEM101 ENST00000206380.8 transmembrane protein 101, transcript variant 1 (from RefSeq NM_032376.4) B2R9N6 ENST00000206380.1 ENST00000206380.2 ENST00000206380.3 ENST00000206380.4 ENST00000206380.5 ENST00000206380.6 ENST00000206380.7 NM_032376 Q96IK0 TM101_HUMAN uc060fvt.1 uc060fvt.2 May activate NF-kappa-B signaling pathways. Q96IK0; Q12983: BNIP3; NbExp=3; IntAct=EBI-3922699, EBI-749464; Q96IK0; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-3922699, EBI-12003442; Q96IK0; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-3922699, EBI-11991950; Q96IK0; O95167: NDUFA3; NbExp=3; IntAct=EBI-3922699, EBI-1246131; Q96IK0; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-3922699, EBI-10317425; Q96IK0; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-3922699, EBI-716063; Q96IK0; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-3922699, EBI-12257782; Q96IK0; P0DN84: STRIT1; NbExp=3; IntAct=EBI-3922699, EBI-12200293; Q96IK0; O60499-2: STX10; NbExp=3; IntAct=EBI-3922699, EBI-12094584; Q96IK0; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-3922699, EBI-1049004; Q96IK0; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-3922699, EBI-12887458; Q96IK0; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-3922699, EBI-6656213; Q96IK0; P23763-3: VAMP1; NbExp=3; IntAct=EBI-3922699, EBI-12097582; Q96IK0; P63027: VAMP2; NbExp=3; IntAct=EBI-3922699, EBI-520113; Q96IK0; O95292: VAPB; NbExp=3; IntAct=EBI-3922699, EBI-1188298; Membrane ; Multi-pass membrane protein cellular_component membrane integral component of membrane positive regulation of I-kappaB kinase/NF-kappaB signaling uc060fvt.1 uc060fvt.2 
ENST00000206423.8 CCDC80 ENST00000206423.8 coiled-coil domain containing 80, transcript variant 2 (from RefSeq NM_199512.3) CCD80_HUMAN D3DN67 DRO1 ENST00000206423.1 ENST00000206423.2 ENST00000206423.3 ENST00000206423.4 ENST00000206423.5 ENST00000206423.6 ENST00000206423.7 HBE245 NM_199512 Q5PR20 Q6GPG9 Q76M96 Q8IVT6 Q8NBV1 Q8NHY8 URB uc032rxo.1 uc032rxo.2 uc032rxo.3 Promotes cell adhesion and matrix assembly. Binds to various extracellular matrix proteins. Secreted, extracellular space, extracellular matrix Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q76M96-1; Sequence=Displayed; Name=2; IsoId=Q76M96-2; Sequence=VSP_024136; Name=3; IsoId=Q76M96-3; Sequence=VSP_024135; Expressed in dermal papilla and dermal fibroblasts (at protein level). Expressed in heart, thymus, placenta, pancreas, colon, epithelium, spleen and osteoblasts. Down-regulated in cancer and after osteoblastic differentiation. Up-regulated by dihydrotestosterone (DHT). Phosphorylated. Belongs to the CCDC80 family. fibronectin binding glycosaminoglycan binding extracellular region basement membrane interstitial matrix heparin binding response to bacterium positive regulation of cell-substrate adhesion extracellular matrix organization extracellular matrix uc032rxo.1 uc032rxo.2 uc032rxo.3 
ENST00000206451.11 PSME1 ENST00000206451.11 proteasome activator subunit 1, transcript variant 1 (from RefSeq NM_006263.4) A6NJG9 ENST00000206451.1 ENST00000206451.10 ENST00000206451.2 ENST00000206451.3 ENST00000206451.4 ENST00000206451.5 ENST00000206451.6 ENST00000206451.7 ENST00000206451.8 ENST00000206451.9 H0YNE3 IFI5111 NM_006263 PSME1_HUMAN Q06323 Q6IBM2 Q9UEF4 uc001wmg.1 uc001wmg.2 uc001wmg.3 uc001wmg.4 uc001wmg.5 The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the alpha subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three alpha and three beta subunits combine to form a heterohexameric ring. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]. Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome. Heterodimer of PSME1 and PSME2, which forms a hexameric ring. PSME1 can form homoheptamers. Q06323; P22607: FGFR3; NbExp=3; IntAct=EBI-712149, EBI-348399; Q06323; Q14957: GRIN2C; NbExp=3; IntAct=EBI-712149, EBI-8285963; Q06323; P06396: GSN; NbExp=3; IntAct=EBI-712149, EBI-351506; Q06323; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-712149, EBI-1055254; Q06323; Q9UL46: PSME2; NbExp=6; IntAct=EBI-712149, EBI-741630; Q06323; Q5JTV8: TOR1AIP1; NbExp=3; IntAct=EBI-712149, EBI-2559665; Q06323; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-712149, EBI-741480; Q06323; Q9Y649; NbExp=3; IntAct=EBI-712149, EBI-25900580; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q06323-1; Sequence=Displayed; Name=2; IsoId=Q06323-2; Sequence=VSP_046880; Name=3; IsoId=Q06323-3; Sequence=VSP_055166, VSP_055167; By IFNG/IFN-gamma. Belongs to the PA28 family. MAPK cascade protein polyubiquitination proteasome complex stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent protein binding nucleoplasm cytoplasm cytosol regulation of cellular amino acid metabolic process proteasome activator complex positive regulation of endopeptidase activity negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination antigen processing and presentation of exogenous antigen anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process regulation of mRNA stability post-translational protein modification T cell receptor signaling pathway transmembrane transport Wnt signaling pathway, planar cell polarity pathway endopeptidase activator activity regulation of proteasomal protein catabolic process regulation of transcription from RNA polymerase II promoter in response to hypoxia extracellular exosome interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation regulation of G1/S transition of mitotic cell cycle uc001wmg.1 uc001wmg.2 uc001wmg.3 uc001wmg.4 uc001wmg.5 
ENST00000206513.6 CEBPE ENST00000206513.6 CCAAT enhancer binding protein epsilon (from RefSeq NM_001805.4) CEBPE_HUMAN ENST00000206513.1 ENST00000206513.2 ENST00000206513.3 ENST00000206513.4 ENST00000206513.5 NM_001805 Q15744 Q15745 Q8IYI2 Q99803 uc001wiv.1 uc001wiv.2 uc001wiv.3 uc001wiv.4 The protein encoded by this gene is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. It can also form heterodimers with the related protein CEBP-delta. The encoded protein may be essential for terminal differentiation and functional maturation of committed granulocyte progenitor cells. Mutations in this gene have been associated with Specific Granule Deficiency, a rare congenital disorder. Multiple variants of this gene have been described, but the full-length nature of only one has been determined. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC035797.1, U48866.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcriptional activator (PubMed:26019275). C/EBP are DNA- binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Required for the promyelocyte-myelocyte transition in myeloid differentiation (PubMed:10359588). Binds DNA as a homodimer and as a heterodimer (PubMed:26019275). Can form stable heterodimers with CEBPA, CEBPB and CEBPD (By similarity). Interacts with GATA1 and SPI1 (PubMed:26019275). Interacts with SMARCD2 (PubMed:28369036). Q15744; P18847: ATF3; NbExp=2; IntAct=EBI-3907048, EBI-712767; Q15744; P18848: ATF4; NbExp=2; IntAct=EBI-3907048, EBI-492498; Q15744; Q16520: BATF; NbExp=2; IntAct=EBI-3907048, EBI-749503; Q15744; Q9NR55: BATF3; NbExp=2; IntAct=EBI-3907048, EBI-10312707; Q15744; P49715: CEBPA; NbExp=2; IntAct=EBI-3907048, EBI-1172054; Q15744; P53567: CEBPG; NbExp=2; IntAct=EBI-3907048, EBI-740209; Q15744; P35638: DDIT3; NbExp=3; IntAct=EBI-3907048, EBI-742651; Nucleus Strongest expression occurs in promyelocyte and late-myeloblast-like cell lines. Phosphorylated. Specific granule deficiency 1 (SGD1) [MIM:245480]: An immunologic disorder characterized by recurrent pyogenic infections, defective neutrophil chemotaxis and bactericidal activity, and lack of neutrophil secondary granule proteins. Neutrophils of affected individuals lack lactoferrin and show abnormal nuclear segmentation, bilobed nuclei, low alkaline phosphatase, and increased number of neutrophil mitochondria and ribosomes. SGD1 inheritance can be autosomal dominant or recessive. te=The disease is caused by variants affecting the gene represented in this entry. Immunodeficiency 108 with autoinflammation (IMD108) [MIM:260570]: An autosomal recessive disorder characterized by autoinflammation and immune impairment of neutrophils, manifesting around adolescence. Affected individuals have recurrent episodes of abdominal pain associated with fever and elevated inflammatory markers. Additional features include recurrent infections, particularly of the skin and nails, poor wound healing, and mild bleeding tendencies. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the bZIP family. C/EBP subfamily. Sequence=AAC51130.1; Type=Frameshift; Evidence=; Name=CEBPEbase; Note=CEBPE mutation db; URL="http://structure.bmc.lu.se/idbase/CEBPEbase/"; nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm regulation of transcription, DNA-templated phagocytosis defense response positive regulation of gene expression myeloid cell differentiation macrophage differentiation granulocyte differentiation cytokine biosynthetic process defense response to bacterium protein homodimerization activity positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity cellular response to lipopolysaccharide uc001wiv.1 uc001wiv.2 uc001wiv.3 uc001wiv.4 
ENST00000206542.9 OSGEP ENST00000206542.9 O-sialoglycoprotein endopeptidase (from RefSeq NM_017807.4) ENST00000206542.1 ENST00000206542.2 ENST00000206542.3 ENST00000206542.4 ENST00000206542.5 ENST00000206542.6 ENST00000206542.7 ENST00000206542.8 GCPL1 NM_017807 OSGEP OSGEP_HUMAN Q6IAC3 Q9NPF4 uc001vxf.1 uc001vxf.2 uc001vxf.3 uc001vxf.4 uc001vxf.5 Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; Evidence= Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence=; Note=Binds 1 divalent metal cation per subunit. Component of the EKC/KEOPS complex composed of at least GON7, TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. Interacts with PRAME. Q9NPF4; O95817: BAG3; NbExp=3; IntAct=EBI-1056510, EBI-747185; Q9NPF4; Q14657: LAGE3; NbExp=4; IntAct=EBI-1056510, EBI-1052105; Q9NPF4; Q96S44: TP53RK; NbExp=4; IntAct=EBI-1056510, EBI-739588; Cytoplasm cleus Widely expressed at low level. Expressed in heart, placenta, liver, kidney, lung, brain, skeletal muscle and pancreas. Galloway-Mowat syndrome 3 (GAMOS3) [MIM:617729]: A form of Galloway-Mowat syndrome, a severe renal-neurological disease characterized by early-onset nephrotic syndrome associated with microcephaly, central nervous system abnormalities, developmental delays, and a propensity for seizures. Brain anomalies include gyration defects ranging from lissencephaly to pachygyria and polymicrogyria, and cerebellar hypoplasia. Most patients show facial dysmorphism characterized by a small, narrow forehead, large/floppy ears, deep-set eyes, hypertelorism and micrognathia. Additional variable features are visual impairment and arachnodactyly. Most patients die in early childhood. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the KAE1 / TsaD family. EKC/KEOPS complex tRNA threonylcarbamoyladenosine modification protein binding nucleus nucleoplasm cytoplasm plasma membrane tRNA processing nuclear speck transferase activity transferase activity, transferring acyl groups transferase activity, transferring acyl groups other than amino-acyl groups metal ion binding N(6)-L-threonylcarbamoyladenine synthase uc001vxf.1 uc001vxf.2 uc001vxf.3 uc001vxf.4 uc001vxf.5 
ENST00000206595.11 G2E3 ENST00000206595.11 G2/M-phase specific E3 ubiquitin protein ligase, transcript variant 1 (from RefSeq NM_017769.5) ENST00000206595.1 ENST00000206595.10 ENST00000206595.2 ENST00000206595.3 ENST00000206595.4 ENST00000206595.5 ENST00000206595.6 ENST00000206595.7 ENST00000206595.8 ENST00000206595.9 G2E3_HUMAN KIAA1333 NM_017769 Q7L622 Q9BVR2 Q9H9E9 Q9NXC0 Q9P2L3 uc001wqk.1 uc001wqk.2 uc001wqk.3 uc001wqk.4 E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Essential in early embryonic development to prevent apoptotic death. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Protein modification; protein ubiquitination. Q7L622; Q86V38: ATN1; NbExp=3; IntAct=EBI-751757, EBI-11954292; Q7L622; P42858: HTT; NbExp=6; IntAct=EBI-751757, EBI-466029; Q7L622; Q92876: KLK6; NbExp=3; IntAct=EBI-751757, EBI-2432309; Q7L622; P07196: NEFL; NbExp=3; IntAct=EBI-751757, EBI-475646; Q7L622; P62841: RPS15; NbExp=3; IntAct=EBI-751757, EBI-372635; Q7L622; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-751757, EBI-5235340; Q7L622; O76024: WFS1; NbExp=3; IntAct=EBI-751757, EBI-720609; Nucleus, nucleolus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. In the nucleus, delocalizes from the nucleolus to the nucleoplasm in response to DNA damage. Predominantly expressed in brain, liver, kidney, testes and ovary. Up-regulated approximately 4-fold in G2 when compared to S phase. Down-regulated approximately 3-fold by gamma-irradiation. Ubiquitin ligase activity is mediated by two distinct domains, PHD-type zinc fingers 2 and 3. The use of these distinct domains may allow ubiquitination of different targets by each domain. The HECT domain is catalytically inactive and does not contribute to this activity. Sequence=BAA92571.1; Type=Erroneous initiation; Evidence=; Sequence=BAB14280.1; Type=Erroneous initiation; Evidence=; ubiquitin-protein transferase activity protein binding nucleus nucleolus cytoplasm cytosol apoptotic process multicellular organism development protein ubiquitination transferase activity intracellular membrane-bounded organelle metal ion binding uc001wqk.1 uc001wqk.2 uc001wqk.3 uc001wqk.4 
ENST00000206765.11 TGM1 ENST00000206765.11 transglutaminase 1 (from RefSeq NM_000359.3) B4DWR7 ENST00000206765.1 ENST00000206765.10 ENST00000206765.2 ENST00000206765.3 ENST00000206765.4 ENST00000206765.5 ENST00000206765.6 ENST00000206765.7 ENST00000206765.8 ENST00000206765.9 KTG NM_000359 P22735 Q197M4 TGM1_HUMAN uc001wod.1 uc001wod.2 uc001wod.3 uc001wod.4 The protein encoded by this gene is a membrane protein that catalyzes the addition of an alkyl group from an akylamine to a glutamine residue of a protein, forming an alkylglutamine in the protein. This protein alkylation leads to crosslinking of proteins and catenation of polyamines to proteins. This gene contains either one or two copies of a 22 nt repeat unit in its 3' UTR. Mutations in this gene have been associated with autosomal recessive lamellar ichthyosis (LI) and nonbullous congenital ichthyosiform erythroderma (NCIE). [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC034699.1, AK315819.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000206765.11/ ENSP00000206765.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum. Involved in cell proliferation (PubMed:26220141). Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L- lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence= Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.; Interacts with PLAAT4. P22735; P28330: ACADL; NbExp=3; IntAct=EBI-2562368, EBI-12059321; P22735; P05187: ALPP; NbExp=3; IntAct=EBI-2562368, EBI-1211484; P22735; Q9BXJ1-2: C1QTNF1; NbExp=6; IntAct=EBI-2562368, EBI-11536642; P22735; P55212: CASP6; NbExp=3; IntAct=EBI-2562368, EBI-718729; P22735; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-2562368, EBI-741032; P22735; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-2562368, EBI-713677; P22735; Q92608: DOCK2; NbExp=3; IntAct=EBI-2562368, EBI-448771; P22735; P09211: GSTP1; NbExp=3; IntAct=EBI-2562368, EBI-353467; P22735; P13284: IFI30; NbExp=3; IntAct=EBI-2562368, EBI-2868897; P22735; Q969P0: IGSF8; NbExp=3; IntAct=EBI-2562368, EBI-8293590; P22735; P16144-2: ITGB4; NbExp=3; IntAct=EBI-2562368, EBI-11051601; P22735; Q15040: JOSD1; NbExp=3; IntAct=EBI-2562368, EBI-2510602; P22735; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-2562368, EBI-739863; P22735; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-2562368, EBI-3958099; P22735; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2562368, EBI-21591415; P22735; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-2562368, EBI-10245913; P22735; Q5T753: LCE1E; NbExp=3; IntAct=EBI-2562368, EBI-11955335; P22735; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-2562368, EBI-9394625; P22735; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-2562368, EBI-10246358; P22735; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-2562368, EBI-2858213; P22735; Q92692-2: NECTIN2; NbExp=3; IntAct=EBI-2562368, EBI-6979889; P22735; Q9Y5Y2: NUBP2; NbExp=3; IntAct=EBI-2562368, EBI-1048886; P22735; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2562368, EBI-5280197; P22735; Q14162: SCARF1; NbExp=3; IntAct=EBI-2562368, EBI-12056025; P22735; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2562368, EBI-2623095; P22735; Q9BR01: SULT4A1; NbExp=3; IntAct=EBI-2562368, EBI-6690555; P22735; B2RWP4: TACC2; NbExp=3; IntAct=EBI-2562368, EBI-14211313; P22735; P22735: TGM1; NbExp=3; IntAct=EBI-2562368, EBI-2562368; P22735; Q8WVR3: TRAPPC14; NbExp=3; IntAct=EBI-2562368, EBI-719893; P22735; Q6EMK4: VASN; NbExp=3; IntAct=EBI-2562368, EBI-10249550; P22735; Q8IW00: VSTM4; NbExp=3; IntAct=EBI-2562368, EBI-4311759; Membrane ; Lipid- anchor Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P22735-1; Sequence=Displayed; Name=2; IsoId=P22735-2; Sequence=VSP_056840; Palmitoylated. The membrane anchorage region possesses a cluster of five cysteines within which fatty acid(s) may become thioester-linked. It is subject to phorbol ester-stimulated phosphorylation and is hypersensitive to proteolysis, which releases the enzyme in a soluble form. Tyrosine-phosphorylated. Ichthyosis, congenital, autosomal recessive 1 (ARCI1) [MIM:242300]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non- bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the transglutaminase superfamily. Transglutaminase family. Sequence=AAA61166.1; Type=Frameshift; Evidence=; Sequence=M86360; Type=Frameshift; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tgm1/"; cornified envelope protein-glutamine gamma-glutamyltransferase activity protein binding cytosol plasma membrane cellular protein modification process positive regulation of keratinocyte proliferation membrane transferase activity transferase activity, transferring acyl groups peptide cross-linking keratinocyte differentiation intrinsic component of membrane keratinization cell envelope organization positive regulation of cell cycle metal ion binding extracellular exosome cornification uc001wod.1 uc001wod.2 uc001wod.3 uc001wod.4 
ENST00000207457.8 TEKT2 ENST00000207457.8 tektin 2 (from RefSeq NM_014466.3) A6NIS6 ENST00000207457.1 ENST00000207457.2 ENST00000207457.3 ENST00000207457.4 ENST00000207457.5 ENST00000207457.6 ENST00000207457.7 NM_014466 O60638 Q9UIF3 TEKT2 TEKT2_HUMAN uc001bzr.1 uc001bzr.2 uc001bzr.3 uc001bzr.4 This gene product belongs to the tektin family of proteins. Tektins comprise a family of filament-forming proteins that are coassembled with tubulins to form ciliary and flagellar microtubules. This gene is expressed in the testis and its protein is localized to the flagella of the sperms, indicating that it may play a role in spermatogenesis. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AF054910.1, SRR5189667.198951.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2144120 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000207457.8/ ENSP00000207457.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme (PubMed:36191189). Plays a key role in the assembly or attachment of the inner dynein arm to microtubules in sperm flagella and tracheal cilia. Forms filamentous polymers in the walls of ciliary and flagellar microtubules. May interact with CCDC172. Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, flagellum axoneme Cytoplasm, cytoskeleton, microtubule organizing center Note=Colocalized with CCDC172 at the perinuclear region. Expressed at high levels in testis, trachea and fetal lung, and at lower levels in ovary, pituitary, adult lung, fetal brain and fetal kidney. Tyrosine phosphorylated. Belongs to the tektin family. nucleus cytoplasm microtubule organizing center cytoskeleton microtubule cilium microtubule cytoskeleton cell projection organization flagellated sperm motility motile cilium inner dynein arm assembly cell projection cilium assembly cilium movement involved in cell motility uc001bzr.1 uc001bzr.2 uc001bzr.3 uc001bzr.4 
ENST00000207549.9 UNC13D ENST00000207549.9 unc-13 homolog D (from RefSeq NM_199242.3) B4DWG9 ENST00000207549.1 ENST00000207549.2 ENST00000207549.3 ENST00000207549.4 ENST00000207549.5 ENST00000207549.6 ENST00000207549.7 ENST00000207549.8 NM_199242 Q70J99 Q9H7K5 UN13D_HUMAN uc002jpp.1 uc002jpp.2 uc002jpp.3 uc002jpp.4 uc002jpp.5 uc002jpp.6 This gene encodes a protein that is a member of the UNC13 family, containing similar domain structure as other family members but lacking an N-terminal phorbol ester-binding C1 domain present in other Munc13 proteins. The protein appears to play a role in vesicle maturation during exocytosis and is involved in regulation of cytolytic granules secretion. Mutations in this gene are associated with familial hemophagocytic lymphohistiocytosis type 3, a genetically heterogeneous, rare autosomal recessive disorder. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC067084.1, AJ578444.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)- dependent secretory lysosome exocytosis in mast cells. Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Interacts with DOC2A (By similarity). Interacts with RAB27A (PubMed:15548590, PubMed:17237785). Interacts with RHOG; the interaction increases RhoG affinity to the membrane lipids, targets UNC13D to membrane lipids and facilitates cytotoxic granule (CG) docking to the plasma membrane (PubMed:33513601). Q70J99; P51159: RAB27A; NbExp=3; IntAct=EBI-11479429, EBI-716881; Q70J99; P84095: RHOG; NbExp=6; IntAct=EBI-11479429, EBI-446579; Cytoplasm. Membrane; Peripheral membrane protein. Late endosome. Recycling endosome. Lysosome. Note=Colocalizes with cytotoxic granules at the plasma membrane. Localizes to endosomal exocytic vesicles. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q70J99-1; Sequence=Displayed; Name=2; IsoId=Q70J99-2; Sequence=VSP_011385, VSP_011386, VSP_011387; Name=3; IsoId=Q70J99-3; Sequence=VSP_037949; Expressed at high levels in spleen, thymus and leukocytes. Also expressed in lung and placenta, and at very low levels in brain, heart, skeletal muscle and kidney. Expressed in cytotoxic T- lymphocytes (CTL) and mast cells. The MHD1 and MHD2 domains mediate localization on recycling endosomes and lysosome. Hemophagocytic lymphohistiocytosis, familial, 3 (FHL3) [MIM:608898]: A rare disorder characterized by immune dysregulation with hypercytokinemia, defective function of natural killer cell, and massive infiltration of several organs by activated lymphocytes and macrophages. The clinical features of the disease include fever, hepatosplenomegaly, cytopenia, and less frequently neurological abnormalities ranging from irritability and hypotonia to seizures, cranial nerve deficits and ataxia. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the unc-13 family. Sequence=BAB15764.1; Type=Erroneous initiation; Evidence=; Name=UNC13Dbase; Note=UNC13D mutation db; URL="http://structure.bmc.lu.se/idbase/UNC13Dbase/"; granuloma formation germinal center formation protein binding extracellular region cytoplasm lysosome endosome late endosome cytosol exocytosis phagocytosis membrane Rab GTPase binding Weibel-Palade body azurophil granule lumen intracellular membrane-bounded organelle regulation of mast cell degranulation neutrophil degranulation natural killer cell degranulation positive regulation of exocytosis defense response to virus recycling endosome exocytic vesicle positive regulation of substrate adhesion-dependent cell spreading positive regulation of regulated secretory pathway uc002jpp.1 uc002jpp.2 uc002jpp.3 uc002jpp.4 uc002jpp.5 uc002jpp.6 
ENST00000207870.8 XYLB ENST00000207870.8 xylulokinase, transcript variant 2 (from RefSeq NM_005108.4) B2RAW4 B4DDT2 B9EH64 ENST00000207870.1 ENST00000207870.2 ENST00000207870.3 ENST00000207870.4 ENST00000207870.5 ENST00000207870.6 ENST00000207870.7 NM_005108 O75191 XYLB_HUMAN uc003cic.1 uc003cic.2 uc003cic.3 uc003cic.4 The protein encoded by this gene shares 22% sequence identity with Hemophilus influenzae xylulokinase, and even higher identity to other gene products in C.elegans (45%) and yeast (31-35%), which are thought to belong to a family of enzymes that include fucokinase, gluconokinase, glycerokinase and xylulokinase. These proteins play important roles in energy metabolism. [provided by RefSeq, Aug 2009]. Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+); Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140, ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216; EC=2.7.1.17; Evidence=; Kinetic parameters: KM=24 uM for D-xylulose ; Monomer. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75191-1; Sequence=Displayed; Name=2; IsoId=O75191-2; Sequence=VSP_055522; Belongs to the FGGY kinase family. Sequence=BAA31527.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence=; nucleotide binding xylulokinase activity ATP binding cytosol carbohydrate metabolic process xylulose metabolic process xylulose catabolic process generation of precursor metabolites and energy kinase activity phosphorylation transferase activity phosphotransferase activity, alcohol group as acceptor glucuronate catabolic process to xylulose 5-phosphate D-xylose metabolic process carbohydrate phosphorylation uc003cic.1 uc003cic.2 uc003cic.3 uc003cic.4 
ENST00000209668.3 ADH1A ENST00000209668.3 alcohol dehydrogenase 1A (class I), alpha polypeptide (from RefSeq NM_000667.4) A8K3E3 ADH1 ADH1A_HUMAN ENST00000209668.1 ENST00000209668.2 NM_000667 P07327 Q17R68 uc003hur.1 uc003hur.2 uc003hur.3 uc003hur.4 This gene encodes a member of the alcohol dehydrogenase family. The encoded protein is the alpha subunit of class I alcohol dehydrogenase, which consists of several homo- and heterodimers of alpha, beta and gamma subunits. Alcohol dehydrogenases catalyze the oxidation of alcohols to aldehydes. This gene is active in the liver in early fetal life but only weakly active in adult liver. This gene is found in a cluster with six additional alcohol dehydrogenase genes, including those encoding the beta and gamma subunits, on the long arm of chromosome 4. Mutations in this gene may contribute to variation in certain personality traits and substance dependence. [provided by RefSeq, Nov 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK290558.1, SRR5189664.58023.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968540, SAMEA1968968 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000209668.3/ ENSP00000209668.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed:2738060). Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence=; Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence=; Reaction=butan-1-ol + NAD(+) = butanal + H(+) + NADH; Xref=Rhea:RHEA:33199, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743, ChEBI:CHEBI:28885, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; Reaction=1-propanol + NAD(+) = H(+) + NADH + propanal; Xref=Rhea:RHEA:50704, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153, ChEBI:CHEBI:28831, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 2 Zn(2+) ions per subunit. Kinetic parameters: KM=32 uM for butan-1-ol ; KM=14 uM for 1-propanol ; KM=6100 uM for ethanol ; Dimer of identical or heterodimer of closely related subunits alpha, beta, or gamma that are encoded by genes ADH1A, ADH1B, and ADH1C, respectively. Cytoplasm. There are 7 different ADH's isozymes in human: three belongs to class-I: ADH1A, ADH1B, and ADH1C, one to class-II: ADH4, one to class-III: ADH5, one to class-IV: ADH7 and one to class-V: ADH6. Belongs to the zinc-containing alcohol dehydrogenase family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/adh1a/"; alcohol dehydrogenase (NAD) activity alcohol dehydrogenase activity, zinc-dependent retinol dehydrogenase activity protein binding nucleoplasm cytoplasm cytosol plasma membrane alcohol metabolic process ethanol oxidation zinc ion binding oxidoreductase activity drug metabolic process retinol metabolic process retinoic acid metabolic process metal ion binding oxidation-reduction process uc003hur.1 uc003hur.2 uc003hur.3 uc003hur.4 
ENST00000209718.8 KRT23 ENST00000209718.8 keratin 23, transcript variant 1 (from RefSeq NM_015515.5) A8K084 B7Z7J2 ENST00000209718.1 ENST00000209718.2 ENST00000209718.3 ENST00000209718.4 ENST00000209718.5 ENST00000209718.6 ENST00000209718.7 I3L3Q6 K1C23_HUMAN NM_015515 Q9C075 Q9NUR6 uc002hvm.1 uc002hvm.2 uc002hvm.3 uc002hvm.4 The protein encoded by this gene is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]. Heterotetramer of two type I and two type II keratins. Q9C075; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-3211278, EBI-11984663; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9C075-1; Sequence=Displayed; Name=2; IsoId=Q9C075-2; Sequence=VSP_055662; There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa). Belongs to the intermediate filament family. structural molecule activity cytosol intermediate filament keratinization cornification uc002hvm.1 uc002hvm.2 uc002hvm.3 uc002hvm.4 
ENST00000209728.9 CDC6 ENST00000209728.9 cell division cycle 6 (from RefSeq NM_001254.4) CDC18L CDC6_HUMAN ENST00000209728.1 ENST00000209728.2 ENST00000209728.3 ENST00000209728.4 ENST00000209728.5 ENST00000209728.6 ENST00000209728.7 ENST00000209728.8 NM_001254 Q8TB30 Q99741 uc002huj.1 uc002huj.2 uc002huj.3 The protein encoded by this gene is highly similar to Saccharomyces cerevisiae Cdc6, a protein essential for the initiation of DNA replication. This protein functions as a regulator at the early steps of DNA replication. It localizes in cell nucleus during cell cyle G1, but translocates to the cytoplasm at the start of S phase. The subcellular translocation of this protein during cell cyle is regulated through its phosphorylation by Cdks. Transcription of this protein was reported to be regulated in response to mitogenic signals through transcriptional control mechanism involving E2F proteins. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803617.4610.1, AK313620.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000209728.9/ ENSP00000209728.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated. Interacts with PCNA, ORC1, cyclin-CDK (PubMed:9566895). Interacts with HUWE1 (PubMed:17567951). Interacts with ANKRD17 (PubMed:23711367). Interacts with GRWD1; origin binding of GRWD1 is dependent on CDC6 (PubMed:25990725). Interacts with CDT1; are mutually dependent on one another for loading MCM complexes onto chromatin (PubMed:14672932). Interacts with TTC4 (PubMed:18320024). Interacts (via Cy motif) with CCNF; the interaction takes place during G2 and M phase (PubMed:26818844). Interacts with CDH1 (PubMed:26818844). Q99741; P06493: CDK1; NbExp=2; IntAct=EBI-374862, EBI-444308; Q99741; P38936: CDKN1A; NbExp=2; IntAct=EBI-374862, EBI-375077; Q99741; Q9H211: CDT1; NbExp=3; IntAct=EBI-374862, EBI-456953; Q99741; P53350: PLK1; NbExp=6; IntAct=EBI-374862, EBI-476768; Nucleus toplasm Note=The protein is nuclear in G1 and cytoplasmic in S-phase cells (PubMed:9566895). Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase complex. Meier-Gorlin syndrome 5 (MGORS5) [MIM:613805]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the CDC6/cdc18 family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40014/CDC6"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc6/"; DNA replication checkpoint regulation of cyclin-dependent protein serine/threonine kinase activity G1/S transition of mitotic cell cycle regulation of transcription involved in G1/S transition of mitotic cell cycle nucleotide binding mitotic cell cycle spindle pole DNA replication origin binding protein binding ATP binding nucleus nucleoplasm cytoplasm cytosol DNA replication DNA replication initiation cell cycle traversing start control point of mitotic cell cycle negative regulation of DNA replication negative regulation of cell proliferation kinase binding regulation of mitotic metaphase/anaphase transition positive regulation of cytokinesis mitotic DNA replication checkpoint positive regulation of cyclin-dependent protein serine/threonine kinase activity positive regulation of fibroblast proliferation spindle midzone cell division positive regulation of chromosome segregation cellular response to vasopressin cellular response to angiotensin nucleolus uc002huj.1 uc002huj.2 uc002huj.3 
ENST00000209873.9 AAAS ENST00000209873.9 aladin WD repeat nucleoporin, transcript variant 1 (from RefSeq NM_015665.6) AAAS_HUMAN ADRACALA ENST00000209873.1 ENST00000209873.2 ENST00000209873.3 ENST00000209873.4 ENST00000209873.5 ENST00000209873.6 ENST00000209873.7 ENST00000209873.8 GL003 NM_015665 Q5JB47 Q9NRG9 Q9NWI6 Q9UG19 uc001scr.1 uc001scr.2 uc001scr.3 uc001scr.4 uc001scr.5 uc001scr.6 The protein encoded by this gene is a member of the WD-repeat family of regulatory proteins and may be involved in normal development of the peripheral and central nervous system. The encoded protein is part of the nuclear pore complex and is anchored there by NDC1. Defects in this gene are a cause of achalasia-addisonianism-alacrima syndrome (AAAS), also called triple-A syndrome or Allgrove syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2010]. Plays a role in the normal development of the peripheral and central nervous system (PubMed:11062474, PubMed:11159947, PubMed:16022285). Required for the correct localization of aurora kinase AURKA and the microtubule minus end-binding protein NUMA1 as well as a subset of AURKA targets which ensures proper spindle formation and timely chromosome alignment (PubMed:26246606). Interacts with NDC1, the interaction is required for nuclear pore localization (PubMed:19782045). Interacts with the inactive form aurora kinase AURKA (PubMed:26246606). Interacts with PGRMC2 (PubMed:27754849). Nucleus, nuclear pore complex Cytoplasm, cytoskeleton, spindle pole Nucleus envelope Note=In metaphase cells localizes within the spindle with some accumulation around spindle poles, with the highest concentration between the centrosome and metaphase plate (PubMed:26246606). The localization to the spindle is microtubule- mediated (PubMed:26246606). Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=AAAS-v1; IsoId=Q9NRG9-1; Sequence=Displayed; Name=2; Synonyms=AAAS-v2; IsoId=Q9NRG9-2; Sequence=VSP_043014; Widely expressed (PubMed:11159947, PubMed:16022285). Particularly abundant in cerebellum, corpus callosum, adrenal gland, pituitary gland, gastrointestinal structures and fetal lung (PubMed:11159947). Achalasia-addisonianism-alacrima syndrome (AAAS) [MIM:231550]: An autosomal recessive disorder characterized by adreno-corticotropic hormone (ACTH)-resistant adrenal failure, achalasia of the esophageal cardia and alacrima. The syndrome is associated with variable and progressive neurological impairment involving the central, peripheral, and autonomic nervous system. Other features such as palmoplantar hyperkeratosis, short stature, facial dysmorphy and osteoporosis may also be present. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 2]: Ubiquitously expressed. spindle pole microtubule bundle formation molecular_function nucleus nuclear envelope nuclear pore nucleoplasm cytoplasm centrosome cytosol cytoskeleton regulation of glycolytic process mRNA export from nucleus tRNA export from nucleus nucleocytoplasmic transport learning fertilization protein transport membrane viral process protein sumoylation viral transcription nuclear membrane host cell regulation of nucleocytoplasmic transport mRNA transport regulation of gene silencing by miRNA mitotic spindle intracellular transport of virus mitotic spindle assembly regulation of cellular response to heat uc001scr.1 uc001scr.2 uc001scr.3 uc001scr.4 uc001scr.5 uc001scr.6 
ENST00000209875.9 CBX5 ENST00000209875.9 chromobox 5, transcript variant 3 (from RefSeq NM_012117.3) ENST00000209875.1 ENST00000209875.2 ENST00000209875.3 ENST00000209875.4 ENST00000209875.5 ENST00000209875.6 ENST00000209875.7 ENST00000209875.8 HEL25 NM_012117 V9HWG0 V9HWG0_HUMAN uc001sfk.1 uc001sfk.2 uc001sfk.3 uc001sfk.4 uc001sfk.5 uc001sfk.6 uc001sfk.7 This gene encodes a highly conserved nonhistone protein, which is a member of the heterochromatin protein family. The protein is enriched in the heterochromatin and associated with centromeres. The protein has a single N-terminal chromodomain which can bind to histone proteins via methylated lysine residues, and a C-terminal chromo shadow-domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated nonhistone proteins. The encoded product is involved in the formation of functional kinetochore through interaction with essential kinetochore proteins. The gene has a pseudogene located on chromosome 3. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jul 2008]. V9HWG0; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-10183977, EBI-10181276; V9HWG0; Q9BZ95: NSD3; NbExp=3; IntAct=EBI-10183977, EBI-3390132; V9HWG0; P23497: SP100; NbExp=3; IntAct=EBI-10183977, EBI-751145; V9HWG0; O43463: SUV39H1; NbExp=3; IntAct=EBI-10183977, EBI-349968; V9HWG0; Q9H5I1: SUV39H2; NbExp=3; IntAct=EBI-10183977, EBI-723127; V9HWG0; Q548N1: VPS28; NbExp=3; IntAct=EBI-10183977, EBI-10243107; histone deacetylase complex kinetochore nuclear chromosome, telomeric region heterochromatin chromatin binding protein binding nucleus nuclear heterochromatin pericentric heterochromatin nucleolus chromocenter transcriptional repressor complex protein binding, bridging methylated histone binding histone methyltransferase complex protein homodimerization activity histone deacetylase binding negative regulation of transcription, DNA-templated repressing transcription factor binding uc001sfk.1 uc001sfk.2 uc001sfk.3 uc001sfk.4 uc001sfk.5 uc001sfk.6 uc001sfk.7 
ENST00000209884.5 KLHL20 ENST00000209884.5 kelch like family member 20 (from RefSeq NM_014458.4) B3KMA0 B4DUR0 ENST00000209884.1 ENST00000209884.2 ENST00000209884.3 ENST00000209884.4 KLEIP KLH20_HUMAN KLHLX NM_014458 Q5TZF2 Q5ZF45 Q9H457 Q9Y2M5 uc001gjc.1 uc001gjc.2 uc001gjc.3 uc001gjc.4 uc001gjc.5 uc001gjc.6 The protein encoded by this gene is a member of the kelch family of proteins, which is characterized by a 44-56 amino acid repeat motif. The kelch motif appears in many different polypeptide contexts and contains multiple potential protein-protein contact sites. Members of this family are present both throughout the cell and extracellularly, with diverse activities. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.43618.1, SRR1660803.104669.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000209884.5/ ENSP00000209884.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis (PubMed:20389280). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination (PubMed:24768539). Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking (PubMed:24768539). Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (PubMed:21670212). In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression (PubMed:21840486). Protein modification; protein ubiquitination. Component of the BCR(KLHL20) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL20 and RBX1. Interacts with PDZ- RhoGEF/ARHGEF11, DAPK1, PML and CORO7. Interacts with F-actin. Interacts with IFN-gamma (IFNG). Interacts (via kelch repeats) with IVNS1ABP (via kelch repeats); this interaction blocks the assembly of CUL3-KLHL20 complex (PubMed:25619834). Q9Y2M5; Q86V38: ATN1; NbExp=3; IntAct=EBI-714379, EBI-11954292; Q9Y2M5; P54253: ATXN1; NbExp=6; IntAct=EBI-714379, EBI-930964; Q9Y2M5; P54252: ATXN3; NbExp=3; IntAct=EBI-714379, EBI-946046; Q9Y2M5; P46379-2: BAG6; NbExp=3; IntAct=EBI-714379, EBI-10988864; Q9Y2M5; P02489: CRYAA; NbExp=3; IntAct=EBI-714379, EBI-6875961; Q9Y2M5; Q13618: CUL3; NbExp=8; IntAct=EBI-714379, EBI-456129; Q9Y2M5; P53355: DAPK1; NbExp=11; IntAct=EBI-714379, EBI-358616; Q9Y2M5; P09172: DBH; NbExp=3; IntAct=EBI-714379, EBI-8589586; Q9Y2M5; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-714379, EBI-25840379; Q9Y2M5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-714379, EBI-10976677; Q9Y2M5; P00488: F13A1; NbExp=3; IntAct=EBI-714379, EBI-2565863; Q9Y2M5; P22607: FGFR3; NbExp=3; IntAct=EBI-714379, EBI-348399; Q9Y2M5; P14136: GFAP; NbExp=3; IntAct=EBI-714379, EBI-744302; Q9Y2M5; O14908-2: GIPC1; NbExp=3; IntAct=EBI-714379, EBI-25913156; Q9Y2M5; Q53GS7: GLE1; NbExp=3; IntAct=EBI-714379, EBI-1955541; Q9Y2M5; P28799: GRN; NbExp=3; IntAct=EBI-714379, EBI-747754; Q9Y2M5; P06396: GSN; NbExp=3; IntAct=EBI-714379, EBI-351506; Q9Y2M5; P04792: HSPB1; NbExp=3; IntAct=EBI-714379, EBI-352682; Q9Y2M5; O43464: HTRA2; NbExp=3; IntAct=EBI-714379, EBI-517086; Q9Y2M5; P42858: HTT; NbExp=9; IntAct=EBI-714379, EBI-466029; Q9Y2M5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-714379, EBI-10975473; Q9Y2M5; O14901: KLF11; NbExp=3; IntAct=EBI-714379, EBI-948266; Q9Y2M5; Q92876: KLK6; NbExp=3; IntAct=EBI-714379, EBI-2432309; Q9Y2M5; P51608: MECP2; NbExp=3; IntAct=EBI-714379, EBI-1189067; Q9Y2M5; P19404: NDUFV2; NbExp=3; IntAct=EBI-714379, EBI-713665; Q9Y2M5; P29474: NOS3; NbExp=3; IntAct=EBI-714379, EBI-1391623; Q9Y2M5; Q13153: PAK1; NbExp=3; IntAct=EBI-714379, EBI-1307; Q9Y2M5; O14832: PHYH; NbExp=3; IntAct=EBI-714379, EBI-721853; Q9Y2M5; P29590: PML; NbExp=9; IntAct=EBI-714379, EBI-295890; Q9Y2M5; D3DTS7: PMP22; NbExp=3; IntAct=EBI-714379, EBI-25882629; Q9Y2M5; O60260-5: PRKN; NbExp=3; IntAct=EBI-714379, EBI-21251460; Q9Y2M5; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-714379, EBI-912440; Q9Y2M5; P60891: PRPS1; NbExp=3; IntAct=EBI-714379, EBI-749195; Q9Y2M5; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-714379, EBI-396669; Q9Y2M5; P37840: SNCA; NbExp=3; IntAct=EBI-714379, EBI-985879; Q9Y2M5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-714379, EBI-5235340; Q9Y2M5; Q13148: TARDBP; NbExp=3; IntAct=EBI-714379, EBI-372899; Q9Y2M5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-714379, EBI-12806590; Q9Y2M5; P02766: TTR; NbExp=3; IntAct=EBI-714379, EBI-711909; Q9Y2M5; O76024: WFS1; NbExp=3; IntAct=EBI-714379, EBI-720609; Cytoplasm, perinuclear region. Nucleus. Golgi apparatus, trans-Golgi network. Cell projection, axon Cell projection, dendrite Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN- gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (PubMed:20389280). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y2M5-1; Sequence=Displayed; Name=2; IsoId=Q9Y2M5-2; Sequence=VSP_057026, VSP_057027; By hypoxia. actin binding ubiquitin-protein transferase activity protein binding nucleus cytoplasm Golgi apparatus trans-Golgi network cytosol Golgi to endosome transport cytoskeleton organization protein transport actin cytoskeleton protein ubiquitination PML body interferon-gamma binding axon dendrite Cul3-RING ubiquitin ligase complex response to interferon-alpha cell projection negative regulation of apoptotic process proteasome-mediated ubiquitin-dependent protein catabolic process post-translational protein modification perinuclear region of cytoplasm protein K33-linked ubiquitination uc001gjc.1 uc001gjc.2 uc001gjc.3 uc001gjc.4 uc001gjc.5 uc001gjc.6 
ENST00000209929.10 FMO2 ENST00000209929.10 flavin containing dimethylaniline monoxygenase 2, transcript variant 6 (from RefSeq NR_160266.1) ENST00000209929.1 ENST00000209929.2 ENST00000209929.3 ENST00000209929.4 ENST00000209929.5 ENST00000209929.6 ENST00000209929.7 ENST00000209929.8 ENST00000209929.9 FMO2 FMO2_HUMAN NR_160266 Q5EBX4 Q86U73 Q99518 Q9BRX1 uc057ngi.1 uc057ngi.2 This gene encodes a flavin-containing monooxygenase family member. It is an NADPH-dependent enzyme that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, some human populations contain an allele (FMO2*2A) with a premature stop codon, resulting in a protein that is C-terminally-truncated, has no catalytic activity, and is likely degraded rapidly. This gene is found in a cluster with other related family members on chromosome 1. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2014]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.72069.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1968189 [ECO:0000348] ##Evidence-Data-END## Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation (PubMed:9804831, PubMed:15294458, PubMed:15144220, PubMed:18948378, PubMed:18930751). Specifically catalyzes S-oxygenation of sulfur derived compounds such as thioureas-derived compounds, thioetherorganophosphates to their sulfenic acid (PubMed:9804831, PubMed:15144220). In vitro, catalyzes S-oxygenation of the second-line antitubercular drugs thiacetazone (TAZ) and ethionamide (ETA), forming a sulfinic acid and a carbodiimide via a postulated sulfenic acid intermediate (PubMed:18948378, PubMed:18930751). Also catalyzes S- oxygenation of the thioether-containing organophosphate insecticides, phorate and disulfoton (PubMed:15294458). Name=FAD; Xref=ChEBI:CHEBI:57692; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Kinetic parameters: KM=411 uM for methimazole ; KM=27 uM for thiourea ; KM=14 uM for ethylenethiourea ; KM=29 uM for N-phenylthiourea ; KM=42 uM for ANTU ; KM=5.8 uM for thioacetazone ; KM=575.75 uM for methimazole ; KM=261 uM for ethionamide ; KM=57 uM for phorate ; KM=32 uM for disulfoton ; Microsome membrane ; Single-pass membrane protein Endoplasmic reticulum membrane ; Single-pass membrane protein Expressed in lung (at protein level). Expressed predominantly in lung, and at a much lesser extent in kidney. Also expressed in fetal lung, but not in liver, kidney and brain. The sequence shown is that of the allele FMO2*1. FMO2*2A is the major allele in the human population, however it encodes a truncated and catalytically inactive protein (PubMed:9804831). FMO2*2A occurs in essentially 100% of Caucasians and Asians (PubMed:9804831). FMO2*1 is present at a frequency of approximately 4% to 13% in the sample of population of African descent (PubMed:9804831, PubMed:11042094, PubMed:18794725). Belongs to the FMO family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fmo2/"; monooxygenase activity N,N-dimethylaniline monooxygenase activity endoplasmic reticulum endoplasmic reticulum membrane organic acid metabolic process NADP metabolic process xenobiotic metabolic process toxin metabolic process membrane integral component of membrane oxidoreductase activity drug metabolic process organelle membrane intracellular membrane-bounded organelle flavin adenine dinucleotide binding NADP binding oxidation-reduction process NADPH oxidation oxygen metabolic process uc057ngi.1 uc057ngi.2 
ENST00000210060.12 DHPS ENST00000210060.12 deoxyhypusine synthase, transcript variant 11 (from RefSeq NR_161469.1) A8K688 DHYS_HUMAN DS ENST00000210060.1 ENST00000210060.10 ENST00000210060.11 ENST00000210060.2 ENST00000210060.3 ENST00000210060.4 ENST00000210060.5 ENST00000210060.6 ENST00000210060.7 ENST00000210060.8 ENST00000210060.9 M0R1I5 NR_161469 P49366 Q13184 Q13276 Q9UDG0 uc002muh.1 uc002muh.2 uc002muh.3 uc002muh.4 This gene encodes a protein that is required for the formation of hypusine, a unique amino acid formed by the posttranslational modification of only one protein, eukaryotic translation initiation factor 5A. The encoded protein catalyzes the first step in hypusine formation by transferring the butylamine moiety of spermidine to a specific lysine residue of the eukaryotic translation initiation factor 5A precursor, forming an intermediate deoxyhypusine residue. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 2011]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.499141.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue (PubMed:30661771). This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function. Reaction=[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]- deoxyhypusine + propane-1,3-diamine; Xref=Rhea:RHEA:33299, Rhea:RHEA- COMP:10143, Rhea:RHEA-COMP:10144, ChEBI:CHEBI:29969, ChEBI:CHEBI:57484, ChEBI:CHEBI:57834, ChEBI:CHEBI:82657; EC=2.5.1.46; Evidence=; Name=NAD(+); Xref=ChEBI:CHEBI:57540; Protein modification; eIF5A hypusination. Homotetramer formed by a dimer of dimers. P49366; P49366: DHPS; NbExp=4; IntAct=EBI-741925, EBI-741925; P49366; P63241: EIF5A; NbExp=6; IntAct=EBI-741925, EBI-373150; P49366; Q9GZV4: EIF5A2; NbExp=7; IntAct=EBI-741925, EBI-748028; P49366; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-741925, EBI-739832; P49366; P27361: MAPK3; NbExp=10; IntAct=EBI-741925, EBI-73995; P49366; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-741925, EBI-16439278; P49366; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-741925, EBI-740897; P49366; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-741925, EBI-741158; P49366; Q6ZVK8: NUDT18; NbExp=3; IntAct=EBI-741925, EBI-740486; P49366; P26367: PAX6; NbExp=3; IntAct=EBI-741925, EBI-747278; P49366; Q9HD43: PTPRH; NbExp=3; IntAct=EBI-741925, EBI-1267176; P49366; O00194: RAB27B; NbExp=6; IntAct=EBI-741925, EBI-10179046; P49366; P09455: RBP1; NbExp=3; IntAct=EBI-741925, EBI-2623483; P49366; Q04864: REL; NbExp=3; IntAct=EBI-741925, EBI-307352; P49366; Q04864-2: REL; NbExp=3; IntAct=EBI-741925, EBI-10829018; P49366; P32969: RPL9P9; NbExp=11; IntAct=EBI-741925, EBI-358122; P49366; Q7L8A9: VASH1; NbExp=3; IntAct=EBI-741925, EBI-10256546; P49366; P52744: ZNF138; NbExp=3; IntAct=EBI-741925, EBI-10746567; P49366; P52744-2: ZNF138; NbExp=3; IntAct=EBI-741925, EBI-10213071; Event=Alternative splicing; Named isoforms=3; Name=Long; IsoId=P49366-1; Sequence=Displayed; Name=Short; IsoId=P49366-2; Sequence=VSP_001351; Name=3; IsoId=P49366-3; Sequence=VSP_047564; Neurodevelopmental disorder with seizures and speech and walking impairment (NEDSSWI) [MIM:618480]: An autosomal recessive disorder characterized by global developmental delay with intellectual disability and poor speech acquisition, and walking difficulties due to hypotonia, hypertonia, spasticity, or poor coordination. Additional features include seizures, mild dysmorphic features, and variable short stature. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform Short]: Inactive. Belongs to the deoxyhypusine synthase family. Sequence=AL520040; Type=Frameshift; Evidence=; protein binding cytoplasm cytosol translation spermidine metabolic process positive regulation of cell proliferation peptidyl-lysine modification to peptidyl-hypusine transferase activity deoxyhypusine synthase activity identical protein binding uc002muh.1 uc002muh.2 uc002muh.3 uc002muh.4 
ENST00000210187.11 RAB26 ENST00000210187.11 RAB26, member RAS oncogene family, transcript variant 1 (from RefSeq NM_014353.5) B2RAA6 ENST00000210187.1 ENST00000210187.10 ENST00000210187.2 ENST00000210187.3 ENST00000210187.4 ENST00000210187.5 ENST00000210187.6 ENST00000210187.7 ENST00000210187.8 ENST00000210187.9 NM_014353 Q3L6K5 Q6NXS7 Q9ULW5 RAB26_HUMAN uc002cou.1 uc002cou.2 uc002cou.3 uc002cou.4 uc002cou.5 Members of the RAB protein family, including RAB26, are important regulators of vesicular fusion and trafficking. The RAB family of small G proteins regulates intercellular vesicle trafficking, including exocytosis, endocytosis, and recycling (summary by Seki et al., 2000 [PubMed 11043516]).[supplied by OMIM, Nov 2010]. The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach. Plays a role in the secretion of amylase from acinar granules in the parotid gland. Interacts with RIMS1 (By similarity). Interacts with ADRA2B. Q9ULW5; P18089: ADRA2B; NbExp=4; IntAct=EBI-958239, EBI-9077302; Q9ULW5; Q5TD97: FHL5; NbExp=3; IntAct=EBI-958239, EBI-750641; Q9ULW5; Q14525: KRT33B; NbExp=3; IntAct=EBI-958239, EBI-1049638; Q9ULW5; O43482: OIP5; NbExp=3; IntAct=EBI-958239, EBI-536879; Q9ULW5; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-958239, EBI-12817837; Golgi apparatus membrane ; Lipid-anchor ; Cytoplasmic side Cytoplasmic vesicle, secretory vesicle membrane ; Lipid-anchor ; Cytoplasmic side Note=Not localized at the plasma membrane (By similarity). Inhibition of S-geranylgeranyl cysteine formation abolishes membrane location. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9ULW5-1; Sequence=Displayed; Name=2; IsoId=Q9ULW5-2; Sequence=VSP_056879; Predominantly expressed in brain. Belongs to the small GTPase superfamily. Rab family. Sequence=BAA84707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Golgi membrane nucleotide binding GTPase activity protein binding GTP binding Golgi apparatus intracellular protein transport protein transport membrane regulation of exocytosis GMP binding transport vesicle membrane secretory granule membrane intrinsic component of plasma membrane cytoplasmic vesicle Rab protein signal transduction exocrine system development Golgi to plasma membrane protein transport regulated exocytosis anchored component of synaptic vesicle membrane regulation of protein catabolic process at presynapse, modulating synaptic transmission uc002cou.1 uc002cou.2 uc002cou.3 uc002cou.4 uc002cou.5 
ENST00000210313.8 PSMD5 ENST00000210313.8 proteasome 26S subunit, non-ATPase 5, transcript variant 1 (from RefSeq NM_005047.4) B4DZM8 ENST00000210313.1 ENST00000210313.2 ENST00000210313.3 ENST00000210313.4 ENST00000210313.5 ENST00000210313.6 ENST00000210313.7 KIAA0072 NM_005047 PSMD5_HUMAN Q15045 Q16401 Q4VXG8 uc004bko.1 uc004bko.2 uc004bko.3 uc004bko.4 uc004bko.5 uc004bko.6 The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a non-ATPase subunit of the 19S regulator base that functions as a chaperone protein during 26S proteasome assembly. [provided by RefSeq, Jul 2012]. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5. Interacts with PSMC1, PSMC2, PSMD1 and PSMD6. Part of transient complex containing PSMD5, PSMC2, PSMC1 and PSMD2 formed during the assembly of the 26S proteasome. Q16401; Q9H0C5: BTBD1; NbExp=3; IntAct=EBI-752143, EBI-935503; Q16401; Q9BX70: BTBD2; NbExp=3; IntAct=EBI-752143, EBI-710091; Q16401; Q8WTX7: CASTOR1; NbExp=3; IntAct=EBI-752143, EBI-10276168; Q16401; P49821: NDUFV1; NbExp=3; IntAct=EBI-752143, EBI-748312; Q16401; P62191: PSMC1; NbExp=12; IntAct=EBI-752143, EBI-357598; Q16401; P35998: PSMC2; NbExp=23; IntAct=EBI-752143, EBI-359710; Q16401; Q12800: TFCP2; NbExp=3; IntAct=EBI-752143, EBI-717422; Q16401; O76024: WFS1; NbExp=3; IntAct=EBI-752143, EBI-720609; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q16401-1; Sequence=Displayed; Name=2; IsoId=Q16401-2; Sequence=VSP_045176; Rich in dileucine repeats, which have been implicated in trafficking of a variety of transmembrane proteins. Belongs to the proteasome subunit S5B/HSM3 family. Was initially identified as a genuine component of the 26S proteasome. MAPK cascade protein polyubiquitination proteasome complex stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent protein binding nucleoplasm cytosol regulation of cellular amino acid metabolic process proteasome regulatory particle, base subcomplex negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination proteasome accessory complex anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process proteasome assembly regulation of mRNA stability post-translational protein modification T cell receptor signaling pathway transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia interleukin-1-mediated signaling pathway proteasome regulatory particle assembly negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation uc004bko.1 uc004bko.2 uc004bko.3 uc004bko.4 uc004bko.5 uc004bko.6 
ENST00000210444.6 NANS ENST00000210444.6 N-acetylneuraminate synthase (from RefSeq NM_018946.4) B2RE98 ENST00000210444.1 ENST00000210444.2 ENST00000210444.3 ENST00000210444.4 ENST00000210444.5 NM_018946 Q8WUV9 Q9BWS6 Q9NR45 Q9NVD4 SAS SIAS_HUMAN uc004ayc.1 uc004ayc.2 uc004ayc.3 uc004ayc.4 uc004ayc.5 This gene encodes an enzyme that functions in the biosynthetic pathways of sialic acids. In vitro, the encoded protein uses N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), respectively; however, it exhibits much higher activity toward the Neu5Ac phosphate product. In insect cells, expression of this gene results in Neu5Ac and KDN production. This gene is related to the E. coli sialic acid synthase gene neuB, and it can partially restore sialic acid synthase activity in an E. coli neuB-negative mutant. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.231306.1, BC000008.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000210444.6/ ENSP00000210444.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy- D-glycero-D-galacto-nononic acid (KDN) (PubMed:10749855, PubMed:27213289). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively (PubMed:10749855). Reaction=H2O + N-acetyl-D-mannosamine + phosphoenolpyruvate = N- acetylneuraminate + phosphate; Xref=Rhea:RHEA:19273, ChEBI:CHEBI:15377, ChEBI:CHEBI:17122, ChEBI:CHEBI:35418, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=2.5.1.56; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19274; Evidence=; Reaction=an N-acyl-D-mannosamine 6-phosphate + H2O + phosphoenolpyruvate = an N-acylneuraminate 9-phosphate + phosphate; Xref=Rhea:RHEA:13421, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57537, ChEBI:CHEBI:57666, ChEBI:CHEBI:58702; EC=2.5.1.57; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13422; Evidence=; Ubiquitous. Spondyloepimetaphyseal dysplasia, Genevieve type (SEMDG) [MIM:610442]: An autosomal recessive disorder characterized by global developmental delay with infantile onset, intellectual disability, skeletal dysplasia, and short stature. Skeletal findings include flat vertebral bodies with irregular vertebral plates, irregular and flared metaphyses with vertical striations, small and irregular epiphyses, premature carpal ossification and small carpal bones. Note=The disease is caused by variants affecting the gene represented in this entry. catalytic activity cytoplasm cytosol CMP-N-acetylneuraminate biosynthetic process N-acylneuraminate cytidylyltransferase activity carbohydrate biosynthetic process transferase activity N-acylneuraminate-9-phosphate synthase activity N-acetylneuraminate synthase activity extracellular exosome uc004ayc.1 uc004ayc.2 uc004ayc.3 uc004ayc.4 uc004ayc.5 
ENST00000210633.4 SEMA4G ENST00000210633.4 semaphorin 4G, transcript variant 8 (from RefSeq NR_172057.1) A1A5C6 A6NJY8 ENST00000210633.1 ENST00000210633.2 ENST00000210633.3 KIAA1619 NR_172057 Q58EY1 Q9HCF3 Q9NTN9 SEM4G_HUMAN uc001krw.1 uc001krw.2 uc001krw.3 uc001krw.4 Cell surface receptor for PLXNB2. May play a role in axon guidance (By similarity). Interacts with PLXNB2. Q9NTN9; Q9HD26: GOPC; NbExp=3; IntAct=EBI-6447340, EBI-349832; Q9NTN9; Q15645: TRIP13; NbExp=3; IntAct=EBI-6447340, EBI-358993; Q9NTN9-2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12913124, EBI-11343438; Q9NTN9-2; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-12913124, EBI-6942903; Q9NTN9-2; O15121: DEGS1; NbExp=3; IntAct=EBI-12913124, EBI-1052713; Q9NTN9-2; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-12913124, EBI-1044859; Q9NTN9-3; Q86V38: ATN1; NbExp=3; IntAct=EBI-9089805, EBI-11954292; Q9NTN9-3; Q13554: CAMK2B; NbExp=3; IntAct=EBI-9089805, EBI-1058722; Q9NTN9-3; P55212: CASP6; NbExp=3; IntAct=EBI-9089805, EBI-718729; Q9NTN9-3; P48643: CCT5; NbExp=3; IntAct=EBI-9089805, EBI-355710; Q9NTN9-3; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-9089805, EBI-745535; Q9NTN9-3; P02489: CRYAA; NbExp=3; IntAct=EBI-9089805, EBI-6875961; Q9NTN9-3; P99999: CYCS; NbExp=3; IntAct=EBI-9089805, EBI-446479; Q9NTN9-3; P22607: FGFR3; NbExp=3; IntAct=EBI-9089805, EBI-348399; Q9NTN9-3; Q14957: GRIN2C; NbExp=3; IntAct=EBI-9089805, EBI-8285963; Q9NTN9-3; P28799: GRN; NbExp=3; IntAct=EBI-9089805, EBI-747754; Q9NTN9-3; P06396: GSN; NbExp=3; IntAct=EBI-9089805, EBI-351506; Q9NTN9-3; P30519: HMOX2; NbExp=3; IntAct=EBI-9089805, EBI-712096; Q9NTN9-3; P04792: HSPB1; NbExp=3; IntAct=EBI-9089805, EBI-352682; Q9NTN9-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9089805, EBI-10975473; Q9NTN9-3; Q92876: KLK6; NbExp=3; IntAct=EBI-9089805, EBI-2432309; Q9NTN9-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9089805, EBI-21591415; Q9NTN9-3; Q13153: PAK1; NbExp=3; IntAct=EBI-9089805, EBI-1307; Q9NTN9-3; O43933: PEX1; NbExp=3; IntAct=EBI-9089805, EBI-988601; Q9NTN9-3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-9089805, EBI-25882629; Q9NTN9-3; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-9089805, EBI-5280197; Q9NTN9-3; P60891: PRPS1; NbExp=3; IntAct=EBI-9089805, EBI-749195; Q9NTN9-3; P62826: RAN; NbExp=3; IntAct=EBI-9089805, EBI-286642; Q9NTN9-3; Q93062: RBPMS; NbExp=3; IntAct=EBI-9089805, EBI-740322; Q9NTN9-3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-9089805, EBI-396669; Q9NTN9-3; Q15645: TRIP13; NbExp=3; IntAct=EBI-9089805, EBI-358993; Q9NTN9-3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-9089805, EBI-741480; Q9NTN9-3; O76024: WFS1; NbExp=3; IntAct=EBI-9089805, EBI-720609; Q9NTN9-3; Q9Y649; NbExp=3; IntAct=EBI-9089805, EBI-25900580; Cell membrane; Single-pass type I membrane protein. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NTN9-1; Sequence=Displayed; Name=2; IsoId=Q9NTN9-2; Sequence=VSP_035067; Name=3; IsoId=Q9NTN9-3; Sequence=VSP_035067, VSP_043883; Belongs to the semaphorin family. Sequence=BAB13445.1; Type=Erroneous initiation; Evidence=; neural crest cell migration protein binding extracellular space plasma membrane integral component of plasma membrane multicellular organism development nervous system development membrane integral component of membrane cell differentiation semaphorin receptor binding positive regulation of cell migration chemorepellent activity negative regulation of axon extension involved in axon guidance negative chemotaxis semaphorin-plexin signaling pathway uc001krw.1 uc001krw.2 uc001krw.3 uc001krw.4 
ENST00000211076.5 TPSD1 ENST00000211076.5 tryptase delta 1 (from RefSeq NM_012217.3) ENST00000211076.1 ENST00000211076.2 ENST00000211076.3 ENST00000211076.4 NM_012217 O95824 Q8TDI6 Q96L36 Q96RZ5 Q9BZJ3 Q9H2Y6 Q9UQI8 TRYD_HUMAN uc002clb.1 uc002clb.2 uc002clb.3 Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3. These genes are characterized by several distinct features. They have a highly conserved 3' UTR and contain tandem repeat sequences at the 5' flank and 3' UTR which are thought to play a role in regulation of the mRNA stability. Although this gene may be an exception, most of the tryptase genes have an intron immediately upstream of the initiator Met codon, which separates the site of transcription initiation from protein coding sequence. This feature is characteristic of tryptases but is unusual in other genes. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders. This gene was once considered to be a pseudogene, although it is now believed to be a functional gene that encodes a protein. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC069143.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000211076.5/ ENSP00000211076.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.; EC=3.4.21.59; Evidence=; Homotetramer. Secreted Note=Released from the secretory granules upon mast cell activation. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BZJ3-1; Sequence=Displayed; Name=2; IsoId=Q9BZJ3-2; Sequence=VSP_008319; Expressed in colon, lung, heart and synovial tissue. May be specific to mast cells. Belongs to the peptidase S1 family. Tryptase subfamily. Although PubMed:11174199 reported this as a pseudogene, PubMed:12391231 showed it is expressed and has proteolytic activity when expressed in bacterial cells. Sequence=AAD17861.1; Type=Erroneous initiation; Evidence=; Sequence=AAK12909.1; Type=Erroneous initiation; Evidence=; serine-type endopeptidase activity extracellular region extracellular space proteolysis peptidase activity serine-type peptidase activity hydrolase activity uc002clb.1 uc002clb.2 uc002clb.3 
ENST00000211122.4 GSTA3 ENST00000211122.4 glutathione S-transferase alpha 3, transcript variant 1 (from RefSeq NM_000847.5) ENST00000211122.1 ENST00000211122.2 ENST00000211122.3 GSTA3 GSTA3_HUMAN NM_000847 O43468 Q068V6 Q16772 Q8WWA8 Q9H415 uc003pbb.1 uc003pbb.2 uc003pbb.3 uc003pbb.4 uc003pbb.5 Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-tranferase belonging to the alpha class genes that are located in a cluster mapped to chromosome 6. Genes of the alpha class are highly related and encode enzymes with glutathione peroxidase activity. However, during evolution, this alpha class gene diverged accumulating mutations in the active site that resulted in differences in substrate specificity and catalytic activity. The enzyme encoded by this gene catalyzes the double bond isomerization of precursors for progesterone and testosterone during the biosynthesis of steroid hormones. An additional transcript variant has been identified, but its full length sequence has not been determined. [provided by RefSeq, Jul 2008]. Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively. Has substantial activity toward aflatoxin B1-8,9-epoxide (By similarity). Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence=; Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione; Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937; Evidence=; Reaction=pregn-5-ene-3,20-dione = progesterone; Xref=Rhea:RHEA:43928, ChEBI:CHEBI:17026, ChEBI:CHEBI:63837; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43929; Evidence=; Kinetic parameters: KM=23 uM for androst-5-ene-3,17-dione ; KM=24 uM for androst-5-ene-3,17-dione (at pH 8.0 and 30 degrees Celsius) ; KM=24 uM for androst-5-ene-3,17-dione (at pH 7.4 and 37 degrees Celsius) ; KM=17 uM for pregn-5-ene-3,20-dione (at pH 8.0 and 30 degrees Celsius) ; KM=17 uM for pregn-5-ene-3,20-dione (at pH 7.4 and 37 degrees Celsius) ; Vmax=99 umol/min/mg enzyme for delta(5)-androstene-3,17-dione isomerization ; Note=kcats are 102 sec(-1) and 27 sec(-1) for androst-5-ene-3,17- dione and pregn-5-ene-3,20-dione as substrates, respectively (at pH 8.0 and 30 degrees Celsius). ; Homodimer. Cytoplasm. Belongs to the GST superfamily. Alpha family. Sequence=AAA74634.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAD04712.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/gsta3/"; glutathione transferase activity cytoplasm cytosol glutathione metabolic process xenobiotic metabolic process transferase activity extracellular exosome glutathione derivative biosynthetic process uc003pbb.1 uc003pbb.2 uc003pbb.3 uc003pbb.4 uc003pbb.5 
ENST00000211287.9 MAPK13 ENST00000211287.9 mitogen-activated protein kinase 13, transcript variant 1 (from RefSeq NM_002754.5) ENST00000211287.1 ENST00000211287.2 ENST00000211287.3 ENST00000211287.4 ENST00000211287.5 ENST00000211287.6 ENST00000211287.7 ENST00000211287.8 MK13_HUMAN NM_002754 O14739 O15124 O15264 PRKM13 Q5U4A5 Q6FI46 Q9UNU0 SAPK4 uc003ols.1 uc003ols.2 uc003ols.3 uc003ols.4 uc003ols.5 uc003ols.6 This gene encodes a member of the mitogen-activated protein (MAP) kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. The encoded protein is a p38 MAP kinase and is activated by proinflammatory cytokines and cellular stress. Substrates of the encoded protein include the transcription factor ATF2 and the microtubule dynamics regulator stathmin. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, Jul 2012]. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up- regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down- regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Activated by phosphorylation on threonine and tyrosine by dual specificity kinases, MAP2K3/MKK3, MAP2K6/MKK6, MAP2K4/MKK4 and MAP2K7/MKK7. Activation by ultraviolet radiation, hyperosmotic shock, anisomycin or by TNF-alpha is mediated by MAP2K3/MKK3. Inhibited by dual specificity phosphatase DUSP1. Interacts with MAPK8IP2. O15264; P21462: FPR1; NbExp=3; IntAct=EBI-2116951, EBI-2869495; O15264; Q15139: PRKD1; NbExp=6; IntAct=EBI-2116951, EBI-1181072; O15264; P40763: STAT3; NbExp=2; IntAct=EBI-2116951, EBI-518675; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O15264-1; Sequence=Displayed; Name=2; IsoId=O15264-2; Sequence=VSP_056558, VSP_056559; Expressed in testes, pancreas, small intestine, lung and kidney. Abundant in macrophages, also present in neutrophils, CD4+ T-cells, and endothelial cells. The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the enzyme. Dephosphorylated by dual specificity phosphatase DUSP1. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41291/MAPK13"; MAPK cascade nucleotide binding protein kinase activity protein serine/threonine kinase activity MAP kinase activity protein binding ATP binding nucleus cytoplasm cytosol protein phosphorylation response to osmotic stress cell cycle regulation of gene expression kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation positive regulation of interleukin-6 production cellular response to UV intracellular signal transduction positive regulation of inflammatory response stress-activated MAPK cascade cellular response to hydrogen peroxide cellular response to interleukin-1 cellular response to sorbitol cellular response to anisomycin cellular response to sodium arsenite uc003ols.1 uc003ols.2 uc003ols.3 uc003ols.4 uc003ols.5 uc003ols.6 
ENST00000211314.5 TMEM14A ENST00000211314.5 transmembrane protein 14A (from RefSeq NM_014051.4) B2R552 C6orf73 ENST00000211314.1 ENST00000211314.2 ENST00000211314.3 ENST00000211314.4 NM_014051 PTD011 Q9Y6G1 TM14A_HUMAN uc003pax.1 uc003pax.2 uc003pax.3 uc003pax.4 uc003pax.5 Inhibits apoptosis via negative regulation of the mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway. Q9Y6G1; Q13520: AQP6; NbExp=3; IntAct=EBI-2800360, EBI-13059134; Q9Y6G1; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-2800360, EBI-18013275; Q9Y6G1; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-2800360, EBI-6942903; Q9Y6G1; P49682: CXCR3; NbExp=3; IntAct=EBI-2800360, EBI-12836456; Q9Y6G1; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2800360, EBI-781551; Q9Y6G1; Q96PL5: ERMAP; NbExp=3; IntAct=EBI-2800360, EBI-13361852; Q9Y6G1; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-2800360, EBI-725665; Q9Y6G1; O95279: KCNK5; NbExp=3; IntAct=EBI-2800360, EBI-3934936; Q9Y6G1; Q9Y2L9-3: LRCH1; NbExp=3; IntAct=EBI-2800360, EBI-12082218; Q9Y6G1; Q9BS40: LXN; NbExp=3; IntAct=EBI-2800360, EBI-1044504; Q9Y6G1; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-2800360, EBI-6163737; Q9Y6G1; P15941-11: MUC1; NbExp=3; IntAct=EBI-2800360, EBI-17263240; Q9Y6G1; O14524-2: NEMP1; NbExp=3; IntAct=EBI-2800360, EBI-10969203; Q9Y6G1; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-2800360, EBI-716063; Q9Y6G1; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-2800360, EBI-17247926; Q9Y6G1; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2800360, EBI-18159983; Q9Y6G1; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-2800360, EBI-17595455; Q9Y6G1; Q9BZV2: SLC19A3; NbExp=3; IntAct=EBI-2800360, EBI-3923779; Q9Y6G1; P30825: SLC7A1; NbExp=3; IntAct=EBI-2800360, EBI-4289564; Q9Y6G1; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-2800360, EBI-17280858; Q9Y6G1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2800360, EBI-8638294; Q9Y6G1; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-2800360, EBI-11724423; Q9Y6G1; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-2800360, EBI-726044; Q9Y6G1; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-2800360, EBI-11742770; Q9Y6G1; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2800360, EBI-2548832; Mitochondrion membrane ; Multi-pass membrane protein Endoplasmic reticulum membrane Expressed at significantly higher levels in ovarian cancer tissues than in normal tissues (at protein level). Belongs to the TMEM14 family. protein binding mitochondrion endoplasmic reticulum endoplasmic reticulum membrane apoptotic process membrane integral component of membrane mitochondrial membrane negative regulation of apoptotic process negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway uc003pax.1 uc003pax.2 uc003pax.3 uc003pax.4 uc003pax.5 
ENST00000211377.7 GPANK1 ENST00000211377.7 G-patch domain and ankyrin repeats 1, transcript variant 2 (from RefSeq NM_033177.4) A6NG25 ANKRD59 B0UXA2 BAT4 ENST00000211377.1 ENST00000211377.2 ENST00000211377.3 ENST00000211377.4 ENST00000211377.5 ENST00000211377.6 G5 GPAN1_HUMAN GPATCH10 NM_033177 O95872 Q5SQ49 uc302whi.1 This gene is located in a cluster of HLA-B-associated transcripts, which is included in the human major histocompatability complex III region. This gene encodes a protein which is thought to play a role in immunity. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Nov 2010]. O95872; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-751540, EBI-11096309; O95872; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-751540, EBI-357530; O95872; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-751540, EBI-12224467; O95872; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-751540, EBI-11978055; O95872; P63010-2: AP2B1; NbExp=3; IntAct=EBI-751540, EBI-11529439; O95872; O95429: BAG4; NbExp=3; IntAct=EBI-751540, EBI-2949658; O95872; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-751540, EBI-2817707; O95872; A2RRN7: CADPS; NbExp=3; IntAct=EBI-751540, EBI-10179719; O95872; Q52MB2: CCDC184; NbExp=6; IntAct=EBI-751540, EBI-10179526; O95872; P40199: CEACAM6; NbExp=3; IntAct=EBI-751540, EBI-4314501; O95872; A8MTA8-2: CIMIP2B; NbExp=3; IntAct=EBI-751540, EBI-12160437; O95872; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-751540, EBI-3867333; O95872; Q8WTU0: DDI1; NbExp=3; IntAct=EBI-751540, EBI-748248; O95872; O43143: DHX15; NbExp=3; IntAct=EBI-751540, EBI-1237044; O95872; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-751540, EBI-11988027; O95872; Q16610: ECM1; NbExp=3; IntAct=EBI-751540, EBI-947964; O95872; O43281-2: EFS; NbExp=3; IntAct=EBI-751540, EBI-11525448; O95872; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-751540, EBI-18138793; O95872; Q08379: GOLGA2; NbExp=4; IntAct=EBI-751540, EBI-618309; O95872; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-751540, EBI-5916454; O95872; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-751540, EBI-11519926; O95872; P31943: HNRNPH1; NbExp=3; IntAct=EBI-751540, EBI-351590; O95872; O75031: HSF2BP; NbExp=3; IntAct=EBI-751540, EBI-7116203; O95872; P04792: HSPB1; NbExp=3; IntAct=EBI-751540, EBI-352682; O95872; Q96EL1: INKA1; NbExp=3; IntAct=EBI-751540, EBI-10285157; O95872; Q1MX18: INSC; NbExp=3; IntAct=EBI-751540, EBI-12081118; O95872; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-751540, EBI-2556193; O95872; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-751540, EBI-715394; O95872; Q7L273: KCTD9; NbExp=3; IntAct=EBI-751540, EBI-4397613; O95872; O60333-2: KIF1B; NbExp=3; IntAct=EBI-751540, EBI-10975473; O95872; O95678: KRT75; NbExp=3; IntAct=EBI-751540, EBI-2949715; O95872; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-751540, EBI-10171774; O95872; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-751540, EBI-10176379; O95872; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-751540, EBI-10241252; O95872; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-751540, EBI-1048945; O95872; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-751540, EBI-12805508; O95872; O95751: LDOC1; NbExp=3; IntAct=EBI-751540, EBI-740738; O95872; Q9BRK4: LZTS2; NbExp=4; IntAct=EBI-751540, EBI-741037; O95872; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-751540, EBI-716006; O95872; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-751540, EBI-746778; O95872; Q99750: MDFI; NbExp=3; IntAct=EBI-751540, EBI-724076; O95872; P50221: MEOX1; NbExp=3; IntAct=EBI-751540, EBI-2864512; O95872; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-751540, EBI-16439278; O95872; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-751540, EBI-8487781; O95872; Q8TCB7: METTL6; NbExp=3; IntAct=EBI-751540, EBI-17861723; O95872; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-751540, EBI-10172526; O95872; Q6PF18: MORN3; NbExp=3; IntAct=EBI-751540, EBI-9675802; O95872; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-751540, EBI-748610; O95872; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-751540, EBI-10271199; O95872; Q13133-3: NR1H3; NbExp=3; IntAct=EBI-751540, EBI-11952806; O95872; O43482: OIP5; NbExp=3; IntAct=EBI-751540, EBI-536879; O95872; Q96CV9: OPTN; NbExp=3; IntAct=EBI-751540, EBI-748974; O95872; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-751540, EBI-11022007; O95872; P26367: PAX6; NbExp=3; IntAct=EBI-751540, EBI-747278; O95872; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-751540, EBI-10302990; O95872; Q99471: PFDN5; NbExp=3; IntAct=EBI-751540, EBI-357275; O95872; Q9HDD0: PLAAT1; NbExp=3; IntAct=EBI-751540, EBI-12387058; O95872; Q8ND90: PNMA1; NbExp=4; IntAct=EBI-751540, EBI-302345; O95872; P60510: PPP4C; NbExp=3; IntAct=EBI-751540, EBI-1046072; O95872; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-751540, EBI-11320284; O95872; Q03431: PTH1R; NbExp=3; IntAct=EBI-751540, EBI-2860297; O95872; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-751540, EBI-10182375; O95872; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-751540, EBI-396669; O95872; A6ZKI3: RTL8C; NbExp=3; IntAct=EBI-751540, EBI-10174072; O95872; O60504: SORBS3; NbExp=3; IntAct=EBI-751540, EBI-741237; O95872; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-751540, EBI-744066; O95872; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-751540, EBI-725557; O95872; Q13190: STX5; NbExp=3; IntAct=EBI-751540, EBI-714206; O95872; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-751540, EBI-11139477; O95872; Q12800: TFCP2; NbExp=3; IntAct=EBI-751540, EBI-717422; O95872; Q08117-2: TLE5; NbExp=3; IntAct=EBI-751540, EBI-11741437; O95872; Q12933: TRAF2; NbExp=3; IntAct=EBI-751540, EBI-355744; O95872; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-751540, EBI-11119202; O95872; P36406: TRIM23; NbExp=7; IntAct=EBI-751540, EBI-740098; O95872; P14373: TRIM27; NbExp=7; IntAct=EBI-751540, EBI-719493; O95872; Q86WV8: TSC1; NbExp=5; IntAct=EBI-751540, EBI-12806590; O95872; Q6DKK2: TTC19; NbExp=4; IntAct=EBI-751540, EBI-948354; O95872; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-751540, EBI-9090990; O95872; P61758: VBP1; NbExp=3; IntAct=EBI-751540, EBI-357430; O95872; O76024: WFS1; NbExp=3; IntAct=EBI-751540, EBI-720609; O95872; Q05516: ZBTB16; NbExp=3; IntAct=EBI-751540, EBI-711925; O95872; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-751540, EBI-12956041; O95872; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-751540, EBI-7850213; O95872; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-751540, EBI-4395732; O95872; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-751540, EBI-527853; O95872; G4XUV3; NbExp=3; IntAct=EBI-751540, EBI-10177989; nucleic acid binding protein binding uc302whi.1 
ENST00000211402.10 VARS1 ENST00000211402.10 valyl-tRNA synthetase 1 (from RefSeq NM_006295.3) B0V1N1 B4DZ61 ENST00000211402.1 ENST00000211402.2 ENST00000211402.3 ENST00000211402.4 ENST00000211402.5 ENST00000211402.6 ENST00000211402.7 ENST00000211402.8 ENST00000211402.9 G7A NM_006295 P26640 Q5JQ90 Q96E77 Q9UQM2 SYVC_HUMAN VARS VARS1 VARS2 uc302whj.1 Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. The protein encoded by this gene belongs to class-I aminoacyl-tRNA synthetase family and is located in the class III region of the major histocompatibility complex. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X59303.1, BC012808.2 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: inferred from homology MANE Ensembl match :: ENST00000375663.8/ ENSP00000364815.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Catalyzes the attachment of valine to tRNA(Val). Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl- tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA- COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762, ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10705; Evidence=; Can be regulated by protein kinase C-dependent phosphorylation. Forms high-molecular-mass aggregates with elongation factor 1. P26640; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-355765, EBI-739580; P26640; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-355765, EBI-1383687; P26640; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-355765, EBI-11523526; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P26640-1; Sequence=Displayed; Name=2; IsoId=P26640-2; Sequence=VSP_056480, VSP_056481, VSP_056482; Neurodevelopmental disorder with microcephaly, seizures, and cortical atrophy (NDMSCA) [MIM:617802]: An autosomal recessive neurodevelopmental disorder characterized by severe developmental delay, intellectual disability, severe microcephaly, and cortical atrophy. Note=The disease may be caused by variants affecting the gene represented in this entry. Belongs to the class-I aminoacyl-tRNA synthetase family. Sequence=CAA41990.1; Type=Frameshift; Evidence=; nucleotide binding aminoacyl-tRNA editing activity aminoacyl-tRNA ligase activity valine-tRNA ligase activity protein binding ATP binding cytoplasm cytosol translation tRNA aminoacylation for protein translation valyl-tRNA aminoacylation ligase activity uc302whj.1 
ENST00000211413.10 PRRT1 ENST00000211413.10 proline rich transmembrane protein 1, transcript variant 1 (from RefSeq NM_030651.4) A6ND08 A6ND40 B0S869 C6orf31 ENST00000211413.1 ENST00000211413.2 ENST00000211413.3 ENST00000211413.4 ENST00000211413.5 ENST00000211413.6 ENST00000211413.7 ENST00000211413.8 ENST00000211413.9 NG5 NM_030651 PRRT1 PRRT1_HUMAN Q5SSW4 Q5SSX7 Q5STI1 Q96DW3 Q96NQ8 Q99946 uc003nzt.1 uc003nzt.2 uc003nzt.3 uc003nzt.4 uc003nzt.5 Required to maintain a pool of extrasynaptic AMPA-regulated glutamate receptors (AMPAR) which is necessary for synapse development and function. Regulates basal AMPAR function and synaptic transmission during development but is dispensable at mature hippocampal synapses. Plays a role in regulating basal phosphorylation levels of glutamate receptor GRIA1 and promotes GRIA1 and GRIA2 cell surface expression. Component of the outer core of AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing (By similarity). Q99946-2; P21145: MAL; NbExp=3; IntAct=EBI-12211089, EBI-3932027; Q99946-2; Q99946-2: PRRT1; NbExp=3; IntAct=EBI-12211089, EBI-12211089; Cell membrane ; Single-pass type II membrane protein Synapse Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q99946-1; Sequence=Displayed; Name=2; IsoId=Q99946-2; Sequence=VSP_003808; Belongs to the CD225/Dispanin family. plasma membrane membrane integral component of membrane cell junction synapse glutamatergic synapse integral component of postsynaptic membrane uc003nzt.1 uc003nzt.2 uc003nzt.3 uc003nzt.4 uc003nzt.5 
ENST00000211998.10 VCL ENST00000211998.10 vinculin, transcript variant 1 (from RefSeq NM_014000.3) ENST00000211998.1 ENST00000211998.2 ENST00000211998.3 ENST00000211998.4 ENST00000211998.5 ENST00000211998.6 ENST00000211998.7 ENST00000211998.8 ENST00000211998.9 HEL114 NM_014000 V9HWK2 V9HWK2_HUMAN VCL hCG_2024635 uc001jwd.1 uc001jwd.2 uc001jwd.3 uc001jwd.4 uc001jwd.5 uc001jwd.6 Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane. Defects in VCL are the cause of cardiomyopathy dilated type 1W. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined. [provided by RefSeq, Jul 2008]. Actin filament (F-actin)-binding protein involved in cell- matrix adhesion and cell-cell adhesion. Regulates cell-surface E- cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. Cell junction, adherens junction Cell membrane, sarcolemma ; Peripheral membrane protein ; Cytoplasmic side Cell membrane ; Peripheral membrane protein ; Cytoplasmic side Cell projection, podosome Membrane ; Peripheral membrane protein ; Cytoplasmic side Belongs to the vinculin/alpha-catenin family. podosome actin binding structural molecule activity cytoplasm plasma membrane cell-cell junction adherens junction fascia adherens focal adhesion cell adhesion actin cytoskeleton lamellipodium assembly regulation of cell migration sarcolemma costamere axon extension actin filament binding uc001jwd.1 uc001jwd.2 uc001jwd.3 uc001jwd.4 uc001jwd.5 uc001jwd.6 
ENST00000212015.11 SIRT1 ENST00000212015.11 sirtuin 1, transcript variant 1 (from RefSeq NM_012238.5) ENST00000212015.1 ENST00000212015.10 ENST00000212015.2 ENST00000212015.3 ENST00000212015.4 ENST00000212015.5 ENST00000212015.6 ENST00000212015.7 ENST00000212015.8 ENST00000212015.9 NM_012238 Q2XNF6 Q5JVQ0 Q96EB6 Q9GZR9 Q9Y6F0 SIR1_HUMAN SIR2L1 SIRT1 uc001jnd.1 uc001jnd.2 uc001jnd.3 uc001jnd.4 This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2008]. NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17290224, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:20955178, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21947282, PubMed:22274616, PubMed:24415752, PubMed:24824780, PubMed:29765047, PubMed:30409912, PubMed:29681526). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (PubMed:15469825). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (PubMed:15152190, PubMed:14980222, PubMed:14976264). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (PubMed:15205477). Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT) (By similarity). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (PubMed:18485871). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18485871, PubMed:21504832). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (PubMed:21504832). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:19188449). Deacetylates H2A and 'Lys-26' of H1-4 (PubMed:15469825). Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression (PubMed:20375098). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (By similarity). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (PubMed:15469825, PubMed:18004385). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (PubMed:18004385, PubMed:21504832). This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response (PubMed:18004385, PubMed:21504832). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672523, PubMed:12006491). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (By similarity). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (PubMed:19364925, PubMed:21807113). Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation (PubMed:14980222, PubMed:14976264, PubMed:21841822). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (PubMed:15126506). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (PubMed:21947282). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha (PubMed:15152190). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17620057, PubMed:17283066, PubMed:20100829, PubMed:20620956). Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15692560). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (PubMed:12535671). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (PubMed:21698133). Deacetylates MEF2D (PubMed:16166628). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (PubMed:17505061). Represses HNF1A-mediated transcription (By similarity). Required for the repression of ESRRG by CREBZF (PubMed:19690166). Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed (PubMed:17936707). Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis (PubMed:20817729, PubMed:29765047). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (By similarity). Deacetylates p300/EP300 and PRMT1 (By similarity). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:21701047). Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis (PubMed:23142079). Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression (PubMed:17290224, PubMed:20817729). Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2 (PubMed:15205477, PubMed:17334224, PubMed:16998810, PubMed:17612497, PubMed:20670893, PubMed:21149730). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN (PubMed:15205477, PubMed:17334224, PubMed:20097625). Promotes DNA double-strand breaks by mediating deacetylation of SIRT6 (PubMed:32538779). Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage (PubMed:18203716). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (PubMed:19934257). Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER) (PubMed:32034146). Increases p53/TP53-mediated transcription- independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (PubMed:21775285). Proposed to play role in regulation of STK11/LBK1- dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear (PubMed:18687677, PubMed:20203304). In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability (PubMed:21890893). Deacetylates MECOM/EVI1 (PubMed:21555002). Deacetylates PML at 'Lys- 487' and this deacetylation promotes PML control of PER2 nuclear localization (PubMed:22274616). During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling (PubMed:18662546). Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (By similarity). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome (By similarity). Protects cardiomyocytes against palmitate-induced apoptosis (By similarity). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (By similarity). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein depropionylation and decrotonylation (PubMed:28497810). Mediates depropionylation of Osterix (SP7) (By similarity). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase (PubMed:28497810). Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity (By similarity). Involved in the regulation of centrosome duplication. Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (PubMed:31722219). Deacetylates NDC80/HEC1 (PubMed:30409912). [Isoform 2]: Deacetylates 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. [SirtT1 75 kDa fragment]: Catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly. (Microbial infection) In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection. Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl- ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence= Reaction=H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD(+) = 3''-O- propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:23500, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13758, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:138019, ChEBI:CHEBI:145015; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23501; Evidence=; Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] + NAD(+) = 2''-O- (2E)-but-2-enoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:69332, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:137954, ChEBI:CHEBI:183235; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69333; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Inhibited by nicotinamide. Activated by resveratrol (3,5,4'-trihydroxy-trans-stilbene), butein (3,4,2',4'- tetrahydroxychalcone), piceatannol (3,5,3',4'-tetrahydroxy-trans- stilbene), Isoliquiritigenin (4,2',4'-trihydroxychalcone), fisetin (3,7,3',4'-tetrahydroxyflavone) and quercetin (3,5,7,3',4'- pentahydroxyflavone). MAPK8/JNK1 and RPS19BP1/AROS act as positive regulators of deacetylation activity. Negatively regulated by CCAR2. Interacts with XBP1 isoform 2 (PubMed:20955178). Found in a complex with PCAF and MYOD1. Interacts with FOXO1; the interaction deacetylates FOXO1, resulting in its nuclear retention and promotion of its transcriptional activity Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Interacts with HES1, HEY2 and PML. Interacts with RPS19BP1/AROS. Interacts with CCAR2 (via N-terminus); the interaction disrupts the interaction between SIRT1 and p53/TP53. Interacts with SETD7; the interaction induces the dissociation of SIRT1 from p53/TP53 and increases p53/TP53 activity. Interacts with MYCN, NR1I2, CREBZF, TSC2, TLE1, FOS, JUN, NR0B2, PPARG, NCOR, IRS1, IRS2 and NMNAT1. Interacts with HNF1A; the interaction occurs under nutrient restriction. Interacts with SUZ12; the interaction mediates the association with the PRC4 histone methylation complex which is specific as an association with PCR2 and PCR3 complex variants is not found. Interacts with BCL6; leads to a epigenetic repression of specific target genes. Interacts with CLOCK, BMAL1 and PER2 (By similarity). Interacts with PPARA; the interaction seems to be modulated by NAD(+) levels (PubMed:24043310). Interacts with NR1H3 and this interaction is inhibited in the presence of CCAR2. Interacts with CHEK2. Interacts with p53/TP53. Exhibits a preferential interaction with sumoylated CCAR2 over its unmodified form. Interacts with PACS2 (PubMed:29656858). Interacts with SIRT7 (By similarity). Interacts with PUS7 (PubMed:31451225). Interacts with TULP3 (PubMed:35397207). Interacts with MORN3; the interaction enhances the ubiquitination of p53/TP53 (PubMed:29681526). (Microbial infection) Interacts with HIV-1 Tat. Q96EB6; Q13085: ACACA; NbExp=3; IntAct=EBI-1802965, EBI-717681; Q96EB6; P31749: AKT1; NbExp=5; IntAct=EBI-1802965, EBI-296087; Q96EB6; P27695: APEX1; NbExp=6; IntAct=EBI-1802965, EBI-1048805; Q96EB6; O95352: ATG7; NbExp=3; IntAct=EBI-1802965, EBI-987834; Q96EB6; Q8N163: CCAR2; NbExp=16; IntAct=EBI-1802965, EBI-355410; Q96EB6; P33076: CIITA; NbExp=4; IntAct=EBI-1802965, EBI-1538819; Q96EB6; Q9NS37: CREBZF; NbExp=3; IntAct=EBI-1802965, EBI-632965; Q96EB6; Q9Y5P2: CSAG3; NbExp=8; IntAct=EBI-1802965, EBI-26354757; Q96EB6; P68400: CSNK2A1; NbExp=5; IntAct=EBI-1802965, EBI-347804; Q96EB6; P67870: CSNK2B; NbExp=5; IntAct=EBI-1802965, EBI-348169; Q96EB6; P26358: DNMT1; NbExp=11; IntAct=EBI-1802965, EBI-719459; Q96EB6; O14640: DVL1; NbExp=2; IntAct=EBI-1802965, EBI-723489; Q96EB6; Q92997: DVL3; NbExp=3; IntAct=EBI-1802965, EBI-739789; Q96EB6; Q01094: E2F1; NbExp=3; IntAct=EBI-1802965, EBI-448924; Q96EB6; Q09472: EP300; NbExp=4; IntAct=EBI-1802965, EBI-447295; Q96EB6; Q14192: FHL2; NbExp=2; IntAct=EBI-1802965, EBI-701903; Q96EB6; Q12778: FOXO1; NbExp=4; IntAct=EBI-1802965, EBI-1108782; Q96EB6; O43524: FOXO3; NbExp=5; IntAct=EBI-1802965, EBI-1644164; Q96EB6; P98177: FOXO4; NbExp=3; IntAct=EBI-1802965, EBI-4481939; Q96EB6; P51610: HCFC1; NbExp=2; IntAct=EBI-1802965, EBI-396176; Q96EB6; Q14469: HES1; NbExp=4; IntAct=EBI-1802965, EBI-2832522; Q96EB6; Q9UBP5: HEY2; NbExp=3; IntAct=EBI-1802965, EBI-750630; Q96EB6; Q9Y4H2: IRS2; NbExp=2; IntAct=EBI-1802965, EBI-1049582; Q96EB6; Q92831: KAT2B; NbExp=3; IntAct=EBI-1802965, EBI-477430; Q96EB6; Q03164: KMT2A; NbExp=5; IntAct=EBI-1802965, EBI-591370; Q96EB6; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-1802965, EBI-373144; Q96EB6; Q03112: MECOM; NbExp=2; IntAct=EBI-1802965, EBI-1384862; Q96EB6; P42345: MTOR; NbExp=2; IntAct=EBI-1802965, EBI-359260; Q96EB6; P01106: MYC; NbExp=4; IntAct=EBI-1802965, EBI-447544; Q96EB6; P04198: MYCN; NbExp=3; IntAct=EBI-1802965, EBI-878369; Q96EB6; O60934: NBN; NbExp=5; IntAct=EBI-1802965, EBI-494844; Q96EB6; Q02577: NHLH2; NbExp=2; IntAct=EBI-1802965, EBI-5378683; Q96EB6; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-1802965, EBI-3917542; Q96EB6; Q15466: NR0B2; NbExp=6; IntAct=EBI-1802965, EBI-3910729; Q96EB6; P27986: PIK3R1; NbExp=3; IntAct=EBI-1802965, EBI-79464; Q96EB6; P37231: PPARG; NbExp=5; IntAct=EBI-1802965, EBI-781384; Q96EB6; P10276: RARA; NbExp=3; IntAct=EBI-1802965, EBI-413374; Q96EB6; Q04206: RELA; NbExp=5; IntAct=EBI-1802965, EBI-73886; Q96EB6; Q86WX3: RPS19BP1; NbExp=11; IntAct=EBI-1802965, EBI-4479407; Q96EB6; Q8N122: RPTOR; NbExp=3; IntAct=EBI-1802965, EBI-1567928; Q96EB6; O43159: RRP8; NbExp=3; IntAct=EBI-1802965, EBI-2008793; Q96EB6; Q8WTS6: SETD7; NbExp=11; IntAct=EBI-1802965, EBI-1268586; Q96EB6; Q13573: SNW1; NbExp=7; IntAct=EBI-1802965, EBI-632715; Q96EB6; P36956-3: SREBF1; NbExp=2; IntAct=EBI-1802965, EBI-948338; Q96EB6; O43463: SUV39H1; NbExp=5; IntAct=EBI-1802965, EBI-349968; Q96EB6; Q04724: TLE1; NbExp=4; IntAct=EBI-1802965, EBI-711424; Q96EB6; P04637: TP53; NbExp=18; IntAct=EBI-1802965, EBI-366083; Q96EB6; O15350: TP73; NbExp=4; IntAct=EBI-1802965, EBI-389606; Q96EB6; P49815: TSC2; NbExp=2; IntAct=EBI-1802965, EBI-396587; Q96EB6; Q14191: WRN; NbExp=9; IntAct=EBI-1802965, EBI-368417; Q96EB6; P23025: XPA; NbExp=8; IntAct=EBI-1802965, EBI-295222; Q96EB6; P12956: XRCC6; NbExp=7; IntAct=EBI-1802965, EBI-353208; Q96EB6; Q9R1E0: Foxo1; Xeno; NbExp=2; IntAct=EBI-1802965, EBI-1371343; Q96EB6; Q60974: Ncor1; Xeno; NbExp=2; IntAct=EBI-1802965, EBI-349004; Q96EB6; Q60644: Nr1h2; Xeno; NbExp=2; IntAct=EBI-1802965, EBI-5276809; Q96EB6; Q9Z0Y9: Nr1h3; Xeno; NbExp=2; IntAct=EBI-1802965, EBI-5276764; Q96EB6; P37238: Pparg; Xeno; NbExp=3; IntAct=EBI-1802965, EBI-5260705; Q96EB6; P37238-1: Pparg; Xeno; NbExp=2; IntAct=EBI-1802965, EBI-6267861; Q96EB6; P04608: tat; Xeno; NbExp=3; IntAct=EBI-1802965, EBI-6164389; Nucleus, PML body Cytoplasm Nucleus te=Recruited to the nuclear bodies via its interaction with PML (PubMed:12006491). Colocalized with APEX1 in the nucleus (PubMed:19934257). May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane (PubMed:15469825). Shuttles between nucleus and cytoplasm (By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (PubMed:20955178). [SirtT1 75 kDa fragment]: Cytoplasm Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96EB6-1; Sequence=Displayed; Name=2; Synonyms=delta-exon8; IsoId=Q96EB6-2; Sequence=VSP_042189; Widely expressed. Up-regulated by methyl methanesulfonate (MMS). In H293T cells by presence of rat calorie restriction (CR) serum. Methylated on multiple lysine residues; methylation is enhanced after DNA damage and is dispensable for deacetylase activity toward p53/TP53. Phosphorylated. Phosphorylated by STK4/MST1, resulting in inhibition of SIRT1-mediated p53/TP53 deacetylation. Phosphorylation by MAPK8/JNK1 at Ser-27, Ser-47, and Thr-530 leads to increased nuclear localization and enzymatic activity. Phosphorylation at Thr-530 by DYRK1A and DYRK3 activates deacetylase activity and promotes cell survival. Phosphorylation by mammalian target of rapamycin complex 1 (mTORC1) at Ser-47 inhibits deacetylation activity. Phosphorylated by CaMK2, leading to increased p53/TP53 and NF-kappa-B p65/RELA deacetylation activity (By similarity). Phosphorylation at Ser-27 implicating MAPK9 is linked to protein stability. There is some ambiguity for some phosphosites: Ser-159/Ser-162 and Thr-544/Ser-545. Proteolytically cleaved by cathepsin B upon TNF-alpha treatment to yield catalytic inactive but stable SirtT1 75 kDa fragment (75SirT1). S-nitrosylated by GAPDH, leading to inhibit the NAD-dependent protein deacetylase activity. Acetylated at various Lys residues. Deacetylated via an autocatalytic mechanism. Autodeacetylation at Lys-238 promotes its protein deacetylase activity. Red wine, which contains resveratrol, may participate in activation of sirtuin proteins, and may therefore participate in an extended lifespan as it has been observed in yeast. Calf histone H1 is used as substrate in the in vitro deacetylation assay (PubMed:15469825). As, in vivo, interaction occurs between SIRT1 with H1-4, deacetylation has been validated only for H1- 4. The reported ADP-ribosyltransferase activity of sirtuins is likely some inefficient side reaction of the deacetylase activity and may not be physiologically relevant. Belongs to the sirtuin family. Class I subfamily. Sequence=AAH12499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/sirt1/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44006/SIRT1"; single strand break repair negative regulation of transcription from RNA polymerase II promoter chromatin silencing at rDNA pyrimidine dimer repair by nucleotide-excision repair DNA synthesis involved in DNA repair chromatin nuclear chromatin RNA polymerase II distal enhancer sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding angiogenesis ovulation from ovarian follicle cellular glucose homeostasis positive regulation of protein phosphorylation positive regulation of endothelial cell proliferation p53 binding positive regulation of adaptive immune response transcription corepressor activity histone deacetylase activity protein binding nucleus nuclear envelope nuclear inner membrane nucleoplasm chromatin silencing complex nuclear euchromatin nuclear heterochromatin nucleolus cytoplasm mitochondrion cytosol chromatin organization establishment of chromatin silencing maintenance of chromatin silencing methylation-dependent chromatin silencing rRNA processing protein deacetylation triglyceride mobilization apoptotic process cellular response to DNA damage stimulus response to oxidative stress transforming growth factor beta receptor signaling pathway multicellular organism development spermatogenesis regulation of mitotic cell cycle muscle organ development cell aging circadian rhythm protein C-terminus binding transcription factor binding positive regulation of cell proliferation intrinsic apoptotic signaling pathway in response to DNA damage cellular response to starvation negative regulation of gene expression positive regulation of cholesterol efflux regulation of lipid storage regulation of glucose metabolic process macrophage cytokine production positive regulation of phosphatidylinositol 3-kinase signaling viral process positive regulation of macroautophagy protein ubiquitination histone deacetylation PML body hydrolase activity NAD-dependent histone deacetylase activity peptidyl-lysine acetylation deacetylase activity enzyme binding protein domain specific binding cell differentiation macrophage differentiation negative regulation of cell growth negative regulation of transforming growth factor beta receptor signaling pathway negative regulation of prostaglandin biosynthetic process protein destabilization positive regulation of chromatin silencing negative regulation of TOR signaling regulation of endodeoxyribonuclease activity negative regulation of NF-kappaB transcription factor activity response to insulin circadian regulation of gene expression leptin-mediated signaling pathway rDNA heterochromatin protein deacetylase activity regulation of smooth muscle cell apoptotic process NAD-dependent protein deacetylase activity peptidyl-lysine deacetylation nuclear hormone receptor binding cellular triglyceride homeostasis regulation of peroxisome proliferator activated receptor signaling pathway regulation of cell proliferation negative regulation of phosphorylation histone binding response to hydrogen peroxide behavioral response to starvation cholesterol homeostasis intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator identical protein binding regulation of apoptotic process positive regulation of apoptotic process negative regulation of apoptotic process negative regulation of I-kappaB kinase/NF-kappaB signaling proteasome-mediated ubiquitin-dependent protein catabolic process positive regulation of cysteine-type endopeptidase activity involved in apoptotic process HLH domain binding bHLH transcription factor binding negative regulation of sequence-specific DNA binding transcription factor activity negative regulation of DNA damage response, signal transduction by p53 class mediator positive regulation of blood vessel endothelial cell migration response to leptin positive regulation of MHC class II biosynthetic process negative regulation of fat cell differentiation positive regulation of gluconeogenesis positive regulation of DNA repair positive regulation of angiogenesis negative regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter positive regulation of insulin receptor signaling pathway metal ion binding NAD-dependent histone deacetylase activity (H3-K9 specific) rhythmic process white fat cell differentiation mitogen-activated protein kinase binding negative regulation of helicase activity positive regulation of smooth muscle cell differentiation positive regulation of histone H3-K9 methylation negative regulation of protein kinase B signaling fatty acid homeostasis negative regulation of androgen receptor signaling pathway histone H3-K9 modification cellular response to hydrogen peroxide NAD+ binding regulation of bile acid biosynthetic process UV-damage excision repair histone H3 deacetylation cellular response to tumor necrosis factor negative regulation of histone H3-K14 acetylation cellular response to hypoxia cellular response to ionizing radiation regulation of protein serine/threonine kinase activity regulation of brown fat cell differentiation stress-induced premature senescence regulation of cellular response to heat negative regulation of histone H3-K9 trimethylation negative regulation of neuron death negative regulation of protein acetylation negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway positive regulation of adipose tissue development keratin filament binding histone H3-K9 deacetylation cellular response to leukemia inhibitory factor positive regulation of macrophage apoptotic process negative regulation of cAMP-dependent protein kinase activity positive regulation of cAMP-dependent protein kinase activity negative regulation of histone H4-K16 acetylation negative regulation of cellular response to testosterone stimulus negative regulation of peptidyl-lysine acetylation negative regulation of cellular senescence positive regulation of cellular senescence ESC/E(Z) complex NAD+ ADP-ribosyltransferase activity protein ADP-ribosylation uc001jnd.1 uc001jnd.2 uc001jnd.3 uc001jnd.4 
ENST00000212355.9 TGFBR3 ENST00000212355.9 transforming growth factor beta receptor 3, transcript variant 4 (from RefSeq NR_036634.2) A0AUW8 A8K5N0 B9EG88 ENST00000212355.1 ENST00000212355.2 ENST00000212355.3 ENST00000212355.4 ENST00000212355.5 ENST00000212355.6 ENST00000212355.7 ENST00000212355.8 NR_036634 Q03167 Q5T2T4 Q5U731 Q9UGI2 TGBR3_HUMAN TGFBR3 uc001doh.1 uc001doh.2 uc001doh.3 uc001doh.4 uc001doh.5 This locus encodes the transforming growth factor (TGF)-beta type III receptor. The encoded receptor is a membrane proteoglycan that often functions as a co-receptor with other TGF-beta receptor superfamily members. Ectodomain shedding produces soluble TGFBR3, which may inhibit TGFB signaling. Decreased expression of this receptor has been observed in various cancers. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[provided by RefSeq, Sep 2010]. Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors (By similarity). In gonadotrope cells, acts as an inhibin A coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility (PubMed:34910520). Interacts with DYNLT4. Q03167; O14908: GIPC1; NbExp=3; IntAct=EBI-2852679, EBI-373132; Q03167; P01137: TGFB1; NbExp=2; IntAct=EBI-2852679, EBI-779636; Cell membrane ; Single-pass type I membrane protein Secreted Secreted, extracellular space, extracellular matrix Note=Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q03167-1; Sequence=Displayed; Name=2; IsoId=Q03167-2; Sequence=VSP_040018; Extensively modified by glycosaminoglycan groups (GAG). Sequence=AAA67061.1; Type=Frameshift; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42541/TGFBR3"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tgfbr3/"; response to hypoxia epithelial to mesenchymal transition liver development heart morphogenesis muscular septum morphogenesis outflow tract morphogenesis ventricular compact myocardium morphogenesis transforming growth factor beta-activated receptor activity type II transforming growth factor beta receptor binding transforming growth factor beta receptor binding protein binding glycosaminoglycan binding extracellular region extracellular space cytoplasm plasma membrane integral component of plasma membrane immune response transforming growth factor beta receptor signaling pathway transforming growth factor beta receptor complex assembly heparin binding external side of plasma membrane cell surface coreceptor activity membrane integral component of membrane cell migration fibroblast growth factor binding PDZ domain binding BMP signaling pathway positive regulation of transforming growth factor beta receptor signaling pathway negative regulation of transforming growth factor beta receptor signaling pathway extracellular matrix animal organ regeneration response to follicle-stimulating hormone inhibin-betaglycan-ActRII complex response to prostaglandin E response to luteinizing hormone intracellular signal transduction receptor complex regulation of protein binding SMAD binding activin binding transforming growth factor beta binding negative regulation of epithelial cell proliferation negative regulation of cellular component movement ventricular cardiac muscle tissue morphogenesis cardiac muscle cell proliferation positive regulation of cardiac muscle cell proliferation definitive hemopoiesis cardiac epithelial to mesenchymal transition definitive erythrocyte differentiation heart trabecula formation pathway-restricted SMAD protein phosphorylation ventricular septum morphogenesis epicardium-derived cardiac fibroblast cell development vasculogenesis involved in coronary vascular morphogenesis heart trabecula morphogenesis macromolecular complex assembly extracellular exosome transforming growth factor beta receptor activity, type III regulation of JNK cascade regulation of ERK1 and ERK2 cascade uc001doh.1 uc001doh.2 uc001doh.3 uc001doh.4 uc001doh.5 
ENST00000214869.7 TMED1 ENST00000214869.7 transmembrane p24 trafficking protein 1, transcript variant 1 (from RefSeq NM_006858.4) ENST00000214869.1 ENST00000214869.2 ENST00000214869.3 ENST00000214869.4 ENST00000214869.5 ENST00000214869.6 IL1RL1L IL1RL1LG NM_006858 Q13445 TMED1_HUMAN uc002mpy.1 uc002mpy.2 uc002mpy.3 uc002mpy.4 uc002mpy.5 uc002mpy.6 This gene belongs to the TMED (transmembrane emp24 domain-containing) protein family, which is involved in the vesicular trafficking of proteins. The protein encoded by this gene was identified by its interaction with interleukin 1 receptor-like 1 (IL1RL1) and may play a role in innate immunity. This protein lacks any similarity to other interleukin 1 ligands. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jul 2013]. Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side. Plays a positive role in IL-33-mediated IL-8 and IL-6 production by interacting with interleukin-33 receptor IL1RL1 (PubMed:23319592). Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). Homodimer in endoplasmic reticulum, endoplasmic reticulum- Golgi intermediate compartment and cis-Golgi network. Interacts with IL1RL1 (PubMed:23319592). Interacts with RNF26; this interaction is important to modulate innate immune signaling through the cGAS-STING pathway (PubMed:32614325). Cell membrane ; Single-pass type I membrane protein Endoplasmic reticulum membrane ingle-pass type I membrane protein Golgi apparatus, cis-Golgi network membrane ingle-pass type I membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane ; Single-pass type I membrane protein Widely expressed. Found only in very low concentrations in the endoplasmic reticulum, Golgi apparatus and endoplasmic reticulum-Golgi intermediate compartment compared to other members of the EMP24/GP25L family. Belongs to the EMP24/GP25L family. receptor binding protein binding endoplasmic reticulum endoplasmic reticulum membrane endoplasmic reticulum-Golgi intermediate compartment Golgi apparatus plasma membrane intracellular protein transport ER to Golgi vesicle-mediated transport Golgi organization signal transduction cell-cell signaling protein transport membrane integral component of membrane ER to Golgi transport vesicle endoplasmic reticulum-Golgi intermediate compartment membrane uc002mpy.1 uc002mpy.2 uc002mpy.3 uc002mpy.4 uc002mpy.5 uc002mpy.6 
ENST00000215057.7 MZF1 ENST00000215057.7 myeloid zinc finger 1, transcript variant 2 (from RefSeq NM_198055.2) ENST00000215057.1 ENST00000215057.2 ENST00000215057.3 ENST00000215057.4 ENST00000215057.5 ENST00000215057.6 M0QXU0 MZF MZF1_HUMAN NM_198055 P28698 Q7Z729 Q96I71 Q9NRY0 Q9UBW2 ZNF42 ZSCAN6 uc002qto.1 uc002qto.2 uc002qto.3 uc002qto.4 uc002qto.5 Binds to target promoter DNA and functions as a transcription regulator. Regulates transcription from the PADI1 and CDH2 promoter. May be one regulator of transcriptional events during hemopoietic development. Homodimer. Nucleus. Event=Alternative splicing; Named isoforms=3; Name=MZF1A; Synonyms=MZF1B; IsoId=P28698-1; Sequence=Displayed; Name=MZF1B-C; IsoId=P28698-2; Sequence=VSP_006889, VSP_006890; Name=3; IsoId=P28698-3; Sequence=VSP_047013, VSP_047014; Preferentially expressed in differentiating myeloid cells. Detected in osteoblasts. By retinoic acid. Belongs to the krueppel C2H2-type zinc-finger protein family. negative regulation of transcription from RNA polymerase II promoter RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated protein homodimerization activity transcription regulatory region DNA binding positive regulation of transcription from RNA polymerase II promoter metal ion binding uc002qto.1 uc002qto.2 uc002qto.3 uc002qto.4 uc002qto.5 
ENST00000215061.9 OCEL1 ENST00000215061.9 occludin/ELL domain containing 1 (from RefSeq NM_024578.3) ENST00000215061.1 ENST00000215061.2 ENST00000215061.3 ENST00000215061.4 ENST00000215061.5 ENST00000215061.6 ENST00000215061.7 ENST00000215061.8 NM_024578 OCEL1_HUMAN Q9H607 uc002nfp.1 uc002nfp.2 uc002nfp.3 uc002nfp.4 uc002nfp.5 Belongs to the ELL/occludin family. uc002nfp.1 uc002nfp.2 uc002nfp.3 uc002nfp.4 uc002nfp.5 
ENST00000215071.9 PSMD8 ENST00000215071.9 proteasome 26S subunit, non-ATPase 8 (from RefSeq NM_002812.5) ENST00000215071.1 ENST00000215071.2 ENST00000215071.3 ENST00000215071.4 ENST00000215071.5 ENST00000215071.6 ENST00000215071.7 ENST00000215071.8 HEL-S-91n NM_002812 V9HW09 V9HW09_HUMAN uc002oii.1 uc002oii.2 uc002oii.3 uc002oii.4 uc002oii.5 uc002oii.6 The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 1. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: EU668354.1, BC001164.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Belongs to the proteasome subunit S14 family. proteasome regulatory particle proteolysis proteasome accessory complex uc002oii.1 uc002oii.2 uc002oii.3 uc002oii.4 uc002oii.5 uc002oii.6 
ENST00000215095.11 STX1B ENST00000215095.11 syntaxin 1B (from RefSeq NM_052874.5) ENST00000215095.1 ENST00000215095.10 ENST00000215095.2 ENST00000215095.3 ENST00000215095.4 ENST00000215095.5 ENST00000215095.6 ENST00000215095.7 ENST00000215095.8 ENST00000215095.9 NM_052874 P61266 Q15531 Q2VPS2 STX1B1 STX1B2 STX1B_HUMAN uc010cad.1 uc010cad.2 uc010cad.3 uc010cad.4 uc010cad.5 The protein encoded by this gene belongs to a family of proteins thought to play a role in the exocytosis of synaptic vesicles. Vesicle exocytosis releases vesicular contents and is important to various cellular functions. For instance, the secretion of transmitters from neurons plays an important role in synaptic transmission. After exocytosis, the membrane and proteins from the vesicle are retrieved from the plasma membrane through the process of endocytosis. Mutations in this gene have been identified as one cause of fever-associated epilepsy syndromes. A possible link between this gene and Parkinson's disease has also been suggested. [provided by RefSeq, Jan 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY028792.1, SRR3476690.311163.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215095.11/ ENSP00000215095.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity). Interacts with OTOF. Interacts with SYT6 and SYT8; the interaction is Ca(2+)-dependent (By similarity). P61266; O95870: ABHD16A; NbExp=3; IntAct=EBI-9071709, EBI-348517; P61266; Q5T8D3-2: ACBD5; NbExp=3; IntAct=EBI-9071709, EBI-10961679; P61266; Q13520: AQP6; NbExp=3; IntAct=EBI-9071709, EBI-13059134; P61266; O15155: BET1; NbExp=3; IntAct=EBI-9071709, EBI-749204; P61266; Q15125: EBP; NbExp=3; IntAct=EBI-9071709, EBI-3915253; P61266; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-9071709, EBI-781551; P61266; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-9071709, EBI-7225287; P61266; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-9071709, EBI-18304435; P61266; Q8TBF8: FAM81A; NbExp=3; IntAct=EBI-9071709, EBI-11993062; P61266; Q9NVF7: FBXO28; NbExp=3; IntAct=EBI-9071709, EBI-740282; P61266; P02671-2: FGA; NbExp=3; IntAct=EBI-9071709, EBI-9640259; P61266; P48165: GJA8; NbExp=3; IntAct=EBI-9071709, EBI-17458373; P61266; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-9071709, EBI-13345167; P61266; O15554: KCNN4; NbExp=3; IntAct=EBI-9071709, EBI-2924473; P61266; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-9071709, EBI-6163737; P61266; Q9H115: NAPB; NbExp=5; IntAct=EBI-9071709, EBI-3921185; P61266; O95721: SNAP29; NbExp=3; IntAct=EBI-9071709, EBI-490676; P61266; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-9071709, EBI-10244848; P61266; P32856-2: STX2; NbExp=3; IntAct=EBI-9071709, EBI-11956649; P61266; Q12846: STX4; NbExp=3; IntAct=EBI-9071709, EBI-744942; P61266; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-9071709, EBI-17684533; P61266; P40222: TXLNA; NbExp=3; IntAct=EBI-9071709, EBI-359793; P61266; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-9071709, EBI-10180829; P61266; P23763-3: VAMP1; NbExp=3; IntAct=EBI-9071709, EBI-12097582; P61266; P63027: VAMP2; NbExp=3; IntAct=EBI-9071709, EBI-520113; P61266; O95183: VAMP5; NbExp=3; IntAct=EBI-9071709, EBI-10191195; [Isoform 1]: Membrane ; Single-pass type IV membrane protein [Isoform 2]: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Note=Colocalizes with Lamin A/C and NuMA in interphasic nuclei, and with NuMA and gamma- tubulin in the pericentrosomal region of the mitotic spindle in dividing cells. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P61266-1; Sequence=Displayed; Name=2; Synonyms=STX1B-DeltaTMD; IsoId=P61266-2; Sequence=VSP_047681; Phosphorylated by CK2. Generalized epilepsy with febrile seizures plus 9 (GEFSP9) [MIM:616172]: An autosomal dominant neurologic disorder characterized by febrile and/or afebrile seizures manifesting in early childhood. Seizure are variable and include generalized tonic-clonic, atonic, myoclonic, complex partial, and absence types. Most patients have remission of seizures later in childhood with no residual neurologic deficits. Rarely, patients may show mild developmental delay or mild intellectual disabilities. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 2]: The glycine-rich C-terminus serves as an unconventional nuclear localization signal. Belongs to the syntaxin family. SNARE binding positive regulation of neurotransmitter secretion receptor binding SNAP receptor activity nucleus nuclear lamina nucleoplasm cytoplasm centrosome microtubule organizing center spindle cytosol cytoskeleton plasma membrane neurotransmitter transport intracellular protein transport exocytosis vesicle docking involved in exocytosis vesicle fusion regulation of gene expression regulation of synaptic vesicle priming negative regulation of neuron projection development endomembrane system protein transport membrane integral component of membrane synaptic vesicle exocytosis synaptic vesicle docking vesicle-mediated transport regulation of exocytosis protein kinase binding protein domain specific binding axon SNARE complex neuromuscular junction synaptic vesicle fusion to presynaptic active zone membrane presynaptic membrane vesicle docking presynaptic active zone membrane calcium ion-regulated exocytosis of neurotransmitter regulation of synaptic activity spontaneous neurotransmitter secretion protein localization to membrane presynapse exocytic insertion of neurotransmitter receptor to postsynaptic membrane negative regulation of synaptic vesicle recycling positive regulation of spontaneous neurotransmitter secretion negative regulation of macropinocytosis positive regulation of excitatory postsynaptic potential uc010cad.1 uc010cad.2 uc010cad.3 uc010cad.4 uc010cad.5 
ENST00000215115.5 BCL7C ENST00000215115.5 BAF chromatin remodeling complex subunit BCL7C, transcript variant 2 (from RefSeq NM_004765.4) BCL7C_HUMAN ENST00000215115.1 ENST00000215115.2 ENST00000215115.3 ENST00000215115.4 NM_004765 O43770 Q6PD89 Q8WUZ0 uc002dzv.1 uc002dzv.2 uc002dzv.3 uc002dzv.4 uc002dzv.5 uc002dzv.6 This gene is identified by the similarity of its product to the N-terminal region of BCL7A protein. The BCL7A protein is encoded by the gene known to be directly involved in a three-way gene translocation in a Burkitt lymphoma cell line. The function of this gene has not yet been determined. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2013]. May play an anti-apoptotic role. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8WUZ0-1; Sequence=Displayed; Name=2; IsoId=Q8WUZ0-2; Sequence=VSP_019282; Ubiquitous. Belongs to the BCL7 family. apoptotic process uc002dzv.1 uc002dzv.2 uc002dzv.3 uc002dzv.4 uc002dzv.5 uc002dzv.6 
ENST00000215368.4 EFNA2 ENST00000215368.4 ephrin A2 (from RefSeq NM_001405.4) EFNA2_HUMAN ENST00000215368.1 ENST00000215368.2 ENST00000215368.3 EPLG6 LERK6 NM_001405 O43921 O76020 uc002lry.1 uc002lry.2 uc002lry.3 uc002lry.4 This gene encodes a member of the ephrin family. The protein is composed of a signal sequence, a receptor-binding region, a spacer region, and a hydrophobic region. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Posttranslational modifications determine whether this protein localizes to the nucleus or the cytoplasm. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AJ007292.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215368.4/ ENSP00000215368.1 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis (By similarity). Binds to the receptor tyrosine kinases EPHA3, EPHA4 and EPHA5. Interacts with EPHA8; activates EPHA8. O43921; P54764: EPHA4; NbExp=4; IntAct=EBI-8603210, EBI-5773557; Cell membrane ; Lipid-anchor, GPI- anchor Belongs to the ephrin family. protein binding plasma membrane cell-cell signaling axon guidance membrane olfactory bulb development osteoclast differentiation anchored component of membrane neuromuscular junction perikaryon bone remodeling ephrin receptor binding ephrin receptor signaling pathway uc002lry.1 uc002lry.2 uc002lry.3 uc002lry.4 
ENST00000215375.7 ATP5F1D ENST00000215375.7 ATP synthase F1 subunit delta, transcript variant 1 (from RefSeq NM_001687.5) ATP5D ATP5F1D ATPD_HUMAN D6W5Y3 ENST00000215375.1 ENST00000215375.2 ENST00000215375.3 ENST00000215375.4 ENST00000215375.5 ENST00000215375.6 NM_001687 P30049 Q6FG90 uc002lro.1 uc002lro.2 uc002lro.3 uc002lro.4 uc002lro.5 This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the delta subunit of the catalytic core. Alternatively spliced transcript variants encoding the same isoform have been identified. [provided by RefSeq, Jul 2008]. Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:29478781). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (PubMed:1531933). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). P30049; P56381: ATP5F1E; NbExp=4; IntAct=EBI-1049505, EBI-3904845; P30049; P54253: ATXN1; NbExp=3; IntAct=EBI-1049505, EBI-930964; P30049; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1049505, EBI-10171774; P30049; Q99750: MDFI; NbExp=3; IntAct=EBI-1049505, EBI-724076; P30049; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1049505, EBI-22310682; P30049; Q05519-2: SRSF11; NbExp=3; IntAct=EBI-1049505, EBI-11975029; P30049; Q63HR2: TNS2; NbExp=3; IntAct=EBI-1049505, EBI-949753; Mitochondrion. Mitochondrion inner membrane. Mitochondrial complex V deficiency, nuclear type 5 (MC5DN5) [MIM:618120]: A mitochondrial disorder characterized by childhood onset of episodic metabolic decompensation featuring lactic acidosis and hyperammonemia accompanied by ketoacidosis or hypoglycemia. Chronic manifestations include developmental delay, easy fatiguability, and 3- methylglutaconic aciduria. The transmission pattern of MC5DN5 is consistent with autosomal recessive inheritance. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the ATPase epsilon chain family. mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) protein binding mitochondrion mitochondrial inner membrane mitochondrial proton-transporting ATP synthase complex mitochondrial matrix oxidative phosphorylation ATP biosynthetic process ion transport aerobic respiration ATP synthesis coupled proton transport membrane ATPase activity transmembrane transporter activity mitochondrial proton-transporting ATP synthase complex assembly cristae formation mitochondrial ATP synthesis coupled proton transport proton-transporting ATP synthase complex, catalytic core F(1) response to copper ion proton-transporting ATP synthase activity, rotational mechanism ATP binding ADP binding uc002lro.1 uc002lro.2 uc002lro.3 uc002lro.4 uc002lro.5 
ENST00000215530.7 FGF22 ENST00000215530.7 fibroblast growth factor 22, transcript variant 1 (from RefSeq NM_020637.2) B2RPH4 ENST00000215530.1 ENST00000215530.2 ENST00000215530.3 ENST00000215530.4 ENST00000215530.5 ENST00000215530.6 FGF22_HUMAN NM_020637 Q9HCT0 UNQ2500/PRO5800 uc010xfq.1 uc010xfq.2 uc010xfq.3 uc010xfq.4 uc010xfq.5 The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The mouse homolog of this gene was found to be preferentially expressed in the inner root sheath of the hair follicle, which suggested a role in hair development. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014]. Plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis. Can stimulate cell proliferation (in vitro). May be involved in hair development. Interacts with FGFR1 and FGFR2. Interacts with FGFBP1. Secreted Belongs to the heparin-binding growth factors family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fgf22/"; MAPK cascade fibroblast growth factor receptor binding extracellular region extracellular space nucleolus Golgi apparatus growth factor activity fibroblast growth factor receptor signaling pathway cell surface cell differentiation positive regulation of protein kinase B signaling uc010xfq.1 uc010xfq.2 uc010xfq.3 uc010xfq.4 uc010xfq.5 
ENST00000215531.6 SMIM24 ENST00000215531.6 small integral membrane protein 24 (from RefSeq NM_001136503.2) B9EJF4 C19orf77 ENST00000215531.1 ENST00000215531.2 ENST00000215531.3 ENST00000215531.4 ENST00000215531.5 HSPC323 NM_001136503 O75264 Q9P059 SIM24_HUMAN uc010xhk.1 uc010xhk.2 uc010xhk.3 Membrane ; Single-pass membrane protein Sequence=AAC33194.1; Type=Erroneous gene model prediction; Note=Wrong choice of frame and superfluous exons were predicted.; Evidence=; Sequence=AAF29001.1; Type=Frameshift; Evidence=; Sequence=EAW69320.1; Type=Erroneous gene model prediction; Note=Wrong choice of frame and superfluous exons were predicted.; Evidence=; molecular_function biological_process membrane integral component of membrane uc010xhk.1 uc010xhk.2 uc010xhk.3 
ENST00000215539.4 IGFALS ENST00000215539.4 insulin like growth factor binding protein acid labile subunit, transcript variant 2 (from RefSeq NM_004970.3) ALS ALS_HUMAN B4DZY8 E9PGU3 ENST00000215539.1 ENST00000215539.2 ENST00000215539.3 NM_004970 P35858 uc002cmy.1 uc002cmy.2 uc002cmy.3 uc002cmy.4 uc002cmy.5 The protein encoded by this gene is a serum protein that binds insulin-like growth factors, increasing their half-life and their vascular localization. Production of the encoded protein, which contains twenty leucine-rich repeats, is stimulated by growth hormone. Defects in this gene are a cause of acid-labile subunit deficiency, which maifests itself in a delayed and slow puberty. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Mar 2009]. Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion. Forms a ternary complex of about 140 to 150 kDa with IGF-I or IGF-II and IGFBP-3. Secreted, extracellular space. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P35858-1; Sequence=Displayed; Name=2; IsoId=P35858-2; Sequence=VSP_044605; Plasma. Acid-labile subunit deficiency (ACLSD) [MIM:615961]: A disorder characterized by severely reduced serum IGF-I and IGFBP-3 concentrations and mild growth retardation. Pubertal delay in boys and insulin insensitivity are common findings. te=The disease is caused by variants affecting the gene represented in this entry. insulin-like growth factor binding extracellular region extracellular space nucleoplasm cell adhesion signal transduction extracellular matrix insulin-like growth factor ternary complex cellular protein metabolic process extracellular exosome uc002cmy.1 uc002cmy.2 uc002cmy.3 uc002cmy.4 uc002cmy.5 
ENST00000215555.7 MARCHF2 ENST00000215555.7 membrane associated ring-CH-type finger 2, transcript variant 8 (from RefSeq NR_163145.1) A6NP10 ENST00000215555.1 ENST00000215555.2 ENST00000215555.3 ENST00000215555.4 ENST00000215555.5 ENST00000215555.6 HSPC240 MARCH2 MARCHF2 MARH2_HUMAN NR_163145 Q5H785 Q8N5A3 Q96B78 Q9P0N8 RNF172 uc002mjw.1 uc002mjw.2 uc002mjw.3 uc002mjw.4 uc002mjw.5 MARCH2 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 6.3.2.19). MARCH enzymes add ubiquitin (see MIM 191339) to target lysines in substrate proteins, thereby signaling their vesicular transport between membrane compartments. MARCH2 reduces surface accumulation of several glycoproteins and appears to regulate early endosome-to-trans-Golgi network (TGN) trafficking (Bartee et al., 2004 [PubMed 14722266]; Nakamura et al., 2005 [PubMed 15689499]).[supplied by OMIM, Mar 2010]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.487821.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## E3 ubiquitin-protein ligase that may mediate ubiquitination of TFRC and CD86, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (PubMed:14722266, PubMed:16428329). Together with GOPC/CAL mediates the ubiquitination and lysosomal degradation of CFTR (PubMed:23818989). Ubiquitinates and therefore mediates the degradation of DLG1 (PubMed:17980554). Regulates the intracellular trafficking and secretion of alpha1-antitrypsin/SERPINA1 and HP/haptoglobin via ubiquitination and degradation of the cargo receptor ERGIC3 (PubMed:31142615). Negatively regulates the antiviral and antibacterial immune response by repression of the NF-kB and type 1 IFN signaling pathways, via MARCHF2-mediated K48-linked polyubiquitination of IKBKG/NEMO, resulting in its proteasomal degradation (PubMed:32935379). May be involved in endosomal trafficking through interaction with STX6 (PubMed:15689499). (Microbial infection) Positively regulates the degradation of Vesicular stomatitis virus (VSV) G protein via the lysosomal degradation pathway (PubMed:29573664). Represses HIV-1 viral production and may inhibit the translocation of HIV-1 env to the cell surface, resulting in decreased viral cell-cell transmission (PubMed:29573664). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence= Protein modification; protein ubiquitination. Interacts with STX6; the interaction promotes MARCHF2-mediated ubiquitination and degradation of CFTR (PubMed:23818989). Interacts with MARCHF3 (PubMed:16428329). Interacts with GOPC/CAL; the interaction leads to CFTR ubiquitination and degradation (PubMed:23818989). Interacts with CFTR; the interaction leads to CFTR ubiqtuitination and degradation (PubMed:23818989). Interacts (via PDZ domain) with DLG1 (via PDZ domains); the interaction leads to DLG1 ubiqtuitination and degradation (PubMed:17980554). Interacts with ERGIC3 (PubMed:31142615). Interacts with ADRB2 (PubMed:23166351). Interacts with IKBKG/NEMO; during the late stages of macrophage viral and bacterial infection; the interaction leads to ubiquitination and degradation of IKBKG/NEMO (PubMed:32935379). Q9P0N8; Q13520: AQP6; NbExp=3; IntAct=EBI-10317612, EBI-13059134; Q9P0N8; P13236: CCL4; NbExp=3; IntAct=EBI-10317612, EBI-2873970; Q9P0N8; P11912: CD79A; NbExp=3; IntAct=EBI-10317612, EBI-7797864; Q9P0N8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10317612, EBI-6942903; Q9P0N8; Q9Y282: ERGIC3; NbExp=8; IntAct=EBI-10317612, EBI-781551; Q9P0N8; Q9Y624: F11R; NbExp=3; IntAct=EBI-10317612, EBI-742600; Q9P0N8; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10317612, EBI-18304435; Q9P0N8; Q969F0: FATE1; NbExp=6; IntAct=EBI-10317612, EBI-743099; Q9P0N8; P48165: GJA8; NbExp=3; IntAct=EBI-10317612, EBI-17458373; Q9P0N8; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10317612, EBI-11721746; Q9P0N8; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10317612, EBI-749265; Q9P0N8; Q5T700: LDLRAD1; NbExp=7; IntAct=EBI-10317612, EBI-10173166; Q9P0N8; Q9BXB1-2: LGR4; NbExp=3; IntAct=EBI-10317612, EBI-17443382; Q9P0N8; P15941-11: MUC1; NbExp=3; IntAct=EBI-10317612, EBI-17263240; Q9P0N8; O00623: PEX12; NbExp=3; IntAct=EBI-10317612, EBI-594836; Q9P0N8; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-10317612, EBI-12955265; Q9P0N8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-10317612, EBI-17247926; Q9P0N8; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10317612, EBI-17280858; Q9P0N8; Q8N205: SYNE4; NbExp=3; IntAct=EBI-10317612, EBI-7131783; Q9P0N8; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-10317612, EBI-2821497; Q9P0N8; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-10317612, EBI-11724423; Q9P0N8; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10317612, EBI-18178701; Q9P0N8; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-10317612, EBI-2548832; Q9P0N8; O95859: TSPAN12; NbExp=3; IntAct=EBI-10317612, EBI-2466403; Q9P0N8; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-10317612, EBI-12195249; Endoplasmic reticulum membrane ; Multi-pass membrane protein Lysosome membrane ; Multi-pass membrane protein Endosome membrane ; Multi- pass membrane protein Golgi apparatus membrane ; Multi-pass membrane protein Cytoplasm Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9P0N8-1; Sequence=Displayed; Name=2; IsoId=Q9P0N8-2; Sequence=VSP_041478; Broadly expressed. (Microbial infection) Induced by HIV-1 infection. The RING-CH-type zinc finger domain is required for E3 ligase activity. ubiquitin-protein transferase activity protein binding lysosome lysosomal membrane endosome endoplasmic reticulum endoplasmic reticulum membrane endocytosis zinc ion binding endosome membrane membrane integral component of membrane protein ubiquitination transferase activity cytoplasmic vesicle metal ion binding uc002mjw.1 uc002mjw.2 uc002mjw.3 uc002mjw.4 uc002mjw.5 
ENST00000215565.3 NDUFB7 ENST00000215565.3 NADH:ubiquinone oxidoreductase subunit B7 (from RefSeq NM_004146.6) ENST00000215565.1 ENST00000215565.2 NDUB7_HUMAN NM_004146 P17568 Q6ICN9 Q9UI16 uc002mzg.1 uc002mzg.2 uc002mzg.3 uc002mzg.4 uc002mzg.5 The protein encoded by this gene is a subunit of the multisubunit NADH:ubiquinone oxidoreductase (complex I). Mammalian complex I is composed of 45 different subunits. It is located at the mitochondrial inner membrane. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.221643.1, SRR1163658.407215.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000215565.3/ ENSP00000215565.1 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Complex I is composed of 45 different subunits. P17568; Q5U5Z8-3: AGBL2; NbExp=3; IntAct=EBI-1246238, EBI-12226473; P17568; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-1246238, EBI-8643161; P17568; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-1246238, EBI-12170453; P17568; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-1246238, EBI-12006308; P17568; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-1246238, EBI-1104933; P17568; P24863: CCNC; NbExp=3; IntAct=EBI-1246238, EBI-395261; P17568; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-1246238, EBI-5278764; P17568; P55273: CDKN2D; NbExp=3; IntAct=EBI-1246238, EBI-745859; P17568; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-1246238, EBI-741528; P17568; Q9BW66: CINP; NbExp=3; IntAct=EBI-1246238, EBI-739784; P17568; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-1246238, EBI-11980535; P17568; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-1246238, EBI-11962928; P17568; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-1246238, EBI-744099; P17568; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-1246238, EBI-7225287; P17568; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-1246238, EBI-6658203; P17568; P55040: GEM; NbExp=3; IntAct=EBI-1246238, EBI-744104; P17568; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-1246238, EBI-11959863; P17568; P13807: GYS1; NbExp=3; IntAct=EBI-1246238, EBI-740553; P17568; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-1246238, EBI-11955579; P17568; P25791-3: LMO2; NbExp=3; IntAct=EBI-1246238, EBI-11959475; P17568; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-1246238, EBI-746778; P17568; O14770-4: MEIS2; NbExp=3; IntAct=EBI-1246238, EBI-8025850; P17568; Q13064: MKRN3; NbExp=3; IntAct=EBI-1246238, EBI-2340269; P17568; Q15653: NFKBIB; NbExp=3; IntAct=EBI-1246238, EBI-352889; P17568; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-1246238, EBI-10271199; P17568; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-1246238, EBI-1504830; P17568; Q6P9E2: RECK; NbExp=3; IntAct=EBI-1246238, EBI-10253121; P17568; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-1246238, EBI-10226430; P17568; Q5TAB7: RIPPLY2; NbExp=3; IntAct=EBI-1246238, EBI-10246897; P17568; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-1246238, EBI-748391; P17568; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1246238, EBI-5235340; P17568; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-1246238, EBI-7082156; P17568; Q9BX79-6: STRA6; NbExp=3; IntAct=EBI-1246238, EBI-12140683; P17568; Q01664: TFAP4; NbExp=3; IntAct=EBI-1246238, EBI-2514218; P17568; Q08117-2: TLE5; NbExp=3; IntAct=EBI-1246238, EBI-11741437; P17568; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=3; IntAct=EBI-1246238, EBI-12369705; P17568; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-1246238, EBI-373456; P17568; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1246238, EBI-740727; P17568; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-1246238, EBI-10273713; P17568; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-1246238, EBI-6427977; Mitochondrion inner membrane ; Peripheral membrane protein Mitochondrion intermembrane space Contains two C-X9-C motifs that are predicted to form a helix- coil-helix structure, permitting the formation of intramolecular disulfide bonds. Mitochondrial complex I deficiency, nuclear type 39 (MC1DN39) [MIM:620135]: A form of mitochondrial complex I deficiency, the most common biochemical signature of mitochondrial disorders, a group of highly heterogeneous conditions characterized by defective oxidative phosphorylation, which collectively affects 1 in 5-10000 live births. Clinical disorders have variable severity, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. MC1DN39 is an autosomal recessive form characterized by intrauterine growth retardation, anemia, and postpartum hypertrophic cardiomyopathy, lactic acidosis, encephalopathy, and a severe complex I defect with a fatal outcome. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the complex I NDUFB7 subunit family. Sequence=AAA35675.1; Type=Frameshift; Evidence=; NADH dehydrogenase activity mitochondrion mitochondrial inner membrane mitochondrial respiratory chain complex I mitochondrial intermembrane space mitochondrial electron transport, NADH to ubiquinone NADH dehydrogenase (ubiquinone) activity membrane mitochondrial respiratory chain complex I assembly oxidation-reduction process respiratory chain uc002mzg.1 uc002mzg.2 uc002mzg.3 uc002mzg.4 uc002mzg.5 
ENST00000215567.10 TECR ENST00000215567.10 trans-2,3-enoyl-CoA reductase, transcript variant 1 (from RefSeq NM_138501.6) B2RD55 ENST00000215567.1 ENST00000215567.2 ENST00000215567.3 ENST00000215567.4 ENST00000215567.5 ENST00000215567.6 ENST00000215567.7 ENST00000215567.8 ENST00000215567.9 GPSN2 NM_138501 O75350 Q6IBB2 Q9BWK3 Q9NZ01 Q9Y6P0 SC2 TECR_HUMAN uc002mza.1 uc002mza.2 uc002mza.3 uc002mza.4 uc002mza.5 This gene encodes a multi-pass membrane protein that resides in the endoplasmic reticulum, and belongs to the steroid 5-alpha reductase family. The elongation of microsomal long and very long chain fatty acid consists of 4 sequential reactions. This protein catalyzes the final step, reducing trans-2,3-enoyl-CoA to saturated acyl-CoA. Alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Apr 2011]. Involved in both the production of very long-chain fatty acids for sphingolipid synthesis and the degradation of the sphingosine moiety in sphingolipids through the sphingosine 1-phosphate metabolic pathway (PubMed:25049234). Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle (PubMed:12482854). This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle (PubMed:12482854). This enzyme reduces the trans-2,3-enoyl- CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation (PubMed:12482854). Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (PubMed:12482854). Catalyzes the saturation step of the sphingosine 1-phosphate metabolic pathway, the conversion of trans-2-hexadecenoyl-CoA to palmitoyl-CoA (PubMed:25049234). Reaction=a very-long-chain 2,3-saturated fatty acyl-CoA + NADP(+) = a very-long-chain (2E)-enoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:14473, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.1.93; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14475; Evidence=; Reaction=NADP(+) + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:35351, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:71412; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35353; Evidence=; Reaction=(2E,7Z,10Z,13Z,16Z)-docosapentaenoyl-CoA + H(+) + NADPH = (7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + NADP(+); Xref=Rhea:RHEA:39331, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73856, ChEBI:CHEBI:76416; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39332; Evidence=; Reaction=(2E,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + H(+) + NADPH = (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + NADP(+); Xref=Rhea:RHEA:39467, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73870, ChEBI:CHEBI:76461; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39468; Evidence=; Reaction=(2E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + NADPH = (8Z,11Z,14Z)-eicosatrienoyl-CoA + NADP(+); Xref=Rhea:RHEA:39319, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:74264, ChEBI:CHEBI:76412; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39320; Evidence=; Reaction=(2E)-hexadecenoyl-CoA + H(+) + NADPH = hexadecanoyl-CoA + NADP(+); Xref=Rhea:RHEA:36143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61526; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36144; Evidence=; Lipid metabolism; fatty acid biosynthesis. Lipid metabolism; sphingolipid metabolism. Interacts with ELOVL1 and LASS2. Q9NZ01; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2877718, EBI-11343438; Q9NZ01; P11912: CD79A; NbExp=3; IntAct=EBI-2877718, EBI-7797864; Q9NZ01; O00501: CLDN5; NbExp=3; IntAct=EBI-2877718, EBI-18400628; Q9NZ01; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-2877718, EBI-17233035; Q9NZ01; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2877718, EBI-6942903; Q9NZ01; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-2877718, EBI-18535450; Q9NZ01; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2877718, EBI-781551; Q9NZ01; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2877718, EBI-18304435; Q9NZ01; O00258: GET1; NbExp=3; IntAct=EBI-2877718, EBI-18908258; Q9NZ01; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-2877718, EBI-17231387; Q9NZ01; B0YJ81: HACD1; NbExp=3; IntAct=EBI-2877718, EBI-12051643; Q9NZ01; Q6Y1H2: HACD2; NbExp=7; IntAct=EBI-2877718, EBI-530257; Q9NZ01; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2877718, EBI-10266796; Q9NZ01; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2877718, EBI-373355; Q9NZ01; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-2877718, EBI-6163737; Q9NZ01; P15941-11: MUC1; NbExp=3; IntAct=EBI-2877718, EBI-17263240; Q9NZ01; O15173: PGRMC2; NbExp=3; IntAct=EBI-2877718, EBI-1050125; Q9NZ01; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-2877718, EBI-10192441; Q9NZ01; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2877718, EBI-18159983; Q9NZ01; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-2877718, EBI-5235586; Q9NZ01; Q86WV6: STING1; NbExp=3; IntAct=EBI-2877718, EBI-2800345; Q9NZ01; P27105: STOM; NbExp=3; IntAct=EBI-2877718, EBI-1211440; Q9NZ01; Q00059: TFAM; NbExp=3; IntAct=EBI-2877718, EBI-1049924; Q9NZ01; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-2877718, EBI-1055364; Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NZ01-1; Sequence=Displayed; Name=2; IsoId=Q9NZ01-2; Sequence=VSP_005957; Expressed in most tissues tested. Highly expressed in skeletal muscle. Glycosylated. Intellectual developmental disorder, autosomal recessive 14 (MRT14) [MIM:614020]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the steroid 5-alpha reductase family. protein binding nucleus endoplasmic reticulum endoplasmic reticulum membrane lipid metabolic process fatty acid metabolic process fatty acid biosynthetic process sphingolipid metabolic process membrane integral component of membrane oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors integral component of endoplasmic reticulum membrane fatty acid elongation long-chain fatty-acyl-CoA biosynthetic process very long-chain fatty acid biosynthetic process oxidation-reduction process uc002mza.1 uc002mza.2 uc002mza.3 uc002mza.4 uc002mza.5 
ENST00000215570.8 TIMM13 ENST00000215570.8 translocase of inner mitochondrial membrane 13 (from RefSeq NM_012458.4) ENST00000215570.1 ENST00000215570.2 ENST00000215570.3 ENST00000215570.4 ENST00000215570.5 ENST00000215570.6 ENST00000215570.7 NM_012458 P62206 Q9UHL8 Q9WTL1 Q9Y5L4 TIM13B TIM13_HUMAN TIMM13A TIMM13B uc002lvx.1 uc002lvx.2 uc002lvx.3 uc002lvx.4 This gene encodes a member of the evolutionarily conserved TIMM (translocase of inner mitochondrial membrane) family of proteins that function as chaperones in the import of proteins from the cytoplasm into the mitochondrial inner membrane. Proteins of this family play a role in collecting substrate proteins from the translocase of the outer mitochondrial membrane (TOM) complex and delivering them to either the sorting and assembly machinery in the outer mitochondrial membrane (SAM) complex or the TIMM22 complex in the inner mitochondrial membrane. The encoded protein and the translocase of mitochondrial inner membrane 8a protein form a 70 kDa complex in the intermembrane space. [provided by RefSeq, Jul 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.773314.1, SRR3476690.880947.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2148874, SAMEA2163105 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000215570.8/ ENSP00000215570.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8- TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9- TIMM10 70 kDa complex mediates the import of much more proteins. Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22. Q9Y5L4; O60220: TIMM8A; NbExp=2; IntAct=EBI-1057344, EBI-1049822; Q9Y5L4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1057344, EBI-739895; Mitochondrion inner membrane ; Peripheral membrane protein ; Intermembrane side Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM13 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity). Belongs to the small Tim family. fibrillar center mitochondrion mitochondrial inner membrane mitochondrial intermembrane space protein targeting to mitochondrion sensory perception of sound zinc ion binding protein transport membrane mitochondrial intermembrane space protein transporter complex protein import into mitochondrial inner membrane metal ion binding chaperone-mediated protein transport uc002lvx.1 uc002lvx.2 uc002lvx.3 uc002lvx.4 
ENST00000215574.9 CDC34 ENST00000215574.9 cell division cycle 34, ubiqiutin conjugating enzyme (from RefSeq NM_004359.2) A8K689 ENST00000215574.1 ENST00000215574.2 ENST00000215574.3 ENST00000215574.4 ENST00000215574.5 ENST00000215574.6 ENST00000215574.7 ENST00000215574.8 NM_004359 P49427 UB2R1_HUMAN UBCH3 UBE2R1 uc002lov.1 uc002lov.2 uc002lov.3 uc002lov.4 uc002lov.5 uc002lov.6 The protein encoded by this gene is a member of the ubiquitin-conjugating enzyme family. Ubiquitin-conjugating enzyme catalyzes the covalent attachment of ubiquitin to other proteins. This protein is a part of the large multiprotein complex, which is required for ubiquitin-mediated degradation of cell cycle G1 regulators, and for the initiation of DNA replication. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC009850.2, SRR1163655.656271.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215574.9/ ENSP00000215574.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'- linked polyubiquitination (PubMed:22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3- primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed:10329681, PubMed:10373550, PubMed:10871850, PubMed:11675391, PubMed:12037680, PubMed:15652359, PubMed:17461777, PubMed:17698585, PubMed:19112177, PubMed:19126550, PubMed:19945379, PubMed:20061386, PubMed:20347421). Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin- activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin- conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence= Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L- cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.24; Evidence=; CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit. Kinetic parameters: KM=0.11 uM for beta-catenin-monoubiquin ; Protein modification; protein ubiquitination. Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and RBX1. When cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened (PubMed:10918611, PubMed:11675391, PubMed:18851830, PubMed:19945379, PubMed:19112177, PubMed:24316736). When phosphorylated, interacts with beta-TrCP (BTRC) (PubMed:12037680). Interacts with human herpes virus 1 protein ICP0 and associates with the proteasome for degradation (PubMed:11447293, PubMed:11805320, PubMed:12060736). Interacts with casein kinase subunit CSNK2B (PubMed:11546811). Interacts with CNTD1; this interaction regulates the cell-cycle progression (By similarity). P49427; Q13616: CUL1; NbExp=3; IntAct=EBI-975634, EBI-359390; P49427; P50221: MEOX1; NbExp=3; IntAct=EBI-975634, EBI-2864512; P49427; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-975634, EBI-16439278; P49427; O00560: SDCBP; NbExp=6; IntAct=EBI-975634, EBI-727004; P49427; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-975634, EBI-747107; Cytoplasm. Nucleus. Note=The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase. Expressed in testes during spermatogenesis to regulate repression of cAMP-induced transcription. Negatively regulated by the let-7 microRNA. The C-terminal acidic tail is required for nuclear localization and is involved in the binding to SCF E3 ligase complexes, and more specifically with the CUL1 subunit. Autoubiquitinated (PubMed:22496338, PubMed:11805320, PubMed:12060736). Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin- proteasomal pathway (PubMed:11805320, PubMed:12060736). Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controls the nuclear localization. Belongs to the ubiquitin-conjugating enzyme family. Sequence=AAC37534.1; Type=Erroneous initiation; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc34/"; G1/S transition of mitotic cell cycle nucleotide binding protein polyubiquitination ubiquitin-protein transferase activity protein binding ATP binding nucleus nucleoplasm cytoplasm cytosol DNA replication initiation cellular protein modification process cell cycle protein ubiquitination nuclear speck transferase activity cellular response to interferon-beta proteasome-mediated ubiquitin-dependent protein catabolic process positive regulation of neuron apoptotic process negative regulation of cAMP-mediated signaling ubiquitin conjugating enzyme activity response to growth factor protein K48-linked ubiquitination positive regulation of inclusion body assembly uc002lov.1 uc002lov.2 uc002lov.3 uc002lov.4 uc002lov.5 uc002lov.6 
ENST00000215582.8 MISP ENST00000215582.8 mitotic spindle positioning, transcript variant 2 (from RefSeq NR_135168.2) C19orf21 ENST00000215582.1 ENST00000215582.2 ENST00000215582.3 ENST00000215582.4 ENST00000215582.5 ENST00000215582.6 ENST00000215582.7 MISP MISP_HUMAN NR_135168 Q8IVT2 uc002lpo.1 uc002lpo.2 uc002lpo.3 uc002lpo.4 uc002lpo.5 uc002lpo.6 The protein encoded by this gene is an actin-bundling protein involved in determining cell morphology and mitotic progression. The encoded protein is required for the proper positioning of the mitotic spindle. Two transcript variants, one protein-coding and the other non-protein coding, have been found for this gene. [provided by RefSeq, Feb 2016]. Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus. Associates with F-actin. Interacts with DCTN1; this interaction regulates DCTN1 distribution at the cell cortex. Interacts with PTK2/FAK and MAPRE1. Q8IVT2; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-2555085, EBI-11976299; Q8IVT2; Q9H2G9: BLZF1; NbExp=5; IntAct=EBI-2555085, EBI-2548012; Q8IVT2; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-2555085, EBI-11983447; Q8IVT2; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-2555085, EBI-2802782; Q8IVT2; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-2555085, EBI-742887; Q8IVT2; Q96SW2: CRBN; NbExp=3; IntAct=EBI-2555085, EBI-2510250; Q8IVT2; Q9BQC3: DPH2; NbExp=3; IntAct=EBI-2555085, EBI-10237931; Q8IVT2; Q7L190: DPPA4; NbExp=3; IntAct=EBI-2555085, EBI-710457; Q8IVT2; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-2555085, EBI-2349927; Q8IVT2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2555085, EBI-744099; Q8IVT2; P15311: EZR; NbExp=4; IntAct=EBI-2555085, EBI-1056902; Q8IVT2; Q14192: FHL2; NbExp=3; IntAct=EBI-2555085, EBI-701903; Q8IVT2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-2555085, EBI-750641; Q8IVT2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2555085, EBI-618309; Q8IVT2; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-2555085, EBI-11519926; Q8IVT2; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-2555085, EBI-7060731; Q8IVT2; O75031: HSF2BP; NbExp=3; IntAct=EBI-2555085, EBI-7116203; Q8IVT2; Q16082: HSPB2; NbExp=3; IntAct=EBI-2555085, EBI-739395; Q8IVT2; Q9UJY1: HSPB8; NbExp=3; IntAct=EBI-2555085, EBI-739074; Q8IVT2; Q9UKT9: IKZF3; NbExp=5; IntAct=EBI-2555085, EBI-747204; Q8IVT2; Q5VVH5: IRAK1BP1; NbExp=3; IntAct=EBI-2555085, EBI-9658404; Q8IVT2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-2555085, EBI-11953334; Q8IVT2; P25800: LMO1; NbExp=8; IntAct=EBI-2555085, EBI-8639312; Q8IVT2; P25791-3: LMO2; NbExp=5; IntAct=EBI-2555085, EBI-11959475; Q8IVT2; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-2555085, EBI-2603996; Q8IVT2; Q6PF18: MORN3; NbExp=3; IntAct=EBI-2555085, EBI-9675802; Q8IVT2; Q5VZ52: MORN5; NbExp=3; IntAct=EBI-2555085, EBI-12835568; Q8IVT2; O43482: OIP5; NbExp=3; IntAct=EBI-2555085, EBI-536879; Q8IVT2; P26367: PAX6; NbExp=3; IntAct=EBI-2555085, EBI-747278; Q8IVT2; Q99471: PFDN5; NbExp=3; IntAct=EBI-2555085, EBI-357275; Q8IVT2; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-2555085, EBI-357318; Q8IVT2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-2555085, EBI-10232538; Q8IVT2; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-2555085, EBI-302355; Q8IVT2; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-2555085, EBI-10293968; Q8IVT2; Q6MZQ0: PRR5L; NbExp=3; IntAct=EBI-2555085, EBI-1567866; Q8IVT2; Q8N443: RIBC1; NbExp=3; IntAct=EBI-2555085, EBI-10265323; Q8IVT2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-2555085, EBI-726876; Q8IVT2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-2555085, EBI-6257312; Q8IVT2; Q15428: SF3A2; NbExp=3; IntAct=EBI-2555085, EBI-2462271; Q8IVT2; Q13573: SNW1; NbExp=3; IntAct=EBI-2555085, EBI-632715; Q8IVT2; O14512: SOCS7; NbExp=3; IntAct=EBI-2555085, EBI-1539606; Q8IVT2; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-2555085, EBI-11995806; Q8IVT2; Q496A3: SPATS1; NbExp=3; IntAct=EBI-2555085, EBI-3923692; Q8IVT2; P54274-2: TERF1; NbExp=5; IntAct=EBI-2555085, EBI-711018; Q8IVT2; Q12933: TRAF2; NbExp=3; IntAct=EBI-2555085, EBI-355744; Q8IVT2; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-2555085, EBI-492476; Q8IVT2; Q15654: TRIP6; NbExp=3; IntAct=EBI-2555085, EBI-742327; Q8IVT2; P61758: VBP1; NbExp=3; IntAct=EBI-2555085, EBI-357430; Q8IVT2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-2555085, EBI-4395669; Q8IVT2; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-2555085, EBI-10251462; Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Note=Predominantly localizes to cortical actin structures during interphase and mitosis. Present in retraction fibers, which are formed at former adhesion sites during mitosis, and at spicular membrane protrusions in re-attaching cytokinetic cells. Partially colocalizes with cytoplasmic F-actin. Not detected at microtubules at interphase, nor at spindle during mitosis. Regulated in a cell-cycle dependent manner. Weakly expressed in G1 and S phases. Expression increases in G2/M phases and persisting until the end of mitosis (at protein level). Phosphorylated by CDK1 and PLK1. CDK1 is the priming kinase for PLK1 phosphorylation. Phosphorylation by PLK1 is required for proper spindle orientation at metaphase. Belongs to the MISP family. establishment of mitotic spindle orientation actin binding protein binding cytoplasm cytoskeleton plasma membrane focal adhesion cell cortex cell cycle cell migration cell junction spindle pole centrosome intracellular membrane-bounded organelle actin filament binding cell division organelle localization establishment of centrosome localization mitotic spindle assembly regulation of protein localization to cell cortex actin filament adherens junction cortical actin cytoskeleton mitotic spindle astral microtubule end uc002lpo.1 uc002lpo.2 uc002lpo.3 uc002lpo.4 uc002lpo.5 uc002lpo.6 
ENST00000215631.9 GADD45B ENST00000215631.9 growth arrest and DNA damage inducible beta (from RefSeq NM_015675.4) A8KAM2 ENST00000215631.1 ENST00000215631.2 ENST00000215631.3 ENST00000215631.4 ENST00000215631.5 ENST00000215631.6 ENST00000215631.7 ENST00000215631.8 GA45B_HUMAN MYD118 NM_015675 O75293 O75960 Q17R46 uc002lwb.1 uc002lwb.2 uc002lwb.3 uc002lwb.4 This gene is a member of a group of genes whose transcript levels are increased following stressful growth arrest conditions and treatment with DNA-damaging agents. The genes in this group respond to environmental stresses by mediating activation of the p38/JNK pathway. This activation is mediated via their proteins binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. The function of these genes or their protein products is involved in the regulation of growth and apoptosis. These genes are regulated by different mechanisms, but they are often coordinately expressed and can function cooperatively in inhibiting cell growth. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.236157.1, SRR3476690.397772.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215631.9/ ENSP00000215631.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK. Interacts with GADD45GIP1. O75293; Q92600-3: CNOT9; NbExp=3; IntAct=EBI-448187, EBI-12907584; O75293; Q5JVL4: EFHC1; NbExp=5; IntAct=EBI-448187, EBI-743105; O75293; O14733: MAP2K7; NbExp=8; IntAct=EBI-448187, EBI-492605; O75293; Q9Y6R4: MAP3K4; NbExp=2; IntAct=EBI-448187, EBI-448104; Belongs to the GADD45 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/gadd45b/"; Name=Wikipedia; Note=GADD45B entry; URL="https://en.wikipedia.org/wiki/GADD45B"; activation of MAPKKK activity activation of MAPKK activity protein binding nucleus cytoplasm negative regulation of protein kinase activity apoptotic process multicellular organism development cell differentiation positive regulation of apoptotic process positive regulation of JNK cascade regulation of cell cycle positive regulation of p38MAPK cascade uc002lwb.1 uc002lwb.2 uc002lwb.3 uc002lwb.4 
ENST00000215637.8 MADCAM1 ENST00000215637.8 mucosal vascular addressin cell adhesion molecule 1, transcript variant 1 (from RefSeq NM_130760.3) A5PKV4 B2RPL9 ENST00000215637.1 ENST00000215637.2 ENST00000215637.3 ENST00000215637.4 ENST00000215637.5 ENST00000215637.6 ENST00000215637.7 MADCA_HUMAN NM_130760 O60222 O75867 Q13477 Q5UGI7 uc002los.1 uc002los.2 uc002los.3 uc002los.4 uc002los.5 uc002los.6 The protein encoded by this gene is an endothelial cell adhesion molecule that interacts preferentially with the leukocyte beta7 integrin LPAM-1 (alpha4beta7), L-selectin, and VLA-4 (alpha4beta1) on myeloid cells to direct leukocytes into mucosal and inflamed tissues. It is a member of the immunoglobulin family and is similar to ICAM1 and VCAM1. At least seven alternatively spliced transcripts encoding different protein isoforms have been found for this gene, but the full-length nature of some variants has not been determined. [provided by RefSeq, Jul 2008]. Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7- dependent adhesion strengthening, independent of L-selectin binding. Homodimer. Membrane; Single-pass type I membrane protein. Event=Alternative splicing; Named isoforms=4; Comment=Additional isoforms seem to exist.; Name=1; IsoId=Q13477-1; Sequence=Displayed; Name=2; IsoId=Q13477-2; Sequence=VSP_050014; Name=3; IsoId=Q13477-3; Sequence=VSP_043202; Name=4; IsoId=Q13477-4; Sequence=VSP_047694, VSP_043202; Highly expressed on high endothelial venules (HEV) and lamina propia venules found in the small intestine, and to a lesser extent in the colon and spleen. Very low levels of expression found in pancreas and brain. Not expressed in the thymus, prostate, ovaries, testis, heart, placenta, lung, liver, skeletal muscle, kidney or peripheral blood leukocytes. The Ser/Thr-rich mucin-like domain may provide possible sites for O-glycosylation. The number of repeats in the mucin domain varies between 5 and 8 repeats. positive regulation of leukocyte migration plasma membrane immune response cell adhesion cell-matrix adhesion signal transduction integrin-mediated signaling pathway membrane integral component of membrane extracellular matrix organization heterotypic cell-cell adhesion receptor clustering regulation of immune response leukocyte tethering or rolling integrin binding involved in cell-matrix adhesion positive regulation of lymphocyte migration uc002los.1 uc002los.2 uc002los.3 uc002los.4 uc002los.5 uc002los.6 
ENST00000215659.13 MAPK12 ENST00000215659.13 mitogen-activated protein kinase 12, transcript variant 1 (from RefSeq NM_002969.6) ENST00000215659.1 ENST00000215659.10 ENST00000215659.11 ENST00000215659.12 ENST00000215659.2 ENST00000215659.3 ENST00000215659.4 ENST00000215659.5 ENST00000215659.6 ENST00000215659.7 ENST00000215659.8 ENST00000215659.9 ERK6 MK12_HUMAN NM_002969 P53778 Q14260 Q6IC53 Q99588 Q99672 SAPK3 uc003bkm.1 uc003bkm.2 uc003bkm.3 Activation of members of the mitogen-activated protein kinase family is a major mechanism for transduction of extracellular signals. Stress-activated protein kinases are one subclass of MAP kinases. The protein encoded by this gene functions as a signal transducer during differentiation of myoblasts to myotubes. [provided by RefSeq, Jul 2008]. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down- regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12- signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Binds 2 magnesium ions. ; Activated by phosphorylation on threonine and tyrosine. MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK12 induced by environmental stress, whereas MAP2K6/MKK6 is the major MAPK12 activator in response to TNF-alpha. Kinetic parameters: KM=37 uM for ATP ; KM=313 uM for EGFR substrate peptide ; KM=254 uM for GST-ATF2 ; Monomer. Interacts with the PDZ domain of the syntrophin SNTA1. Interacts with SH3BP5. Interacts with LIN7C, SCRIB and SYNJ2BP (By similarity). Interacts with PTPN4; this interaction induces the activation of PTPN4 phosphatase activity. P53778; P05067: APP; NbExp=3; IntAct=EBI-602406, EBI-77613; P53778; Q12959: DLG1; NbExp=2; IntAct=EBI-602406, EBI-357481; P53778; Q16512: PKN1; NbExp=2; IntAct=EBI-602406, EBI-602382; P53778; P29074: PTPN4; NbExp=2; IntAct=EBI-602406, EBI-710431; P53778; Q14160: SCRIB; NbExp=6; IntAct=EBI-602406, EBI-357345; P53778; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-602406, EBI-747107; Cytoplasm. Nucleus. Mitochondrion. Note=Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma (By similarity). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P53778-1; Sequence=Displayed; Name=2; IsoId=P53778-2; Sequence=VSP_055224; Highly expressed in skeletal muscle and heart. Expression of MAPK12 is down-regulation by MAPK14 activation. The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme. Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway. Note=MAPK is overexpressed in highly metastatic breast cancer cell lines and its expression is preferentially associated with basal- like and metastatic phenotypes of breast tumor samples. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41290/MAPK12"; MAPK cascade nucleotide binding magnesium ion binding protein kinase activity protein serine/threonine kinase activity MAP kinase activity protein binding ATP binding nucleus nucleoplasm cytoplasm mitochondrion cytosol protein phosphorylation DNA damage induced protein phosphorylation cell cycle cell cycle arrest signal transduction muscle organ development regulation of gene expression positive regulation of peptidase activity kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation intracellular signal transduction myoblast differentiation negative regulation of cell cycle metal ion binding positive regulation of muscle cell differentiation uc003bkm.1 uc003bkm.2 uc003bkm.3 
ENST00000215727.10 SERPIND1 ENST00000215727.10 serpin family D member 1 (from RefSeq NM_000185.4) B2RAI1 D3DX34 ENST00000215727.1 ENST00000215727.2 ENST00000215727.3 ENST00000215727.4 ENST00000215727.5 ENST00000215727.6 ENST00000215727.7 ENST00000215727.8 ENST00000215727.9 HCF2 HEP2_HUMAN NM_000185 P05546 Q6IBZ5 uc002ztb.1 uc002ztb.2 uc002ztb.3 This gene belongs to the serpin gene superfamily. Serpins play roles in many processes including inflammation, blood clotting, and cancer metastasis. Members of this family have highly conserved secondary structures with a reactive center loop that interacts with the protease active site to inhibit protease activity. This gene encodes a plasma serine protease that functions as a thrombin and chymotrypsin inhibitor. The protein is activated by heparin, dermatan sulfate, and glycosaminoglycans. Allelic variations in this gene are associated with heparin cofactor II deficiency. [provided by RefSeq, Jul 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC035028.2, SRR1803613.60943.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142853, SAMEA2144120 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215727.10/ ENSP00000215727.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan- independent manner. Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils. Expressed predominantly in liver. Also present in plasma. The N-terminal acidic repeat region mediates, in part, the glycosaminoglycan-accelerated thrombin inhibition. Phosphorylated by FAM20C in the extracellular medium. Thrombophilia due to heparin cofactor 2 deficiency (THPH10) [MIM:612356]: A hemostatic disorder characterized by a tendency to recurrent thrombosis. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the serpin family. Sequence=CAG30459.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; endopeptidase inhibitor activity serine-type endopeptidase inhibitor activity extracellular region extracellular space endoplasmic reticulum lumen chemotaxis blood coagulation hemostasis heparin binding negative regulation of peptidase activity negative regulation of endopeptidase activity peptidase inhibitor activity post-translational protein modification cellular protein metabolic process extracellular exosome uc002ztb.1 uc002ztb.2 uc002ztb.3 
ENST00000215730.12 SNAP29 ENST00000215730.12 synaptosome associated protein 29 (from RefSeq NM_004782.4) ENST00000215730.1 ENST00000215730.10 ENST00000215730.11 ENST00000215730.2 ENST00000215730.3 ENST00000215730.4 ENST00000215730.5 ENST00000215730.6 ENST00000215730.7 ENST00000215730.8 ENST00000215730.9 NM_004782 O95721 SNAP29 SNP29_HUMAN uc011ahw.1 uc011ahw.2 uc011ahw.3 uc011ahw.4 This gene, a member of the SNAP25 gene family, encodes a protein involved in multiple membrane trafficking steps. Two other members of this gene family, SNAP23 and SNAP25, encode proteins that bind a syntaxin protein and mediate synaptic vesicle membrane docking and fusion to the plasma membrane. The protein encoded by this gene binds tightly to multiple syntaxins and is localized to intracellular membrane structures rather than to the plasma membrane. While the protein is mostly membrane-bound, a significant fraction of it is found free in the cytoplasm. Use of multiple polyadenylation sites has been noted for this gene. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.113951.1, SRR1660809.243742.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215730.12/ ENSP00000215730.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions. Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17, involved in fusion of autophagosome with lysosome (PubMed:23217709, PubMed:25686604). Interacts with multiple syntaxins including STX6 (By similarity). Interacts with EIPR1 (PubMed:27440922). Interacts with STX17; this interaction is increased in the absence of TMEM39A (PubMed:31806350, PubMed:33422265). (Microbial infection) Interacts with Hantaan hantavirus nucleoprotein; this interaction prevents the breakdown of the viral glycoprotein N by virus-triggered autophagy. (Microbial infection) The interaction with STX17 is decreased in presence of SARS coronavirus-2/SARS-CoV-2 ORF3A protein. O95721; P54253: ATXN1; NbExp=3; IntAct=EBI-490676, EBI-930964; O95721; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-490676, EBI-3866319; O95721; Q9H4M9: EHD1; NbExp=3; IntAct=EBI-490676, EBI-490691; O95721; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-490676, EBI-10175124; O95721; Q8IZT9: FAM9C; NbExp=3; IntAct=EBI-490676, EBI-2870039; O95721; P42858: HTT; NbExp=3; IntAct=EBI-490676, EBI-466029; O95721; Q9H115: NAPB; NbExp=8; IntAct=EBI-490676, EBI-3921185; O95721; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-490676, EBI-741158; O95721; O15294: OGT; NbExp=2; IntAct=EBI-490676, EBI-539828; O95721; Q86Y82: STX12; NbExp=5; IntAct=EBI-490676, EBI-2691717; O95721; O14662-5: STX16; NbExp=3; IntAct=EBI-490676, EBI-9089968; O95721; P56962: STX17; NbExp=10; IntAct=EBI-490676, EBI-2797775; O95721; P61266: STX1B; NbExp=3; IntAct=EBI-490676, EBI-9071709; O95721; P32856-2: STX2; NbExp=3; IntAct=EBI-490676, EBI-11956649; O95721; Q13277: STX3; NbExp=3; IntAct=EBI-490676, EBI-1394295; O95721; O43752: STX6; NbExp=3; IntAct=EBI-490676, EBI-2695795; O95721; Q13114: TRAF3; NbExp=4; IntAct=EBI-490676, EBI-357631; O95721; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-490676, EBI-12003468; O95721; Q6F5E7: TXNRD3NB; NbExp=3; IntAct=EBI-490676, EBI-18122152; O95721; P23763: VAMP1; NbExp=3; IntAct=EBI-490676, EBI-10201335; O95721; P63027: VAMP2; NbExp=3; IntAct=EBI-490676, EBI-520113; O95721; Q15836: VAMP3; NbExp=3; IntAct=EBI-490676, EBI-722343; O95721; O75379-2: VAMP4; NbExp=3; IntAct=EBI-490676, EBI-10187996; O95721; O95183: VAMP5; NbExp=9; IntAct=EBI-490676, EBI-10191195; O95721; Q9BV40: VAMP8; NbExp=6; IntAct=EBI-490676, EBI-727028; Cytoplasm Golgi apparatus membrane ; Peripheral membrane protein Cytoplasmic vesicle, autophagosome membrane ; Peripheral membrane protein Cell projection, cilium membrane ; Peripheral membrane protein Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. Found in brain, heart, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas. Cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma syndrome (CEDNIK) [MIM:609528]: A neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis and palmoplantar keratoderma. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the SNAP-25 family. Golgi membrane autophagosome membrane SNAP receptor activity protein binding nucleoplasm cytoplasm autophagosome Golgi apparatus centrosome cytosol plasma membrane cilium exocytosis vesicle targeting vesicle fusion autophagy protein transport membrane synaptic vesicle priming autophagosome docking syntaxin binding ciliary pocket membrane cell projection organization SNARE complex cytoplasmic vesicle synaptic vesicle fusion to presynaptic active zone membrane azurophil granule membrane cell projection neutrophil degranulation ciliary membrane cilium assembly membrane fusion autophagosome maturation presynapse uc011ahw.1 uc011ahw.2 uc011ahw.3 uc011ahw.4 
ENST00000215742.9 THAP7 ENST00000215742.9 THAP domain containing 7, transcript variant 1 (from RefSeq NM_030573.3) B2RD97 D3DX40 ENST00000215742.1 ENST00000215742.2 ENST00000215742.3 ENST00000215742.4 ENST00000215742.5 ENST00000215742.6 ENST00000215742.7 ENST00000215742.8 NM_030573 Q9BT49 THAP7_HUMAN uc002zts.1 uc002zts.2 uc002zts.3 Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors. Interacts with HDAC3 and nuclear hormone receptor corepressors. Q9BT49; O15084: ANKRD28; NbExp=3; IntAct=EBI-741350, EBI-359567; Q9BT49; P27797: CALR; NbExp=3; IntAct=EBI-741350, EBI-1049597; Q9BT49; O95273: CCNDBP1; NbExp=4; IntAct=EBI-741350, EBI-748961; Q9BT49; Q16543: CDC37; NbExp=3; IntAct=EBI-741350, EBI-295634; Q9BT49; P12830: CDH1; NbExp=3; IntAct=EBI-741350, EBI-727477; Q9BT49; Q15078: CDK5R1; NbExp=3; IntAct=EBI-741350, EBI-746189; Q9BT49; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-741350, EBI-3867333; Q9BT49; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-741350, EBI-12878374; Q9BT49; P36957: DLST; NbExp=3; IntAct=EBI-741350, EBI-351007; Q9BT49; Q92997: DVL3; NbExp=3; IntAct=EBI-741350, EBI-739789; Q9BT49; O95967: EFEMP2; NbExp=3; IntAct=EBI-741350, EBI-743414; Q9BT49; Q13643: FHL3; NbExp=3; IntAct=EBI-741350, EBI-741101; Q9BT49; A1L4K1: FSD2; NbExp=3; IntAct=EBI-741350, EBI-5661036; Q9BT49; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-741350, EBI-746969; Q9BT49; Q08379: GOLGA2; NbExp=4; IntAct=EBI-741350, EBI-618309; Q9BT49; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-741350, EBI-5916454; Q9BT49; P49639: HOXA1; NbExp=3; IntAct=EBI-741350, EBI-740785; Q9BT49; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-741350, EBI-3044087; Q9BT49; Q15323: KRT31; NbExp=6; IntAct=EBI-741350, EBI-948001; Q9BT49; O76011: KRT34; NbExp=3; IntAct=EBI-741350, EBI-1047093; Q9BT49; Q6A162: KRT40; NbExp=3; IntAct=EBI-741350, EBI-10171697; Q9BT49; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-741350, EBI-11749135; Q9BT49; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-741350, EBI-10171774; Q9BT49; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-741350, EBI-11988175; Q9BT49; O95751: LDOC1; NbExp=3; IntAct=EBI-741350, EBI-740738; Q9BT49; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-741350, EBI-739832; Q9BT49; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-741350, EBI-741037; Q9BT49; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-741350, EBI-746778; Q9BT49; P23508: MCC; NbExp=3; IntAct=EBI-741350, EBI-307531; Q9BT49; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-741350, EBI-10172526; Q9BT49; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-741350, EBI-742948; Q9BT49; Q5JR59-3: MTUS2; NbExp=6; IntAct=EBI-741350, EBI-11522433; Q9BT49; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-741350, EBI-1055945; Q9BT49; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-741350, EBI-945833; Q9BT49; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-741350, EBI-22310682; Q9BT49; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-741350, EBI-741158; Q9BT49; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-741350, EBI-713786; Q9BT49; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-741350, EBI-2339674; Q9BT49; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-741350, EBI-79165; Q9BT49; Q13526: PIN1; NbExp=5; IntAct=EBI-741350, EBI-714158; Q9BT49; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-741350, EBI-302355; Q9BT49; Q01105: SET; NbExp=7; IntAct=EBI-741350, EBI-1053182; Q9BT49; Q01105-2: SET; NbExp=5; IntAct=EBI-741350, EBI-7481343; Q9BT49; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-741350, EBI-1105213; Q9BT49; Q9BT49: THAP7; NbExp=6; IntAct=EBI-741350, EBI-741350; Q9BT49; Q08117-2: TLE5; NbExp=3; IntAct=EBI-741350, EBI-11741437; Q9BT49; P06753: TPM3; NbExp=3; IntAct=EBI-741350, EBI-355607; Q9BT49; Q13077: TRAF1; NbExp=6; IntAct=EBI-741350, EBI-359224; Q9BT49; Q12933: TRAF2; NbExp=13; IntAct=EBI-741350, EBI-355744; Q9BT49; O00463: TRAF5; NbExp=3; IntAct=EBI-741350, EBI-523498; Q9BT49; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-741350, EBI-527853; Nucleus. Chromosome. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding nucleic acid binding DNA binding protein binding nucleus chromosome regulation of transcription from RNA polymerase II promoter nuclear speck nuclear membrane identical protein binding intracellular membrane-bounded organelle negative regulation of transcription, DNA-templated metal ion binding protein N-terminus binding C2H2 zinc finger domain binding uc002zts.1 uc002zts.2 uc002zts.3 
ENST00000215743.8 MMP11 ENST00000215743.8 matrix metallopeptidase 11, transcript variant 1 (from RefSeq NM_005940.5) ENST00000215743.1 ENST00000215743.2 ENST00000215743.3 ENST00000215743.4 ENST00000215743.5 ENST00000215743.6 ENST00000215743.7 MMP11_HUMAN NM_005940 P24347 Q5FX24 Q6PEZ6 Q9UC26 STMY3 uc002zxx.1 uc002zxx.2 uc002zxx.3 uc002zxx.4 uc002zxx.5 Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix. [provided by RefSeq, Jul 2008]. May play an important role in the progression of epithelial malignancies. Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Note=Binds 1 Ca(2+) ion per subunit. ; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 2 Zn(2+) ions per subunit. ; Secreted, extracellular space, extracellular matrix Specifically expressed in stromal cells of breast carcinomas. The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation- peptide release activates the enzyme. The precursor is cleaved by a furin endopeptidase. Belongs to the peptidase M10A family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/200/ST3"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp11/"; metalloendopeptidase activity extracellular region extracellular space Golgi lumen proteolysis multicellular organism development peptidase activity metallopeptidase activity zinc ion binding hydrolase activity extracellular matrix disassembly extracellular matrix organization collagen fibril organization collagen catabolic process extracellular matrix negative regulation of fat cell differentiation metal ion binding basement membrane organization uc002zxx.1 uc002zxx.2 uc002zxx.3 uc002zxx.4 uc002zxx.5 
ENST00000215754.8 MIF ENST00000215754.8 macrophage migration inhibitory factor (from RefSeq NM_002415.2) A5Z1R8 B2R4S3 ENST00000215754.1 ENST00000215754.2 ENST00000215754.3 ENST00000215754.4 ENST00000215754.5 ENST00000215754.6 ENST00000215754.7 GLIF MIF MIF_HUMAN MMIF NM_002415 P14174 Q2V4Y5 Q6FHV0 uc002zyr.1 uc002zyr.2 uc002zyr.3 This gene encodes a lymphokine involved in cell-mediated immunity, immunoregulation, and inflammation. It plays a role in the regulation of macrophage function in host defense through the suppression of anti-inflammatory effects of glucocorticoids. This lymphokine and the JAB1 protein form a complex in the cytosol near the peripheral plasma membrane, which may indicate an additional role in integrin signaling pathways. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BP204676.1, BP317237.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215754.8/ ENSP00000215754.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Pro-inflammatory cytokine involved in the innate immune response to bacterial pathogens (PubMed:15908412, PubMed:17443469, PubMed:23776208). The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense (PubMed:15908412, PubMed:17443469, PubMed:23776208). Counteracts the anti-inflammatory activity of glucocorticoids (PubMed:15908412, PubMed:17443469, PubMed:23776208). Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known (PubMed:11439086, PubMed:17526494). It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity (PubMed:11439086, PubMed:17526494). Reaction=3-phenylpyruvate = enol-phenylpyruvate; Xref=Rhea:RHEA:17097, ChEBI:CHEBI:16815, ChEBI:CHEBI:18005; EC=5.3.2.1; Evidence=; Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate; Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509; EC=5.3.3.12; Evidence=; Kinetic parameters: KM=249 uM for phenylpyruvate ; KM=168 uM for p-hydroxyphenylpyruvate ; Vmax=2113 umol/min/mg enzyme toward phenylpyruvate ; Vmax=524 umol/min/mg enzyme toward p-hydroxyphenylpyruvate ; Homotrimer (PubMed:8610159, PubMed:23776208). Interacts with CXCR2 extracellular domain (By similarity). Interacts with the CD74 extracellular domain, USO1, COPS5 and BNIPL (PubMed:11089976, PubMed:12681488, PubMed:12782713, PubMed:19454686, PubMed:23776208). P14174; O43521-2: BCL2L11; NbExp=5; IntAct=EBI-372712, EBI-526420; P14174; P00533: EGFR; NbExp=3; IntAct=EBI-372712, EBI-297353; P14174; Q92743: HTRA1; NbExp=3; IntAct=EBI-372712, EBI-352256; P14174; P14174: MIF; NbExp=7; IntAct=EBI-372712, EBI-372712; P14174; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-372712, EBI-741158; Secreted toplasm te=Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. Up-regulated in concanavalin-A-treated lymphocytes. Up- regulated in macrophages upon exposure to M.tuberculosis antigens. Rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]: An inflammatory articular disorder with systemic onset beginning before the age of 16. It represents a subgroup of juvenile arthritis associated with severe extraarticular features and occasionally fatal complications. During active phases of the disorder, patients display a typical daily spiking fever, an evanescent macular rash, lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Serum levels of MIF are elevated in patients with severe sepsis or septic shock. High levels of MIF are correlated with low survival. Drugs that inhibit tautomerase activity protect against death due to sepsis. Belongs to the MIF family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mif/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41365/MIF"; prostaglandin biosynthetic process positive regulation of protein phosphorylation protease binding immune system process negative regulation of mature B cell apoptotic process dopachrome isomerase activity receptor binding cytokine activity cytokine receptor binding protein binding extracellular region extracellular space nucleoplasm cytoplasm cytosol plasma membrane inflammatory response cell surface receptor signaling pathway cell aging cell proliferation cell surface negative regulation of gene expression positive regulation of protein kinase A signaling negative regulation of macrophage chemotaxis isomerase activity carboxylic acid metabolic process DNA damage response, signal transduction by p53 class mediator negative regulation of cell migration positive regulation of B cell proliferation positive regulation of lipopolysaccharide-mediated signaling pathway vesicle negative regulation of cellular protein metabolic process positive regulation of tumor necrosis factor production negative regulation of myeloid cell apoptotic process positive regulation of peptidyl-serine phosphorylation secretory granule lumen interleukin-12-mediated signaling pathway chemoattractant activity regulation of cell proliferation positive regulation of phosphorylation identical protein binding regulation of macrophage activation negative regulation of apoptotic process neutrophil degranulation positive regulation of MAP kinase activity negative regulation of DNA damage response, signal transduction by p53 class mediator innate immune response positive regulation of fibroblast proliferation phenylpyruvate tautomerase activity positive regulation of cytokine secretion positive regulation of peptidyl-tyrosine phosphorylation leukocyte migration positive chemotaxis positive regulation of prostaglandin secretion involved in immune response positive regulation of myeloid leukocyte cytokine production involved in immune response extracellular exosome protein homotrimerization positive regulation of ERK1 and ERK2 cascade negative regulation of cell cycle arrest positive regulation of arachidonic acid secretion negative regulation of cell aging negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator ficolin-1-rich granule lumen positive regulation of chemokine (C-X-C motif) ligand 2 production uc002zyr.1 uc002zyr.2 uc002zyr.3 
ENST00000215770.6 DDTL ENST00000215770.6 D-dopachrome tautomerase like (from RefSeq NM_001084393.2) A6NHG4 B4DJJ7 DDTL_HUMAN ENST00000215770.1 ENST00000215770.2 ENST00000215770.3 ENST00000215770.4 ENST00000215770.5 NM_001084393 uc002zyy.1 uc002zyy.2 uc002zyy.3 uc002zyy.4 uc002zyy.5 uc002zyy.6 May have lyase activity. Cytoplasm Belongs to the MIF family. cytoplasm lyase activity extracellular exosome uc002zyy.1 uc002zyy.2 uc002zyy.3 uc002zyy.4 uc002zyy.5 uc002zyy.6 
ENST00000215781.3 OSM ENST00000215781.3 oncostatin M, transcript variant 1 (from RefSeq NM_020530.6) ENST00000215781.1 ENST00000215781.2 NM_020530 ONCM_HUMAN P13725 Q6FHP8 Q9UCP6 uc003ahb.1 uc003ahb.2 uc003ahb.3 uc003ahb.4 uc003ahb.5 This gene encodes a member of the leukemia inhibitory factor/oncostatin-M (LIF/OSM) family of proteins. The encoded preproprotein is proteolytically processed to generate the mature protein. This protein is a secreted cytokine and growth regulator that inhibits the proliferation of a number of tumor cell lines. This protein also regulates the production of other cytokines, including interleukin 6, granulocyte-colony stimulating factor and granulocyte-macrophage colony stimulating factor in endothelial cells. This gene and the related gene, leukemia inhibitory factor, also present on chromosome 22, may have resulted from the duplication of a common ancestral gene. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Jan 2016]. Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIFR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration (By similarity). P13725; P40189: IL6ST; NbExp=2; IntAct=EBI-6595724, EBI-1030834; Secreted. Propeptide processing is not important for receptor binding activity but may be important growth-inhibitory activity. Belongs to the LIF/OSM family. positive regulation of acute inflammatory response cytokine activity oncostatin-M receptor binding protein binding extracellular region extracellular space immune response multicellular organism development growth factor activity positive regulation of cell proliferation negative regulation of cell proliferation positive regulation of phosphatidylinositol 3-kinase signaling cytokine-mediated signaling pathway positive regulation of peptidyl-serine phosphorylation oncostatin-M-mediated signaling pathway regulation of growth positive regulation of tyrosine phosphorylation of STAT protein positive regulation of MAPK cascade positive regulation of transcription from RNA polymerase II promoter negative regulation of hormone secretion positive regulation of inflammatory response positive regulation of peptidyl-tyrosine phosphorylation positive regulation of cell division positive regulation of protein kinase B signaling regulation of hematopoietic stem cell differentiation positive regulation of interleukin-17 secretion uc003ahb.1 uc003ahb.2 uc003ahb.3 uc003ahb.4 uc003ahb.5 
ENST00000215790.12 TBC1D10A ENST00000215790.12 TBC1 domain family member 10A, transcript variant 2 (from RefSeq NM_031937.3) B3KXT8 ENST00000215790.1 ENST00000215790.10 ENST00000215790.11 ENST00000215790.2 ENST00000215790.3 ENST00000215790.4 ENST00000215790.5 ENST00000215790.6 ENST00000215790.7 ENST00000215790.8 ENST00000215790.9 EPI64 NM_031937 O76053 Q20WK7 Q543A2 Q9BXI6 TB10A_HUMAN TBC1D10 uc003ahk.1 uc003ahk.2 uc003ahk.3 uc003ahk.4 uc003ahk.5 uc003ahk.6 Acts as a GTPase-activating protein for RAB27A, but not for RAB2A, RAB3A, nor RAB4A. Binds to the first PDZ domain of NHERF1 and NHERF2. Q9BXI6; Q96AP0: ACD; NbExp=2; IntAct=EBI-7815040, EBI-717666; Q9BXI6; Q9BXU3: TEX13A; NbExp=6; IntAct=EBI-7815040, EBI-10301068; Cell projection, microvillus Note=Localizes to the microvilli-rich region of the syncytiotrophoblast. In melanocytes, located at the periphery of cells. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BXI6-1; Sequence=Displayed; Name=2; IsoId=Q9BXI6-2; Sequence=VSP_043119; The arginine and glutamine fingers are critical for the GTPase- activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. Exists in both phosphorylated and non-phosphorylated state. Sequence=AAC23434.1; Type=Erroneous gene model prediction; Evidence=; guanyl-nucleotide exchange factor activity GTPase activator activity protein binding cytosol plasma membrane microvillus intracellular protein transport Rab GTPase binding PDZ domain binding retrograde transport, endosome to Golgi cell projection cadherin binding positive regulation of proteolysis extracellular exosome activation of GTPase activity activation of cysteine-type endopeptidase activity regulation of cilium assembly uc003ahk.1 uc003ahk.2 uc003ahk.3 uc003ahk.4 uc003ahk.5 uc003ahk.6 
ENST00000215793.13 SF3A1 ENST00000215793.13 splicing factor 3a subunit 1 (from RefSeq NM_005877.6) E9PAW1 ENST00000215793.1 ENST00000215793.10 ENST00000215793.11 ENST00000215793.12 ENST00000215793.2 ENST00000215793.3 ENST00000215793.4 ENST00000215793.5 ENST00000215793.6 ENST00000215793.7 ENST00000215793.8 ENST00000215793.9 NM_005877 Q15459 SAP114 SF3A1_HUMAN uc003ahl.1 uc003ahl.2 uc003ahl.3 uc003ahl.4 uc003ahl.5 This gene encodes a subunit of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer is a component of the mature U2 small nuclear ribonucleoprotein particle (snRNP). U2 small nuclear ribonucleoproteins play a critical role in spliceosome assembly and pre-mRNA splicing. [provided by RefSeq, Aug 2014]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.875500.1, SRR3476690.853979.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215793.13/ ENSP00000215793.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:10882114, PubMed:11533230, PubMed:32494006). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch- site adenosine, the nucleophile for the first step of splicing (PubMed:10882114, PubMed:11533230, PubMed:32494006). Within the 17S U2 SnRNP complex, SF3A1 is part of the SF3A subcomplex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230). Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes (PubMed:29360106, PubMed:30315277). Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:32494006, PubMed:36797247). Part of the SF3A subcomplex of the 17S U2 SnRNP complex which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114 (PubMed:10882114, PubMed:11533230, PubMed:21349847). SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the mature 17S U2 small nuclear ribonucleoprotein complex (17S U2 snRNP) (PubMed:10882114, PubMed:11533230). SF3A1 functions as a scaffold that interacts directly with both SF3A2 and SF3A3 (PubMed:11533230, PubMed:21349847, PubMed:17098193). Identified in the spliceosome 'E' complex, a precursor of the spliceosome 'A' complex (PubMed:10882114). Identified in the spliceosome 'A' and 'B' complexes (PubMed:29360106, PubMed:30315277). Identified in the spliceosome 'C' complex (PubMed:11991638). Q15459; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-1054743, EBI-2603996; Q15459; O75400: PRPF40A; NbExp=2; IntAct=EBI-1054743, EBI-473291; Q15459; P98175: RBM10; NbExp=2; IntAct=EBI-1054743, EBI-721525; Q15459; Q15637: SF1; NbExp=8; IntAct=EBI-1054743, EBI-744603; Q15459; Q15428: SF3A2; NbExp=4; IntAct=EBI-1054743, EBI-2462271; Q15459; Q12874: SF3A3; NbExp=7; IntAct=EBI-1054743, EBI-1051880; Q15459; P08047: SP1; NbExp=2; IntAct=EBI-1054743, EBI-298336; Nucleus cleus speckle Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q15459-1; Sequence=Displayed; Name=2; IsoId=Q15459-2; Sequence=VSP_054090; Ubiquitously expressed. SURP motif 2 mediates direct binding to SF3A3. mRNA 3'-splice site recognition mRNA splicing, via spliceosome RNA binding protein binding nucleus nucleoplasm spliceosomal complex U2-type spliceosomal complex U2 snRNP RNA processing mRNA processing RNA splicing nuclear speck U2-type prespliceosome U2-type precatalytic spliceosome catalytic step 2 spliceosome U2-type prespliceosome assembly uc003ahl.1 uc003ahl.2 uc003ahl.3 uc003ahl.4 uc003ahl.5 
ENST00000215794.8 USP18 ENST00000215794.8 ubiquitin specific peptidase 18 (from RefSeq NM_017414.4) ENST00000215794.1 ENST00000215794.2 ENST00000215794.3 ENST00000215794.4 ENST00000215794.5 ENST00000215794.6 ENST00000215794.7 ISG43 NM_017414 Q53Y90 Q6IAD9 Q9NY71 Q9UMW8 UBP18_HUMAN uc002zny.1 uc002zny.2 uc002zny.3 uc002zny.4 uc002zny.5 The protein encoded by this gene belongs to the ubiquitin-specific proteases (UBP) family of enzymes that cleave ubiquitin from ubiquitinated protein substrates. It is highly expressed in liver and thymus, and is localized to the nucleus. This protein efficiently cleaves only ISG15 (a ubiquitin-like protein) fusions, and deletion of this gene in mice results in a massive increase of ISG15 conjugates in tissues, indicating that this protein is a major ISG15-specific protease. Mice lacking this gene are also hypersensitive to interferon, suggesting a function of this protein in downregulating interferon responses, independent of its isopeptidase activity towards ISG15. [provided by RefSeq, Sep 2011]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AL136690.1, BC014896.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215794.8/ ENSP00000215794.7 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Interferon-induced ISG15-specific protease that plays a crucial role for maintaining a proper balance of ISG15-conjugated proteins in cells (PubMed:11788588). Regulates protein ISGylation by efficiently cleaving ISG15 conjugates linked via isopeptide bonds. Regulates T-cell activation and T-helper 17 (Th17) cell differentiation by deubiquitinating TAK1, likely to keep TAK1-TAB complexes in steady conditions (PubMed:23825189). In turn, restricts activation of NF- kappa-B, NFAT, and JNK as well as expression of IL2 in T-cells after TCR activation (PubMed:23825189). Acts as a molecular adapter with USP20 to promote innate antiviral response through deubiquitinating STING1 (PubMed:27801882). Involved also in the negative regulation of the inflammatory response triggered by type I interferon (PubMed:28165510, PubMed:27325888). Upon recruitment by STAT2 to the type I interferon receptor subunit IFNAR2 interferes with the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and acts as a negative regulator of the type I interferon signaling pathway (PubMed:28165510). [Isoform 2]: Has enzymatic activity similar to isoform 1 and interferes with type I interferon signaling. Major deISGylation enzyme for nuclear proteins (PubMed:22170061). Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence=; Interacts with STAT2; the interaction is direct (PubMed:28165510, PubMed:31836668, PubMed:32092142). Interacts with IFNAR2; indirectly via STAT2, it negatively regulates the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and inhibits type I interferon signaling (PubMed:28165510). Interacts with STING1. Interacts with USP20. Q9UMW8; P42858: HTT; NbExp=3; IntAct=EBI-356206, EBI-466029; Q9UMW8; P48551: IFNAR2; NbExp=4; IntAct=EBI-356206, EBI-958408; Q9UMW8; P05161: ISG15; NbExp=9; IntAct=EBI-356206, EBI-746466; [Isoform 1]: Cytoplasm [Isoform 2]: Nucleus Cytoplasm Event=Alternative initiation; Named isoforms=2; Name=1; IsoId=Q9UMW8-1; Sequence=Displayed; Name=2; Synonyms=USP18-sf; IsoId=Q9UMW8-2; Sequence=VSP_055236; By type I interferon, predominantly IFN-beta. Pseudo-TORCH syndrome 2 (PTORCH2) [MIM:617397]: An autosomal recessive multisystem disorder characterized by antenatal onset of intracranial hemorrhage, calcification, brain malformations, liver dysfunction, and often thrombocytopenia. Affected individuals tend to have respiratory insufficiency and seizures, and die in infancy. The phenotype resembles the sequelae of intrauterine infection, but there is no evidence of an infectious agent. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 2]: Produced by alternative initiation at a CTG start codon. An IRES Element in the 5' region contributes to expression. Belongs to the peptidase C19 family. cysteine-type endopeptidase activity thiol-dependent ubiquitin-specific protease activity protein binding nucleus cytoplasm cytosol proteolysis ubiquitin-dependent protein catabolic process peptidase activity cysteine-type peptidase activity protein deubiquitination hydrolase activity thiol-dependent ubiquitinyl hydrolase activity regulation of inflammatory response regulation of type I interferon-mediated signaling pathway uc002zny.1 uc002zny.2 uc002zny.3 uc002zny.4 uc002zny.5 
ENST00000215812.9 SEC14L3 ENST00000215812.9 SEC14 like lipid binding 3, transcript variant 1 (from RefSeq NM_174975.5) E7EN74 E9PE57 ENST00000215812.1 ENST00000215812.2 ENST00000215812.3 ENST00000215812.4 ENST00000215812.5 ENST00000215812.6 ENST00000215812.7 ENST00000215812.8 NM_174975 Q495V8 Q495W0 Q495W1 Q9UDX4 S14L3_HUMAN TAP2 uc003ahy.1 uc003ahy.2 uc003ahy.3 uc003ahy.4 uc003ahy.5 The protein encoded by this gene is highly similar to the protein encoded by the Saccharomyces cerevisiae SEC14 gene. The SEC14 protein is a phophatidylinositol transfer protein that is essential for biogenesis of Golgi-derived transport vesicles, and thus is required for the export of yeast secretory proteins from the Golgi complex. The specific function of this protein has not yet been determined. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jul 2012]. ##Evidence-Data-START## Transcript exon combination :: AY240872.1, BC101004.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215812.9/ ENSP00000215812.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9UDX4-1; Sequence=Displayed; Name=2; IsoId=Q9UDX4-2; Sequence=VSP_045554; Name=3; IsoId=Q9UDX4-3; Sequence=VSP_045553; lipid binding extracellular exosome uc003ahy.1 uc003ahy.2 uc003ahy.3 uc003ahy.4 uc003ahy.5 
ENST00000215829.8 SNRPD3 ENST00000215829.8 small nuclear ribonucleoprotein D3 polypeptide, transcript variant 1 (from RefSeq NM_004175.5) B4DJP7 B5BU13 ENST00000215829.1 ENST00000215829.2 ENST00000215829.3 ENST00000215829.4 ENST00000215829.5 ENST00000215829.6 ENST00000215829.7 NM_004175 P43331 P62318 SMD3_HUMAN uc003aam.1 uc003aam.2 uc003aam.3 uc003aam.4 This gene encodes a core component of the spliceosome, which is a nuclear ribonucleoprotein complex that functions in pre-mRNA splicing. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]. Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28502770, PubMed:28781166, PubMed:28076346). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (By similarity). Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:10025403, PubMed:19325628, PubMed:21516107, PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346, PubMed:32494006, PubMed:36797247). Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (PubMed:10025403, PubMed:19325628, PubMed:21516107, PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346). Component of the U1 snRNP (PubMed:19325628, PubMed:25555158). The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1- A and SNRPC/U1-C (PubMed:19325628, PubMed:25555158). Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 (PubMed:26912367). Component of the U7 snRNP complex, or U7 Sm protein core complex, that is composed of the U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not contain SNRPD1 and SNRPD2 (PubMed:11574479). Component of the minor spliceosome, which splices U12-type introns (PubMed:15146077, PubMed:33509932). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly (PubMed:16314521). Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. Interacts (via C-terminus) with SMN1 (via Tudor domain); the interaction is direct (PubMed:12628254, PubMed:10500148, PubMed:11135666). P62318; P54253: ATXN1; NbExp=3; IntAct=EBI-372789, EBI-930964; P62318; P54105: CLNS1A; NbExp=9; IntAct=EBI-372789, EBI-724693; P62318; P84090: ERH; NbExp=3; IntAct=EBI-372789, EBI-711389; P62318; P62310: LSM3; NbExp=5; IntAct=EBI-372789, EBI-348239; P62318; Q9UK45: LSM7; NbExp=3; IntAct=EBI-372789, EBI-348372; P62318; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-372789, EBI-741158; P62318; P14678: SNRPB; NbExp=4; IntAct=EBI-372789, EBI-372458; Cytoplasm, cytosol Nucleus te=SMN- mediated assembly into core snRNPs occurs in the cytosol before SMN- mediated transport to the nucleus to be included in spliceosomes. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P62318-1; Sequence=Displayed; Name=2; IsoId=P62318-2; Sequence=VSP_056478; Methylated on arginine residues by PRMT5 and PRMT7; probable asymmetric dimethylation which is required for assembly and biogenesis of snRNPs. In the autoimmune disease systemic lupus erythematosus, antinuclear antibodies are developed with Sm specificity. Belongs to the snRNP core protein family. commitment complex spliceosomal snRNP assembly mRNA splicing, via spliceosome RNA binding protein binding nucleus nucleoplasm spliceosomal complex U5 snRNP U7 snRNP U1 snRNP U2 snRNP U4 snRNP U12-type spliceosomal complex telomerase holoenzyme complex cytoplasm cytosol termination of RNA polymerase II transcription RNA processing mRNA processing protein methylation histone mRNA metabolic process RNA splicing nuclear body enzyme binding small nuclear ribonucleoprotein complex methylosome pICln-Sm protein complex SMN-Sm protein complex U4/U6 x U5 tri-snRNP complex nuclear import telomerase RNA binding U2-type precatalytic spliceosome U2-type catalytic step 2 spliceosome catalytic step 2 spliceosome histone pre-mRNA DCP binding U7 snRNA binding U1 snRNP binding uc003aam.1 uc003aam.2 uc003aam.3 uc003aam.4 
ENST00000215832.11 MAPK1 ENST00000215832.11 mitogen-activated protein kinase 1, transcript variant 1 (from RefSeq NM_002745.5) ENST00000215832.1 ENST00000215832.10 ENST00000215832.2 ENST00000215832.3 ENST00000215832.4 ENST00000215832.5 ENST00000215832.6 ENST00000215832.7 ENST00000215832.8 ENST00000215832.9 MAPK1 NM_002745 Q1HBJ4 Q1HBJ4_HUMAN hCG_32557 uc002zvn.1 uc002zvn.2 uc002zvn.3 uc002zvn.4 uc002zvn.5 This gene encodes a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. The activation of this kinase requires its phosphorylation by upstream kinases. Upon activation, this kinase translocates to the nucleus of the stimulated cells, where it phosphorylates nuclear targets. One study also suggests that this protein acts as a transcriptional repressor independent of its kinase activity. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Two alternatively spliced transcript variants encoding the same protein, but differing in the UTRs, have been reported for this gene. [provided by RefSeq, Jan 2014]. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Activated by threonine and tyrosine phosphorylation. Cell junction, focal adhesion Membrane, caveola Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. MAPK cascade nucleotide binding activation of MAPK activity phosphotyrosine binding double-stranded DNA binding protein kinase activity protein serine/threonine kinase activity MAP kinase activity MAP kinase kinase activity ATP binding nucleus nucleoplasm cytoplasm mitochondrion cytosol plasma membrane caveola protein phosphorylation cellular response to DNA damage stimulus signal transduction heart development aging transcription factor binding positive regulation of cell proliferation RNA polymerase II carboxy-terminal domain kinase activity response to toxic substance animal organ morphogenesis neural crest cell development postsynaptic density diadenosine tetraphosphate biosynthetic process kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation peptidyl-threonine phosphorylation sensory perception of pain cytosine metabolic process protein kinase binding phosphatase binding regulation of ossification positive regulation of cell migration axon regulation of cellular pH thyroid gland development pseudopodium mitogen-activated protein kinase kinase kinase binding lipopolysaccharide-mediated signaling pathway response to lipopolysaccharide dendrite cytoplasm macromolecular complex mammary gland epithelial cell proliferation response to nicotine intracellular signal transduction positive regulation of protein import into nucleus outer ear morphogenesis identical protein binding perikaryon response to exogenous dsRNA response to estrogen negative regulation of cell differentiation positive regulation of translation positive regulation of transcription, DNA-templated decidualization thymus development T cell receptor signaling pathway B cell receptor signaling pathway Bergmann glial cell differentiation positive regulation of cardiac muscle cell proliferation long-term synaptic potentiation face development lung morphogenesis trachea formation labyrinthine layer blood vessel development cardiac neural crest cell development involved in heart development ERK1 and ERK2 cascade cellular response to organic substance cellular response to tumor necrosis factor cellular response to granulocyte macrophage colony-stimulating factor stimulus uc002zvn.1 uc002zvn.2 uc002zvn.3 uc002zvn.4 uc002zvn.5 
ENST00000215838.8 TCN2 ENST00000215838.8 transcobalamin 2, transcript variant 1 (from RefSeq NM_000355.4) ENST00000215838.1 ENST00000215838.2 ENST00000215838.3 ENST00000215838.4 ENST00000215838.5 ENST00000215838.6 ENST00000215838.7 NM_000355 P20062 Q96FD4 Q9BVI8 Q9UCI5 Q9UCI6 Q9UDM0 TC2 TCO2_HUMAN uc003aip.1 uc003aip.2 uc003aip.3 uc003aip.4 This gene encodes a member of the vitamin B12-binding protein family. This family of proteins, alternatively referred to as R binders, is expressed in various tissues and secretions. This plasma protein binds cobalamin and mediates the transport of cobalamin into cells. This protein and other mammalian cobalamin-binding proteins, such as transcobalamin I and gastric intrisic factor, may have evolved by duplication of a common ancestral gene. Alternative splicing results in multiple transcript variants.[provided by RefSeq, May 2010]. Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells. Interacts with CD320 (via LDL-receptor class A domains). P20062; Q9NPF0: CD320; NbExp=11; IntAct=EBI-2853005, EBI-1054562; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P20062-1; Sequence=Displayed; Name=2; IsoId=P20062-2; Sequence=VSP_043711; Pro/Arg-259 polymorphism affects TCN2 plasma concentration and may interfere in vitamin B(12) cellular availability and homocysteine metabolism (PubMed:11159542). Transcobalamin II deficiency (TCN2 deficiency) [MIM:275350]: Results in various forms of anemia. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the eukaryotic cobalamin transport proteins family. Name=TCN2base; Note=TCN2 mutation db; URL="http://structure.bmc.lu.se/idbase/TCN2base/"; protein binding extracellular region extracellular space endosome ion transport cobalt ion transport cobalamin metabolic process cobalamin transport cobalamin binding lysosomal lumen metal ion binding uc003aip.1 uc003aip.2 uc003aip.3 uc003aip.4 
ENST00000215855.7 CRYBB3 ENST00000215855.7 crystallin beta B3 (from RefSeq NM_004076.5) CRBB3_HUMAN CRYB3 ENST00000215855.1 ENST00000215855.2 ENST00000215855.3 ENST00000215855.4 ENST00000215855.5 ENST00000215855.6 NM_004076 P26998 Q3B7S9 Q3T1B7 Q6ISK6 Q92965 Q9UH09 uc003abo.1 uc003abo.2 uc003abo.3 uc003abo.4 Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B2. Mutations in this gene result in cataract congenital nuclear autosomal recessive type 2. [provided by RefSeq, Feb 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC102021.1, CR456427.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1970526, SAMEA2159080 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215855.7/ ENSP00000215855.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Crystallins are the dominant structural components of the vertebrate eye lens. Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). P26998; P55212: CASP6; NbExp=3; IntAct=EBI-1965681, EBI-718729; P26998; P02489: CRYAA; NbExp=3; IntAct=EBI-1965681, EBI-6875961; P26998; P05813: CRYBA1; NbExp=6; IntAct=EBI-1965681, EBI-7043337; P26998; Q6PKX4: DOK6; NbExp=3; IntAct=EBI-1965681, EBI-2880244; P26998; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-1965681, EBI-356015; P26998; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1965681, EBI-21591415; P26998; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1965681, EBI-5280197; Has a two-domain beta-structure, folded into four very similar Greek key motifs. [Beta-crystallin B3]: Mass=24222; Mass_error=3; Method=Electrospray; Evidence=; Cataract 22, multiple types (CTRCT22) [MIM:609741]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT22 includes nuclear cataract among others. Nuclear cataracts affect the central nucleus of the eye, and are often not highly visually significant. The density of the opacities varies greatly from fine dots to a dense, white and chalk-like, central cataract. The condition is usually bilateral. Nuclear cataracts are often combined with opacified cortical fibers encircling the nuclear opacity, which are referred to as cortical riders. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the beta/gamma-crystallin family. lens development in camera-type eye structural constituent of eye lens protein binding visual perception uc003abo.1 uc003abo.2 uc003abo.3 uc003abo.4 
ENST00000215882.10 SLC25A1 ENST00000215882.10 solute carrier family 25 member 1, transcript variant 1 (from RefSeq NM_005984.5) A8K8E8 ENST00000215882.1 ENST00000215882.2 ENST00000215882.3 ENST00000215882.4 ENST00000215882.5 ENST00000215882.6 ENST00000215882.7 ENST00000215882.8 ENST00000215882.9 NM_005984 P53007 Q9BSK6 SLC20A3 TXTP_HUMAN uc002zoz.1 uc002zoz.2 uc002zoz.3 uc002zoz.4 uc002zoz.5 uc002zoz.6 uc002zoz.7 This gene encodes a member of the mitochondrial carrier subfamily of solute carrier proteins. Members of this family include nuclear-encoded transporters that translocate small metabolites across the mitochondrial membrane. This protein regulates the movement of citrate across the inner membranes of the mitochondria. Mutations in this gene have been associated with combined D-2- and L-2-hydroxyglutaric aciduria. Pseudogenes of this gene have been identified on chromosomes 7, 11, 16, and 19. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2013]. Mitochondrial electroneutral antiporter that exports citrate from the mitochondria into the cytosol in exchange for malate (PubMed:29031613, PubMed:29238895). Also able to mediate the exchange of citrate for isocitrate, phosphoenolpyruvate, cis-aconitate and to a lesser extend cis-aconitate, maleate and succinate (PubMed:29031613). In the cytoplasm citrate is important in the regulation of glycolysis through a feedback mechanism and in the production of acetyl-CoA which is needed for the synthesis of fatty acids, sterols, prostaglandins, dolichol and coenzyme Q (CoQ). Required for proper neuromuscular junction formation (Probable). Reaction=(S)-malate(in) + citrate(out) = (S)-malate(out) + citrate(in); Xref=Rhea:RHEA:72483, ChEBI:CHEBI:15589, ChEBI:CHEBI:16947; Evidence=; Reaction=citrate(out) + D-threo-isocitrate(in) = citrate(in) + D-threo- isocitrate(out); Xref=Rhea:RHEA:72471, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; Evidence=; Reaction=citrate(out) + succinate(in) = citrate(in) + succinate(out); Xref=Rhea:RHEA:28835, ChEBI:CHEBI:16947, ChEBI:CHEBI:30031; Evidence=; Reaction=cis-aconitate(in) + citrate(out) = cis-aconitate(out) + citrate(in); Xref=Rhea:RHEA:72475, ChEBI:CHEBI:16383, ChEBI:CHEBI:16947; Evidence=; Reaction=citrate(out) + trans-aconitate(in) = citrate(in) + trans- aconitate(out); Xref=Rhea:RHEA:72479, ChEBI:CHEBI:15708, ChEBI:CHEBI:16947; Evidence=; Reaction=citrate(out) + phosphoenolpyruvate(in) = citrate(in) + phosphoenolpyruvate(out); Xref=Rhea:RHEA:72487, ChEBI:CHEBI:16947, ChEBI:CHEBI:58702; Evidence=; Reaction=citrate(out) + maleate(in) = citrate(in) + maleate(out); Xref=Rhea:RHEA:72491, ChEBI:CHEBI:16947, ChEBI:CHEBI:30780; Evidence=; Kinetic parameters: KM=7.5 uM for citrate ; Mitochondrion inner membrane ; Multi-pass membrane protein Possesses a short cleavable presequence, which, however, is found to be dispensable both for targeting to mitochondria and insertion into the inner membrane. However, the presequence is required to keep SLC25A1 in a soluble state and thus in an import-competent state. Mature SLC25A1 lacking the presequence is prone to aggregation. Combined D-2- and L-2-hydroxyglutaric aciduria (D2L2AD) [MIM:615182]: An autosomal recessive neurometabolic disorder characterized by neonatal-onset encephalopathy with severe muscular weakness, intractable seizures, respiratory distress, and lack of psychomotor development resulting in early death. Brain imaging shows abnormalities including enlarged ventricles, delayed myelination, and germinal layer cysts. te=The disease is caused by variants affecting the gene represented in this entry. Myasthenic syndrome, congenital, 23, presynaptic (CMS23) [MIM:618197]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features include easy fatigability and muscle weakness. CMS23 inheritance is autosomal recessive. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the mitochondrial carrier (TC 2.A.29) family. nucleus mitochondrion mitochondrial inner membrane gluconeogenesis mitochondrial citrate transport citrate transmembrane transporter activity tricarboxylic acid transmembrane transporter activity membrane integral component of membrane transmembrane transporter activity fatty-acyl-CoA biosynthetic process transmembrane transport extracellular exosome citrate secondary active transmembrane transporter activity uc002zoz.1 uc002zoz.2 uc002zoz.3 uc002zoz.4 uc002zoz.5 uc002zoz.6 uc002zoz.7 
ENST00000215885.4 PLA2G3 ENST00000215885.4 phospholipase A2 group III (from RefSeq NM_015715.5) ENST00000215885.1 ENST00000215885.2 ENST00000215885.3 NM_015715 O95768 PA2G3_HUMAN PLA2G3 Q9NZ20 uc003aka.1 uc003aka.2 uc003aka.3 uc003aka.4 uc003aka.5 This gene encodes a protein that belongs to the secreted phospholipase A2 family, whose members include the bee venom enzyme. The encoded enzyme functions in lipid metabolism and catalyzes the calcium-dependent hydrolysis of the sn-2 acyl bond of phospholipids to release arachidonic acid and lysophospholipids. This enzyme acts as a negative regulator of ciliogenesis, and may play a role in cancer development by stimulating tumor cell growth and angiogenesis. This gene is associated with oxidative stress, and polymorphisms in this gene are linked to risk for Alzheimer's disease. [provided by RefSeq, Apr 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC025316.1, AF220490.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2144333, SAMEA2145893 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215885.4/ ENSP00000215885.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids without apparent head group selectivity (PubMed:12522102, PubMed:18801741, PubMed:15863501, PubMed:28947740). Contributes to phospholipid remodeling of low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (PubMed:18801741). May act in an autocrine and paracrine manner (PubMed:23624557). Secreted by immature mast cells, acts on nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2 (PGD2), which in turn promotes mast cell maturation and degranulation via PTGDR (PubMed:23624557). Secreted by epididymal epithelium, acts on immature sperm cells within the duct, modulating the degree of unsaturation of the fatty acyl components of phosphatidylcholines required for acrosome assembly and sperm cell motility. Facilitates the replacement of fatty acyl chains in phosphatidylcholines in sperm membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6 PUFAs to generate oxygenated lipid mediators in the male reproductive tract (By similarity). At pericentrosomal preciliary compartment, negatively regulates ciliogenesis likely by regulating endocytotic recycling of ciliary membrane protein (PubMed:20393563). Coupled to cyclooxygenase pathway provides arachidonate to generate prostaglandin E2 (PGE2), a potent immunomodulatory lipid in inflammation and tumorigenesis (PubMed:12522102, PubMed:15863501). At colonic epithelial barrier, preferentially hydrolyzes phospholipids having arachidonate and docosahexaenoate at sn-2 position, contributing to the generation of oxygenated metabolites involved in colonic stem cell homeostasis (PubMed:28947740). Releases C16:0 and C18:0 lysophosphatidylcholine subclasses from neuron plasma membranes and promotes neurite outgrowth and neuron survival (PubMed:17868035). Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence=; Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn- glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence=; Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence=; Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1- hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence= Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence=; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Note=Binds 1 Ca(2+) ion. ; Arachidonic acid release is markedly increased by glypican, a glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan. Secreted Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Recycling endosome Note=Localized at pericentrosomal preciliary compartment. Expressed in kidney, heart, liver, and skeletal muscle. Also present in placenta and peripheral blood leukocytes. Not detected in colon, thymus, spleen and small intestine. In lung, expressed in bronchial epithelial cells and alveolar macrophages, but scarcely detected in alveolar epithelium, arterial walls and interstitial fibroblasts (at protein level). In joints of osteoarthritis and rheumatoid arthritis, expressed in endothelial cells (at protein level). In normal heart, detected in some vessels. In myocardial tissues with acute infarction, expressed in vascular endothelial cells adjacent to cardiomyocytes and those in lesions with granulation. Expression in cardiomyocytes is scarce (at protein level). In uterus, breast and colon cancers, detected in tumor cells and neighboring microvascular endothelium, but not in normal glandular tissues (at protein level) (PubMed:15863501). Expressed in dermal resting mast cells (at protein level) and pulmonary mast cells (PubMed:23624557). Expressed in neuronal fibers (at protein level) (PubMed:17868035). Highly expressed in dorsal root ganglia neurons (at protein level) (PubMed:17868035). Expressed in Purkinje cells in cerebellum (at protein level) (PubMed:17868035). In stomach is preferentially expressed in neuronal fibers and in microvascular endothelium (PubMed:17868035). Sparsely expressed in normal aorta (at protein level). Highly expressed in macrophages and smooth muscle cells in aorta with atheroma (PubMed:18801741). By IL1B/interleukin-1 beta and TNF in microvascular endothelial cells (at protein level). The phospholipase A2-like domain represents the fully processed form after N- and C-termini are cleaved off. It is the secreted mature form found in biological fluids. N-glycosylation does not affect the catalytic activity, but is required for proper secretion. A nonglycosylated form is observed in several cell types. In several cell types, the N- and C-termini are cleaved off. Belongs to the phospholipase A2 family. Sequence=AAD15617.1; Type=Erroneous gene model prediction; Evidence=; acrosome assembly phospholipase A2 activity extracellular region extracellular space cytoplasm centriole cytoskeleton plasma membrane lipid metabolic process phospholipid metabolic process sperm axoneme assembly membrane lipid catabolic process hydrolase activity lipoxygenase pathway cell projection organization phosphatidylglycerol acyl-chain remodeling phosphatidylcholine acyl-chain remodeling phosphatidylethanolamine acyl-chain remodeling mast cell granule mast cell degranulation phosphatidylcholine metabolic process metal ion binding calcium-dependent phospholipase A2 activity cell development arachidonic acid secretion cilium assembly uc003aka.1 uc003aka.2 uc003aka.3 uc003aka.4 uc003aka.5 
ENST00000215886.6 LGALS2 ENST00000215886.6 galectin 2 (from RefSeq NM_006498.3) ENST00000215886.1 ENST00000215886.2 ENST00000215886.3 ENST00000215886.4 ENST00000215886.5 LEG2_HUMAN NM_006498 P05162 Q6FGY4 uc003ata.1 uc003ata.2 uc003ata.3 uc003ata.4 uc003ata.5 The protein encoded by this gene is a soluble beta-galactoside binding lectin. The encoded protein is found as a homodimer and can bind to lymphotoxin-alpha. A single nucleotide polymorphism in an intron of this gene can alter the transcriptional level of the protein, with a resultant increased risk of myocardial infarction. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BP303532.1, ERR279840.1904.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215886.6/ ENSP00000215886.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## This protein binds beta-galactoside. Its physiological function is not yet known. Homodimer. P05162; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-7181544, EBI-741158; P05162; O00560: SDCBP; NbExp=9; IntAct=EBI-7181544, EBI-727004; P05162; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-7181544, EBI-742426; Name=Functional Glycomics Gateway - Glycan Binding; Note=Galectin-2; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_280"; protein binding galactoside binding carbohydrate binding uc003ata.1 uc003ata.2 uc003ata.3 uc003ata.4 uc003ata.5 
ENST00000215904.7 PDXP ENST00000215904.7 pyridoxal phosphatase (from RefSeq NM_020315.5) CIN ENST00000215904.1 ENST00000215904.2 ENST00000215904.3 ENST00000215904.4 ENST00000215904.5 ENST00000215904.6 NM_020315 PDXP PLP PLPP PLPP_HUMAN Q96GD0 Q9UGY2 uc003atm.1 uc003atm.2 uc003atm.3 Pyridoxal 5-prime-phosphate (PLP) is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis. The preferred degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP (Jang et al., 2003 [PubMed 14522954]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC064922.1, SRR1163655.298190.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215904.7/ ENSP00000215904.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism (PubMed:14522954, PubMed:8132548). Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine (PubMed:15580268). Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal; Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310, ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534; Evidence=; Reaction=H2O + pyridoxine 5'-phosphate = phosphate + pyridoxine; Xref=Rhea:RHEA:25112, ChEBI:CHEBI:15377, ChEBI:CHEBI:16709, ChEBI:CHEBI:43474, ChEBI:CHEBI:58589; EC=3.1.3.74; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25113; Evidence=; Reaction=phosphate + pyridoxamine = H2O + pyridoxamine 5'-phosphate; Xref=Rhea:RHEA:25135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57761, ChEBI:CHEBI:58451; EC=3.1.3.74; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25137; Evidence=; Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Divalent metal ions. Mg(2+) is the most effective. ; Inhibited by NaF, Zn(2+), Ca(2+), Mn(2+) and EDTA. Kinetic parameters: KM=2.5 uM for pyridoxal 5'-phosphate (at pH 7.4 and 37 degrees Celsius) ; KM=43.4 uM for pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees Celsius) ; KM=80.6 uM for pyridoxamine 5'-phosphate (at pH 7.4 and 37 degrees Celsius) ; Vmax=1.42 umol/min/mg enzyme with pyridoxal 5'-phosphate as substrate ; Vmax=1.17 umol/min/mg enzyme with pyridoxine 5'-phosphate as substrate ; Vmax=0.42 umol/min/mg enzyme with pyridoxamine 5'-phosphate as substrate ; Note=kcat is 1.52 sec(-1) for the dephosphorylation of pyridoxal 5'- phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 1.25 sec(-1) for the dephosphorylation of pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 0.45 sec(-1) for the dephosphorylation of pyridoxamine 5'-phosphate (at pH 7.4 and 37 degrees Celsius). ; Homodimer. Q96GD0; P29066: Arrb1; Xeno; NbExp=2; IntAct=EBI-4303060, EBI-4303019; Cytoplasm, cytosol Cytoplasm, cytoskeleton Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side Cell projection, lamellipodium membrane ; Peripheral membrane protein ; Cytoplasmic side Cell membrane ; Peripheral membrane protein ; Cytoplasmic side Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody. Event=Alternative splicing, Alternative initiation; Named isoforms=3; Name=CIN ; IsoId=Q96GD0-1; Sequence=Displayed; Name=Long BGIN ; IsoId=Q6ZT62-1; Sequence=External; Name=Short BGIN ; IsoId=Q6ZT62-2; Sequence=External; Ubiquitously expressed (at protein level) (PubMed:23223568). Highly expressed in all the regions of central nerve system except the spinal cord. Also expressed at high level in liver and testis. In fetus, it is weakly expressed in all organs except brain (PubMed:14522954, PubMed:15580268). Belongs to the HAD-like hydrolase superfamily. magnesium ion binding phosphoserine phosphatase activity phosphoprotein phosphatase activity protein binding cytoplasm cytosol cytoskeleton plasma membrane cell-cell junction protein dephosphorylation regulation of mitotic nuclear division membrane dephosphorylation hydrolase activity phosphatase activity positive regulation of actin filament depolymerization heat shock protein binding actin rod assembly lamellipodium membrane pyridoxal phosphate catabolic process regulation of cytokinesis ruffle membrane pyridoxal phosphatase activity protein homodimerization activity cell projection metal ion binding cellular response to ATP actin cytoskeleton lamellipodium midbody cleavage furrow contractile ring uc003atm.1 uc003atm.2 uc003atm.3 
ENST00000215906.6 ASPHD2 ENST00000215906.6 aspartate beta-hydroxylase domain containing 2 (from RefSeq NM_020437.5) ASPH2_HUMAN B2RCH3 ENST00000215906.1 ENST00000215906.2 ENST00000215906.3 ENST00000215906.4 ENST00000215906.5 NM_020437 Q6ICH7 Q7L0W3 Q9NSN3 uc003acg.1 uc003acg.2 uc003acg.3 uc003acg.4 May function as 2-oxoglutarate-dependent dioxygenase. Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence=; Membrane ; Single-pass type II membrane protein Belongs to the aspartyl/asparaginyl beta-hydroxylase family. Sequence=AAH36753.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAG37570.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; membrane integral component of membrane oxidoreductase activity peptidyl-amino acid modification metal ion binding dioxygenase activity oxidation-reduction process uc003acg.1 uc003acg.2 uc003acg.3 uc003acg.4 
ENST00000215909.10 LGALS1 ENST00000215909.10 galectin 1 (from RefSeq NM_002305.4) B2R5E8 ENST00000215909.1 ENST00000215909.2 ENST00000215909.3 ENST00000215909.4 ENST00000215909.5 ENST00000215909.6 ENST00000215909.7 ENST00000215909.8 ENST00000215909.9 LEG1_HUMAN LGALS1 NM_002305 P09382 Q9UDK5 uc003atn.1 uc003atn.2 uc003atn.3 uc003atn.4 uc003atn.5 The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. This gene product may act as an autocrine negative growth factor that regulates cell proliferation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC020675.1, GQ891519.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000215909.10/ ENSP00000215909.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N- acetyllactosamine). Interacts with SUSD2. Interacts with cargo receptor TMED10; the interaction mediates the translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and thereby secretion (PubMed:32272059). P09382; Q13740: ALCAM; NbExp=3; IntAct=EBI-1048875, EBI-1188108; P09382; P02649: APOE; NbExp=3; IntAct=EBI-1048875, EBI-1222467; P09382; P27797: CALR; NbExp=3; IntAct=EBI-1048875, EBI-1049597; P09382; P30203: CD6; NbExp=2; IntAct=EBI-1048875, EBI-2873748; P09382; P36957: DLST; NbExp=3; IntAct=EBI-1048875, EBI-351007; P09382; P35968: KDR; NbExp=3; IntAct=EBI-1048875, EBI-1005487; P09382; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-1048875, EBI-1055945; P09382; P16284: PECAM1; NbExp=4; IntAct=EBI-1048875, EBI-716404; P09382; P08575: PTPRC; NbExp=2; IntAct=EBI-1048875, EBI-1341; Secreted, extracellular space, extracellular matrix Cytoplasm Secreted Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum- Golgi intermediate compartment) followed by vesicle entry and secretion. Expressed in placenta, maternal decidua and fetal membranes. Within placenta, expressed in trophoblasts, stromal cells, villous endothelium, syncytiotrophoblast apical membrane and villous stroma. Within fetal membranes, expressed in amnion, chorioamniotic mesenchyma and chorion (at protein level). Expressed in cardiac, smooth, and skeletal muscle, neurons, thymus, kidney and hematopoietic cells. Name=Functional Glycomics Gateway - Glycan Binding; Note=Galectin-1; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00116"; plasma cell differentiation RNA binding protein binding extracellular region extracellular space intracellular nucleus cytoplasm endoplasmic reticulum lumen cytosol apoptotic process cell surface negative regulation of cell-substrate adhesion negative regulation of neuron projection development carbohydrate binding lactose binding T cell costimulation positive regulation of erythrocyte aggregation response to isolation stress response to drug protein homodimerization activity regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling laminin binding post-translational protein modification cellular protein metabolic process myoblast differentiation positive regulation of viral entry into host cell response to axon injury extracellular exosome cellular response to glucose stimulus cellular response to organic cyclic compound positive regulation of dendritic cell differentiation uc003atn.1 uc003atn.2 uc003atn.3 uc003atn.4 uc003atn.5 
ENST00000215912.10 PIK3IP1 ENST00000215912.10 phosphoinositide-3-kinase interacting protein 1, transcript variant 1 (from RefSeq NM_052880.5) B4DRR9 D1MEI0 ENST00000215912.1 ENST00000215912.2 ENST00000215912.3 ENST00000215912.4 ENST00000215912.5 ENST00000215912.6 ENST00000215912.7 ENST00000215912.8 ENST00000215912.9 HGFL NM_052880 O00318 P3IP1_HUMAN Q49A94 Q86YW2 Q8NCJ9 Q96FE7 uc003akm.1 uc003akm.2 uc003akm.3 uc003akm.4 uc003akm.5 Negative regulator of hepatic phosphatidylinositol 3-kinase (PI3K) activity. Q96FE7; P43364: MAGEA11; NbExp=3; IntAct=EBI-10285708, EBI-739552; Q96FE7; O43934: MFSD11; NbExp=3; IntAct=EBI-10285708, EBI-17633886; Q96FE7; P78382: SLC35A1; NbExp=3; IntAct=EBI-10285708, EBI-12870360; Q96FE7; A2RU14: TMEM218; NbExp=3; IntAct=EBI-10285708, EBI-10173151; Q96FE7; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10285708, EBI-741480; Q96FE7; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-10285708, EBI-10173939; Q96FE7; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10285708, EBI-947187; Q96FE7; O75841: UPK1B; NbExp=3; IntAct=EBI-10285708, EBI-12237619; Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=5; Name=1; Synonyms=HGFL(L); IsoId=Q96FE7-1; Sequence=Displayed; Name=2; Synonyms=HGFL(S); IsoId=Q96FE7-2; Sequence=VSP_023639, VSP_023640; Name=3; IsoId=Q96FE7-3; Sequence=VSP_023638; Name=4; IsoId=Q96FE7-4; Sequence=VSP_043368; Name=5; Synonyms=PIK3IP1-v1; IsoId=Q96FE7-5; Sequence=VSP_053370; N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan heterogeneity at Asn-66: dHex1Hex5HexNAc4 (major) and dHex1Hex6HexNAc5 (minor). serine-type endopeptidase activity protein binding plasma membrane proteolysis negative regulation of phosphatidylinositol 3-kinase signaling membrane integral component of membrane phosphatidylinositol 3-kinase catalytic subunit binding negative regulation of phosphatidylinositol 3-kinase activity uc003akm.1 uc003akm.2 uc003akm.3 uc003akm.4 uc003akm.5 
ENST00000215917.11 SRRD ENST00000215917.11 SRR1 domain containing (from RefSeq NM_001013694.3) ENST00000215917.1 ENST00000215917.10 ENST00000215917.2 ENST00000215917.3 ENST00000215917.4 ENST00000215917.5 ENST00000215917.6 ENST00000215917.7 ENST00000215917.8 ENST00000215917.9 NM_001013694 Q6NXP8 Q9UH36 SRR1L SRR1L_HUMAN uc010gve.1 uc010gve.2 uc010gve.3 uc010gve.4 Plays a role in the regulation of heme biosynthesis and in the regulation of the expression of core clock genes. Cytoplasm Note=Also found in intracellular organelles. Up-regulated by hemin and 5-aminolevulinic acid. Belongs to the SRR1 family. nucleus cytoplasm heme biosynthetic process microtubule-based process circadian rhythm regulation of circadian rhythm rhythmic process regulation of heme biosynthetic process uc010gve.1 uc010gve.2 uc010gve.3 uc010gve.4 
ENST00000215941.9 ANKRD54 ENST00000215941.9 ankyrin repeat domain 54, transcript variant 4 (from RefSeq NR_146280.1) ANR54_HUMAN ENST00000215941.1 ENST00000215941.2 ENST00000215941.3 ENST00000215941.4 ENST00000215941.5 ENST00000215941.6 ENST00000215941.7 ENST00000215941.8 LIAR NR_146280 Q6NXT1 Q6ZSB1 Q9UGV1 uc003auc.1 uc003auc.2 uc003auc.3 uc003auc.4 uc003auc.5 Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. Interacts (via ankyrin repeat region) with LYN (via SH3- domain) in an activation-independent status of LYN. Forms a multiprotein complex with LYN and HCLS1. Interacts with TSN2, VAV1, DBNL and LASP1. Q6NXT1; O75386: TULP3; NbExp=8; IntAct=EBI-10102770, EBI-5357290; Nucleus Cytoplasm Midbody Note=Shuttles between nucleus and cytoplasm during the cell cycle. EPO stimulation induces nuclear accumulation (By similarity). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6NXT1-1; Sequence=Displayed; Name=2; IsoId=Q6NXT1-2; Sequence=VSP_022770, VSP_022771; protein binding nucleus cytoplasm nucleocytoplasmic transport protein kinase regulator activity midbody macromolecular complex binding positive regulation of erythrocyte differentiation regulation of protein kinase activity regulation of intracellular signal transduction uc003auc.1 uc003auc.2 uc003auc.3 uc003auc.4 uc003auc.5 
ENST00000215957.10 MICALL1 ENST00000215957.10 MICAL like 1, transcript variant 3 (from RefSeq NM_033386.4) ENST00000215957.1 ENST00000215957.2 ENST00000215957.3 ENST00000215957.4 ENST00000215957.5 ENST00000215957.6 ENST00000215957.7 ENST00000215957.8 ENST00000215957.9 KIAA1668 MILK1_HUMAN MIRAB13 NM_033386 Q5TI16 Q7RTP5 Q8N3F8 Q8N3N8 Q9BVL9 Q9BY92 Q9UH43 Q9UH44 Q9UH45 uc003aui.1 uc003aui.2 uc003aui.3 uc003aui.4 Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth. Homooligomer (Probable). Interacts (via NPF1 motif) with EHD1 (via EH domain); the interaction is direct and probably recruits EHD1 to membranes. Interacts with EHD3 (via EH domain). Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits MICALL1 to membranes. Interacts with ACAP2; the interaction is indirect through RAB35. Interacts with RAB8A (GTP-bound form); regulates RAB8A association with recycling endosomes. Interacts with RAB13 (GTP-bound form). Interacts with ARF6 (GTP-bound form). Interacts with PACSIN2 (via the SH3 domain). Interacts with DPYSL2. Q8N3F8; Q9H4M9: EHD1; NbExp=12; IntAct=EBI-1056885, EBI-490691; Q8N3F8; Q9NZN3: EHD3; NbExp=5; IntAct=EBI-1056885, EBI-2870749; Q8N3F8; Q15286: RAB35; NbExp=2; IntAct=EBI-1056885, EBI-722275; Q8N3F8; Q5ZXN6: ankX; Xeno; NbExp=2; IntAct=EBI-1056885, EBI-26359852; Q8N3F8; O02675: DPYSL2; Xeno; NbExp=2; IntAct=EBI-1056885, EBI-8783505; Recycling endosome membrane; Peripheral membrane protein. Late endosome membrane. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6. Probably exists in a closed and an opened conformation due to interaction of the C-terminal RAB-binding domain (RBD), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, with the N-terminal calponin-homology (CH) domain. The conformational change is regulated by RAB13 and may modulate MICALL1 interactions with functional partners. Sequence=CAD39036.1; Type=Frameshift; Evidence=; protein binding endosome late endosome microtubule organizing center protein targeting to membrane endocytosis receptor-mediated endocytosis endosome membrane protein transport membrane Rab GTPase binding extrinsic component of membrane actin cytoskeleton organization neuron projection development late endosome membrane filamentous actin endocytic recycling slow endocytic recycling protein localization to endosome identical protein binding cadherin binding metal ion binding recycling endosome membrane phosphatidic acid binding plasma membrane tubulation cellular response to nerve growth factor stimulus retrograde transport, endosome to plasma membrane early endosome trans-Golgi network uc003aui.1 uc003aui.2 uc003aui.3 uc003aui.4 
ENST00000215980.10 CENPM ENST00000215980.10 centromere protein M, transcript variant 1 (from RefSeq NM_024053.5) A7LM22 B1AHQ9 C22orf18 CENPM_HUMAN ENST00000215980.1 ENST00000215980.2 ENST00000215980.3 ENST00000215980.4 ENST00000215980.5 ENST00000215980.6 ENST00000215980.7 ENST00000215980.8 ENST00000215980.9 ICEN39 NM_024053 PANE1 Q6I9W3 Q9NSP4 uc003bbn.1 uc003bbn.2 uc003bbn.3 uc003bbn.4 uc003bbn.5 The protein encoded by this gene is an inner protein of the kinetochore, the multi-protein complex that binds spindle microtubules to regulate chromosome segregation during cell division. It belongs to the constitutive centromere-associated network protein group, whose members interact with outer kinetochore proteins and help to maintain centromere identity at each cell division cycle. The protein is structurally related to GTPases but cannot bind guanosine triphosphate. A point mutation that affects interaction with another constitutive centromere-associated network protein, CENP-I, impairs kinetochore assembly and chromosome alignment, suggesting that it is required for kinetochore formation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2015]. Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Nucleus. Cytoplasm. Chromosome, centromere, kinetochore. Note=Nuclear in non-confluent cells and cytoplasmic in confluent or dividing cells (By similarity). Localizes in the kinetochore domain of centromeres. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9NSP4-1; Sequence=Displayed; Name=2; IsoId=Q9NSP4-2; Sequence=VSP_010259, VSP_010260; Name=3; IsoId=Q9NSP4-3; Sequence=VSP_017726, VSP_017725; Name=4; IsoId=Q9NSP4-4; Sequence=VSP_046189; Isoform 3 is highly expressed in spleen, and intermediately in heart, prostate and ovary. Isoform 3 is highly expressed in resting CD19 B-cells and B-lineage chronic lymphocytic leukemia (B-CLL) cells and weakly expressed in activated B-cells. Isoform 1 is selectively expressed in activated CD19 cells and weakly in resting CD19 B-cells. [Isoform 2]: Due to intron retention. chromosome, centromeric region kinetochore condensed chromosome kinetochore nucleus nucleoplasm chromosome cytoplasm cytosol CENP-A containing nucleosome assembly uc003bbn.1 uc003bbn.2 uc003bbn.3 uc003bbn.4 uc003bbn.5 
ENST00000216014.9 KDELR3 ENST00000216014.9 KDEL endoplasmic reticulum protein retention receptor 3, transcript variant 1 (from RefSeq NM_006855.4) A8K7T7 B8ZZ26 ENST00000216014.1 ENST00000216014.2 ENST00000216014.3 ENST00000216014.4 ENST00000216014.5 ENST00000216014.6 ENST00000216014.7 ENST00000216014.8 ERD23 ERD23_HUMAN NM_006855 O43731 O95557 Q4V750 Q4V767 Q53FP4 Q53GK1 uc003avv.1 uc003avv.2 uc003avv.3 uc003avv.4 uc003avv.5 This gene encodes a member of the KDEL endoplasmic reticulum protein retention receptor family. Retention of resident soluble proteins in the lumen of the endoplasmic reticulum (ER) is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu (HDEL) in S. cerevisiae. This process is mediated by a receptor that recognizes, and binds the tetrapeptide-containing protein, and returns it to the ER. In yeast, the sorting receptor encoded by a single gene, ERD2, is a seven-transmembrane protein. Unlike yeast, several human homologs of the ERD2 gene, constituting the KDEL receptor gene family, have been described. KDELR3 was the third member of the family to be identified. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]. Receptor for the C-terminal sequence motif K-D-E-L that is present on endoplasmic reticulum resident proteins and that mediates their recycling from the Golgi back to the endoplasmic reticulum. O43731-2; O60636: TSPAN2; NbExp=3; IntAct=EBI-18157502, EBI-3914288; Endoplasmic reticulum membrane ; Multi-pass membrane protein Golgi apparatus membrane ; Multi-pass membrane protein Cytoplasmic vesicle, COPI-coated vesicle membrane ; Multi-pass membrane protein Note=Localized in the Golgi in the absence of bound proteins with the sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum together with cargo proteins containing the sequence motif K-D-E-L. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43731-1; Sequence=Displayed; Name=2; IsoId=O43731-2; Sequence=VSP_022856; Binds the C-terminal sequence motif K-D-E-L in a hydrophilic cavity between the transmembrane domains. This triggers a conformation change that exposes a Lys-rich patch on the cytosolic surface of the protein (By similarity). This patch mediates recycling from the Golgi to the endoplasmic reticulum, probably via COPI vesicles (By similarity). Belongs to the ERD2 family. Golgi membrane KDEL sequence binding endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus cis-Golgi network protein retention in ER lumen ER to Golgi vesicle-mediated transport retrograde vesicle-mediated transport, Golgi to ER protein transport membrane integral component of membrane vesicle-mediated transport transport vesicle COPI-coated vesicle membrane cytoplasmic vesicle IRE1-mediated unfolded protein response ER retention sequence binding uc003avv.1 uc003avv.2 uc003avv.3 uc003avv.4 uc003avv.5 
ENST00000216024.7 DMC1 ENST00000216024.7 DNA meiotic recombinase 1, transcript variant 1 (from RefSeq NM_007068.4) A8K9A2 B4DMW6 DMC1H DMC1_HUMAN ENST00000216024.1 ENST00000216024.2 ENST00000216024.3 ENST00000216024.4 ENST00000216024.5 ENST00000216024.6 LIM15 NM_007068 Q08AI1 Q14565 Q99498 Q9UH11 uc003avz.1 uc003avz.2 uc003avz.3 uc003avz.4 This gene encodes a member of the superfamily of recombinases (also called DNA strand-exchange proteins). Recombinases are important for repairing double-strand DNA breaks during mitosis and meiosis. This protein, which is evolutionarily conserved, is reported to be essential for meiotic homologous recombination and may thus play an important role in generating diversity of genetic information. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2013]. Participates in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks. Double stacked ring-shaped homooctamer (PubMed:15125839). Interacts with BRCA2 (PubMed:20729832). Interacts with the MND1-PSMC3IP heterodimer (By similarity). Interacts with RAD51AP1; the interaction is direct and stimulates DMC1-mediated homologous recombination (PubMed:21307306, PubMed:21903585). Q14565; P51587: BRCA2; NbExp=12; IntAct=EBI-930865, EBI-79792; Q14565; Q14565: DMC1; NbExp=3; IntAct=EBI-930865, EBI-930865; Q14565; Q9H8Y8: GORASP2; NbExp=8; IntAct=EBI-930865, EBI-739467; Q14565; Q8N5Z5: KCTD17; NbExp=4; IntAct=EBI-930865, EBI-743960; Q14565; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-930865, EBI-739832; Q14565; Q9GZT8: NIF3L1; NbExp=9; IntAct=EBI-930865, EBI-740897; Q14565; O75928-2: PIAS2; NbExp=3; IntAct=EBI-930865, EBI-348567; Q14565; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-930865, EBI-79165; Q14565; P25788: PSMA3; NbExp=7; IntAct=EBI-930865, EBI-348380; Q14565; Q96B01-2: RAD51AP1; NbExp=3; IntAct=EBI-930865, EBI-1178743; Q14565; O00560: SDCBP; NbExp=7; IntAct=EBI-930865, EBI-727004; Q14565; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-930865, EBI-742426; Q14565; P36406: TRIM23; NbExp=3; IntAct=EBI-930865, EBI-740098; Q14565; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-930865, EBI-10180829; Nucleus Chromosome Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q14565-1; Sequence=Displayed; Name=2; IsoId=Q14565-2; Sequence=VSP_055357; Belongs to the RecA family. DMC1 subfamily. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/dmc1/"; recombinase activity nucleotide binding DNA recombinase assembly chromosome, telomeric region condensed nuclear chromosome ovarian follicle development oocyte maturation DNA binding double-stranded DNA binding single-stranded DNA binding protein binding ATP binding nucleus chromosome DNA metabolic process DNA repair mitotic recombination cell cycle synapsis reciprocal meiotic recombination male meiosis I gamete generation spermatogenesis spermatid development female gamete generation DNA-dependent ATPase activity strand invasion meiotic cell cycle uc003avz.1 uc003avz.2 uc003avz.3 uc003avz.4 
ENST00000216027.8 HSCB ENST00000216027.8 HscB mitochondrial iron-sulfur cluster cochaperone, transcript variant 1 (from RefSeq NM_172002.5) DNAJC20 ENST00000216027.1 ENST00000216027.2 ENST00000216027.3 ENST00000216027.4 ENST00000216027.5 ENST00000216027.6 ENST00000216027.7 HSC20 HSC20_HUMAN HSCB NM_172002 Q8IWL3 Q9BWS7 uc003aea.1 uc003aea.2 uc003aea.3 uc003aea.4 uc003aea.5 This gene encodes a DnaJ-type co-chaperone and member of the heat shock cognate B (HscB) family of proteins. The encoded protein plays a role in the synthesis of iron-sulfur clusters, protein cofactors that are involved in the redox reactions of mitochondrial electron transport and other processes. Cells in which this gene is knocked down exhibit reduced activity of iron-sulfur cluster-dependent enzymes including succinate dehydrogenase and aconitase. The encoded protein may stimulate the ATPase activity of the mitochondrial stress-70 protein. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2015]. [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria (PubMed:20668094). Required for incorporation of iron- sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate dehydrogenase that is involved in complex II of the mitochondrial electron transport chain (PubMed:26749241). Recruited to SDHB by interaction with SDHAF1 which first binds SDHB and then recruits the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241). Plays an essential role in hematopoiesis (By similarity). [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Acts as a co-chaperone in iron-sulfur cluster assembly in the cytoplasm (PubMed:29309586). Also mediates complex formation between components of the cytosolic iron-sulfur biogenesis pathway and the CIA targeting complex composed of CIAO1, DIPK1B/FAM69B and MMS19 by binding directly to the scaffold protein ISCU and to CIAO1 (PubMed:29309586). This facilitates iron-sulfur cluster insertion into a number of cytoplasmic and nuclear proteins including POLD1, ELP3, DPYD and PPAT (PubMed:29309586). Cofactor biosynthesis; iron-sulfur cluster biosynthesis. [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Interacts with ISCU and HSPA9 to form an iron-sulfur transfer complex (PubMed:20668094). Interacts with SDHAF1 (via the first LYR motif); the interaction recruits the iron-sulfur transfer complex composed of HSC20, HSPA9 and ISCU and mediates the incorporation of iron-sulfur clusters into SDHB which also interacts with HSC20 (PubMed:26749241). Interacts with the cytoplasmic form of ISCU and with CIA complex member CIAO1 (via LYR motif) (PubMed:29309586). [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Homodimer (PubMed:29309586). Interacts with ISCU (cytoplasmic form); this interaction stabilzes the (Fe-S) clusters on ISCU (PubMed:29309586). Interacts with the CIA complex member CIAO1 (via LYR motif) (PubMed:29309586). Q8IWL3; Q6RW13: AGTRAP; NbExp=4; IntAct=EBI-1805738, EBI-741181; Q8IWL3; P07814: EPRS1; NbExp=4; IntAct=EBI-1805738, EBI-355315; Q8IWL3; P13804: ETFA; NbExp=3; IntAct=EBI-1805738, EBI-1052886; Q8IWL3; Q86SX6: GLRX5; NbExp=3; IntAct=EBI-1805738, EBI-1049910; Q8IWL3; P42694: HELZ; NbExp=4; IntAct=EBI-1805738, EBI-1210654; Q8IWL3; Q8IWL3: HSCB; NbExp=3; IntAct=EBI-1805738, EBI-1805738; Q8IWL3; P38646: HSPA9; NbExp=14; IntAct=EBI-1805738, EBI-354932; Q8IWL3; Q5U5X0: LYRM7; NbExp=7; IntAct=EBI-1805738, EBI-13943106; Q8IWL3; P19404: NDUFV2; NbExp=6; IntAct=EBI-1805738, EBI-713665; Q8IWL3; P16083: NQO2; NbExp=4; IntAct=EBI-1805738, EBI-358466; Q8IWL3; A6NFY7: SDHAF1; NbExp=5; IntAct=EBI-1805738, EBI-12011488; Q8IWL3; P21912: SDHB; NbExp=22; IntAct=EBI-1805738, EBI-1056481; Q8IWL3; Q96I99: SUCLG2; NbExp=4; IntAct=EBI-1805738, EBI-2511878; [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Cytoplasm [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Mitochondrion Expressed in lung, brain, stomach, spleen, ovary, testis, liver, muscle and heart. Anemia, sideroblastic, 5 (SIDBA5) [MIM:619523]: A form of sideroblastic anemia, a bone marrow disorder defined by the presence of pathologic iron deposits in erythroblast mitochondria. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus. SIDBA5 inheritance is autosomal recessive. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the HscB family. ATPase activator activity molecular_function protein binding nucleus cytoplasm mitochondrion cytosol iron-sulfur cluster assembly positive regulation of ATPase activity identical protein binding [2Fe-2S] cluster assembly metal ion binding chaperone binding protein oligomerization protein maturation by iron-sulfur cluster transfer uc003aea.1 uc003aea.2 uc003aea.3 uc003aea.4 uc003aea.5 
ENST00000216029.8 CBY1 ENST00000216029.8 chibby 1, beta catenin antagonist, transcript variant 1 (from RefSeq NM_015373.4) ARB1 B2R4S2 C22orf2 CBY CBY1_HUMAN ENST00000216029.1 ENST00000216029.2 ENST00000216029.3 ENST00000216029.4 ENST00000216029.5 ENST00000216029.6 ENST00000216029.7 HRIHFB2025 NM_015373 PGEA1 Q66GT6 Q9UIK9 Q9Y3M2 uc003awc.1 uc003awc.2 uc003awc.3 uc003awc.4 uc003awc.5 uc003awc.6 Beta-catenin is a transcriptional activator and oncoprotein involved in the development of several cancers. The protein encoded by this gene interacts directly with the C-terminal region of beta-catenin, inhibiting oncogenic beta-catenin-mediated transcriptional activation by competing with transcription factors for binding to beta-catenin. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta- catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation. Homodimer. Interacts with polycystin-2/PKD2 and GM130. Interacts with the C-terminal region of CTNNB1 (PubMed:12712206, PubMed:16424001). Interacts (C-terminus) with TCIM (C-terminus), TCIM competes with CTNNB1 for the interaction with CBY1 (PubMed:16424001). Interacts with FAM92A; this interaction facilitates targeting of FAM92A to cilium basal body (PubMed:27528616, PubMed:30395363). Interacts with CIBAR2 (PubMed:27528616). Q9Y3M2; Q96M91: CFAP53; NbExp=4; IntAct=EBI-947308, EBI-742422; Q9Y3M2; A1XBS5: CIBAR1; NbExp=3; IntAct=EBI-947308, EBI-2349888; Q9Y3M2; A1XBS5-3: CIBAR1; NbExp=3; IntAct=EBI-947308, EBI-12348777; Q9Y3M2; Q8IYY4: DZIP1L; NbExp=3; IntAct=EBI-947308, EBI-10264440; Q9Y3M2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-947308, EBI-744099; Q9Y3M2; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-947308, EBI-7225287; Q9Y3M2; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-947308, EBI-739467; Q9Y3M2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-947308, EBI-739832; Q9Y3M2; Q15311: RALBP1; NbExp=4; IntAct=EBI-947308, EBI-749285; Q9Y3M2; A6NK89: RASSF10; NbExp=3; IntAct=EBI-947308, EBI-6912267; Q9Y3M2; Q5GJ75: TNFAIP8L3; NbExp=3; IntAct=EBI-947308, EBI-14222571; Q9Y3M2; Q99816: TSG101; NbExp=3; IntAct=EBI-947308, EBI-346882; Q9Y3M2; Q6PF05-3: TTC23L; NbExp=3; IntAct=EBI-947308, EBI-10182647; Q9Y3M2; P62258: YWHAE; NbExp=3; IntAct=EBI-947308, EBI-356498; Q9Y3M2; P63104: YWHAZ; NbExp=3; IntAct=EBI-947308, EBI-347088; Nucleus speckle Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Golgi apparatus. Golgi apparatus, trans- Golgi network Widely expressed. Expressed at higher levels in heart, skeletal muscle, kidney and placenta. Also found in brain, lung, liver and testis. Significantly down-regulated in thyroid and metastatic uterine tumors. 'Chibby' is Japanese for 'small'; the gene was so named for the RNAi phenotype seen in flies. Belongs to the chibby family. protein binding nucleus nucleoplasm cytoplasm Golgi apparatus trans-Golgi network centriole cytosol cytoskeleton beta-catenin binding protein localization nuclear speck cell projection organization cell differentiation negative regulation of Wnt signaling pathway ciliary basal body identical protein binding protein homodimerization activity cell projection fat cell differentiation negative regulation of transcription, DNA-templated protein homotetramerization cardiac muscle cell differentiation cilium assembly ciliary transition zone assembly uc003awc.1 uc003awc.2 uc003awc.3 uc003awc.4 uc003awc.5 uc003awc.6 
ENST00000216034.6 TOMM22 ENST00000216034.6 translocase of outer mitochondrial membrane 22 (from RefSeq NM_020243.5) ENST00000216034.1 ENST00000216034.2 ENST00000216034.3 ENST00000216034.4 ENST00000216034.5 NM_020243 Q9NS69 TOM22 TOM22_HUMAN uc003awe.1 uc003awe.2 uc003awe.3 uc003awe.4 uc003awe.5 The protein encoded by this gene is an integral membrane protein of the mitochondrial outer membrane. The encoded protein interacts with TOMM20 and TOMM40, and forms a complex with several other proteins to import cytosolic preproteins into the mitochondrion. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.833620.1, SRR3476690.976671.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000216034.6/ ENSP00000216034.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore (PubMed:10982837). Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases (By similarity). Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70) (PubMed:18331822). Interacts with TOMM40. Interacts with PPP2R2B (By similarity). Q9NS69; Q13520: AQP6; NbExp=3; IntAct=EBI-1047508, EBI-13059134; Q9NS69; P42858: HTT; NbExp=6; IntAct=EBI-1047508, EBI-466029; Q9NS69; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1047508, EBI-21591415; Q9NS69; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1047508, EBI-2623095; Q9NS69; Q9P0U1: TOMM7; NbExp=2; IntAct=EBI-1047508, EBI-1180558; Q9NS69; P0DOE7: M; Xeno; NbExp=2; IntAct=EBI-1047508, EBI-10042882; Mitochondrion outer membrane ; Single-pass membrane protein Ubiquitous. Requires the transmembrane domain (TMD), a short segment (the import sequence) in the cytoplasmic domain localizing separately from the TMD and the C-tail signal in the C-terminal domain for efficient targeting and integration into the TOM complex (By similarity). The N- terminal domain (residues 1-62) is important for binding to the unfolded mature imported proteins. Residues (49-71) of the cytoplasmic domain interacts with TOMM20 while the C-terminal segment (residues 63- 82) binds presequence of preproteins. Belongs to the Tom22 family. protein binding mitochondrion mitochondrial outer membrane mitochondrial outer membrane translocase complex protein targeting to mitochondrion intracellular protein transport protein transmembrane transporter activity protein transport membrane integral component of membrane macroautophagy positive regulation of apoptotic process protein import into mitochondrial outer membrane protein insertion into mitochondrial membrane protein transmembrane transport uc003awe.1 uc003awe.2 uc003awe.3 uc003awe.4 uc003awe.5 
ENST00000216036.9 RSPH14 ENST00000216036.9 radial spoke head 14 homolog (from RefSeq NM_014433.3) ENST00000216036.1 ENST00000216036.2 ENST00000216036.3 ENST00000216036.4 ENST00000216036.5 ENST00000216036.6 ENST00000216036.7 ENST00000216036.8 NM_014433 Q9UHP6 RSP14_HUMAN RSPH14 RTDR1 uc002zwt.1 uc002zwt.2 uc002zwt.3 uc002zwt.4 uc002zwt.5 This gene encodes a protein with no known function but with slight similarity to a yeast vacuolar protein. The gene is located in a region deleted in pediatric rhabdoid tumors of the brain, kidney and soft tissues, but mutations in this gene have not been associated with the disease. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AF133587.1, BC008986.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158188 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216036.9/ ENSP00000216036.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Functions as part of axonemal radial spoke complexes that play an important part in the motility of sperm and cilia. Component of the axonemal radial spoke complex 1 (RS1), at least composed of spoke head proteins RSPH1, RSPH3, RSPH9 and the cilia-specific component RSPH4A or sperm-specific component RSPH6A, spoke stalk proteins RSPH14, DNAJB13, DYDC1, ROPN1L and NME5, and the anchor protein IQUB. Q9UHP6; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-748350, EBI-11096309; Q9UHP6; Q9UPQ3: AGAP1; NbExp=3; IntAct=EBI-748350, EBI-7159788; Q9UHP6; Q60I27: ALS2CL; NbExp=3; IntAct=EBI-748350, EBI-12078276; Q9UHP6; Q9BXS5: AP1M1; NbExp=6; IntAct=EBI-748350, EBI-541426; Q9UHP6; Q96CW1: AP2M1; NbExp=6; IntAct=EBI-748350, EBI-297683; Q9UHP6; Q9Y2T2: AP3M1; NbExp=11; IntAct=EBI-748350, EBI-2371151; Q9UHP6; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-748350, EBI-953896; Q9UHP6; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-748350, EBI-10171570; Q9UHP6; Q01850: CDR2; NbExp=3; IntAct=EBI-748350, EBI-1181367; Q9UHP6; Q8N137: CNTROB; NbExp=3; IntAct=EBI-748350, EBI-947360; Q9UHP6; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-748350, EBI-3866319; Q9UHP6; Q13643: FHL3; NbExp=3; IntAct=EBI-748350, EBI-741101; Q9UHP6; Q06547: GABPB1; NbExp=3; IntAct=EBI-748350, EBI-618165; Q9UHP6; Q08379: GOLGA2; NbExp=6; IntAct=EBI-748350, EBI-618309; Q9UHP6; P14923: JUP; NbExp=3; IntAct=EBI-748350, EBI-702484; Q9UHP6; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-748350, EBI-749265; Q9UHP6; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-748350, EBI-2125614; Q9UHP6; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-748350, EBI-14069005; Q9UHP6; P19012: KRT15; NbExp=3; IntAct=EBI-748350, EBI-739566; Q9UHP6; Q15323: KRT31; NbExp=6; IntAct=EBI-748350, EBI-948001; Q9UHP6; Q6A162: KRT40; NbExp=3; IntAct=EBI-748350, EBI-10171697; Q9UHP6; O95678: KRT75; NbExp=4; IntAct=EBI-748350, EBI-2949715; Q9UHP6; Q01546: KRT76; NbExp=3; IntAct=EBI-748350, EBI-2952745; Q9UHP6; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-748350, EBI-1216080; Q9UHP6; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-748350, EBI-743811; Q9UHP6; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-748350, EBI-14066006; Q9UHP6; O15160: POLR1C; NbExp=3; IntAct=EBI-748350, EBI-1055079; Q9UHP6; Q04864: REL; NbExp=3; IntAct=EBI-748350, EBI-307352; Q9UHP6; Q9UNE2: RPH3AL; NbExp=3; IntAct=EBI-748350, EBI-2855824; Q9UHP6; Q86UC2: RSPH3; NbExp=3; IntAct=EBI-748350, EBI-6873025; Q9UHP6; Q8IYM1: SEPTIN12; NbExp=3; IntAct=EBI-748350, EBI-2585067; Q9UHP6; P15884: TCF4; NbExp=3; IntAct=EBI-748350, EBI-533224; Q9UHP6; P15884-3: TCF4; NbExp=3; IntAct=EBI-748350, EBI-13636688; Q9UHP6; Q12933: TRAF2; NbExp=3; IntAct=EBI-748350, EBI-355744; Q9UHP6; P14373: TRIM27; NbExp=3; IntAct=EBI-748350, EBI-719493; Q9UHP6; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-748350, EBI-9867283; Q9UHP6; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-748350, EBI-749955; Q9UHP6; Q86WT6-2: TRIM69; NbExp=5; IntAct=EBI-748350, EBI-11525489; Q9UHP6; Q9C029: TRIM7; NbExp=3; IntAct=EBI-748350, EBI-2813981; Q9UHP6; Q9Y2B5: VPS9D1; NbExp=3; IntAct=EBI-748350, EBI-9031083; Q9UHP6; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-748350, EBI-17269964; Q9UHP6; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-748350, EBI-9977294; Cytoplasm, cytoskeleton, flagellum axoneme Expressed in adult cerebellum, spinal cord, spleen, skeletal muscle and some/5 out of 9 rhabdoid tumors. Detected in fetal brain, lung, liver and kidney. Belongs to the flagellar radial spoke RSP14 family. molecular_function protein binding cellular_component biological_process uc002zwt.1 uc002zwt.2 uc002zwt.3 uc002zwt.4 uc002zwt.5 
ENST00000216038.6 RTCB ENST00000216038.6 RNA 2',3'-cyclic phosphate and 5'-OH ligase (from RefSeq NM_014306.5) B2R6A8 C22orf28 ENST00000216038.1 ENST00000216038.2 ENST00000216038.3 ENST00000216038.4 ENST00000216038.5 HSPC117 NM_014306 Q6IAI0 Q9BWL4 Q9NTH1 Q9P037 Q9P0J3 Q9Y3I0 RTCB RTCB_HUMAN uc003amm.1 uc003amm.2 uc003amm.3 uc003amm.4 Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs. Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho- ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP; Xref=Rhea:RHEA:68076, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8; Evidence= Reaction=a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl- ribonucleotide-RNA + diphosphate + GMP + H(+); Xref=Rhea:RHEA:68080, Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83064, ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8; Evidence= Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence= Note=Binds 2 manganese ions per subunit. Protein archease stimulates the activity of the tRNA ligase complex with high efficiency in the presence of GTP. Catalytic component of the tRNA-splicing ligase complex. Q9Y3I0; Q9UKG1: APPL1; NbExp=3; IntAct=EBI-2107208, EBI-741243; Q9Y3I0; Q9Y224: RTRAF; NbExp=4; IntAct=EBI-2107208, EBI-1104547; Q9Y3I0; Q8IWT0: ZBTB8OS; NbExp=2; IntAct=EBI-2107208, EBI-2808825; Nucleus Cytoplasm Note=Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low. Ligation probably proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RTCB reacts with GTP to form a covalent RTCB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP. Belongs to the RtcB family. Sequence=AAF29081.1; Type=Frameshift; Evidence=; Sequence=AAF67477.1; Type=Frameshift; Evidence=; nucleotide binding tRNA exon ligation utilizing 2',3' cyclic phosphate of 5'-exon as source of linkage phosphate in utero embryonic development placenta development RNA binding RNA ligase (ATP) activity protein binding ATP binding nucleus nuclear envelope nucleoplasm cytoplasm endoplasmic reticulum membrane cytosol tRNA splicing, via endonucleolytic cleavage and ligation RNA processing tRNA processing RNA ligase activity ligase activity vinculin binding intracellular membrane-bounded organelle metal ion binding tRNA-splicing ligase complex uc003amm.1 uc003amm.2 uc003amm.3 uc003amm.4 
ENST00000216044.10 GTPBP1 ENST00000216044.10 GTP binding protein 1 (from RefSeq NM_004286.5) ENST00000216044.1 ENST00000216044.2 ENST00000216044.3 ENST00000216044.4 ENST00000216044.5 ENST00000216044.6 ENST00000216044.7 ENST00000216044.8 ENST00000216044.9 GTPB1_HUMAN NM_004286 O00178 Q6IC67 uc003awg.1 uc003awg.2 uc003awg.3 uc003awg.4 uc003awg.5 This gene is upregulated by interferon-gamma and encodes a protein that is a member of the AGP11/GTPBP1 family of GTP-binding proteins. A structurally similar protein has been found in mouse, where disruption of the gene for that protein had no observable phenotype. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.199191.1, SRR1660807.264517.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216044.10/ ENSP00000216044.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46, HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with AANAT mRNA, but does not bind mRNA by itself (By similarity). O00178; Q9BPX7: C7orf25; NbExp=3; IntAct=EBI-4403245, EBI-718586; Cytoplasm Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. GTPBP1 subfamily. Sequence=AAB51273.1; Type=Erroneous initiation; Evidence=; Sequence=CAG30387.1; Type=Erroneous initiation; Evidence=; nucleotide binding cytoplasmic exosome (RNase complex) RNA binding translation elongation factor activity GTPase activity GTP binding cytoplasm cytosol translational elongation immune response signal transduction membrane GTP metabolic process positive regulation of mRNA catabolic process uc003awg.1 uc003awg.2 uc003awg.3 uc003awg.4 uc003awg.5 
ENST00000216068.9 DNAL4 ENST00000216068.9 dynein axonemal light chain 4 (from RefSeq NM_005740.3) DNAL4_HUMAN ENST00000216068.1 ENST00000216068.2 ENST00000216068.3 ENST00000216068.4 ENST00000216068.5 ENST00000216068.6 ENST00000216068.7 ENST00000216068.8 NM_005740 O96015 Q6FGB2 Q6FGD0 uc003awj.1 uc003awj.2 uc003awj.3 uc003awj.4 uc003awj.5 This gene encodes an axonemal dynein light chain which functions as a component of the outer dynein arms complex. This complex acts as the molecular motor that provides the force to move cilia in an ATP-dependent manner. The encoded protein is expressed in tissues with motile cilia or flagella and may be involved in the movement of sperm flagella. [provided by RefSeq, Dec 2014]. ##Evidence-Data-START## Transcript exon combination :: AL035366.1, SRR3476690.696320.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA2142586, SAMEA2145245 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216068.9/ ENSP00000216068.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity (By similarity). Consists of at least two heavy chains and a number of intermediate and light chains. O96015; Q13557: CAMK2D; NbExp=4; IntAct=EBI-742362, EBI-351018; O96015; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-742362, EBI-741528; O96015; O96015: DNAL4; NbExp=3; IntAct=EBI-742362, EBI-742362; O96015; P63167: DYNLL1; NbExp=3; IntAct=EBI-742362, EBI-349105; O96015; Q96FJ2: DYNLL2; NbExp=6; IntAct=EBI-742362, EBI-742371; O96015; Q5TD97: FHL5; NbExp=10; IntAct=EBI-742362, EBI-750641; O96015; O95837: GNA14; NbExp=3; IntAct=EBI-742362, EBI-7951023; O96015; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-742362, EBI-11953334; O96015; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-742362, EBI-11958364; O96015; Q8NCF5-2: NFATC2IP; NbExp=6; IntAct=EBI-742362, EBI-12305293; O96015; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-742362, EBI-945833; O96015; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742362, EBI-741158; O96015; Q9BRQ3: NUDT22; NbExp=7; IntAct=EBI-742362, EBI-10297093; O96015; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-742362, EBI-2130429; Cytoplasm, cytoskeleton, cilium axoneme Mirror movements 3 (MRMV3) [MIM:616059]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the dynein light chain family. motor activity microtubule motor activity protein binding cytoplasm cytoskeleton microtubule plasma membrane cilium microtubule-based process microtubule-based movement dynein complex cell projection dynein intermediate chain binding dynein light intermediate chain binding positive regulation of ATP-dependent microtubule motor activity, plus-end-directed ATP-dependent microtubule motor activity, plus-end-directed uc003awj.1 uc003awj.2 uc003awj.3 uc003awj.4 uc003awj.5 
ENST00000216071.5 C22orf31 ENST00000216071.5 chromosome 22 open reading frame 31, transcript variant 1 (from RefSeq NM_015370.2) A0AV97 CV031_HUMAN ENST00000216071.1 ENST00000216071.2 ENST00000216071.3 ENST00000216071.4 NM_015370 O95567 uc003aej.1 uc003aej.2 uc003aej.3 uc003aej.1 uc003aej.2 uc003aej.3 
ENST00000216075.11 MIOX ENST00000216075.11 myo-inositol oxygenase (from RefSeq NM_017584.6) ALDRL6 ENST00000216075.1 ENST00000216075.10 ENST00000216075.2 ENST00000216075.3 ENST00000216075.4 ENST00000216075.5 ENST00000216075.6 ENST00000216075.7 ENST00000216075.8 ENST00000216075.9 KSP32 MIOX_HUMAN NM_017584 Q05DJ6 Q5S8C9 Q9BZZ1 Q9UGB7 Q9UHB8 RSOR uc003bll.1 uc003bll.2 uc003bll.3 Reaction=myo-inositol + O2 = D-glucuronate + H(+) + H2O; Xref=Rhea:RHEA:23696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17268, ChEBI:CHEBI:58720; EC=1.13.99.1; Evidence=; Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence=; Note=Binds 2 iron ions per subunit. ; Polyol metabolism; myo-inositol degradation into D- glucuronate; D-glucuronate from myo-inositol: step 1/1. Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UGB7-1; Sequence=Displayed; Name=2; IsoId=Q9UGB7-2; Sequence=VSP_041667, VSP_041668; Kidney specific. Belongs to the myo-inositol oxygenase family. aldo-keto reductase (NADP) activity iron ion binding cytoplasm cytosol ferric iron binding inclusion body oxidoreductase activity oxidoreductase activity, acting on NAD(P)H oxidoreductase activity, acting on single donors with incorporation of molecular oxygen inositol catabolic process inositol phosphate metabolic process metal ion binding inositol oxygenase activity oxidation-reduction process uc003bll.1 uc003bll.2 uc003bll.3 
ENST00000216085.12 RHBDD3 ENST00000216085.12 rhomboid domain containing 3, transcript variant 1 (from RefSeq NM_012265.3) C22orf3 ENST00000216085.1 ENST00000216085.10 ENST00000216085.11 ENST00000216085.2 ENST00000216085.3 ENST00000216085.4 ENST00000216085.5 ENST00000216085.6 ENST00000216085.7 ENST00000216085.8 ENST00000216085.9 NM_012265 Q6I9X3 Q9UGQ7 Q9Y3P4 RHBD3_HUMAN uc003aeq.1 uc003aeq.2 uc003aeq.3 Membrane ; Multi-pass membrane protein MAPK cascade liver development regulation of acute inflammatory response serine-type endopeptidase activity proteolysis response to xenobiotic stimulus membrane integral component of membrane negative regulation of natural killer cell activation positive regulation of protein catabolic process regulation of protein secretion uc003aeq.1 uc003aeq.2 uc003aeq.3 
ENST00000216099.13 APOBEC3D ENST00000216099.13 apolipoprotein B mRNA editing enzyme catalytic subunit 3D, transcript variant 1 (from RefSeq NM_152426.4) ABC3D_HUMAN APOBEC3D APOBEC3DE ENST00000216099.1 ENST00000216099.10 ENST00000216099.11 ENST00000216099.12 ENST00000216099.2 ENST00000216099.3 ENST00000216099.4 ENST00000216099.5 ENST00000216099.6 ENST00000216099.7 ENST00000216099.8 ENST00000216099.9 NM_152426 Q5JZ91 Q7Z2N2 Q7Z2N5 Q7Z2N6 Q96AK3 uc003awt.1 uc003awt.2 uc003awt.3 uc003awt.4 uc003awt.5 uc003awt.6 This gene is a member of the cytidine deaminase gene family. It is one of a group of related genes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1 and inhibit retroviruses, such as HIV, by deaminating cytosine residues in nascent retroviral cDNA. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC017022.1, SRR1803613.102281.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216099.13/ ENSP00000216099.7 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase- dependent and -independent mechanisms (PubMed:16920826, PubMed:20062055, PubMed:21835787). Exhibits antiviral activity against HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single- strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA (PubMed:16920826). The resultant detrimental levels of mutations in the proviral genome, along with a deamination- independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Inhibits also the mobility of LTR and non-LTR retrotransposons (PubMed:27428332). (Microbial infection) Enhances hepatitis B virus/HBV replication by excluding restriction factors APOBEC3F and APOBEC3G from HBV capsids. Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'- deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948, Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452, ChEBI:CHEBI:133902; EC=3.5.4.38; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; (Microbial infection) Antiviral activity is neutralized by the HIV-1 virion infectivity factor (Vif), that prevents its incorporation into progeny virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome. Can form homo- and heterodimers with APOBEC3F and APOBEC3G (PubMed:16920826, PubMed:27289067). Interacts with L1RE1; this interaction inhibits LINE-1 retrotransposition (PubMed:27428332). (Microbial infection) Interacts with HIV-1 Vif (PubMed:16920826, PubMed:23001005). This interaction triggers APOBEC3D polyubiquitylation and degradation by the 26S proteasome (PubMed:16920826). Cytoplasm toplasm, P-body. Expressed in lymphoid organs. Also detected in non- lymphoid tissues including lung. The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA- dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase activity and substrate sequence specificity. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Belongs to the cytidine and deoxycytidylate deaminase family. P-body immune system process RNA binding catalytic activity cytidine deaminase activity nucleus cytoplasm zinc ion binding cytidine deamination negative regulation of transposition cytidine to uridine editing hydrolase activity innate immune response negative regulation of single stranded viral RNA replication via double stranded DNA intermediate metal ion binding deoxycytidine deaminase activity defense response to virus DNA cytosine deamination DNA demethylation uc003awt.1 uc003awt.2 uc003awt.3 uc003awt.4 uc003awt.5 uc003awt.6 
ENST00000216101.7 RASL10A ENST00000216101.7 RAS like family 10 member A (from RefSeq NM_006477.5) ENST00000216101.1 ENST00000216101.2 ENST00000216101.3 ENST00000216101.4 ENST00000216101.5 ENST00000216101.6 NM_006477 Q49AU5 Q6PI03 Q92737 RRP22 RSLAA_HUMAN uc003aff.1 uc003aff.2 uc003aff.3 uc003aff.4 uc003aff.5 Potent inhibitor of cellular proliferation. Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence=; Cell membrane ; Lipid-anchor ; Cytoplasmic side Nucleus, nucleolus Note=May cycle in and out of the nucleolus in a GTP-dependent manner. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q92737-1; Sequence=Displayed; Name=2; Synonyms=B; IsoId=Q92737-2; Sequence=VSP_013372; Expression appears to be strictly limited to the central nervous system. Isoprenylation is essential for nucleolar localization, and the proliferation-inhibiting activity of RASL10A. Belongs to the small GTPase superfamily. Ras family. nucleotide binding GTPase activity GTP binding nucleus nucleolus plasma membrane signal transduction small GTPase mediated signal transduction membrane uc003aff.1 uc003aff.2 uc003aff.3 uc003aff.4 uc003aff.5 
ENST00000216106.6 HMGXB4 ENST00000216106.6 HMG-box containing 4, transcript variant 3 (from RefSeq NM_001362972.2) ENST00000216106.1 ENST00000216106.2 ENST00000216106.3 ENST00000216106.4 ENST00000216106.5 HMG2L1 HMGBCG HMGX4_HUMAN NM_001362972 O75672 O75673 Q9UGU5 Q9UMT5 uc003anl.1 uc003anl.2 uc003anl.3 uc003anl.4 uc003anl.5 High mobility group (HMG) proteins are nonhistone chromosomal proteins. See HMG2 (MIM 163906) for additional information on HMG proteins.[supplied by OMIM, Nov 2010]. Negatively regulates Wnt/beta-catenin signaling during development. Q9UGU5; Q02040: AKAP17A; NbExp=3; IntAct=EBI-7261162, EBI-1042725; Q9UGU5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-7261162, EBI-10175300; Q9UGU5; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-7261162, EBI-744099; Q9UGU5; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-7261162, EBI-7261162; Q9UGU5; Q9C086: INO80B; NbExp=3; IntAct=EBI-7261162, EBI-715611; Q9UGU5; Q96PV6: LENG8; NbExp=3; IntAct=EBI-7261162, EBI-739546; Q9UGU5; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-7261162, EBI-3920396; Q9UGU5; O75928-2: PIAS2; NbExp=3; IntAct=EBI-7261162, EBI-348567; Q9UGU5; Q96MF2: STAC3; NbExp=3; IntAct=EBI-7261162, EBI-745680; Q9UGU5; Q96SI9: STRBP; NbExp=3; IntAct=EBI-7261162, EBI-740355; Q9UGU5; Q96A09: TENT5B; NbExp=3; IntAct=EBI-7261162, EBI-752030; Q9UGU5; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-7261162, EBI-947459; Q9UGU5; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-7261162, EBI-10180829; Q9UGU5; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-7261162, EBI-607755; Q9UGU5; Q8TBK6: ZCCHC10; NbExp=5; IntAct=EBI-7261162, EBI-597063; Nucleus DNA binding nucleus endosome to lysosome transport Wnt signaling pathway NURF complex negative regulation of Wnt signaling pathway uc003anl.1 uc003anl.2 uc003anl.3 uc003anl.4 uc003anl.5 
ENST00000216115.3 BIK ENST00000216115.3 BCL2 interacting killer (from RefSeq NM_001197.5) BIK_HUMAN ENST00000216115.1 ENST00000216115.2 NBK NM_001197 Q13323 Q16582 Q6FH93 uc003bdk.1 uc003bdk.2 uc003bdk.3 uc003bdk.4 The protein encoded by this gene shares a critical BH3 domain with other death-promoting proteins, such as BID, BAK, BAD and BAX, that is required for its pro-apoptotic activity, and for interaction with anti-apoptotic members of the BCL2 family, and viral survival-promoting proteins. Since the activity of this protein is suppressed in the presence of survival-promoting proteins, it is suggested as a likely target for anti-apoptotic proteins. [provided by RefSeq, Sep 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.81286.1, SRR1163657.62147.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216115.3/ ENSP00000216115.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Accelerates programmed cell death. Association to the apoptosis repressors Bcl-X(L), BHRF1, Bcl-2 or its adenovirus homolog E1B 19k protein suppresses this death-promoting activity. Does not interact with BAX. Interacts with RHBDL4/RHBDD1 (PubMed:18953687). Interacts with BCL2L10/BCL-B (PubMed:23235460, PubMed:23563182). Q13323; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-700794, EBI-11277970; Q13323; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-700794, EBI-10827839; Q13323; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-700794, EBI-11957045; Q13323; Q9BVK2: ALG8; NbExp=3; IntAct=EBI-700794, EBI-3921603; Q13323; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-700794, EBI-12109402; Q13323; P05090: APOD; NbExp=3; IntAct=EBI-700794, EBI-715495; Q13323; P10415: BCL2; NbExp=6; IntAct=EBI-700794, EBI-77694; Q13323; Q16548: BCL2A1; NbExp=10; IntAct=EBI-700794, EBI-1003550; Q13323; A0A0S2Z3D2: BCL2L1; NbExp=3; IntAct=EBI-700794, EBI-16431449; Q13323; Q07817: BCL2L1; NbExp=12; IntAct=EBI-700794, EBI-78035; Q13323; Q07817-1: BCL2L1; NbExp=4; IntAct=EBI-700794, EBI-287195; Q13323; Q9HD36: BCL2L10; NbExp=8; IntAct=EBI-700794, EBI-2126349; Q13323; Q92843: BCL2L2; NbExp=22; IntAct=EBI-700794, EBI-707714; Q13323; O95393: BMP10; NbExp=3; IntAct=EBI-700794, EBI-3922513; Q13323; Q12983: BNIP3; NbExp=3; IntAct=EBI-700794, EBI-749464; Q13323; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-700794, EBI-12244618; Q13323; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-700794, EBI-8648738; Q13323; O14523: C2CD2L; NbExp=3; IntAct=EBI-700794, EBI-12822627; Q13323; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-700794, EBI-12003442; Q13323; Q06432: CACNG1; NbExp=3; IntAct=EBI-700794, EBI-9686780; Q13323; P19397: CD53; NbExp=3; IntAct=EBI-700794, EBI-6657396; Q13323; P21854: CD72; NbExp=3; IntAct=EBI-700794, EBI-307924; Q13323; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-700794, EBI-12256978; Q13323; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-700794, EBI-11522780; Q13323; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-700794, EBI-2807956; Q13323; O95406: CNIH1; NbExp=3; IntAct=EBI-700794, EBI-12172273; Q13323; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-700794, EBI-12208021; Q13323; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-700794, EBI-12019274; Q13323; P49447: CYB561; NbExp=3; IntAct=EBI-700794, EBI-8646596; Q13323; O43169: CYB5B; NbExp=3; IntAct=EBI-700794, EBI-1058710; Q13323; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-700794, EBI-18535450; Q13323; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-700794, EBI-781551; Q13323; Q2M3D2: EXOC3L2; NbExp=3; IntAct=EBI-700794, EBI-14890134; Q13323; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-700794, EBI-18304435; Q13323; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-700794, EBI-12118888; Q13323; Q92520: FAM3C; NbExp=3; IntAct=EBI-700794, EBI-2876774; Q13323; Q969F0: FATE1; NbExp=8; IntAct=EBI-700794, EBI-743099; Q13323; P12314: FCGR1A; NbExp=3; IntAct=EBI-700794, EBI-2869867; Q13323; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-700794, EBI-11991950; Q13323; Q8TED1: GPX8; NbExp=3; IntAct=EBI-700794, EBI-11721746; Q13323; Q14416: GRM2; NbExp=3; IntAct=EBI-700794, EBI-10232876; Q13323; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-700794, EBI-8503746; Q13323; O15554: KCNN4; NbExp=3; IntAct=EBI-700794, EBI-2924473; Q13323; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-700794, EBI-2341610; Q13323; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-700794, EBI-12070086; Q13323; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-700794, EBI-2863634; Q13323; Q8N912: NRAC; NbExp=3; IntAct=EBI-700794, EBI-12051377; Q13323; Q8IXM6: NRM; NbExp=3; IntAct=EBI-700794, EBI-10262547; Q13323; Q96AL5: PBX3; NbExp=3; IntAct=EBI-700794, EBI-741171; Q13323; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-700794, EBI-12092917; Q13323; O00264: PGRMC1; NbExp=3; IntAct=EBI-700794, EBI-1045534; Q13323; P26678: PLN; NbExp=3; IntAct=EBI-700794, EBI-692836; Q13323; P60201-2: PLP1; NbExp=3; IntAct=EBI-700794, EBI-12188331; Q13323; Q04941: PLP2; NbExp=3; IntAct=EBI-700794, EBI-608347; Q13323; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-700794, EBI-10485931; Q13323; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-700794, EBI-7545592; Q13323; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-700794, EBI-8636004; Q13323; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-700794, EBI-4403649; Q13323; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-700794, EBI-8652744; Q13323; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-700794, EBI-9679163; Q13323; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-700794, EBI-10329948; Q13323; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-700794, EBI-749270; Q13323; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-700794, EBI-10262251; Q13323; Q96G79: SLC35A4; NbExp=3; IntAct=EBI-700794, EBI-12363689; Q13323; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-700794, EBI-13389236; Q13323; O43826: SLC37A4; NbExp=3; IntAct=EBI-700794, EBI-6269684; Q13323; Q92504: SLC39A7; NbExp=3; IntAct=EBI-700794, EBI-1051105; Q13323; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-700794, EBI-12188413; Q13323; P0DN84: STRIT1; NbExp=3; IntAct=EBI-700794, EBI-12200293; Q13323; Q9UNK0: STX8; NbExp=3; IntAct=EBI-700794, EBI-727240; Q13323; Q969X1: TMBIM1; NbExp=3; IntAct=EBI-700794, EBI-2820569; Q13323; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-700794, EBI-12845616; Q13323; P17152: TMEM11; NbExp=3; IntAct=EBI-700794, EBI-723946; Q13323; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-700794, EBI-727322; Q13323; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-700794, EBI-8638294; Q13323; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-700794, EBI-2339195; Q13323; Q8N511: TMEM199; NbExp=3; IntAct=EBI-700794, EBI-10265825; Q13323; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-700794, EBI-347385; Q13323; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-700794, EBI-12195227; Q13323; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-700794, EBI-12887458; Q13323; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-700794, EBI-11956809; Q13323; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-700794, EBI-2852148; Q13323; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-700794, EBI-11742770; Q13323; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-700794, EBI-2548832; Q13323; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-700794, EBI-12111910; Q13323; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-700794, EBI-12195249; Q13323; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-700794, EBI-10243654; Q13323; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-700794, EBI-11988865; Q13323; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-700794, EBI-2819725; Q13323; Q15836: VAMP3; NbExp=3; IntAct=EBI-700794, EBI-722343; Q13323; O95183: VAMP5; NbExp=3; IntAct=EBI-700794, EBI-10191195; Q13323; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-700794, EBI-6256462; Q13323; O95159: ZFPL1; NbExp=3; IntAct=EBI-700794, EBI-718439; Endomembrane system; Single-pass membrane protein. Mitochondrion membrane ; Single-pass membrane protein Note=Around the nuclear envelope, and in cytoplasmic membranes. Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti- apoptotic members of the Bcl-2 family. Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome- dependent mechanism. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/bik/"; protein binding mitochondrion apoptotic process male gonad development apoptotic mitochondrial changes endomembrane system membrane integral component of membrane positive regulation of protein complex assembly mitochondrial membrane regulation of apoptotic process positive regulation of release of cytochrome c from mitochondria uc003bdk.1 uc003bdk.2 uc003bdk.3 uc003bdk.4 
ENST00000216117.9 HMOX1 ENST00000216117.9 heme oxygenase 1 (from RefSeq NM_002133.3) ENST00000216117.1 ENST00000216117.2 ENST00000216117.3 ENST00000216117.4 ENST00000216117.5 ENST00000216117.6 ENST00000216117.7 ENST00000216117.8 HMOX1 NM_002133 Q6FH11 Q6FH11_HUMAN hCG_40033 uc003ant.1 uc003ant.2 uc003ant.3 uc003ant.4 Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1099521.1, X06985.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216117.9/ ENSP00000216117.8 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765; Evidence=; Endoplasmic reticulum membrane ; Single-pass type IV membrane protein ; Cytoplasmic side Belongs to the heme oxygenase family. angiogenesis response to hypoxia heme oxygenase (decyclizing) activity phospholipase D activity nucleus nucleolus endoplasmic reticulum cytosol caveola heme oxidation response to oxidative stress small GTPase mediated signal transduction regulation of blood pressure cell death negative regulation of cell proliferation intrinsic apoptotic signaling pathway in response to DNA damage negative regulation of muscle cell apoptotic process membrane integral component of membrane positive regulation of macroautophagy negative regulation of macroautophagy enzyme binding heme binding cellular response to nutrient negative regulation of mast cell cytokine production regulation of transcription from RNA polymerase II promoter in response to iron intracellular signal transduction heme catabolic process heme metabolic process response to hydrogen peroxide positive regulation of apoptotic process negative regulation of mast cell degranulation negative regulation of DNA binding negative regulation of sequence-specific DNA binding transcription factor activity negative regulation of neuron apoptotic process regulation of transcription from RNA polymerase II promoter in response to oxidative stress response to estrogen positive regulation of angiogenesis metal ion binding negative regulation of smooth muscle cell proliferation regulation of sequence-specific DNA binding transcription factor activity oxidation-reduction process cellular response to arsenic-containing substance cellular response to cadmium ion cellular response to cisplatin liver regeneration negative regulation of epithelial cell apoptotic process negative regulation of vascular smooth muscle cell proliferation uc003ant.1 uc003ant.2 uc003ant.3 uc003ant.4 
ENST00000216121.12 NIPSNAP1 ENST00000216121.12 nipsnap homolog 1, transcript variant 1 (from RefSeq NM_003634.4) B2RAY3 ENST00000216121.1 ENST00000216121.10 ENST00000216121.11 ENST00000216121.2 ENST00000216121.3 ENST00000216121.4 ENST00000216121.5 ENST00000216121.6 ENST00000216121.7 ENST00000216121.8 ENST00000216121.9 NIPS1_HUMAN NM_003634 O43800 Q9BPW8 uc003afx.1 uc003afx.2 uc003afx.3 uc003afx.4 uc003afx.5 uc003afx.6 This gene encodes a member of the NipSnap family of proteins that may be involved in vesicular transport. A similar protein in mice inhibits the calcium channel TRPV6, and is also localized to the inner mitochondrial membrane where it may play a role in mitochondrial DNA maintenance. A pseudogene of this gene is located on the short arm of chromosome 17. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Feb 2011]. Ubiquitous. Highest expression in liver. Belongs to the NipSnap family. protein binding mitochondrion membrane sensory perception of pain neurotransmitter binding synaptic membrane uc003afx.1 uc003afx.2 uc003afx.3 uc003afx.4 uc003afx.5 uc003afx.6 
ENST00000216122.9 MCM5 ENST00000216122.9 minichromosome maintenance complex component 5 (from RefSeq NM_006739.4) CDC46 ENST00000216122.1 ENST00000216122.2 ENST00000216122.3 ENST00000216122.4 ENST00000216122.5 ENST00000216122.6 ENST00000216122.7 ENST00000216122.8 MCM5_HUMAN NM_006739 O60785 P33992 Q14578 Q9BTJ4 Q9BWL8 uc003anu.1 uc003anu.2 uc003anu.3 uc003anu.4 uc003anu.5 uc003anu.6 The protein encoded by this gene is structurally very similar to the CDC46 protein from S. cerevisiae, a protein involved in the initiation of DNA replication. The encoded protein is a member of the MCM family of chromatin-binding proteins and can interact with at least two other members of this family. The encoded protein is upregulated in the transition from the G0 to G1/S phase of the cell cycle and may actively participate in cell cycle regulation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660805.22654.1, SRR1803614.45180.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216122.9/ ENSP00000216122.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232, PubMed:16899510). The active ATPase sites in the MCM2- 7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence=; Component of the MCM2-7 complex (PubMed:17296731, PubMed:16899510). The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:17296731, PubMed:16899510, PubMed:32453425). Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex (PubMed:34700328, PubMed:34694004, PubMed:32453425). Interacts with ANKRD17 (PubMed:23711367). Interacts with MCMBP (PubMed:17296731). Interacts with TONSL; the interaction is direct (PubMed:26527279). P33992; P62805: H4C9; NbExp=2; IntAct=EBI-359410, EBI-302023; P33992; Q9Y468: L3MBTL1; NbExp=2; IntAct=EBI-359410, EBI-1265089; P33992; P49736: MCM2; NbExp=5; IntAct=EBI-359410, EBI-374819; P33992; P25205: MCM3; NbExp=5; IntAct=EBI-359410, EBI-355153; P33992; P33993: MCM7; NbExp=8; IntAct=EBI-359410, EBI-355924; P33992; Q9BTE3: MCMBP; NbExp=13; IntAct=EBI-359410, EBI-749378; Nucleus Chromosome Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. Meier-Gorlin syndrome 8 (MGORS8) [MIM:617564]: A form of Meier-Gorlin syndrome, a syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. MGORS8 inheritance is autosomal recessive. Note=The disease is caused by variants affecting the gene represented in this entry. Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. The MCM2-7 hexamer is the proposed physiological active complex. Belongs to the MCM family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mcm5/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41321/MCM5"; G1/S transition of mitotic cell cycle nucleotide binding double-strand break repair via break-induced replication nuclear chromosome, telomeric region DNA binding DNA helicase activity DNA replication origin binding single-stranded DNA binding helicase activity protein binding ATP binding nucleus nucleoplasm cytoplasm cytosol DNA replication pre-replicative complex assembly involved in nuclear cell cycle DNA replication DNA replication initiation cell cycle membrane hydrolase activity DNA duplex unwinding MCM complex single-stranded DNA-dependent ATP-dependent DNA helicase activity 3'-5' DNA helicase activity uc003anu.1 uc003anu.2 uc003anu.3 uc003anu.4 uc003anu.5 uc003anu.6 
ENST00000216124.10 ARSA ENST00000216124.10 arylsulfatase A, transcript variant 4 (from RefSeq NM_001085427.3) A0A0C4DFZ2 A0A0C4DFZ2_HUMAN ARSA ENST00000216124.1 ENST00000216124.2 ENST00000216124.3 ENST00000216124.4 ENST00000216124.5 ENST00000216124.6 ENST00000216124.7 ENST00000216124.8 ENST00000216124.9 NM_001085427 uc021wse.1 uc021wse.2 uc021wse.3 The protein encoded by this gene hydrolyzes cerebroside sulfate to cerebroside and sulfate. Defects in this gene lead to metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in a variety of neurological symptoms and ultimately death. Alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, Dec 2010]. Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Belongs to the sulfatase family. acrosomal vesicle catalytic activity arylsulfatase activity extracellular space cytoplasm lysosome endosome plasma membrane autophagy binding of sperm to zona pellucida central nervous system development response to nutrient sulfuric ester hydrolase activity response to pH integral component of membrane extrinsic component of external side of plasma membrane response to estrogen response to ethanol response to methylmercury uc021wse.1 uc021wse.2 uc021wse.3 
ENST00000216127.5 RASD2 ENST00000216127.5 RASD family member 2, transcript variant 1 (from RefSeq NM_014310.4) ENST00000216127.1 ENST00000216127.2 ENST00000216127.3 ENST00000216127.4 NM_014310 O95520 Q5THY8 Q96D21 RHES_HUMAN TEM2 uc003anx.1 uc003anx.2 uc003anx.3 uc003anx.4 uc003anx.5 This gene belongs to the Ras superfamily of small GTPases and is enriched in the striatum. The encoded protein functions as an E3 ligase for attachment of small ubiquitin-like modifier (SUMO). This protein also binds to mutant huntingtin (mHtt), the protein mutated in Huntington disease (HD). Sumoylation of mHTT by this protein may cause degeneration of the striatum. The protein functions as an activator of mechanistic target of rapamycin 1 (mTOR1), which in turn plays a role in myelination, axon growth and regeneration. Reduced levels of mRNA expressed by this gene were found in HD patients. [provided by RefSeq, Jan 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC013419.2, SRR1803615.228277.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216127.5/ ENSP00000216127.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## GTPase signaling protein that binds to and hydrolyzes GTP. Regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins such as GNB1, GNB2 and GNB3. May be involved in selected striatal competencies, mainly locomotor activity and motor coordination. Monomer (Potential). Interacts with PIK3CA and UBE2I (By similarity). Interacts with GNB1, GNB2 and GNB3. Interacts with HTT; interacts with mutant HTT (mHTT) with a much higher affinity than wild type HTT. Cell membrane ; Lipid-anchor Pancreatic endocrine cells (islets of Langerhans). Farnesylated. Farnesylation is required for membrane targeting (By similarity). Reduces cell survival in striatal cells with Huntington disease by binding to mutant Huntington disease protein (mHTT; poly-Gln region with 82 repeats) and inducing sumoylation of mHTT. Belongs to the small GTPase superfamily. RasD family. Sequence=AAG00868.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleotide binding synaptic transmission, dopaminergic GTPase activity GTP binding plasma membrane signal transduction locomotory behavior membrane negative regulation of protein ubiquitination ubiquitin conjugating enzyme binding G-protein beta-subunit binding positive regulation of protein sumoylation phosphatidylinositol 3-kinase binding regulation of cAMP-mediated signaling positive regulation of protein kinase B signaling uc003anx.1 uc003anx.2 uc003anx.3 uc003anx.4 uc003anx.5 
ENST00000216129.7 TTLL12 ENST00000216129.7 tubulin tyrosine ligase like 12 (from RefSeq NM_015140.4) ENST00000216129.1 ENST00000216129.2 ENST00000216129.3 ENST00000216129.4 ENST00000216129.5 ENST00000216129.6 KIAA0153 NM_015140 Q14166 Q20WK5 Q9UGU3 TTL12_HUMAN uc003bdq.1 uc003bdq.2 uc003bdq.3 uc003bdq.4 uc003bdq.5 Negatively regulates post-translational modifications of tubulin, including detyrosination of the C-terminus and polyglutamylation of glutamate residues (PubMed:20162578, PubMed:23251473). Also, indirectly promotes histone H4 trimethylation at 'Lys-20' (H4K20me3) (PubMed:23251473). Probably by controlling tubulin and/or histone H4 post-translational modifications, plays a role in mitosis and in maintaining chromosome number stability (PubMed:20162578, PubMed:23251473). During RNA virus-mediated infection, acts as a negative regulator of the RIG-I pathway by preventing MAVS binding to TBK1 and IKBKE (PubMed:28011935). Interacts with MAVS; the interaction prevents MAVS binding to TBK1 and IKBKE (PubMed:28011935). Interacts (via N-terminus) with TBK1 (via protein kinase domain) (PubMed:28011935). Interacts (via TTL domain) with IKBKE (via protein kinase domain) (PubMed:28011935). Interacts with tubulin alpha (PubMed:23251473). Interacts with histone H3 and histone H4 (when trimethylated at 'Lys-20' (H4K20me3)) (PubMed:23251473). Interacts with CBX3 (PubMed:23251473). Q14166; P25685: DNAJB1; NbExp=4; IntAct=EBI-923010, EBI-357034; Q14166; P68104: EEF1A1; NbExp=4; IntAct=EBI-923010, EBI-352162; Q14166; Q05639: EEF1A2; NbExp=4; IntAct=EBI-923010, EBI-354943; Q14166; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-923010, EBI-2807642; Q14166; P0CG20: PRR35; NbExp=3; IntAct=EBI-923010, EBI-11986293; Cytoplasm dbody Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Nucleus Note=Predominantly localizes in the cytoplasm (PubMed:28011935). Partially colocalizes with vimentin in prostate cancer cells (PubMed:20162578). Expressed in the basal layer of prostate and endothelial cells. Increased expression in prostatic intraepithelial neoplasia and metastatic lesions. Belongs to the tubulin--tyrosine ligase family. Although it belongs to the tubulin--tyrosine ligase family, the TTL domain lacks some of the ATP binding sites predicted to be essential for TTL activity (PubMed:23251473). Lacks tyrosine ligase activity in vitro (PubMed:23251473). Lacks glutamylation activity in vitro (By similarity). Although TTLL12 contains a potential SET-like domain in the N-terminus, it does not have lysine methyltransferase activity towards histone in vitro (PubMed:23251473). nucleotide binding protein binding ATP binding cytoplasm cellular protein modification process regulation of mitotic cell cycle tubulin binding histone lysine methylation negative regulation of type I interferon-mediated signaling pathway H4K20me3 modified histone binding tubulin-tyrosine ligase activity histone-lysine N-methyltransferase activity regulation of histone H4-K20 methylation uc003bdq.1 uc003bdq.2 uc003bdq.3 uc003bdq.4 uc003bdq.5 
ENST00000216133.10 CBX7 ENST00000216133.10 chromobox 7, transcript variant 1 (from RefSeq NM_175709.5) CBX7_HUMAN ENST00000216133.1 ENST00000216133.2 ENST00000216133.3 ENST00000216133.4 ENST00000216133.5 ENST00000216133.6 ENST00000216133.7 ENST00000216133.8 ENST00000216133.9 NM_175709 O95931 Q86T17 uc003axb.1 uc003axb.2 uc003axb.3 uc003axb.4 uc003axb.5 This gene encodes a protein that contains the CHROMO (CHRomatin Organization MOdifier) domain. The encoded protein is a component of the Polycomb repressive complex 1 (PRC1), and is thought to control the lifespan of several normal human cells. [provided by RefSeq, Oct 2016]. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to trimethylated lysine residues in histones, and possibly also other proteins. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity. Component of a PRC1-like complex. Interacts with RING1 and RNF2/RING1B, but not with BMI1, EED or EZH2. Interacts with PCGF1, PCGF2, PCGF3, PCGF5 and PCGF6. O95931; P35226: BMI1; NbExp=12; IntAct=EBI-3923843, EBI-2341576; O95931; Q9HCE1: MOV10; NbExp=5; IntAct=EBI-3923843, EBI-1055820; O95931; Q9BSM1: PCGF1; NbExp=2; IntAct=EBI-3923843, EBI-749901; O95931; P35227: PCGF2; NbExp=6; IntAct=EBI-3923843, EBI-2129767; O95931; Q3KNV8: PCGF3; NbExp=2; IntAct=EBI-3923843, EBI-2339807; O95931; Q9BYE7: PCGF6; NbExp=4; IntAct=EBI-3923843, EBI-1048026; O95931; Q06587: RING1; NbExp=5; IntAct=EBI-3923843, EBI-752313; O95931; Q99496: RNF2; NbExp=15; IntAct=EBI-3923843, EBI-722416; O95931; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-3923843, EBI-527853; Nucleus The human orthologuous proteins of Drosophila Polycomb group protein Pc, CBX2, CBX4, CBX6, CBX7 and CBX8, show distinct nuclear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/43845/CBX7"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin protein binding nucleus nucleoplasm cytosol chromatin organization PcG protein complex PRC1 complex uc003axb.1 uc003axb.2 uc003axb.3 uc003axb.4 uc003axb.5 
ENST00000216139.10 ACR ENST00000216139.10 acrosin (from RefSeq NM_001097.3) ACRO_HUMAN ACRS ENST00000216139.1 ENST00000216139.2 ENST00000216139.3 ENST00000216139.4 ENST00000216139.5 ENST00000216139.6 ENST00000216139.7 ENST00000216139.8 ENST00000216139.9 NM_001097 P10323 Q6ICK2 uc003bnh.1 uc003bnh.2 uc003bnh.3 uc003bnh.4 uc003bnh.5 uc003bnh.6 Acrosin is the major proteinase present in the acrosome of mature spermatozoa. It is a typical serine proteinase with trypsin-like specificity. It is stored in the acrosome in its precursor form, proacrosin. The active enzyme functions in the lysis of the zona pellucida, thus facilitating penetration of the sperm through the innermost glycoprotein layers of the ovum. The mRNA for proacrosin is synthesized only in the postmeiotic stages of spermatogenesis. In humans proacrosin first appears in the haploid spermatids. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: Y00970.1, CR456366.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216139.10/ ENSP00000216139.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome. Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10; Inhibited by SERPINA5. Heavy chain (catalytic) and a light chain linked by two disulfide bonds. Forms a heterodimer with SERPINA5. P10323; Q05996: ZP2; NbExp=4; IntAct=EBI-21280149, EBI-1755919; P10323; P21754: ZP3; NbExp=2; IntAct=EBI-21280149, EBI-11783624; P10323; Q12836: ZP4; NbExp=2; IntAct=EBI-21280149, EBI-11783805; Belongs to the peptidase S1 family. acrosomal vesicle protease binding acrosome matrix dispersal DNA binding amidase activity serine-type endopeptidase activity copper ion binding protein binding mannose binding extracellular region nucleus Golgi-associated vesicle proteolysis activation of adenylate cyclase activity single fertilization binding of sperm to zona pellucida acrosome reaction penetration of zona pellucida drug binding peptidase activity serine-type peptidase activity zinc ion binding hydrolase activity protein catabolic process macromolecular complex fucose binding acrosomal matrix response to steroid hormone uc003bnh.1 uc003bnh.2 uc003bnh.3 uc003bnh.4 uc003bnh.5 uc003bnh.6 
ENST00000216144.4 CABP7 ENST00000216144.4 calcium binding protein 7 (from RefSeq NM_182527.3) CABP7_HUMAN CALN2 ENST00000216144.1 ENST00000216144.2 ENST00000216144.3 NM_182527 Q86V35 uc003agl.1 uc003agl.2 uc003agl.3 uc003agl.4 uc003agl.5 Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. Interacts with PI4KB. This binding competes with FREQ/NCS1 binding in a calcium-dependent manner (By similarity). Q86V35; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-23900553, EBI-3923617; Golgi apparatus, trans-Golgi network membrane ; Single-pass type IV membrane protein Cytoplasm, perinuclear region Cell membrane ; Single-pass type IV membrane protein The C-terminal transmembrane domain (TMD) is necessary and sufficient for membrane targeting. calcium ion binding cytoplasm Golgi apparatus plasma membrane membrane integral component of membrane trans-Golgi network membrane metal ion binding perinuclear region of cytoplasm uc003agl.1 uc003agl.2 uc003agl.3 uc003agl.4 uc003agl.5 
ENST00000216146.9 RPL3 ENST00000216146.9 ribosomal protein L3, transcript variant 2 (from RefSeq NM_001033853.2) B2RDV9 ENST00000216146.1 ENST00000216146.2 ENST00000216146.3 ENST00000216146.4 ENST00000216146.5 ENST00000216146.6 ENST00000216146.7 ENST00000216146.8 NM_001033853 OK/SW-cl.32 P39023 Q15548 Q5I0G0 RL3_HUMAN uc003axi.1 uc003axi.2 uc003axi.3 uc003axi.4 uc003axi.5 Ribosomes, the complexes that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L3P family of ribosomal proteins and it is located in the cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has been suggested that the protein contributes to tat-mediated transactivation. This gene is co-transcribed with several small nucleolar RNA genes, which are located in several of this gene's introns. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Jul 2008]. Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547, PubMed:35674491). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). Interacts with DHX33 (PubMed:26100019). P39023; O76024: WFS1; NbExp=3; IntAct=EBI-1056348, EBI-720609; Nucleus, nucleolus Cytoplasm Constitutively monomethylated at His-245 by METTL18 (PubMed:23349634, PubMed:33693809, PubMed:35674491). Methylation at His-245 regulates translation elongation by slowing ribosome traversal on tyrosine codons: slower elongation provides enough time for proper folding of synthesized proteins and prevents cellular aggregation of tyrosine-rich proteins (PubMed:35674491). It is not required for incorporation of RPL3 into ribosomes (PubMed:33693809). Belongs to the universal ribosomal protein uL3 family. ribosomal large subunit assembly nuclear-transcribed mRNA catabolic process, nonsense-mediated decay RNA binding structural constituent of ribosome protein binding nucleus nucleolus cytoplasm cytosol ribosome focal adhesion translation translational initiation SRP-dependent cotranslational protein targeting to membrane 5S rRNA binding viral transcription cytosolic large ribosomal subunit macromolecular complex synapse extracellular exosome cellular response to interleukin-4 uc003axi.1 uc003axi.2 uc003axi.3 uc003axi.4 uc003axi.5 
ENST00000216160.11 TAB1 ENST00000216160.11 TGF-beta activated kinase 1 (MAP3K7) binding protein 1, transcript variant alpha (from RefSeq NM_006116.3) ENST00000216160.1 ENST00000216160.10 ENST00000216160.2 ENST00000216160.3 ENST00000216160.4 ENST00000216160.5 ENST00000216160.6 ENST00000216160.7 ENST00000216160.8 ENST00000216160.9 MAP3K7IP1 NM_006116 Q15750 Q2PP09 Q8IZW2 TAB1_HUMAN uc003axt.1 uc003axt.2 uc003axt.3 uc003axt.4 uc003axt.5 The protein encoded by this gene was identified as a regulator of the MAP kinase kinase kinase MAP3K7/TAK1, which is known to mediate various intracellular signaling pathways, such as those induced by TGF beta, interleukin 1, and WNT-1. This protein interacts and thus activates TAK1 kinase. It has been shown that the C-terminal portion of this protein is sufficient for binding and activation of TAK1, while a portion of the N-terminus acts as a dominant-negative inhibitor of TGF beta, suggesting that this protein may function as a mediator between TGF beta receptors and TAK1. This protein can also interact with and activate the mitogen-activated protein kinase 14 (MAPK14/p38alpha), and thus represents an alternative activation pathway, in addition to the MAPKK pathways, which contributes to the biological responses of MAPK14 to various stimuli. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]. Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines (PubMed:22307082, PubMed:24403530). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation (PubMed:10838074, PubMed:25260751). Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:11847341, PubMed:29229647). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism (PubMed:14592977). Plays also a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits (PubMed:18021073). Interacts with XIAP and BIRC7 (PubMed:17560374, PubMed:11865055). Interacts with TRAF6 and MAP3K7; during IL-1 signaling (PubMed:8638164, PubMed:10094049, PubMed:10838074, PubMed:11323434). Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2 (PubMed:11460167). Interacts with TRAF6 and MAPK14; these interactions allow MAPK14 autophosphorylation (PubMed:11847341). Q15750; P00533: EGFR; NbExp=3; IntAct=EBI-358643, EBI-297353; Q15750; P47929: LGALS7B; NbExp=3; IntAct=EBI-358643, EBI-357504; Q15750; O43318: MAP3K7; NbExp=6; IntAct=EBI-358643, EBI-358684; Q15750; O43318-2: MAP3K7; NbExp=3; IntAct=EBI-358643, EBI-358700; Q15750; O15294: OGT; NbExp=3; IntAct=EBI-358643, EBI-539828; Q15750; Q9NYJ8: TAB2; NbExp=6; IntAct=EBI-358643, EBI-358708; Q15750; P98170: XIAP; NbExp=4; IntAct=EBI-358643, EBI-517127; Q15750; P62258: YWHAE; NbExp=2; IntAct=EBI-358643, EBI-356498; Q15750; PRO_0000449623 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-358643, EBI-25475864; Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=TAB1alpha; IsoId=Q15750-1; Sequence=Displayed; Name=2; Synonyms=TAB1beta; IsoId=Q15750-2; Sequence=VSP_042024; Ubiquitous. Phosphorylated at all three sites Ser-423, Thr-431 and Ser-438 by MAPK14 when cells were exposed to cellular stresses, or stimulated with TNF-alpha, IL1 or LPS (PubMed:14592977). These phosphorylations inhibit TAK1 activation by a feedback control mechanism (PubMed:14592977). Dephosphorylated by DUSP14 at Ser-438, leading to TAB1-MAP3K7/TAK1 complex inactivation in T-cells (PubMed:24403530). Ubiquitinated by MAP3K1 with 'Lys-63'-linked polyubiquitin; leading to activation of TAK1 and of JNK and p38 MAP kinases following EGF and TGF-beta stimulation (PubMed:25260751). Ubiquitinated by ITCH with 'Lys-48'-linked polyubiquitin; leading to proteasomal degradation (PubMed:25714464). Ubiquitinated by RNF114 during maternal-to-zygotic transition; leading to degradation (By similarity). (Microbial infection) Deubiquitinated by Y.enterocolitica YopP. O-GlcNAcylated at Ser-395 is required for full MAP3K7/TAK1 activation upon stimulation with IL-1 or osmotic stress. [Isoform 2]: Does not bind nor activate MAP3K7/TAK1. Lacks several key residues involved in metal-binding and catalytic activity, therefore has lost phosphatase activity. activation of MAPKKK activity activation of MAPK activity in utero embryonic development stimulatory C-type lectin receptor signaling pathway MyD88-dependent toll-like receptor signaling pathway heart morphogenesis cardiac septum development catalytic activity protein serine/threonine phosphatase activity magnesium-dependent protein serine/threonine phosphatase activity protein binding nucleus cytosol protein dephosphorylation transforming growth factor beta receptor signaling pathway I-kappaB kinase/NF-kappaB signaling JNK cascade enzyme activator activity endosome membrane protein deubiquitination nuclear speck kinase activator activity lung development macromolecular complex aorta development Fc-epsilon receptor signaling pathway positive regulation of MAP kinase activity macromolecular complex binding mitogen-activated protein kinase p38 binding positive regulation of NF-kappaB transcription factor activity coronary vasculature development nucleotide-binding oligomerization domain containing signaling pathway interleukin-1-mediated signaling pathway uc003axt.1 uc003axt.2 uc003axt.3 uc003axt.4 uc003axt.5 
ENST00000216177.9 PNPLA5 ENST00000216177.9 patatin like phospholipase domain containing 5, transcript variant 1 (from RefSeq NM_138814.4) B1AHL8 B3KPR1 ENST00000216177.1 ENST00000216177.2 ENST00000216177.3 ENST00000216177.4 ENST00000216177.5 ENST00000216177.6 ENST00000216177.7 ENST00000216177.8 GS2L NM_138814 PLPL5_HUMAN PNPLA5 Q6ZST0 Q7Z6Z6 uc062eyk.1 uc062eyk.2 This gene is a member of the patatin-like phospholipase family; its encoded protein has been shown to inhibit transacylation. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Apr 2010]. Has abundant triacylglycerol lipase activity. Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence=; Q7Z6Z6; Q92624: APPBP2; NbExp=3; IntAct=EBI-12241582, EBI-743771; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q7Z6Z6-1; Sequence=Displayed; Name=2; IsoId=Q7Z6Z6-2; Sequence=VSP_026373; Expressed in brain and pituitary gland. No differential expression during adipocyte differentiation. triglyceride lipase activity cytoplasm lipid particle cytosol lipid metabolic process membrane lipid catabolic process hydrolase activity triglyceride catabolic process lipid homeostasis uc062eyk.1 uc062eyk.2 
ENST00000216180.8 PNPLA3 ENST00000216180.8 patatin like phospholipase domain containing 3 (from RefSeq NM_025225.3) ADPN B0QYI0 B2RCL3 B3KW00 C22orf20 ENST00000216180.1 ENST00000216180.2 ENST00000216180.3 ENST00000216180.4 ENST00000216180.5 ENST00000216180.6 ENST00000216180.7 NM_025225 PLPL3_HUMAN PNPLA3 Q6P1A1 Q96CB4 Q9NST1 uc003bei.1 uc003bei.2 The protein encoded by this gene is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes. The encoded protein, which appears to be membrane bound, may be involved in the balance of energy usage/storage in adipocytes. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK315166.1, AL138578.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1970526, SAMEA2144333 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216180.8/ ENSP00000216180.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. Does not esterify other lysophospholipids. Acyl donors are long chain (at least C16) fatty acyl-CoAs: arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA and at a lesser extent palmitoyl-CoA (PubMed:22560221). Additionally possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides (PubMed:15364929, PubMed:20034933, PubMed:22560221). In vitro may express hydrolytic activity against glycerolipids triacylglycerol, diacylglycerol and monoacylglycerol, with a strong preference for oleic acid as the acyl moiety (PubMed:21878620). However, the triacylglycerol hydrolase activity is controversial and may be very low (PubMed:22560221). Possesses phospholipase A2 activity (PubMed:15364929). Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl- sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence=; Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence= Reaction=a 1,3-diacylglycerol + a 1-acylglycerol = a triacylglycerol + glycerol; Xref=Rhea:RHEA:44440, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855, ChEBI:CHEBI:35759, ChEBI:CHEBI:47777; Evidence=; Reaction=a 1,2-diacylglycerol + a 1-acylglycerol = a triacylglycerol + glycerol; Xref=Rhea:RHEA:44436, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855, ChEBI:CHEBI:35759, ChEBI:CHEBI:49172; Evidence=; Reaction=2 a 1-acylglycerol = a 1,2-diacylglycerol + glycerol; Xref=Rhea:RHEA:44432, ChEBI:CHEBI:17754, ChEBI:CHEBI:35759, ChEBI:CHEBI:49172; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3- phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence=; Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74544, ChEBI:CHEBI:74551; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; Evidence=; Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero- 3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn- glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160; Evidence=; Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn- glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)- eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544, ChEBI:CHEBI:74928; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444; Evidence=; Reaction=2 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)- glycerol + glycerol; Xref=Rhea:RHEA:38323, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323, ChEBI:CHEBI:75342; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38324; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)- glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38327, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323, ChEBI:CHEBI:53753, ChEBI:CHEBI:75342; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38328; Evidence=; Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)- glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38331, ChEBI:CHEBI:17754, ChEBI:CHEBI:53753, ChEBI:CHEBI:75342, ChEBI:CHEBI:75735; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38332; Evidence=; Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)- octadecenoate + 1,3-di-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75735; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38388; Evidence=; Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence=; The triglyceride lipase activity is inhibited by BEL ((E)-6-(bromomethylene)-3-(1-naphthalenyl)-2H-tetrahydropyran-2- one), a suicide substrate inhibitor. Kinetic parameters: KM=32.2 uM for triacylglycerol ; KM=29.1 uM for diacylglycerol ; KM=32.9 uM for monoacylglycerol ; KM=6.2 uM for oleoyl-CoA ; Vmax=10.5 nmol/min/mg enzyme toward triacylglycerol ; Vmax=21.8 nmol/min/mg enzyme toward diacylglycerol ; Vmax=27.4 nmol/min/mg enzyme toward monoacylglycerol ; Vmax=2.8 nmol/min/mg enzyme toward oleoyl-CoA ; Phospholipid metabolism. Glycerolipid metabolism. Membrane ingle-pass type II membrane protein Lipid droplet Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NST1-1; Sequence=Displayed; Name=2; IsoId=Q9NST1-2; Sequence=VSP_036222; By changes in energy balance: down-regulated following very low-calorie diet, whereas refeeding elevates the mRNA level. Polymorphic variation at position 148 influences insulin secretion levels and obesity. In obese subjects the body mass index and waist are higher in carriers of the Ile-148 allele. The Ile-148 carriers also display decreased insulin secretion in response to oral glucose tolerance test. Met-148 allele carriers are seemingly more insulin resistant at a lower body mass index. Non-alcoholic fatty liver disease 1 (NAFLD1) [MIM:613282]: A condition characterized by accumulation of triglycerides in the liver. It is associated with adverse metabolic consequences, including insulin resistance and dyslipidemia. In a subset of individuals, hepatic steatosis promotes an inflammatory response in the liver, referred to as steatohepatitis, which can progress to cirrhosis and liver cancer. NAFLD is the most common form of liver disease in Western countries. te=Disease susceptibility is associated with variants affecting the gene represented in this entry. long-chain fatty acid metabolic process 1-acylglycerol-3-phosphate O-acyltransferase activity phospholipase A2 activity triglyceride lipase activity cytoplasm endoplasmic reticulum membrane lipid particle lipid metabolic process glycerophospholipid metabolic process phosphatidic acid biosynthetic process phospholipid biosynthetic process membrane integral component of membrane lipid catabolic process transferase activity transferase activity, transferring acyl groups hydrolase activity triglyceride biosynthetic process triglyceride catabolic process lipid particle organization lysophosphatidic acid binding long-chain fatty acyl-CoA binding triglyceride acyl-chain remodeling acylglycerol acyl-chain remodeling lysophosphatidic acid acyltransferase activity mono-olein transacylation activity diolein transacylation activity lipid homeostasis uc003bei.1 uc003bei.2 
ENST00000216181.11 MYH9 ENST00000216181.11 myosin heavy chain 9 (from RefSeq NM_002473.6) A8K6E4 ENST00000216181.1 ENST00000216181.10 ENST00000216181.2 ENST00000216181.3 ENST00000216181.4 ENST00000216181.5 ENST00000216181.6 ENST00000216181.7 ENST00000216181.8 ENST00000216181.9 MYH9_HUMAN NM_002473 O60805 P35579 Q60FE2 Q86T83 uc003apg.1 uc003apg.2 uc003apg.3 uc003apg.4 uc003apg.5 uc003apg.6 This gene encodes a conventional non-muscle myosin; this protein should not be confused with the unconventional myosin-9a or 9b (MYO9A or MYO9B). The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. [provided by RefSeq, Dec 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB191263.1, AB290175.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216181.11/ ENSP00000216181.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411). Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with RASIP1 (By similarity). Interacts with DDR1 (By similarity). Interacts with PDLIM2 (By similarity). Interacts with SVIL (PubMed:12917436, PubMed:17925381). Interacts with HTRA3 (PubMed:22229724). Interacts with Myo7a (By similarity). Interacts with CFAP95 (PubMed:28345668). Interacts with LIMCH1; independently of the integration of MYH9 into the myosin complex (PubMed:28228547). Interacts with RAB3A (PubMed:27325790). Interacts with ZBED4 (PubMed:22693546). Interacts with S100A4; this interaction increases cell motility (PubMed:16707441). P35579; P61073: CXCR4; NbExp=5; IntAct=EBI-350338, EBI-489411; P35579; P62993: GRB2; NbExp=3; IntAct=EBI-350338, EBI-401755; P35579; O00255: MEN1; NbExp=3; IntAct=EBI-350338, EBI-592789; P35579; O00255-2: MEN1; NbExp=4; IntAct=EBI-350338, EBI-9869387; P35579; P35579: MYH9; NbExp=8; IntAct=EBI-350338, EBI-350338; P35579; P19338: NCL; NbExp=3; IntAct=EBI-350338, EBI-346967; P35579; P23297: S100A1; NbExp=3; IntAct=EBI-350338, EBI-743686; P35579; P29034: S100A2; NbExp=2; IntAct=EBI-350338, EBI-752230; P35579; P26447: S100A4; NbExp=18; IntAct=EBI-350338, EBI-717058; P35579; P33763: S100A5; NbExp=2; IntAct=EBI-350338, EBI-7211732; P35579; P06703: S100A6; NbExp=2; IntAct=EBI-350338, EBI-352877; P35579; P04271: S100B; NbExp=2; IntAct=EBI-350338, EBI-458391; P35579; P25815: S100P; NbExp=3; IntAct=EBI-350338, EBI-743700; P35579; P0DTC2: S; Xeno; NbExp=8; IntAct=EBI-350338, EBI-25474821; P35579; O46385: SVIL; Xeno; NbExp=2; IntAct=EBI-350338, EBI-6995105; Cytoplasm, cytoskeleton Cytoplasm, cell cortex Cytoplasmic vesicle, secretory vesicle, Cortical granule Note=Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells (PubMed:20052411). In retinal pigment epithelial cells, predominantly localized to stress fiber-like structures with some localization to cytoplasmic puncta (PubMed:27331610). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P35579-1; Sequence=Displayed; Name=2; IsoId=P35579-2; Sequence=VSP_035409, VSP_035410; In the kidney, expressed in the glomeruli. Also expressed in leukocytes. The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils. ISGylated. Ubiquitination. Macrothrombocytopenia and granulocyte inclusions with or without nephritis or sensorineural hearing loss (MATINS) [MIM:155100]: An autosomal dominant disorder characterized by thrombocytopenia, giant platelets and Dohle body-like inclusions in peripheral blood leukocytes with variable ultrastructural appearance. Some affected individuals lack leukocyte inclusion bodies on classic staining of peripheral blood smears. Alport syndrome-like features of nephritis, hearing loss, and eye abnormalities are present in some patients. te=The disease is caused by variants affecting the gene represented in this entry. Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration. Note=The disease is caused by variants affecting the gene represented in this entry. Note=Subjects with mutations in the motor domain of MYH9 present with severe thrombocytopenia and develop nephritis and deafness before the age of 40 years, while those with mutations in the tail domain have a much lower risk of noncongenital complications and significantly higher platelet counts. The clinical course of patients with mutations in the four most frequently affected residues of MYH9 (responsible for 70% of MYH9-related cases) were evaluated. Mutations at residue 1933 do not induce kidney damage or cataracts and cause deafness only in the elderly, those in position 702 result in severe thrombocytopenia and produce nephritis and deafness at a juvenile age, while alterations at residue 1424 or 1841 result in intermediate clinical pictures. Note=Genetic variations in MYH9 are associated with non- diabetic end stage renal disease (ESRD). Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. Sequence=CAD89954.1; Type=Frameshift; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/481/MYH9"; microfilament motor activity nucleotide binding meiotic spindle organization cell morphogenesis involved in differentiation angiogenesis in utero embryonic development stress fiber ruffle establishment of T cell polarity immunological synapse plasma membrane repair uropod RNA binding motor activity actin binding integrin binding protein binding calmodulin binding ATP binding nucleus cytoplasm spindle actomyosin contractile ring cytosol cytoskeleton plasma membrane brush border cell-cell adherens junction focal adhesion cell cortex membrane protein ectodomain proteolysis phagocytosis, engulfment cell adhesion integrin-mediated signaling pathway myoblast fusion regulation of cell shape protein transport actin cytoskeleton membrane myosin complex myosin II complex ATPase activity protein domain specific binding actin filament-based movement platelet formation monocyte differentiation cortical cytoskeleton actin-dependent ATPase activity actomyosin structure organization cell leading edge actin cytoskeleton reorganization neuromuscular junction cleavage furrow lysosome localization cytokinetic process uropod organization macromolecular complex actomyosin protein homodimerization activity protein anchor ADP binding blood vessel endothelial cell migration regulated exocytosis cadherin binding leukocyte migration actin filament binding establishment of meiotic spindle localization extracellular exosome platelet aggregation myosin II filament cell-cell adhesion negative regulation of actin filament severing positive regulation of protein processing in phagocytic vesicle regulation of plasma membrane repair COP9 signalosome uc003apg.1 uc003apg.2 uc003apg.3 uc003apg.4 uc003apg.5 uc003apg.6 
ENST00000216185.7 TXN2 ENST00000216185.7 thioredoxin 2 (from RefSeq NM_012473.4) ENST00000216185.1 ENST00000216185.2 ENST00000216185.3 ENST00000216185.4 ENST00000216185.5 ENST00000216185.6 NM_012473 Q5JZA0 Q6FH60 Q99757 Q9UH29 THIOM_HUMAN TRX2 uc003apk.1 uc003apk.2 uc003apk.3 This nuclear gene encodes a mitochondrial member of the thioredoxin family, a group of small multifunctional redox-active proteins. The encoded protein may play important roles in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1074468.1, SRR3476690.1132764.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2152474, SAMEA2152568 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000216185.7/ ENSP00000216185.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity. Monomer. Q99757; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-2932492, EBI-742038; Q99757; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-2932492, EBI-741181; Q99757; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2932492, EBI-11522760; Q99757; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-2932492, EBI-12170453; Q99757; P63010: AP2B1; NbExp=3; IntAct=EBI-2932492, EBI-432924; Q99757; P63010-2: AP2B1; NbExp=3; IntAct=EBI-2932492, EBI-11529439; Q99757; O75934: BCAS2; NbExp=3; IntAct=EBI-2932492, EBI-1050106; Q99757; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-2932492, EBI-750686; Q99757; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-2932492, EBI-1773949; Q99757; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2932492, EBI-739624; Q99757; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-2932492, EBI-723153; Q99757; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-2932492, EBI-1057156; Q99757; A0PJX0: CIB4; NbExp=3; IntAct=EBI-2932492, EBI-12868028; Q99757; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-2932492, EBI-11982645; Q99757; Q9H6J7-2: CSTPP1; NbExp=3; IntAct=EBI-2932492, EBI-13328871; Q99757; P32321: DCTD; NbExp=3; IntAct=EBI-2932492, EBI-739870; Q99757; P35638: DDIT3; NbExp=3; IntAct=EBI-2932492, EBI-742651; Q99757; O95571: ETHE1; NbExp=3; IntAct=EBI-2932492, EBI-715318; Q99757; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2932492, EBI-10175124; Q99757; Q5TD97: FHL5; NbExp=3; IntAct=EBI-2932492, EBI-750641; Q99757; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2932492, EBI-5916454; Q99757; Q96D09: GPRASP2; NbExp=4; IntAct=EBI-2932492, EBI-473189; Q99757; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-2932492, EBI-11519926; Q99757; Q9BX10: GTPBP2; NbExp=5; IntAct=EBI-2932492, EBI-6115579; Q99757; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-2932492, EBI-11978177; Q99757; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-2932492, EBI-2514791; Q99757; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-2932492, EBI-2558143; Q99757; P42858: HTT; NbExp=3; IntAct=EBI-2932492, EBI-466029; Q99757; Q674X7-2: KAZN; NbExp=3; IntAct=EBI-2932492, EBI-12024294; Q99757; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2932492, EBI-3044087; Q99757; Q6A162: KRT40; NbExp=3; IntAct=EBI-2932492, EBI-10171697; Q99757; P80188: LCN2; NbExp=3; IntAct=EBI-2932492, EBI-11911016; Q99757; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-2932492, EBI-10178634; Q99757; P43358: MAGEA4; NbExp=3; IntAct=EBI-2932492, EBI-743122; Q99757; O15479: MAGEB2; NbExp=3; IntAct=EBI-2932492, EBI-1057615; Q99757; Q15555: MAPRE2; NbExp=6; IntAct=EBI-2932492, EBI-739717; Q99757; Q9UPY8: MAPRE3; NbExp=6; IntAct=EBI-2932492, EBI-726739; Q99757; Q99750: MDFI; NbExp=3; IntAct=EBI-2932492, EBI-724076; Q99757; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2932492, EBI-16439278; Q99757; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-2932492, EBI-2548751; Q99757; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-2932492, EBI-995714; Q99757; Q96HT8: MRFAP1L1; NbExp=6; IntAct=EBI-2932492, EBI-748896; Q99757; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-2932492, EBI-742948; Q99757; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2932492, EBI-11522433; Q99757; P24844-2: MYL9; NbExp=3; IntAct=EBI-2932492, EBI-13066228; Q99757; Q96M63: ODAD1; NbExp=3; IntAct=EBI-2932492, EBI-10173858; Q99757; P40855: PEX19; NbExp=3; IntAct=EBI-2932492, EBI-594747; Q99757; P01189: POMC; NbExp=3; IntAct=EBI-2932492, EBI-12219503; Q99757; Q96CD2: PPCDC; NbExp=6; IntAct=EBI-2932492, EBI-724333; Q99757; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-2932492, EBI-10293968; Q99757; P61289: PSME3; NbExp=3; IntAct=EBI-2932492, EBI-355546; Q99757; Q9UJ41: RABGEF1; NbExp=3; IntAct=EBI-2932492, EBI-913954; Q99757; Q8IUH3: RBM45; NbExp=3; IntAct=EBI-2932492, EBI-2512147; Q99757; Q8IUH3-3: RBM45; NbExp=3; IntAct=EBI-2932492, EBI-10964453; Q99757; Q96HR9: REEP6; NbExp=3; IntAct=EBI-2932492, EBI-750345; Q99757; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-2932492, EBI-14065960; Q99757; P49247: RPIA; NbExp=6; IntAct=EBI-2932492, EBI-744831; Q99757; P21673: SAT1; NbExp=3; IntAct=EBI-2932492, EBI-711613; Q99757; Q8IZE3: SCYL3; NbExp=4; IntAct=EBI-2932492, EBI-1380680; Q99757; Q8IZE3-2: SCYL3; NbExp=3; IntAct=EBI-2932492, EBI-11959369; Q99757; P02549: SPTA1; NbExp=3; IntAct=EBI-2932492, EBI-375617; Q99757; O43805: SSNA1; NbExp=6; IntAct=EBI-2932492, EBI-2515299; Q99757; Q9H668: STN1; NbExp=3; IntAct=EBI-2932492, EBI-746930; Q99757; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-2932492, EBI-357085; Q99757; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-2932492, EBI-6872807; Q99757; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2932492, EBI-1105213; Q99757; Q96CG3: TIFA; NbExp=3; IntAct=EBI-2932492, EBI-740711; Q99757; Q9NZQ9: TMOD4; NbExp=3; IntAct=EBI-2932492, EBI-9393504; Q99757; P19474: TRIM21; NbExp=6; IntAct=EBI-2932492, EBI-81290; Q99757; Q15654: TRIP6; NbExp=3; IntAct=EBI-2932492, EBI-742327; Q99757; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-2932492, EBI-8636434; Q99757; Q9BRT2: UQCC2; NbExp=3; IntAct=EBI-2932492, EBI-1054584; Q99757; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-2932492, EBI-2799833; Q99757; O43829: ZBTB14; NbExp=3; IntAct=EBI-2932492, EBI-10176632; Q99757; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2932492, EBI-12030590; Q99757; Q6ZN96; NbExp=3; IntAct=EBI-2932492, EBI-10255097; Mitochondrion Widely expressed in adult (at protein level) and fetal tissues. Combined oxidative phosphorylation deficiency 29 (COXPD29) [MIM:616811]: An autosomal recessive, infantile-onset, neurodegenerative disorder characterized by decreased activities of mitochondrial respiratory complexes I and III, severe cerebellar atrophy, epilepsy, dystonia, optic atrophy, and peripheral neuropathy. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the thioredoxin family. sulfur amino acid catabolic process response to hypoxia protein binding nucleolus mitochondrion mitochondrial matrix glycerol ether metabolic process response to oxidative stress peptide-methionine (S)-S-oxide reductase activity response to hormone response to glucose response to organic cyclic compound protein disulfide oxidoreductase activity dendrite cellular response to nutrient levels peptide-methionine (R)-S-oxide reductase activity response to drug neuronal cell body macromolecular complex binding cell redox homeostasis response to axon injury oxidation-reduction process uc003apk.1 uc003apk.2 uc003apk.3 
ENST00000216190.13 EIF3D ENST00000216190.13 eukaryotic translation initiation factor 3 subunit D, transcript variant 2 (from RefSeq NR_156418.2) A8MWD3 B2R7D4 B4DTF8 B4DVY1 EIF3D EIF3D_HUMAN EIF3S7 ENST00000216190.1 ENST00000216190.10 ENST00000216190.11 ENST00000216190.12 ENST00000216190.2 ENST00000216190.3 ENST00000216190.4 ENST00000216190.5 ENST00000216190.6 ENST00000216190.7 ENST00000216190.8 ENST00000216190.9 NR_156418 O15371 Q3MJD9 Q5M9Q6 uc003apr.1 uc003apr.2 uc003apr.3 uc003apr.4 uc003apr.5 Eukaryotic translation initiation factor-3 (eIF3), the largest of the eIFs, is a multiprotein complex composed of at least ten nonidentical subunits. The complex binds to the 40S ribosome and helps maintain the 40S and 60S ribosomal subunits in a dissociated state. It is also thought to play a role in the formation of the 40S initiation complex by interacting with the ternary complex of eIF2/GTP/methionyl-tRNA, and by promoting mRNA binding. The protein encoded by this gene is the major RNA binding subunit of the eIF3 complex. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660805.157599.1, SRR7410570.685658.1 [ECO:0000332] ##Evidence-Data-END## mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:18599441, PubMed:25849773). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs (PubMed:27462815). (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. (Microbial infection) Interacts with Norwalk virus VPg protein (PubMed:12773399). O15371; O15084: ANKRD28; NbExp=3; IntAct=EBI-353818, EBI-359567; O15371; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-353818, EBI-724373; O15371; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-353818, EBI-11977221; O15371; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-353818, EBI-10961624; O15371; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-353818, EBI-739624; O15371; Q92997: DVL3; NbExp=3; IntAct=EBI-353818, EBI-739789; O15371; P60228: EIF3E; NbExp=6; IntAct=EBI-353818, EBI-347740; O15371; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-353818, EBI-5916454; O15371; Q9NSC5: HOMER3; NbExp=8; IntAct=EBI-353818, EBI-748420; O15371; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-353818, EBI-10961706; O15371; O75031: HSF2BP; NbExp=3; IntAct=EBI-353818, EBI-7116203; O15371; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-353818, EBI-14069005; O15371; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-353818, EBI-741037; O15371; Q6PF18: MORN3; NbExp=3; IntAct=EBI-353818, EBI-9675802; O15371; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-353818, EBI-11522433; O15371; Q8WV24: PHLDA1; NbExp=2; IntAct=EBI-353818, EBI-738731; O15371; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-353818, EBI-79165; O15371; P62487: POLR2G; NbExp=3; IntAct=EBI-353818, EBI-347928; O15371; Q04864: REL; NbExp=3; IntAct=EBI-353818, EBI-307352; O15371; P21673: SAT1; NbExp=3; IntAct=EBI-353818, EBI-711613; O15371; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-353818, EBI-1105213; O15371; P36406: TRIM23; NbExp=3; IntAct=EBI-353818, EBI-740098; O15371; P14373: TRIM27; NbExp=6; IntAct=EBI-353818, EBI-719493; O15371; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-353818, EBI-527853; O15371; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-353818, EBI-6248094; Cytoplasm Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O15371-1; Sequence=Displayed; Name=2; IsoId=O15371-2; Sequence=VSP_055473; Name=3; IsoId=O15371-3; Sequence=VSP_055474; The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of EIF3D into the full eukaryotic translation initiation factor 3 (eIF-3) complex. Mass=63972.9; Method=Unknown; Evidence=; Mass=64046.7; Mass_error=1.4; Method=MALDI; Evidence=; Note=Defects in EIF3D are associated with some cancers, such as prostate, breast and colon cancers. Disease susceptibility may be associated with variants affecting the gene represented in this entry. Down-regulation inhibits proliferation of cancers (PubMed:25370813, PubMed:25322666, PubMed:25682860, PubMed:26617750, PubMed:26008152, PubMed:26036682, PubMed:27035563). Belongs to the eIF-3 subunit D family. formation of cytoplasmic translation initiation complex cytoplasmic translational initiation cap-dependent translational initiation RNA binding translation initiation factor activity protein binding cytoplasm cytosol eukaryotic translation initiation factor 3 complex translation translational initiation membrane eukaryotic 43S preinitiation complex eukaryotic 48S preinitiation complex positive regulation of translation eukaryotic translation initiation factor 3 complex, eIF3m IRES-dependent viral translational initiation viral translational termination-reinitiation mRNA cap binding positive regulation of mRNA binding uc003apr.1 uc003apr.2 uc003apr.3 uc003apr.4 uc003apr.5 
ENST00000216211.9 UPK3A ENST00000216211.9 uroplakin 3A, transcript variant 1 (from RefSeq NM_006953.4) B0QY25 ENST00000216211.1 ENST00000216211.2 ENST00000216211.3 ENST00000216211.4 ENST00000216211.5 ENST00000216211.6 ENST00000216211.7 ENST00000216211.8 NM_006953 O60261 O75631 Q32N05 Q5TII6 UPK3 UPK3A_HUMAN uc003bfy.1 uc003bfy.2 uc003bfy.3 uc003bfy.4 uc003bfy.5 This gene encodes a member of the uroplakin family, a group of transmembrane proteins that form complexes on the apical surface of the bladder epithelium. Mutations in this gene may be associated with renal adysplasia. Alternatively spliced transcript variants have been described.[provided by RefSeq, Nov 2009]. Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity). Heterodimer with uroplakin-1B (UPK1B). O75631; O43765: SGTA; NbExp=3; IntAct=EBI-10188907, EBI-347996; O75631; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-10188907, EBI-744081; Endoplasmic reticulum membrane ; Single-pass type I membrane protein Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75631-1; Sequence=Displayed; Name=2; IsoId=O75631-2; Sequence=VSP_030004; Expressed in ureter. Note=Mutations in UPK3A have been detected in patients with renal adyplasia suggesting a possible involvement of this gene in kidney and urinary tract anomalies. Belongs to the uroplakin-3 family. cell morphogenesis kidney development protein binding endoplasmic reticulum endoplasmic reticulum membrane water transport urea transport membrane integral component of membrane apical plasma membrane epithelial cell differentiation potassium ion homeostasis sodium ion homeostasis urinary bladder development extracellular exosome uc003bfy.1 uc003bfy.2 uc003bfy.3 uc003bfy.4 uc003bfy.5 
ENST00000216218.8 ST13 ENST00000216218.8 ST13 Hsp70 interacting protein, transcript variant 1 (from RefSeq NM_003932.5) AAG2 ENST00000216218.1 ENST00000216218.2 ENST00000216218.3 ENST00000216218.4 ENST00000216218.5 ENST00000216218.6 ENST00000216218.7 F10A1_HUMAN FAM10A1 HIP NM_003932 O14999 P50502 Q2TU77 SNC6 uc003aze.1 uc003aze.2 uc003aze.3 uc003aze.4 uc003aze.5 uc003aze.6 The protein encoded by this gene is an adaptor protein that mediates the association of the heat shock proteins HSP70 and HSP90. This protein has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of this gene is reported to be downregulated in colorectal carcinoma tissue suggesting that it is a candidate tumor suppressor gene. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jun 2013]. One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity). Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90 (By similarity). Interacts (via the C-terminus 303- 319 AA) with GRK5. P50502; P02649: APOE; NbExp=3; IntAct=EBI-357285, EBI-1222467; P50502; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-357285, EBI-12300031; P50502; P42858: HTT; NbExp=13; IntAct=EBI-357285, EBI-466029; P50502; P29474: NOS3; NbExp=3; IntAct=EBI-357285, EBI-1391623; P50502; P49768: PSEN1; NbExp=3; IntAct=EBI-357285, EBI-297277; Cytoplasm Belongs to the FAM10 family. protein binding cytoplasm cytosol protein folding response to bacterium protein domain specific binding Hsp70 protein binding protein binding, bridging dATP binding macromolecular complex identical protein binding macromolecular complex binding protein dimerization activity unfolded protein binding chaperone mediated protein folding requiring cofactor chaperone binding protein homooligomerization protein homotetramerization negative regulation of protein refolding extracellular exosome uc003aze.1 uc003aze.2 uc003aze.3 uc003aze.4 uc003aze.5 uc003aze.6 
ENST00000216223.10 IL2RB ENST00000216223.10 interleukin 2 receptor subunit beta, transcript variant 1 (from RefSeq NM_000878.5) B2R765 ENST00000216223.1 ENST00000216223.2 ENST00000216223.3 ENST00000216223.4 ENST00000216223.5 ENST00000216223.6 ENST00000216223.7 ENST00000216223.8 ENST00000216223.9 IL15RB IL2RB IL2RB_HUMAN NM_000878 P14784 uc003aqv.1 uc003aqv.2 uc003aqv.3 The interleukin 2 receptor, which is involved in T cell-mediated immune responses, is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. The protein encoded by this gene represents the beta subunit and is a type I membrane protein. The use of alternative promoters results in multiple transcript variants encoding the same protein. The protein is primarily expressed in the hematopoietic system. The use by some variants of an alternate promoter in an upstream long terminal repeat (LTR) results in placenta-specific expression. [provided by RefSeq, Sep 2016]. Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770, PubMed:31040185). Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit. Interacts with SHB upon interleukin stimulation. (Microbial infection) Interacts with HTLV-1 accessory protein p12I. P14784; P40933: IL15; NbExp=3; IntAct=EBI-2866779, EBI-980274; P14784; P60568: IL2; NbExp=5; IntAct=EBI-2866779, EBI-12508717; P14784; Q15645: TRIP13; NbExp=3; IntAct=EBI-2866779, EBI-358993; Cell membrane ingle-pass type I membrane protein The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box 1 motif is required for JAK interaction and/or activation. Immunodeficiency 63 with lymphoproliferation and autoimmunity (IMD63) [MIM:618495]: An autosomal recessive disorder characterized by immune dysregulation resulting in lymphoid proliferation, dermatitis, enteropathy, autoantibodies, hypergammaglobulinemia, and immunodeficiency with recurrent infections. Patients show increased susceptibility to viral infections, particularly cytomegalovirus disease. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the type I cytokine receptor family. Type 4 subfamily. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/il2rb/"; MAPK cascade cytokine receptor activity interleukin-2 receptor activity protein binding endosome cytosol plasma membrane integral component of plasma membrane interleukin-2 receptor complex signal transduction external side of plasma membrane cell surface membrane integral component of membrane viral process cytokine-mediated signaling pathway interleukin-2 binding interleukin-15-mediated signaling pathway interleukin-2-mediated signaling pathway interleukin-15 receptor activity negative regulation of apoptotic process positive regulation of phagocytosis macromolecular complex assembly uc003aqv.1 uc003aqv.2 uc003aqv.3 
ENST00000216225.9 RBX1 ENST00000216225.9 ring-box 1 (from RefSeq NM_014248.4) B2RDY1 ENST00000216225.1 ENST00000216225.2 ENST00000216225.3 ENST00000216225.4 ENST00000216225.5 ENST00000216225.6 ENST00000216225.7 ENST00000216225.8 NM_014248 P62877 Q8N6Z8 Q9D1S2 Q9WUK9 Q9Y254 RBX1 RBX1_HUMAN RNF75 ROC1 uc003azk.1 uc003azk.2 uc003azk.3 uc003azk.4 uc003azk.5 This locus encodes a RING finger-like domain-containing protein. The encoded protein interacts with cullin proteins and likely plays a role in ubiquitination processes necessary for cell cycle progression. This protein may also affect protein turnover. Related pseudogenes exist on chromosomes 2 and 5.[provided by RefSeq, Sep 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803617.60101.1, SRR1803614.52727.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216225.9/ ENSP00000216225.8 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair (PubMed:10230407, PubMed:10579999, PubMed:15983046, PubMed:16678110, PubMed:19112177, PubMed:19679664, PubMed:23455478, PubMed:27565346, PubMed:29769719, PubMed:11961546, PubMed:22748924). CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (PubMed:27565346). The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. As part of a multisubunit complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence=; Reaction=S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.; EC=2.3.2.32; Evidence=; Protein modification; protein ubiquitination. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2 (PubMed:10230406, PubMed:11961546). Part of a SCF-like complex consisting of CUL7, RBX1, SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC complex (ELOB and ELOC), CUL2 or CUL5 and VHL (PubMed:10213691). Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II (PubMed:12732143). Part of multisubunit E3 ubiquitin ligase complexes with elongin BC complex (ELOB and ELOC), CUL2 and MED8; elongin BC complex (ELOB and ELOC), CUL5 and MUF1 (PubMed:11384984, PubMed:12149480). Part of multisubunit complexes with elongin BC complex (ELOB and ELOC), SOCS1 or WSB1 and CUL5. Part of a multisubunit ubiquitin ligase complex consisting of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5 (PubMed:19920177). Interacts directly with CUL1 and probably also with CUL2, CUL3, CUL4A, CUL4B, CUL5 and CUL7 (PubMed:10230407, PubMed:12481031). Interacts with CDC34 (PubMed:22748924). Interacts with GLMN. GLMN competes for the binding site of the E2 ubiquitin-conjugating enzyme CDC34 and disrupts CDC34 binding (PubMed:22748924). Interacts with COPS6 (PubMed:11337588). Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1 (PubMed:14739464). Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or CUL4B (PubMed:16678110). Interacts with UBE2M (PubMed:19250909). Part of a SCF complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via FBXO3 (PubMed:18809579). Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF (PubMed:20596027). Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and CDC34 (PubMed:19112177). Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein (PubMed:15983046). Part of the BCR(ENC1) complex containing ENC1 (PubMed:15983046). Part of the BCR(GAN) complex containing GAN (PubMed:15983046). Part of the BCR(KLHL41) complex containing KLHL41 (PubMed:15983046). Part of the BCR(KEAP1) complex containing KEAP1 (PubMed:15983046). Interacts with SESN1 and SESN2 (PubMed:23274085). Interacts with NOTCH2 (PubMed:29149593). Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL22 and RBX1 (PubMed:23455478). Interacts with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5 (PubMed:26906416, PubMed:24192928, PubMed:25349211). Component of a BCR3 (BTB-CUL3-RBX1) E3 ubiquitin ligase complex, also named Cul3-RING ubiquitin ligase complex CUL3(KBTBD6/7), composed of CUL3, RBX1, KBTBD6 and KBTBD7 (PubMed:25684205). Component of the ECS(LRR1) complex with the substrate recognition component LRR1 (PubMed:34700328). (Microbial infection) Interacts with human adenovirus 5 protein E1A; this interaction inhibits RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the SCF(FBW7) complex. P62877; Q13616: CUL1; NbExp=30; IntAct=EBI-398523, EBI-359390; P62877; Q13617: CUL2; NbExp=8; IntAct=EBI-398523, EBI-456179; P62877; Q13618: CUL3; NbExp=4; IntAct=EBI-398523, EBI-456129; P62877; Q13620: CUL4B; NbExp=7; IntAct=EBI-398523, EBI-456067; P62877; Q93034: CUL5; NbExp=3; IntAct=EBI-398523, EBI-1057139; P62877; Q92990: GLMN; NbExp=6; IntAct=EBI-398523, EBI-726150; P62877; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-398523, EBI-10176379; P62877; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-398523, EBI-10302990; P62877; P58004: SESN2; NbExp=3; IntAct=EBI-398523, EBI-3939642; P62877; Q13309: SKP2; NbExp=3; IntAct=EBI-398523, EBI-456291; P62877; P61081: UBE2M; NbExp=7; IntAct=EBI-398523, EBI-1041660; Cytoplasm Nucleus Widely expressed. The RING-type zinc finger domain is essential for ubiquitin ligase activity (PubMed:10230407). It coordinates an additional third zinc ion (PubMed:11961546, PubMed:22748924). Belongs to the RING-box family. Sequence=AAH17370.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42075/RBX1"; MAPK cascade protein polyubiquitination nucleotide-excision repair, DNA damage recognition nucleotide-excision repair, DNA duplex unwinding protein binding nucleus nucleoplasm cytoplasm cytosol DNA repair transcription-coupled nucleotide-excision repair nucleotide-excision repair, preincision complex stabilization nucleotide-excision repair, preincision complex assembly nucleotide-excision repair, DNA incision, 3'-to lesion nucleotide-excision repair, DNA incision, 5'-to lesion ubiquitin-dependent protein catabolic process protein monoubiquitination cellular response to DNA damage stimulus transcription factor binding zinc ion binding SCF complex assembly negative regulation of G2/M transition of mitotic cell cycle viral process Wnt signaling pathway protein ubiquitination transferase activity SCF ubiquitin ligase complex NEDD8 transferase activity protein catabolic process VCB complex SCF-dependent proteasomal ubiquitin-dependent protein catabolic process cullin-RING ubiquitin ligase complex Cul2-RING ubiquitin ligase complex Cul3-RING ubiquitin ligase complex Cul4A-RING E3 ubiquitin ligase complex Cul4B-RING E3 ubiquitin ligase complex Cul5-RING ubiquitin ligase complex Cul7-RING ubiquitin ligase complex ubiquitin protein ligase binding positive regulation of proteasomal ubiquitin-dependent protein catabolic process nucleotide-excision repair, DNA incision ubiquitin-ubiquitin ligase activity DNA damage response, detection of DNA damage proteasome-mediated ubiquitin-dependent protein catabolic process nuclear SCF ubiquitin ligase complex post-translational protein modification macromolecular complex binding protein neddylation metal ion binding regulation of transcription from RNA polymerase II promoter in response to hypoxia ubiquitin protein ligase activity interleukin-1-mediated signaling pathway global genome nucleotide-excision repair Cul4-RING E3 ubiquitin ligase complex negative regulation of canonical Wnt signaling pathway cullin family protein binding ubiquitin-protein transferase activity uc003azk.1 uc003azk.2 uc003azk.3 uc003azk.4 uc003azk.5 
ENST00000216237.10 L3MBTL2 ENST00000216237.10 L3MBTL histone methyl-lysine binding protein 2 (from RefSeq NM_031488.5) ENST00000216237.1 ENST00000216237.2 ENST00000216237.3 ENST00000216237.4 ENST00000216237.5 ENST00000216237.6 ENST00000216237.7 ENST00000216237.8 ENST00000216237.9 LMBL2_HUMAN NM_031488 Q8TEN1 Q969R5 Q96SC4 Q9BQI2 Q9UGS4 uc003azo.1 uc003azo.2 uc003azo.3 uc003azo.4 uc003azo.5 Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, BAT8 and YAF2. Q969R5; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-739909, EBI-746752; Q969R5; Q8N7W2-2: BEND7; NbExp=8; IntAct=EBI-739909, EBI-10181188; Q969R5; Q86UB2: BIVM; NbExp=3; IntAct=EBI-739909, EBI-12191873; Q969R5; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-739909, EBI-11530605; Q969R5; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-739909, EBI-711501; Q969R5; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-739909, EBI-742887; Q969R5; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-739909, EBI-2349927; Q969R5; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-739909, EBI-301024; Q969R5; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-739909, EBI-19153639; Q969R5; O95995: GAS8; NbExp=3; IntAct=EBI-739909, EBI-1052570; Q969R5; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-739909, EBI-743722; Q969R5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-739909, EBI-618309; Q969R5; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-739909, EBI-11519926; Q969R5; O15379: HDAC3; NbExp=6; IntAct=EBI-739909, EBI-607682; Q969R5; O75031: HSF2BP; NbExp=3; IntAct=EBI-739909, EBI-7116203; Q969R5; P61244: MAX; NbExp=6; IntAct=EBI-739909, EBI-751711; Q969R5; Q9HAF1: MEAF6; NbExp=4; IntAct=EBI-739909, EBI-399266; Q969R5; P50221: MEOX1; NbExp=3; IntAct=EBI-739909, EBI-2864512; Q969R5; Q16656-4: NRF1; NbExp=3; IntAct=EBI-739909, EBI-11742836; Q969R5; P22234: PAICS; NbExp=6; IntAct=EBI-739909, EBI-712261; Q969R5; Q8WUB8-2: PHF10; NbExp=6; IntAct=EBI-739909, EBI-10276329; Q969R5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-739909, EBI-79165; Q969R5; P78424: POU6F2; NbExp=3; IntAct=EBI-739909, EBI-12029004; Q969R5; P31321: PRKAR1B; NbExp=3; IntAct=EBI-739909, EBI-2805516; Q969R5; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-739909, EBI-1210429; Q969R5; Q04864-2: REL; NbExp=3; IntAct=EBI-739909, EBI-10829018; Q969R5; Q9Y2M2-2: SSUH2; NbExp=3; IntAct=EBI-739909, EBI-12231891; Q969R5; Q96MF2: STAC3; NbExp=6; IntAct=EBI-739909, EBI-745680; Q969R5; O75886: STAM2; NbExp=4; IntAct=EBI-739909, EBI-373258; Q969R5; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-739909, EBI-529518; Q969R5; A1L3A9: TBC1D9B; NbExp=3; IntAct=EBI-739909, EBI-12133518; Q969R5; Q66K14-2: TBC1D9B; NbExp=3; IntAct=EBI-739909, EBI-10217736; Q969R5; Q969V4: TEKT1; NbExp=3; IntAct=EBI-739909, EBI-10180409; Q969R5; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-739909, EBI-741515; Q969R5; Q08117: TLE5; NbExp=3; IntAct=EBI-739909, EBI-717810; Q969R5; P19237: TNNI1; NbExp=3; IntAct=EBI-739909, EBI-746692; Q969R5; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-739909, EBI-5235829; Q969R5; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-739909, EBI-9867283; Q969R5; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-739909, EBI-723389; Q969R5; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-739909, EBI-3918996; Q969R5; P10074: ZBTB48; NbExp=3; IntAct=EBI-739909, EBI-744864; Q969R5; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-739909, EBI-711679; Q969R5; P08048: ZFY; NbExp=6; IntAct=EBI-739909, EBI-12239601; Q969R5; Q7Z7K2: ZNF467; NbExp=3; IntAct=EBI-739909, EBI-11986485; Q969R5; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-739909, EBI-18036029; Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=A; IsoId=Q969R5-1; Sequence=Displayed; Name=2; Synonyms=B; IsoId=Q969R5-2; Sequence=VSP_003904, VSP_003905; Name=3; IsoId=Q969R5-3; Sequence=VSP_003906, VSP_003907; Sequence=BAB84917.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence=; Sequence=BAC04936.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence=; protein binding nucleus nucleoplasm chromatin organization regulation of transcription, DNA-templated zinc ion binding methylated histone binding histone binding metal ion binding negative regulation of G0 to G1 transition uc003azo.1 uc003azo.2 uc003azo.3 uc003azo.4 uc003azo.5 
ENST00000216241.14 CHADL ENST00000216241.14 chondroadherin like (from RefSeq NM_138481.2) CHADL_HUMAN ENST00000216241.1 ENST00000216241.10 ENST00000216241.11 ENST00000216241.12 ENST00000216241.13 ENST00000216241.2 ENST00000216241.3 ENST00000216241.4 ENST00000216241.5 ENST00000216241.6 ENST00000216241.7 ENST00000216241.8 ENST00000216241.9 NM_138481 Q05CY2 Q4G0S0 Q5JY13 Q6NUI6 Q86XY1 Q96E60 SLRR4B uc003azq.1 uc003azq.2 uc003azq.3 uc003azq.4 uc003azq.5 uc003azq.6 Potential negative modulator of chondrocyte differentiation. Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's differentiation by acting on its cellular collagenous microenvironment. Associates with collagen and binds to collagen fibrils. Secreted Secreted, extracellular space, extracellular matrix Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6NUI6-1; Sequence=Displayed; Name=2; IsoId=Q6NUI6-2; Sequence=VSP_027735; Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class IV subfamily. Sequence=AAH19839.1; Type=Frameshift; Evidence=; Sequence=AAH68590.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; collagen binding extracellular region extracellular space extracellular matrix structural constituent conferring compression resistance extracellular matrix negative regulation of chondrocyte differentiation collagen fibril binding negative regulation of collagen fibril organization uc003azq.1 uc003azq.2 uc003azq.3 uc003azq.4 uc003azq.5 uc003azq.6 
ENST00000216252.4 PHF5A ENST00000216252.4 PHD finger protein 5A (from RefSeq NM_032758.4) ENST00000216252.1 ENST00000216252.2 ENST00000216252.3 NM_032758 PHF5A_HUMAN Q7RTV0 Q9UH06 uc003bab.1 uc003bab.2 uc003bab.3 uc003bab.4 uc003bab.5 This gene encodes a subunit of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the intron's branch site in a sequence-independent manner and may anchor the U2 snRNP to the pre-mRNA. The protein encoded by this gene contains a PHD-finger-like domain that is flanked by highly basic N- and C-termini. This protein belongs to the PHD-finger superfamily and may act as a chromatin-associated protein. This gene has several pseudogenes on different chromosomes. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189658.132999.1, SRR1163658.184099.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2467150 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216252.4/ ENSP00000216252.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:27720643, PubMed:28541300, PubMed:12234937, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, PHF5A is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:27720643). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). Also involved in elongation by RNA polymerase II as part of the PAF1 complex (PAF1C) (By similarity). PAF1C is required for maintenance of embryonic stem cell (ESC) self- renewal and cellular reprogramming of stem cells (By similarity). Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes (By similarity). Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes (By similarity). Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self-renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies (By similarity). Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (By similarity). Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha (By similarity). Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:12234937, PubMed:15146077, PubMed:32494006, PubMed:34822310, PubMed:36797247). Part of the SF3B subcomplex of the 17S U2 SnRNP complex (PubMed:12234937, PubMed:12738865, PubMed:28541300, PubMed:27720643). SF3B associates with the splicing subcomplex SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP) (PubMed:12234937). Within the SF3B complex interacts directly with SF3B1 and SF3B3 (PubMed:27720643). Component of the minor spliceosome, which splices U12-type introns (PubMed:15146077, PubMed:33509932). Within this complex, interacts with CRIPT (PubMed:15146077, PubMed:33509932). Interacts (via N-terminus) with U2AF1 and SRSF5; acts to bridge the two (By similarity). Interacts (via C-terminus) with EP400 and DDX1; acts to bridge the two (By similarity). Interacts with the PAF1 complex (PAF1C) composed of CDC73, PAF1, LEO1, CTR9, RTF1 and SKIC8 (By similarity). Within the PAF1C interacts directly with CDC73 and SKIC8. Interacts with RNA polymerase II (By similarity). Q7RTV0; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2555365, EBI-10976677; Q7RTV0; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2555365, EBI-10975473; Q7RTV0; P60891: PRPS1; NbExp=3; IntAct=EBI-2555365, EBI-749195; Q7RTV0; Q15428: SF3A2; NbExp=2; IntAct=EBI-2555365, EBI-2462271; Q7RTV0; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2555365, EBI-5235340; Q7RTV0; O76024: WFS1; NbExp=3; IntAct=EBI-2555365, EBI-720609; Nucleus cleus speckle Belongs to the PHF5 family. mRNA splicing, via spliceosome DNA binding transcription factor activity, sequence-specific DNA binding RNA binding protein binding nucleus nucleoplasm spliceosomal complex U2 snRNP U12-type spliceosomal complex mRNA processing RNA splicing nuclear matrix nuclear speck positive regulation of transcription, DNA-templated metal ion binding U2-type precatalytic spliceosome uc003bab.1 uc003bab.2 uc003bab.3 uc003bab.4 uc003bab.5 
ENST00000216254.9 ACO2 ENST00000216254.9 aconitase 2 (from RefSeq NM_001098.3) ACON_HUMAN ENST00000216254.1 ENST00000216254.2 ENST00000216254.3 ENST00000216254.4 ENST00000216254.5 ENST00000216254.6 ENST00000216254.7 ENST00000216254.8 NM_001098 O75809 Q5JZ41 Q6FHX0 Q8TAQ6 Q99798 uc003bac.1 uc003bac.2 uc003bac.3 uc003bac.4 The protein encoded by this gene belongs to the aconitase/IPM isomerase family. It is an enzyme that catalyzes the interconversion of citrate to isocitrate via cis-aconitate in the second step of the TCA cycle. This protein is encoded in the nucleus and functions in the mitochondrion. It was found to be one of the mitochondrial matrix proteins that are preferentially degraded by the serine protease 15(PRSS15), also known as Lon protease, after oxidative modification. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660803.171951.1, SRR1660809.68762.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000216254.9/ ENSP00000216254.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence=; Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence=; Note=Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme. ; Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. Monomer. Mitochondrion Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers. Infantile cerebellar-retinal degeneration (ICRD) [MIM:614559]: A severe autosomal recessive neurodegenerative disorder characterized by onset between ages 2 and 6 months of truncal hypotonia, athetosis, seizures, and ophthalmologic abnormalities, particularly optic atrophy and retinal degeneration. Affected individuals show profound psychomotor retardation, with only some achieving rolling, sitting, or recognition of family. Brain MRI shows progressive cerebral and cerebellar degeneration. te=The disease is caused by variants affecting the gene represented in this entry. Optic atrophy 9 (OPA9) [MIM:616289]: A condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the aconitase/IPM isomerase family. Name=Wikipedia; Note=Aconitase entry; URL="https://en.wikipedia.org/wiki/Aconitase"; liver development aconitate hydratase activity iron ion binding mitochondrion mitochondrial matrix cytosol generation of precursor metabolites and energy tricarboxylic acid cycle citrate metabolic process isocitrate metabolic process lyase activity response to isolation stress metal ion binding iron-sulfur cluster binding 3 iron, 4 sulfur cluster binding 4 iron, 4 sulfur cluster binding uc003bac.1 uc003bac.2 uc003bac.3 uc003bac.4 
ENST00000216259.8 PMM1 ENST00000216259.8 phosphomannomutase 1 (from RefSeq NM_002676.3) A8K003 ENST00000216259.1 ENST00000216259.2 ENST00000216259.3 ENST00000216259.4 ENST00000216259.5 ENST00000216259.6 ENST00000216259.7 NM_002676 PMM1_HUMAN PMMH22 Q92586 Q92871 uc003bal.1 uc003bal.2 uc003bal.3 uc003bal.4 Phosphomannomutase catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189652.38470.1, SRR5189667.210396.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216259.8/ ENSP00000216259.7 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Involved in the synthesis of the GDP-mannose and dolichol- phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity. Kinetic parameters: KM=54 uM for alpha-D-mannose 1-phosphate ; KM=7.5 uM for alpha-D-glucose 1-phosphate ; Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Homodimer. Q92871; P20340: RAB6A; NbExp=4; IntAct=EBI-746784, EBI-1052826; Q92871; P20340-2: RAB6A; NbExp=3; IntAct=EBI-746784, EBI-8840191; Q92871; Q9NRW1: RAB6B; NbExp=5; IntAct=EBI-746784, EBI-1760079; Cytoplasm Strong expression in liver, heart, brain, and pancreas; lower expression in skeletal muscle. Belongs to the eukaryotic PMM family. phosphomannomutase activity protein binding cytoplasm cytosol mannose metabolic process protein N-linked glycosylation GDP-mannose biosynthetic process isomerase activity neuronal cell body protein targeting to ER metal ion binding cellular response to leukemia inhibitory factor uc003bal.1 uc003bal.2 uc003bal.3 uc003bal.4 
ENST00000216264.13 CERK ENST00000216264.13 ceramide kinase (from RefSeq NM_022766.6) A0JNT4 A8K611 CERK1_HUMAN ENST00000216264.1 ENST00000216264.10 ENST00000216264.11 ENST00000216264.12 ENST00000216264.2 ENST00000216264.3 ENST00000216264.4 ENST00000216264.5 ENST00000216264.6 ENST00000216264.7 ENST00000216264.8 ENST00000216264.9 KIAA1646 NM_022766 Q6NX59 Q8TCT0 Q9BYB3 Q9UGE5 uc003bia.1 uc003bia.2 uc003bia.3 uc003bia.4 uc003bia.5 CERK converts ceramide to ceramide 1-phosphate (C1P), a sphingolipid metabolite. Both CERK and C1P have been implicated in various cellular processes, including proliferation, apoptosis, phagocytosis, and inflammation (Kim et al., 2006 [PubMed 16488390]).[supplied by OMIM, Mar 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB079066.1, SRR1803616.221518.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216264.13/ ENSP00000216264.8 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate (PubMed:11956206, PubMed:16269826, PubMed:19168031). Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2- ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines (PubMed:11956206, PubMed:16269826, PubMed:19168031). Shows a greater preference for D-erythro isomer of ceramides (PubMed:16269826). Binds phosphoinositides (PubMed:19168031). Reaction=an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674, ChEBI:CHEBI:456216; EC=2.7.1.138; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17930; Evidence= Reaction=ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N- hexanoylsphing-4-enine 1-phosphate; Xref=Rhea:RHEA:43312, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63867, ChEBI:CHEBI:82959, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43313; Evidence=; Reaction=ATP + N-(acetyl)-sphing-4-enine = ADP + H(+) + N-(acetyl)- sphing-4-enine-1-phosphate; Xref=Rhea:RHEA:47904, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46979, ChEBI:CHEBI:85375, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47905; Evidence=; Reaction=ATP + N-hexadecanoylsphing-4-enine = ADP + H(+) + N- (hexadecanoyl)-sphing-4-enine-1-phosphate; Xref=Rhea:RHEA:46340, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72959, ChEBI:CHEBI:72963, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46341; Evidence=; Reaction=ATP + N-hexanoyl-(4R)-hydroxysphinganine = ADP + H(+) + N- hexanoyl-(4R)-hydroxysphinganine-1-phosphate; Xref=Rhea:RHEA:47916, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:88095, ChEBI:CHEBI:88096, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47917; Evidence=; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Inhibited by sulfatide (PubMed:19168031). Inhibited by sphinganine, sphingenine, and N,N-Dimethylsphingosine (DMS) (PubMed:16269826). Cardiolipin at 0.1 uM significantly increases activity, whereas at concentrations >1 uM has an inhibitory effect (PubMed:27725450). Kinetic parameters: KM=187 uM for C8 ceramide ; KM=30 uM for C6 ceramide ; KM=22 uM for C2 ceramide ; KM=400 uM for ATP (in the presence of 3 mM Mg(2+)) ; KM=32 uM for ATP ; Vmax=35 nmol/min/mg enzyme for C6 ceramide ; pH dependence: Optimum pH is 6.0-7.8. Q8TCT0; P13196: ALAS1; NbExp=3; IntAct=EBI-10274247, EBI-3905054; Q8TCT0; P05813: CRYBA1; NbExp=3; IntAct=EBI-10274247, EBI-7043337; Q8TCT0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10274247, EBI-3867333; Q8TCT0; O76011: KRT34; NbExp=3; IntAct=EBI-10274247, EBI-1047093; Q8TCT0; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10274247, EBI-11959885; Q8TCT0; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-10274247, EBI-1052037; Q8TCT0; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-10274247, EBI-12811111; Q8TCT0; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-10274247, EBI-12805508; Q8TCT0; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-10274247, EBI-9996449; Q8TCT0; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-10274247, EBI-751260; Q8TCT0; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-10274247, EBI-11962084; Q8TCT0; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-10274247, EBI-1044640; Q8TCT0; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10274247, EBI-742948; Q8TCT0; P0CG21: NHLRC4; NbExp=3; IntAct=EBI-10274247, EBI-12868744; Q8TCT0; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10274247, EBI-945833; Q8TCT0; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10274247, EBI-22310682; Q8TCT0; O43482: OIP5; NbExp=3; IntAct=EBI-10274247, EBI-536879; Q8TCT0; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-10274247, EBI-742388; Q8TCT0; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-10274247, EBI-5235829; Cytoplasm Cell membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8TCT0-1; Sequence=Displayed; Name=2; IsoId=Q8TCT0-2; Sequence=VSP_056944; High level expression in heart, brain, skeletal muscle, kidney and liver; moderate in peripheral blood leukocytes and thymus; very low in spleen, small intestine, placenta and lung. nucleotide binding magnesium ion binding ceramide kinase activity NAD+ kinase activity protein binding ATP binding cytoplasm plasma membrane ceramide metabolic process glycosphingolipid metabolic process membrane integral component of membrane kinase activity phosphorylation transferase activity lipid phosphorylation uc003bia.1 uc003bia.2 uc003bia.3 uc003bia.4 uc003bia.5 
ENST00000216268.6 ZBED4 ENST00000216268.6 zinc finger BED-type containing 4 (from RefSeq NM_014838.3) B2RZH1 ENST00000216268.1 ENST00000216268.2 ENST00000216268.3 ENST00000216268.4 ENST00000216268.5 KIAA0637 NM_014838 O75132 Q1ECU0 Q9UGG8 ZBED4_HUMAN uc003bix.1 uc003bix.2 uc003bix.3 uc003bix.4 Transcriptional regulator that binds to poly-guanine tracts in gene promoters and activates transcription (By similarity). Able to bind single- and double-stranded DNA and RNA (By similarity). Homodimer; via C-terminus (PubMed:17209048). Interacts with MYH9 (PubMed:22693546). Interacts with SAFB/SAFB1 (PubMed:22693546). O75132; P50222: MEOX2; NbExp=3; IntAct=EBI-2860059, EBI-748397; Nucleus toplasm Photoreceptor inner segment Expressed in testis, heart, lung, and weakly expressed in brain, liver, muscle, placenta and small intestine (PubMed:19369242). Expressed in the retina, found in the cone photoreceptors, Mueller cells, cone pedicles and in the innermost retinal layer (PubMed:19369242). Sequence=BAA31612.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding protein binding nucleus nucleoplasm cytoplasm regulation of transcription from RNA polymerase II promoter metal ion binding protein dimerization activity uc003bix.1 uc003bix.2 uc003bix.3 uc003bix.4 
ENST00000216271.10 HDAC10 ENST00000216271.10 histone deacetylase 10, transcript variant 1 (from RefSeq NM_032019.6) ENST00000216271.1 ENST00000216271.2 ENST00000216271.3 ENST00000216271.4 ENST00000216271.5 ENST00000216271.6 ENST00000216271.7 ENST00000216271.8 ENST00000216271.9 HDA10_HUMAN NM_032019 Q08AP4 Q6STF9 Q969S8 Q96P77 Q96P78 Q9H028 Q9UGX1 Q9UGX2 uc003bkg.1 uc003bkg.2 uc003bkg.3 uc003bkg.4 uc003bkg.5 The protein encoded by this gene belongs to the histone deacetylase family, members of which deacetylate lysine residues on the N-terminal part of the core histones. Histone deacetylation modulates chromatin structure, and plays an important role in transcriptional regulation, cell cycle progression, and developmental events. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011]. Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine (PubMed:28516954). Histone deacetylase activity has been observed in vitro (PubMed:11861901, PubMed:11726666, PubMed:11677242, PubMed:11739383). Has also been shown to be involved in MSH2 deacetylation (PubMed:26221039). The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak (PubMed:28516954). May play a role in the promotion of late stages of autophagy, possibly autophagosome- lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells (PubMed:23801752, PubMed:29968769). May play a role in homologous recombination (PubMed:21247901). May promote DNA mismatch repair (PubMed:26221039). Reaction=H2O + N(8)-acetylspermidine = acetate + spermidine; Xref=Rhea:RHEA:23928, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=3.5.1.48; Evidence=; Reaction=H2O + N-acetylputrescine = acetate + putrescine; Xref=Rhea:RHEA:23412, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58263, ChEBI:CHEBI:326268; EC=3.5.1.62; Evidence=; Reaction=H2O + N-acetylcadaverine = acetate + cadaverine; Xref=Rhea:RHEA:51892, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58384, ChEBI:CHEBI:134408; Evidence=; Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl- [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; Evidence= Kinetic parameters: KM=110 uM for acetylcadaverine ; KM=170 uM for acetylputrescine ; KM=100 uM for N(8)-acetylspermidine ; KM=180 uM for N(1)-acetylspermine ; KM=150 uM for N(1),N(8)-diacetylspermidine ; Interacts with HDAC3 (PubMed:11861901). Interacts with HDAC2 and NCOR2/SMRT (PubMed:11739383). Interacts with HSPA8/HSC70 (PubMed:23801752). Interacts with MSH2 (PubMed:26221039). Q969S8; Q92870-2: APBB2; NbExp=3; IntAct=EBI-301762, EBI-21535880; Q969S8; P54252: ATXN3; NbExp=3; IntAct=EBI-301762, EBI-946046; Q969S8; P42858: HTT; NbExp=21; IntAct=EBI-301762, EBI-466029; Q969S8; Q96CV9: OPTN; NbExp=3; IntAct=EBI-301762, EBI-748974; Q969S8; Q7Z412: PEX26; NbExp=3; IntAct=EBI-301762, EBI-752057; Q969S8; D3DTS7: PMP22; NbExp=3; IntAct=EBI-301762, EBI-25882629; Q969S8; P37840: SNCA; NbExp=3; IntAct=EBI-301762, EBI-985879; Q969S8; Q9BYV2: TRIM54; NbExp=2; IntAct=EBI-301762, EBI-2130429; Cytoplasm cleus Note=Excluded from nucleoli. Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=Alpha , HDAC10b , HDAC10v1 ; IsoId=Q969S8-1; Sequence=Displayed; Name=2; Synonyms=Beta ; IsoId=Q969S8-2; Sequence=VSP_002089; Name=4; Synonyms=A, HDAC10v2 ; IsoId=Q969S8-4; Sequence=VSP_002090; Name=5; IsoId=Q969S8-5; Sequence=VSP_014698, VSP_014699; Widely expressed with high levels in liver and kidney. Note=In neuroblastoma cells, may promote autophagy in response to chemotherapy-induced DNA damage and efflux of chemotherapeutics via lysosomal exocytosis, hence protecting cells from cytotoxic agents (PubMed:23801752, PubMed:29968769). Expression levels may correlate with survival in neuroblastoma patients, with low levels in the tumor correlating with long-term patient survival and high expression with poor prognosis (PubMed:23801752). Therefore has been proposed as a biomarker to predict neuroblastoma chemoresistance and treatment outcome (PubMed:23801752). Like some other members of the HD type 2 subfamily, such as HDAC4, inhibited by the antitumor drug trichostatin A (TSA). [Isoform 4]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the histone deacetylase family. HD type 2 subfamily. Protein/histone deacetylase activity in vivo is uncertain. The 3D structure analysis of the zebrafish ortholog shows that a glutamate gatekeeper and a sterically constricted active site confer specificity for N(8)-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Supporting this observation, has been shown to exhibit only very low activity, if any, towards acetyl-lysine peptide substrates (PubMed:28516954). However, histone deacetylase activity has been observed in vitro (PubMed:28516954, PubMed:11861901, PubMed:11726666, PubMed:11677242, PubMed:11739383). Has also been shown to be involved in MSH2 deacetylation (PubMed:26221039). histone deacetylase complex negative regulation of transcription from RNA polymerase II promoter histone deacetylase activity protein binding nucleus nucleoplasm cytoplasm DNA repair DNA recombination chromatin organization regulation of transcription, DNA-templated protein deacetylation autophagy cellular response to DNA damage stimulus zinc ion binding oligodendrocyte development macroautophagy histone deacetylation hydrolase activity deacetylase activity enzyme binding positive regulation of mismatch repair protein deacetylase activity peptidyl-lysine deacetylation reciprocal DNA recombination histone deacetylase binding negative regulation of transcription, DNA-templated metal ion binding acetylputrescine deacetylase activity acetylspermidine deacetylase activity uc003bkg.1 uc003bkg.2 uc003bkg.3 uc003bkg.4 uc003bkg.5 
ENST00000216274.10 RIPK3 ENST00000216274.10 receptor interacting serine/threonine kinase 3 (from RefSeq NM_006871.4) B4DJL9 C4AM87 ENST00000216274.1 ENST00000216274.2 ENST00000216274.3 ENST00000216274.4 ENST00000216274.5 ENST00000216274.6 ENST00000216274.7 ENST00000216274.8 ENST00000216274.9 NM_006871 Q5J795 Q5J796 Q6P5Y1 Q9Y572 RIP3 RIPK3 RIPK3_HUMAN uc001wpb.1 uc001wpb.2 uc001wpb.3 uc001wpb.4 uc001wpb.5 The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC062584.1, AK075275.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216274.10/ ENSP00000216274.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Serine/threonine-protein kinase that activates necroptosis and apoptosis, two parallel forms of cell death (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:29883609, PubMed:32657447). Necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members, is triggered by RIPK3 following activation by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:29883609, PubMed:32298652). Activated RIPK3 forms a necrosis- inducing complex and mediates phosphorylation of MLKL, promoting MLKL localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:25316792, PubMed:29883609). In addition to TNF- induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol (By similarity). Also regulates apoptosis: apoptosis depends on RIPK1, FADD and CASP8, and is independent of MLKL and RIPK3 kinase activity (By similarity). Phosphorylates RIPK1: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). In some cell types, also able to restrict viral replication by promoting cell death- independent responses (By similarity). In response to Zika virus infection in neurons, promotes a cell death-independent pathway that restricts viral replication: together with ZBP1, promotes a death- independent transcriptional program that modifies the cellular metabolism via up-regulation expression of the enzyme ACOD1/IRG1 and production of the metabolite itaconate (By similarity). Itaconate inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes (By similarity). RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL (PubMed:19498109). These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (PubMed:19498109). (Microbial infection) In case of herpes simplex virus 1/HHV-1 infection, forms heteromeric amyloid structures with HHV-1 protein RIR1/ICP6 which may inhibit RIPK3-mediated necroptosis, thereby preventing host cell death pathway and allowing viral evasion. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence= Activity is stimulated by ZBP1, which senses double-stranded Z-RNA structures (By similarity). RIPK3-dependent necroptosis is inhibited by RIPK1: RIPK1 prevents the ZBP1-induced activation of RIPK3 via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (By similarity). Interacts (via RIP homotypic interaction motif) with RIPK1 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necrosis-inducing complex (PubMed:10339433, PubMed:11734559, PubMed:19524512, PubMed:29681455). Interacts with MLKL; the interaction is direct and triggers necroptosis (PubMed:22265413, PubMed:22421439). Interacts with ZBP1 (via RIP homotypic interaction motif); interaction with ZBP1 activates RIPK3, triggering necroptosis (By similarity). Upon TNF- induced necrosis, the RIPK1-RIPK3 dimer further interacts with PGAM5 and MLKL; the formation of this complex leads to PGAM5 phosphorylation and increase in PGAM5 phosphatase activity (PubMed:22265413, PubMed:22265414, PubMed:22421439). Binds TRAF2 and is recruited to the TNFR-1 signaling complex (PubMed:29883609). Interacts with PYGL, GLUL and GLUD1; these interactions result in activation of these metabolic enzymes (PubMed:19498109). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 (PubMed:21931591). Interacts with ARHGEF2 (PubMed:21887730). Interacts with PELI1 (via atypical FHA domain); the phosphorylated form at Thr-182 binds preferentially to PELI1 (PubMed:29883609). Interacts with BUB1B, TRAF2 and STUB1 (PubMed:29883609). Interacts with CASP6 (PubMed:32298652). Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity). (Microbial infection) Interacts (via RIP homotypic interaction motif/RHIM) with herpes simplex virus 1/HHV-1 protein RIR1/ICP6 (via RHIM); this interaction may induce heteromeric amyloid assemblies and prevent necroptosis activation. (Microbial infection) Interacts (via RIP homotypic interaction motif/RHIM) with herpes simplex virus 2/HHV-2 protein RIR1/ICP10 (via RHIM); this interaction prevents necroptosis activation. Q9Y572; Q13490: BIRC2; NbExp=3; IntAct=EBI-298250, EBI-514538; Q9Y572; Q13489: BIRC3; NbExp=3; IntAct=EBI-298250, EBI-517709; Q9Y572; Q8NB16: MLKL; NbExp=10; IntAct=EBI-298250, EBI-1055040; Q9Y572; Q13546: RIPK1; NbExp=26; IntAct=EBI-298250, EBI-358507; Q9Y572; Q9Y572: RIPK3; NbExp=5; IntAct=EBI-298250, EBI-298250; Q9Y572; Q9H171: ZBP1; NbExp=4; IntAct=EBI-298250, EBI-6264672; Q9Y572; J9TC74: ORF3a; Xeno; NbExp=3; IntAct=EBI-298250, EBI-25488975; Cytoplasm, cytosol Nucleus Note=Mainly cytoplasmic. Present in the nucleus in response to influenza A virus (IAV) infection. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9Y572-1; Sequence=Displayed; Name=2; Synonyms=Beta; IsoId=Q9Y572-2; Sequence=VSP_035106; Name=3; Synonyms=Gamma; IsoId=Q9Y572-3; Sequence=VSP_035107; Highly expressed in the pancreas. Detected at lower levels in heart, placenta, lung and kidney. [Isoform 3]: Expression is significantly increased in colon and lung cancers. The RIP homotypic interaction motif/RHIM mediates interaction with the RHIM motif of RIPK1. Both motifs form a hetero-amyloid serpentine fold, stabilized by hydrophobic packing and featuring an unusual Cys-Ser ladder of alternating Ser (from RIPK1) and Cys (from RIPK3). (Microbial infection) The RIP homotypic interaction motif/RHIM mediates interaction with the RHIM motif of the herpes simplex virus 1/HHV-1 protein RIR1/ICP6 to form heteromeric amyloid structures. (Microbial infection) Proteolytically cleaved by S.flexneri OspD3 within the RIP homotypic interaction motif (RHIM), leading to its degradation and inhibition of necroptosis. RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Autophosphorylated following interaction with ZBP1 (By similarity). Phosphorylation of Ser-199 plays a role in the necroptotic function of RIPK3 (PubMed:11734559, PubMed:19524512). Autophosphorylates at Ser-227 following activation by ZBP1: phosphorylation at these sites is a hallmark of necroptosis and is required for binding MLKL (PubMed:22265413). Phosphorylation at Thr-182 is important for its kinase activity, interaction with PELI1 and PELI1- mediated 'Lys-48'-linked polyubiquitination and for its ability to mediate TNF-induced necroptosis (PubMed:29883609). Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B (PubMed:21931591). Polyubiquitinated with 'Lys-48'-linked chains by PELI1 leading to its subsequent proteasome-dependent degradation. Ubiquitinated by STUB1 leading to its subsequent proteasome-dependent degradation (PubMed:29883609). Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. nucleotide binding regulation of T cell mediated cytotoxicity regulation of adaptive immune response transcription coactivator activity protein kinase activity protein serine/threonine kinase activity NF-kappaB-inducing kinase activity protein binding ATP binding cytoplasm mitochondrion cytosol plasma membrane cellular protein modification process protein phosphorylation signal transduction I-kappaB kinase/NF-kappaB signaling positive regulation of phosphatase activity positive regulation of necrotic cell death programmed cell death membrane kinase activity phosphorylation transferase activity activation of protein kinase activity regulation of interferon-gamma production T cell differentiation in thymus NIK/NF-kappaB signaling identical protein binding T cell homeostasis macromolecular complex binding regulation of activated T cell proliferation protein autophosphorylation lymph node development spleen development thymus development positive regulation of NF-kappaB transcription factor activity protein homooligomerization protein heterooligomerization positive regulation of ligase activity positive regulation of oxidoreductase activity positive regulation of necroptotic process regulation of activation-induced cell death of T cells necroptotic process cellular response to hydrogen peroxide apoptotic signaling pathway programmed necrotic cell death positive regulation of nucleic acid-templated transcription amyloid fibril formation regulation of reactive oxygen species metabolic process positive regulation of reactive oxygen species metabolic process regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation positive regulation of intrinsic apoptotic signaling pathway uc001wpb.1 uc001wpb.2 uc001wpb.3 uc001wpb.4 uc001wpb.5 
ENST00000216277.13 PAPOLA ENST00000216277.13 poly(A) polymerase alpha, transcript variant 1 (from RefSeq NM_032632.5) ENST00000216277.1 ENST00000216277.10 ENST00000216277.11 ENST00000216277.12 ENST00000216277.2 ENST00000216277.3 ENST00000216277.4 ENST00000216277.5 ENST00000216277.6 ENST00000216277.7 ENST00000216277.8 ENST00000216277.9 NM_032632 P51003 PAP PAPOA_HUMAN Q86SX4 Q86TV0 Q8IYF5 Q9BVU2 uc001yfq.1 uc001yfq.2 uc001yfq.3 uc001yfq.4 uc001yfq.5 The protein encoded by this gene belongs to the poly(A) polymerase family. It is required for the addition of adenosine residues for the creation of the 3'-poly(A) tail of mRNAs. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011]. Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C- terminus. Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Binds 2 magnesium ions. Also active with manganese. ; Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and FIP1L1; the interaction with AHCYL1 seems to increase interaction with FIP1L1 (PubMed:19224921). Interacts with NUDT21; the interaction is diminished by acetylation. Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP (By similarity). Cytoplasm. Nucleus. Note=The 90 kDa form is nuclear while the 100 kDa and the 106 kDa forms are both nuclear and cytoplasmic. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P51003-1; Sequence=Displayed; Name=2; IsoId=P51003-2; Sequence=VSP_012895, VSP_012896; Polysumoylated. Varying sumoylation depending on tissue- and cell- type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity). Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity). Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex (By similarity). Belongs to the poly(A) polymerase family. nucleotide binding magnesium ion binding mRNA splicing, via spliceosome RNA binding polynucleotide adenylyltransferase activity protein binding ATP binding nucleus nucleoplasm cytoplasm termination of RNA polymerase II transcription mRNA polyadenylation mRNA processing transferase activity nucleotidyltransferase activity manganese ion binding RNA 3'-end processing mRNA 3'-end processing regulation of mRNA 3'-end processing RNA polyadenylation metal ion binding uc001yfq.1 uc001yfq.2 uc001yfq.3 uc001yfq.4 uc001yfq.5 
ENST00000216281.13 HSP90AA1 ENST00000216281.13 heat shock protein 90 alpha family class A member 1, transcript variant 2 (from RefSeq NM_005348.4) A8K500 B3KPJ9 ENST00000216281.1 ENST00000216281.10 ENST00000216281.11 ENST00000216281.12 ENST00000216281.2 ENST00000216281.3 ENST00000216281.4 ENST00000216281.5 ENST00000216281.6 ENST00000216281.7 ENST00000216281.8 ENST00000216281.9 HS90A_HUMAN HSP90A HSP90AA1 HSPC1 HSPCA NM_005348 P07900 Q2PP14 Q5CAQ6 Q5CAQ7 Q9BVQ5 uc001yku.1 uc001yku.2 uc001yku.3 uc001yku.4 uc001yku.5 uc001yku.6 The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]. Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155, PubMed:12526792). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co- chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812). (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence=; In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation (PubMed:18400751). Upon ATP-binding, the N-terminal domain undergoes significant conformational changes and comes in contact to form an active closed conformation (PubMed:18400751). After HSP90 finishes its chaperoning tasks of assisting the proper folding, stabilization and activation of client proteins under the active state, ATP molecule is hydrolyzed to ADP which then dissociates from HSP90 and directs the protein back to the resting state (PubMed:18400751). Co- chaperone TSC1 promotes ATP binding and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Binding to phosphorylated AHSA1 promotes HSP90AA1 ATPase activity (PubMed:29127155). Inhibited by geldanamycin, Ganetespib (STA-9090) and SNX-2112 (PubMed:29127155, PubMed:12526792). Kinetic parameters: KM=300 uM for ATP ; Homodimer (PubMed:7588731, PubMed:8289821, PubMed:18400751, PubMed:29127155). Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1 (PubMed:15383005, PubMed:9195923). Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex (PubMed:29127155). The closed form interacts (via the middle domain and TPR repeat-binding motif) with co-chaperone TSC1 (via C-terminus) (PubMed:29127155). Interacts with TOM34 (PubMed:9660753). Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex (PubMed:11274138, PubMed:9817749). Interacts with CHORDC1 and DNAJC7 (PubMed:12853476, PubMed:19875381). Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems (PubMed:16307917, PubMed:27353360). Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity (PubMed:15383005, PubMed:15577939, PubMed:16531226, PubMed:27353360). Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (PubMed:11276205). Interacts with KSR1 (PubMed:10409742). Interacts with co-chaperone CDC37 (via C- terminus); the interaction inhibits HSP90AA1 ATPase activity (PubMed:23569206, PubMed:27353360). May interact with NWD1 (PubMed:24681825). Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1 ATPase activity (PubMed:17028174, PubMed:27353360). Interacts with co-chaperone AHSA1 (phosphorylated on 'Tyr-223'); the interaction activates HSP90AA1 ATPase activity and results in the dissociation of TSC1 from HSP90AA1 (PubMed:12604615, PubMed:27353360, PubMed:29127155). Interacts with FLCN in the presence of FNIP1 (PubMed:27353360). Interacts with HSP70, STIP1 and PTGES3 (PubMed:27353360). Interacts with SMYD3; this interaction enhances SMYD3 histone-lysine N-methyltransferase (PubMed:15235609, PubMed:25738358). Interacts with SGTA (via TPR repeats) (PubMed:15708368). Interacts with TTC1 (via TPR repeats) (PubMed:15708368). Interacts with HSF1 in an ATP-dependent manner (PubMed:11583998, PubMed:26517842). Interacts with MET; the interaction suppresses MET kinase activity (PubMed:26517842). Interacts with ERBB2 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity (PubMed:26517842). Interacts with HIF1A, KEAP1 and RHOBTB2 (PubMed:26517842). Interacts with HSF1; this interaction is decreased in a IER5-dependent manner, promoting HSF1 accumulation in the nucleus, homotrimerization and DNA-binding activities (PubMed:26754925). Interacts with STUB1 and SMAD3 (PubMed:24613385). Interacts with HSP90AB1; interaction is constitutive (PubMed:20353823). Interacts with HECTD1 (via N-terminus) (By similarity). Interacts with NR3C1 (via domain NR LBD) and NR1D1 (via domain NR LBD) (By similarity). Interacts with NLPR12 (PubMed:30559449, PubMed:17947705). Interacts with PDCL3 (By similarity). Interacts with TOMM70; the interaction is required for preprotein mitochondrial import (PubMed:12526792). Interacts with TOMM70, IRF3 and TBK1; the interactions are direct and mediate the association of TOMM70 with IRF3 and TBK1 (PubMed:20628368). Forms a complex with ASL, ASS1 and NOS2; the complex regulates cell-autonomous L-arginine synthesis and citrulline recycling while channeling extracellular L-arginine to nitric oxide synthesis pathway. (Microbial infection) Interacts with herpes simplex virus 1 protein US11; this interaction inhibits TBK1-induced interferon production. (Microbial infection) Interacts with N.meningitidis serogroup B adhesin A (nadA). Interaction is stabilized by ADP and 17-AAG (17-N- allylamino-17-demethoxygeldanamycin) and inhibited by ATP. Decreasing HSP90 levels increases adhesion and entry of bacterial into human Chang cells; increasing its levels leads to decreased adhseion and invasion. P07900; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-296047, EBI-10173507; P07900; O95433: AHSA1; NbExp=4; IntAct=EBI-296047, EBI-448610; P07900; P05067: APP; NbExp=5; IntAct=EBI-296047, EBI-77613; P07900; Q9H0C5: BTBD1; NbExp=4; IntAct=EBI-296047, EBI-935503; P07900; Q9UQM7: CAMK2A; NbExp=5; IntAct=EBI-296047, EBI-1383687; P07900; Q8IWD4: CCDC117; NbExp=5; IntAct=EBI-296047, EBI-3387963; P07900; Q9BV29: CCDC32; NbExp=3; IntAct=EBI-296047, EBI-2874058; P07900; Q16543: CDC37; NbExp=14; IntAct=EBI-296047, EBI-295634; P07900; Q7L3B6: CDC37L1; NbExp=2; IntAct=EBI-296047, EBI-2841876; P07900; P50750: CDK9; NbExp=3; IntAct=EBI-296047, EBI-1383449; P07900; Q96G23: CERS2; NbExp=2; IntAct=EBI-296047, EBI-1057080; P07900; Q9UHD1: CHORDC1; NbExp=8; IntAct=EBI-296047, EBI-2550959; P07900; O15111: CHUK; NbExp=3; IntAct=EBI-296047, EBI-81249; P07900; Q6QEF8-4: CORO6; NbExp=3; IntAct=EBI-296047, EBI-10699285; P07900; Q14194: CRMP1; NbExp=3; IntAct=EBI-296047, EBI-473101; P07900; P35222: CTNNB1; NbExp=3; IntAct=EBI-296047, EBI-491549; P07900; Q15438: CYTH1; NbExp=3; IntAct=EBI-296047, EBI-997830; P07900; Q9NR20: DYRK4; NbExp=2; IntAct=EBI-296047, EBI-3914009; P07900; P00533: EGFR; NbExp=7; IntAct=EBI-296047, EBI-297353; P07900; P04626: ERBB2; NbExp=6; IntAct=EBI-296047, EBI-641062; P07900; Q02790: FKBP4; NbExp=8; IntAct=EBI-296047, EBI-1047444; P07900; Q13451: FKBP5; NbExp=8; IntAct=EBI-296047, EBI-306914; P07900; Q14318: FKBP8; NbExp=7; IntAct=EBI-296047, EBI-724839; P07900; P06241: FYN; NbExp=6; IntAct=EBI-296047, EBI-515315; P07900; Q96LI6-3: HSFY2; NbExp=3; IntAct=EBI-296047, EBI-25830912; P07900; P07900: HSP90AA1; NbExp=6; IntAct=EBI-296047, EBI-296047; P07900; Q6PK50: HSP90AB1; NbExp=2; IntAct=EBI-296047, EBI-9356629; P07900; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-296047, EBI-81279; P07900; Q9UHH9: IP6K2; NbExp=2; IntAct=EBI-296047, EBI-747509; P07900; P05412: JUN; NbExp=4; IntAct=EBI-296047, EBI-852823; P07900; Q92993-2: KAT5; NbExp=3; IntAct=EBI-296047, EBI-20795332; P07900; Q6VAB6: KSR2; NbExp=6; IntAct=EBI-296047, EBI-6424389; P07900; P06239: LCK; NbExp=3; IntAct=EBI-296047, EBI-1348; P07900; Q99558: MAP3K14; NbExp=5; IntAct=EBI-296047, EBI-358011; P07900; O43318-2: MAP3K7; NbExp=5; IntAct=EBI-296047, EBI-358700; P07900; P00540: MOS; NbExp=2; IntAct=EBI-296047, EBI-1757866; P07900; P04150: NR3C1; NbExp=8; IntAct=EBI-296047, EBI-493507; P07900; Q8WVJ2: NUDCD2; NbExp=4; IntAct=EBI-296047, EBI-1052153; P07900; P43034: PAFAH1B1; NbExp=5; IntAct=EBI-296047, EBI-720620; P07900; P53041: PPP5C; NbExp=12; IntAct=EBI-296047, EBI-716663; P07900; P17612: PRKACA; NbExp=4; IntAct=EBI-296047, EBI-476586; P07900; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-296047, EBI-743880; P07900; Q96QS6: PSKH2; NbExp=2; IntAct=EBI-296047, EBI-6424813; P07900; Q15185: PTGES3; NbExp=6; IntAct=EBI-296047, EBI-1049387; P07900; P04049: RAF1; NbExp=15; IntAct=EBI-296047, EBI-365996; P07900; Q13127: REST; NbExp=4; IntAct=EBI-296047, EBI-926706; P07900; Q9H6T3: RPAP3; NbExp=6; IntAct=EBI-296047, EBI-356928; P07900; P61247: RPS3A; NbExp=3; IntAct=EBI-296047, EBI-352378; P07900; P12931: SRC; NbExp=3; IntAct=EBI-296047, EBI-621482; P07900; Q15831: STK11; NbExp=3; IntAct=EBI-296047, EBI-306838; P07900; Q9UNE7: STUB1; NbExp=9; IntAct=EBI-296047, EBI-357085; P07900; O94826: TOMM70; NbExp=4; IntAct=EBI-296047, EBI-2800236; P07900; Q9BXA6: TSSK6; NbExp=2; IntAct=EBI-296047, EBI-851883; P07900; P10599: TXN; NbExp=3; IntAct=EBI-296047, EBI-594644; P07900; Q9H6R7-2: WDCP; NbExp=3; IntAct=EBI-296047, EBI-25833271; P07900; P26882: PPID; Xeno; NbExp=4; IntAct=EBI-296047, EBI-6477155; P07900; P35467: S100a1; Xeno; NbExp=4; IntAct=EBI-296047, EBI-6477109; Nucleus Cytoplasm Melanosome Cell membrane Mitochondrion Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=HSP90AA1-1, HSP90-alpha 2; IsoId=P07900-1; Sequence=Displayed; Name=2; Synonyms=HSP90AA1-2; IsoId=P07900-2; Sequence=VSP_026604; The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1. ISGylated. S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways. Belongs to the heat shock protein 90 family. G2/M transition of mitotic cell cycle nucleotide binding positive regulation of protein phosphorylation RNA binding protein binding ATP binding extracellular region nucleus nucleoplasm cytoplasm cytosol plasma membrane protein folding mitochondrial transport receptor-mediated endocytosis response to unfolded protein telomere maintenance via telomerase signal transduction response to heat response to cold cell surface regulation of G2/M transition of mitotic cell cycle membrane ATPase activity cytokine-mediated signaling pathway central nervous system neuron axonogenesis MHC class II protein complex binding establishment of cell polarity nitric-oxide synthase regulator activity TPR domain binding regulation of protein ubiquitination ubiquitin protein ligase binding positive regulation of protein polymerization macromolecular complex positive regulation of peptidyl-serine phosphorylation cellular response to heat secretory granule lumen Fc-gamma receptor signaling pathway involved in phagocytosis ERBB2 signaling pathway protein refolding melanosome ATPase activity, coupled identical protein binding protein homodimerization activity histone deacetylase binding neuronal cell body lysosomal lumen myelin sheath regulation of protein complex assembly neutrophil degranulation protein unfolding protein binding involved in protein folding dendritic growth cone axonal growth cone protein import into mitochondrial outer membrane positive regulation of nitric oxide biosynthetic process response to antibiotic vascular endothelial growth factor receptor signaling pathway tau protein binding perinuclear region of cytoplasm axon extension protein stabilization regulation of nitric-oxide synthase activity GTPase binding unfolded protein binding chaperone-mediated protein complex assembly cofactor metabolic process positive regulation of protein kinase B signaling positive regulation of telomerase activity chaperone-mediated autophagy extracellular exosome DNA polymerase binding endocytic vesicle lumen scaffold protein binding ciliary basal body docking disordered domain specific binding regulation of cellular response to heat positive regulation of tau-protein kinase activity positive regulation of cellular protein catabolic process regulation of cellular protein localization ficolin-1-rich granule lumen telomerase holoenzyme complex assembly protein tyrosine kinase binding uc001yku.1 uc001yku.2 uc001yku.3 uc001yku.4 uc001yku.5 uc001yku.6 
ENST00000216286.10 NID2 ENST00000216286.10 nidogen 2 (from RefSeq NM_007361.4) A8K6I7 B4DU19 ENST00000216286.1 ENST00000216286.2 ENST00000216286.3 ENST00000216286.4 ENST00000216286.5 ENST00000216286.6 ENST00000216286.7 ENST00000216286.8 ENST00000216286.9 NID2_HUMAN NM_007361 O43710 Q14112 uc001wzo.1 uc001wzo.2 uc001wzo.3 uc001wzo.4 uc001wzo.5 This gene encodes a member of the nidogen family of basement membrane proteins. This protein is a cell-adhesion protein that binds collagens I and IV and laminin and may be involved in maintaining the structure of the basement membrane.[provided by RefSeq, Jun 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.169212.1, AJ223500.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216286.10/ ENSP00000216286.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Cell adhesion glycoprotein which is widely distributed in basement membranes. Binds to collagens I and IV, to perlecan and to laminin 1. Does not bind fibulins. It probably has a role in cell- extracellular matrix interactions. Interacts with LAMA2 (By similarity). Interacts with COL13A1. Interacts with EFEMP2 (By similarity). Secreted, extracellular space, extracellular matrix, basement membrane. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q14112-1; Sequence=Displayed; Name=2; IsoId=Q14112-2; Sequence=VSP_038779, VSP_038780; Detected in placenta (at protein level) (PubMed:32337544). Heart and bone. Less in pancreas, kidney and skeletal muscle. Highly N-glycosylated. Highly O-glycosylated (PubMed:19159218). Contains chondroitin sulfate which is attached at Ser-452 and at either Ser-358 or Ser-359 (PubMed:32337544). Sequence=BAA13087.1; Type=Frameshift; Evidence=; Sequence=BAA24112.1; Type=Frameshift; Evidence=; extracellular matrix structural constituent calcium ion binding protein binding collagen binding extracellular region basement membrane plasma membrane cell adhesion cell-matrix adhesion extracellular matrix organization extracellular matrix extracellular exosome basement membrane organization uc001wzo.1 uc001wzo.2 uc001wzo.3 uc001wzo.4 uc001wzo.5 
ENST00000216294.5 SNAPC1 ENST00000216294.5 small nuclear RNA activating complex polypeptide 1 (from RefSeq NM_003082.4) ENST00000216294.1 ENST00000216294.2 ENST00000216294.3 ENST00000216294.4 NM_003082 Q16533 SNAP43 SNPC1_HUMAN uc001xft.1 uc001xft.2 uc001xft.3 uc001xft.4 Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box. Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC1 interacts with SNAPC3, SNAPC4 and TBP. Q16533; Q16204: CCDC6; NbExp=3; IntAct=EBI-11915024, EBI-1045350; Q16533; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-11915024, EBI-742102; Q16533; O14929: HAT1; NbExp=3; IntAct=EBI-11915024, EBI-2339359; Q16533; O75031: HSF2BP; NbExp=3; IntAct=EBI-11915024, EBI-7116203; Q16533; Q92966: SNAPC3; NbExp=4; IntAct=EBI-11915024, EBI-1760638; Nucleus. DNA binding protein binding nucleus nucleoplasm nucleolus snRNA-activating protein complex snRNA transcription from RNA polymerase II promoter snRNA transcription from RNA polymerase III promoter sequence-specific DNA binding uc001xft.1 uc001xft.2 uc001xft.3 uc001xft.4 
ENST00000216297.7 SUPT16H ENST00000216297.7 SPT16 homolog, facilitates chromatin remodeling subunit (from RefSeq NM_007192.4) ENST00000216297.1 ENST00000216297.2 ENST00000216297.3 ENST00000216297.4 ENST00000216297.5 ENST00000216297.6 FACT140 FACTP140 NM_007192 Q6GMT8 Q6P2F1 Q6PJM1 Q9NRX0 Q9Y5B9 SP16H_HUMAN uc001wao.1 uc001wao.2 uc001wao.3 Transcription of protein-coding genes can be reconstituted on naked DNA with only the general transcription factors and RNA polymerase II. However, this minimal system cannot transcribe DNA packaged into chromatin, indicating that accessory factors may facilitate access to DNA. One such factor, FACT (facilitates chromatin transcription), interacts specifically with histones H2A/H2B to effect nucleosome disassembly and transcription elongation. FACT is composed of an 80 kDa subunit and a 140 kDa subunit; this gene encodes the 140 kDa subunit. [provided by RefSeq, Feb 2009]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.184381.1, SRR1803612.96622.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216297.7/ ENSP00000216297.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Interacts with MYOG (via C-terminal region) (By similarity). Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H (PubMed:10421373). Also a component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B (PubMed:11239457, PubMed:12393879). Interacts with NEK9 (PubMed:14660563). Binds to histone H2A-H2B (PubMed:10421373). Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292). Interacts with GTF2E2 (PubMed:10792464). (Microbial infection) Interacts with Herpes simplex virus 1 (HHV-1) protein ICP22; this interaction relocalizes the FACT complex to viral genomes in infected cells. Q9Y5B9; P05067: APP; NbExp=3; IntAct=EBI-1046849, EBI-77613; Q9Y5B9; P33991: MCM4; NbExp=3; IntAct=EBI-1046849, EBI-374938; Q9Y5B9; Q08945: SSRP1; NbExp=6; IntAct=EBI-1046849, EBI-353771; Nucleus Chromosome Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ubiquitous. The C-terminal Glu-rich acidic region is essential for FACT activity. ADP-ribosylated. ADP-ribosylation by PARP1 is induced by genotoxic stress and correlates with dissociation of FACT from chromatin. Neurodevelopmental disorder with dysmorphic facies and thin corpus callosum (NEDDFAC) [MIM:619480]: An autosomal dominant disorder characterized by global developmental delay, impaired intellectual development with poor or absent speech and language, and autistic-like behaviors. Corpus callosum anomalies are visible on brain imaging. Most patients have dysmorphic features including tall forehead, down- slanting palpebral fissures, ear anomalies and broad nasal bridge. Other variably present clinical features include seizures, sleeping difficulties and precocious puberty. Note=The disease may be caused by variants affecting the gene represented in this entry. Belongs to the peptidase M24 family. SPT16 subfamily. Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity. Sequence=AAH64561.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; Sequence=AAH73849.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; RNA binding protein binding nucleus nucleoplasm chromosome DNA replication DNA repair nucleosome disassembly transcription from RNA polymerase II promoter transcription elongation from RNA polymerase II promoter cellular response to DNA damage stimulus nucleosome binding positive regulation of DNA-templated transcription, elongation positive regulation of transcription elongation from RNA polymerase II promoter DNA replication-independent nucleosome organization FACT complex histone binding regulation of signal transduction by p53 class mediator uc001wao.1 uc001wao.2 uc001wao.3 
ENST00000216336.3 CTSG ENST00000216336.3 cathepsin G (from RefSeq NM_001911.3) CATG_HUMAN ENST00000216336.1 ENST00000216336.2 NM_001911 P08311 Q6IBJ6 Q9UCA5 Q9UCU6 uc001wpq.1 uc001wpq.2 uc001wpq.3 uc001wpq.4 uc001wpq.5 The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. In addition, the encoded protein is antimicrobial, with bacteriocidal activity against S. aureus and N. gonorrhoeae. Transcript variants utilizing alternative polyadenylation signals exist for this gene. [provided by RefSeq, Sep 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC014460.1, BI833632.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2149004 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216336.3/ ENSP00000216336.2 Protein has antimicrobial activity :: PMID: 2116408 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Serine protease with trypsin- and chymotrypsin-like specificity (PubMed:8194606, PubMed:29652924). Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity (PubMed:2116408, PubMed:2117044). Prefers Phe and Tyr residues in the P1 position of substrates but also cleaves efficiently after Trp and Leu (PubMed:29652924). Shows a preference for negatively charged amino acids in the P2' position and for aliphatic amino acids both upstream and downstream of the cleavage site (PubMed:29652924). Required for recruitment and activation of platelets which is mediated by the F2RL3/PAR4 platelet receptor (PubMed:3390156, PubMed:10702240). Binds reversibly to and stimulates B cells and CD4(+) and CD8(+) T cells (PubMed:7842483, PubMed:9000539). Also binds reversibly to natural killer (NK) cells and enhances NK cell cytotoxicity through its protease activity (PubMed:9000539, PubMed:9536127). Cleaves complement C3 (PubMed:1861080). Cleaves vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1 and acts as either an agonist or an inhibitor, depending on the F2R cleavage site (PubMed:10702240, PubMed:7744748). Cleavage of F2R at '41-Arg-|- Ser-42' results in receptor activation while cleavage at '55-Phe-|-Trp- 56' results in inhibition of receptor activation (PubMed:7744748). Cleaves the synovial mucin-type protein PRG4/lubricin (PubMed:32144329). Cleaves and activates IL36G which promotes expression of chemokines CXCL1 and CXLC8 in keratinocytes (PubMed:30804664). Cleaves IL33 into mature forms which have greater activity than the unprocessed form (PubMed:22307629). Cleaves coagulation factor F8 to produce a partially activated form (PubMed:18217133). Also cleaves and activates coagulation factor F10 (PubMed:8920993). Cleaves leukocyte cell surface protein SPN/CD43 to releases its extracellular domain and trigger its intramembrane proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus (PubMed:18586676). Cleaves CCL5/RANTES to produce RANTES(4-68) lacking the N-terminal three amino acids which exhibits reduced chemotactic and antiviral activities (PubMed:16963625). During apoptosis, cleaves SMARCA2/BRM to produce a 160 kDa cleavage product which localizes to the cytosol (PubMed:11259672). Cleaves myelin basic protein MBP in B cell lysosomes at '224-Phe-|-Lys-225' and '248-Phe-|-Ser-249', degrading the major immunogenic MBP epitope and preventing the activation of MBP-specific autoreactive T cells (PubMed:15100291). Cleaves annexin ANXA1 and antimicrobial peptide CAMP to produce peptides which act on neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Acts as a ligand for the N-formyl peptide receptor FPR1, enhancing phagocyte chemotaxis (PubMed:15210802). Has antibacterial activity against the Gram-negative bacteria N.gonorrhoeae and P.aeruginosa (PubMed:2116408, PubMed:1937776). Likely to act against N.gonorrhoeae by interacting with N.gonorrhoeae penA/PBP2 (PubMed:2126324). Exhibits potent antimicrobial activity against the Gram-positive bacterium L.monocytogenes (PubMed:2117044). Has antibacterial activity against the Gram-positive bacterium S.aureus and degrades S.aureus biofilms, allowing polymorphonuclear leukocytes to penetrate the biofilm and phagocytose bacteria (PubMed:2117044, PubMed:32995850). Has antibacterial activity against M.tuberculosis (PubMed:15385470). Mediates CASP4 activation induced by the Td92 surface protein of the periodontal pathogen T.denticola, causing production and secretion of IL1A and leading to pyroptosis of gingival fibroblasts (PubMed:29077095). Reaction=Specificity similar to chymotrypsin C.; EC=3.4.21.20; Evidence= Inhibited by soybean trypsin inhibitor, benzamidine, the synthetic peptide R13K, Z-Gly-Leu-Phe-CH2Cl, phenylmethylsulfonyl fluoride, 3,4-dichloroisocoumarin, DFP, SBTI and alpha-1-antitrypsin. Inhibited by LPS from P.aeruginosa but not by LPS from S.minnesota. Not inhibited by elastinal, CMK, TLCK, ETDA or leupeptin. (Microbial infection) Inhibited reversibly by S.aureus EapH1. (Microbial infection) Activity is induced by the Td92 surface protein of the periodontal pathogen T.denticola. Kinetic parameters: KM=1.15 mM for Z-Lys-SBzl ; KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl ; (Microbial infection) Interacts with CASP4; the interaction is promoted by the Td92 surface protein of the periodontal pathogen T.denticola and leads to CASP4 activation. (Microbial infection) Interacts with M.tuberculosis protein Rv3364c. (Microbial infection) Interacts with S.aureus EapH1; EapH1 acts as a reversible inhibitor of CATG activity. P08311; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-5462635, EBI-3867333; P08311; Q15323: KRT31; NbExp=3; IntAct=EBI-5462635, EBI-948001; P08311; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-5462635, EBI-945833; P08311; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5462635, EBI-79165; Cell membrane eripheral membrane protein Cytoplasmic granule Secreted toplasm, cytosol Lysosome Nucleus Note=Secreted by activated neutrophils (PubMed:3390156). Detected in synovial fluid (PubMed:32144329). Localizes to lysosomes in B cells where it is not endogenously synthesized but is internalized from the cell membrane (PubMed:15100291). Localizes to the nucleus during apoptosis (PubMed:11259672). Expressed in neutrophils (at protein level) (PubMed:3799965). Expressed in B cells (PubMed:15100291). Induced by the Td92 surface protein of the periodontal pathogen T.denticola (PubMed:29077095). Down-regulated in monocytes following M.tuberculosis infection and exposure to bacterial lipopolysaccharide which coincides with increased M.tuberculosis replication and intracellular survival (PubMed:15385470). Two C-terminal truncation variants have been identified, one which ends at Arg-243 and one which ends at Ser-244. Belongs to the peptidase S1 family. angiotensin maturation serine-type endopeptidase activity protein binding extracellular region extracellular space nucleus cytoplasm plasma membrane protein phosphorylation proteolysis immune response heparin binding peptidase activity serine-type peptidase activity cell surface cytoplasmic stress granule hydrolase activity antimicrobial humoral response antibacterial humoral response extracellular matrix disassembly secretory granule response to lipopolysaccharide azurophil granule lumen defense response to bacterium neutrophil degranulation cellular protein metabolic process positive regulation of immune response defense response to Gram-negative bacterium defense response to Gram-positive bacterium defense response to fungus extracellular exosome neutrophil mediated killing of gram-positive bacterium cellular response to lipopolysaccharide uc001wpq.1 uc001wpq.2 uc001wpq.3 uc001wpq.4 uc001wpq.5 
ENST00000216338.9 GZMH ENST00000216338.9 granzyme H, transcript variant 1 (from RefSeq NM_033423.5) CGL2 CTSGL2 ENST00000216338.1 ENST00000216338.2 ENST00000216338.3 ENST00000216338.4 ENST00000216338.5 ENST00000216338.6 ENST00000216338.7 ENST00000216338.8 G3V2C5 GRAH_HUMAN NM_033423 P20718 Q6XGZ0 Q6XGZ1 uc001wpr.1 uc001wpr.2 uc001wpr.3 uc001wpr.4 This gene encodes a member of the peptidase S1 family of serine proteases. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate a chymotrypsin-like protease. This protein is reported to be constitutively expressed in the NK (natural killer) cells of the immune system and may play a role in the cytotoxic arm of the innate immune response by inducing target cell death and by directly cleaving substrates in pathogen-infected cells. This gene is present in a gene cluster with another member of the granzyme subfamily on chromosome 14. [provided by RefSeq, Nov 2015]. Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication. Inhibited by SERPINB1. Cytolytic granule Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P20718-1; Sequence=Displayed; Name=2; IsoId=P20718-2; Sequence=VSP_047073; Name=3; IsoId=P20718-3; Sequence=VSP_047573; Constitutively expressed in NK cells. Belongs to the peptidase S1 family. Granzyme subfamily. serine-type endopeptidase activity cytoplasm proteolysis apoptotic process peptidase activity serine-type peptidase activity granzyme-mediated apoptotic signaling pathway membrane hydrolase activity cytolysis uc001wpr.1 uc001wpr.2 uc001wpr.3 uc001wpr.4 
ENST00000216341.9 GZMB ENST00000216341.9 granzyme B, transcript variant 1 (from RefSeq NM_004131.6) CGL1 CSPB CTLA1 ENST00000216341.1 ENST00000216341.2 ENST00000216341.3 ENST00000216341.4 ENST00000216341.5 ENST00000216341.6 ENST00000216341.7 ENST00000216341.8 GRAB_HUMAN GRB GZMB NM_004131 P10144 Q8N1D2 Q9UCC1 uc001wps.1 uc001wps.2 uc001wps.3 uc001wps.4 uc001wps.5 This gene encodes a member of the granzyme subfamily of proteins, part of the peptidase S1 family of serine proteases. The encoded preproprotein is secreted by natural killer (NK) cells and cytotoxic T lymphocytes (CTLs) and proteolytically processed to generate the active protease, which induces target cell apoptosis. This protein also processes cytokines and degrades extracellular matrix proteins, and these roles are implicated in chronic inflammation and wound healing. Expression of this gene may be elevated in human patients with cardiac fibrosis. [provided by RefSeq, Sep 2016]. Abundant protease in the cytosolic granules of cytotoxic T- cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:3262682, PubMed:3263427, PubMed:1985927). It cleaves after Asp (PubMed:8258716, PubMed:1985927). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore- forming moiety of GSDME, thereby triggering pyroptosis and target cell death (PubMed:32188940, PubMed:31953257). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -9 and -10 (CASP3, CASP9 and CASP10, respectively) to give rise to active enzymes mediating apoptosis (PubMed:9852092). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity). Reaction=Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|- Xaa-, -Ser-|-Xaa-.; EC=3.4.21.79; Evidence= Inactivated by the serine protease inhibitor diisopropylfluorophosphate. P10144; P14222: PRF1; NbExp=3; IntAct=EBI-2505785, EBI-724466; P10144; P10124: SRGN; NbExp=2; IntAct=EBI-2505785, EBI-744915; Secreted tolytic granule te=Delivered into the target cell by perforin (PubMed:20038786). By staphylococcal enterotoxin A (SEA) in peripheral blood leukocytes. Belongs to the peptidase S1 family. Granzyme subfamily. immunological synapse serine-type endopeptidase activity protein binding nucleus cytoplasm mitochondrion cytosol proteolysis apoptotic process peptidase activity serine-type peptidase activity granzyme-mediated apoptotic signaling pathway membrane hydrolase activity cytolysis natural killer cell mediated cytotoxicity positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway uc001wps.1 uc001wps.2 uc001wps.3 uc001wps.4 uc001wps.5 
ENST00000216367.10 POLE2 ENST00000216367.10 DNA polymerase epsilon 2, accessory subunit, transcript variant 1 (from RefSeq NM_002692.4) A0AV55 A4FU92 A4LBB7 A6NH58 B4DDE6 DPE2 DPOE2_HUMAN ENST00000216367.1 ENST00000216367.2 ENST00000216367.3 ENST00000216367.4 ENST00000216367.5 ENST00000216367.6 ENST00000216367.7 ENST00000216367.8 ENST00000216367.9 NM_002692 O43560 P56282 POLE2 uc001wwu.1 uc001wwu.2 uc001wwu.3 uc001wwu.4 uc001wwu.5 DNA polymerase epsilon, which is involved in DNA repair and replication, is composed of a large catalytic subunit and a small accessory subunit. The protein encoded by this gene represents the small subunit (B). Defects in this gene have been linked to colorectal cancer and to combined immunodeficiency. [provided by RefSeq, Jan 2017]. Accessory component of the DNA polymerase epsilon complex (PubMed:10801849). Participates in DNA repair and in chromosomal DNA replication (By similarity). Component of the DNA polymerase epsilon complex consisting of four subunits: the catalytic subunit POLE and the accessory subunits POLE2, POLE3 and POLE4. P56282; P52594: AGFG1; NbExp=3; IntAct=EBI-713847, EBI-996560; P56282; Q9NPD3: EXOSC4; NbExp=5; IntAct=EBI-713847, EBI-371823; P56282; V9HWB8: HEL-S-30; NbExp=3; IntAct=EBI-713847, EBI-10215395; P56282; Q15691: MAPRE1; NbExp=6; IntAct=EBI-713847, EBI-1004115; P56282; Q07864: POLE; NbExp=8; IntAct=EBI-713847, EBI-348526; P56282; Q04864: REL; NbExp=3; IntAct=EBI-713847, EBI-307352; P56282; O60504: SORBS3; NbExp=3; IntAct=EBI-713847, EBI-741237; P56282; Q96SF7: TBX15; NbExp=3; IntAct=EBI-713847, EBI-10191361; P56282; P14373: TRIM27; NbExp=7; IntAct=EBI-713847, EBI-719493; P56282; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-713847, EBI-947187; P56282; O96006: ZBED1; NbExp=3; IntAct=EBI-713847, EBI-740037; P56282; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-713847, EBI-4395669; Nucleus. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P56282-1; Sequence=Displayed; Name=2; IsoId=P56282-2; Sequence=VSP_042551; Name=3; IsoId=P56282-3; Sequence=VSP_043796; In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis. Belongs to the DNA polymerase epsilon subunit B family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/pole2/"; G1/S transition of mitotic cell cycle DNA binding DNA-directed DNA polymerase activity protein binding nucleus nucleoplasm DNA replication DNA-dependent DNA replication DNA replication initiation DNA repair epsilon DNA polymerase complex nuclear body transferase activity nucleotidyltransferase activity telomere maintenance via semi-conservative replication error-prone translesion synthesis intracellular membrane-bounded organelle uc001wwu.1 uc001wwu.2 uc001wwu.3 uc001wwu.4 uc001wwu.5 
ENST00000216373.10 SOS2 ENST00000216373.10 SOS Ras/Rho guanine nucleotide exchange factor 2, transcript variant 1 (from RefSeq NM_006939.4) B7ZKT6 D3DSB4 ENST00000216373.1 ENST00000216373.2 ENST00000216373.3 ENST00000216373.4 ENST00000216373.5 ENST00000216373.6 ENST00000216373.7 ENST00000216373.8 ENST00000216373.9 NM_006939 Q07890 Q15503 Q17RN1 SOS2_HUMAN uc001wxs.1 uc001wxs.2 uc001wxs.3 uc001wxs.4 uc001wxs.5 uc001wxs.6 This gene encodes a regulatory protein that is involved in the positive regulation of ras proteins. Mutations in this gene are associated with Noonan Syndrome-9. [provided by RefSeq, Jul 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803617.78693.1, SRR1803614.79798.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216373.10/ ENSP00000216373.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Promotes the exchange of Ras-bound GDP by GTP. Q07890; P00519: ABL1; NbExp=2; IntAct=EBI-298181, EBI-375543; Q07890; P46108: CRK; NbExp=2; IntAct=EBI-298181, EBI-886; Q07890; P62993: GRB2; NbExp=11; IntAct=EBI-298181, EBI-401755; Q07890; P16333: NCK1; NbExp=3; IntAct=EBI-298181, EBI-389883; Q07890; Q9UKS6: PACSIN3; NbExp=2; IntAct=EBI-298181, EBI-77926; Q07890; P19174: PLCG1; NbExp=4; IntAct=EBI-298181, EBI-79387; Q07890; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-298181, EBI-77848; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q07890-1; Sequence=Displayed; Name=2; IsoId=Q07890-2; Sequence=VSP_054492; Noonan syndrome 9 (NS9) [MIM:616559]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Note=The disease is caused by variants affecting the gene represented in this entry. Name=Wikipedia; Note=Son of sevenless entry; URL="https://en.wikipedia.org/wiki/Son_of_Sevenless"; nucleosome DNA binding guanyl-nucleotide exchange factor activity Rho guanyl-nucleotide exchange factor activity protein binding cytosol G-protein coupled receptor signaling pathway small GTPase mediated signal transduction regulation of Rho protein signal transduction positive regulation of apoptotic process protein heterodimerization activity regulation of small GTPase mediated signal transduction positive regulation of small GTPase mediated signal transduction uc001wxs.1 uc001wxs.2 uc001wxs.3 uc001wxs.4 uc001wxs.5 uc001wxs.6 
ENST00000216392.8 PYGL ENST00000216392.8 glycogen phosphorylase L, transcript variant 1 (from RefSeq NM_002863.5) A6NDQ4 B4DUB7 ENST00000216392.1 ENST00000216392.2 ENST00000216392.3 ENST00000216392.4 ENST00000216392.5 ENST00000216392.6 ENST00000216392.7 F5H816 NM_002863 O60567 O60752 O60913 P06737 PYGL PYGL_HUMAN Q501V9 Q641R5 Q96G82 uc001wyu.1 uc001wyu.2 uc001wyu.3 uc001wyu.4 uc001wyu.5 This gene encodes a homodimeric protein that catalyses the cleavage of alpha-1,4-glucosidic bonds to release glucose-1-phosphate from liver glycogen stores. This protein switches from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of this enzyme is further regulated by multiple allosteric effectors and hormonal controls. Humans have three glycogen phosphorylase genes that encode distinct isozymes that are primarily expressed in liver, brain and muscle, respectively. The liver isozyme serves the glycemic demands of the body in general while the brain and muscle isozymes supply just those tissues. In glycogen storage disease type VI, also known as Hers disease, mutations in liver glycogen phosphorylase inhibit the conversion of glycogen to glucose and results in moderate hypoglycemia, mild ketosis, growth retardation and hepatomegaly. Alternative splicing results in multiple transcript variants encoding different isoforms.[provided by RefSeq, Feb 2011]. Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733; Evidence=; Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence= Allosterically regulated through the non-covalent binding of metabolites, being activated by AMP and inhibited by ATP, ADP, and glucose-6-phosphate. The activity is also controlled by post- translational modifications including phosphorylation and acetylation. Homodimer; enzymatically active (PubMed:10980448, PubMed:10949035). Interacts with PPP1R3B; recruits the phosphatase PP1 which dephosphorylates and inactivates PYGL/glycogen phosphorylase (PubMed:22225877). P06737; P11216: PYGB; NbExp=9; IntAct=EBI-2511865, EBI-1047231; P06737; P11217: PYGM; NbExp=3; IntAct=EBI-2511865, EBI-357469; Cytoplasm, cytosol Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P06737-1; Sequence=Displayed; Name=2; IsoId=P06737-2; Sequence=VSP_045339; Acetylation, which is up-regulated by glucose and insulin and down-regulated by glucagon, inhibits the glycogen phosphorylase activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1 and Ser-15 dephosphorylation. Phosphorylation at Ser-15 converts inactive phosphorylase b into active phosphorylase a (PubMed:10949035). Dephosphorylation of Ser-15 by phosphatase PP1 inactivates the enzyme (PubMed:22225877). Glycogen storage disease 6 (GSD6) [MIM:232700]: A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycogen phosphorylase family. nucleotide binding purine nucleobase binding catalytic activity phosphorylase activity protein binding ATP binding glucose binding extracellular region cytoplasm cytosol carbohydrate metabolic process glycogen metabolic process glycogen catabolic process 5-phosphoribose 1-diphosphate biosynthetic process drug binding metabolic process glycogen phosphorylase activity response to bacterium AMP binding transferase activity transferase activity, transferring glycosyl groups vitamin binding pyridoxal phosphate binding carbohydrate binding bile acid binding secretory granule lumen glucose homeostasis protein homodimerization activity neutrophil degranulation extracellular exosome necroptotic process ficolin-1-rich granule lumen uc001wyu.1 uc001wyu.2 uc001wyu.3 uc001wyu.4 uc001wyu.5 
ENST00000216410.8 GNPNAT1 ENST00000216410.8 glucosamine-phosphate N-acetyltransferase 1 (from RefSeq NM_198066.4) ENST00000216410.1 ENST00000216410.2 ENST00000216410.3 ENST00000216410.4 ENST00000216410.5 ENST00000216410.6 ENST00000216410.7 GNA1 GNA1_HUMAN NM_198066 Q96EK6 uc001xab.1 uc001xab.2 uc001xab.3 uc001xab.4 uc001xab.5 Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N- acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4; Evidence=; Kinetic parameters: KM=26 uM for acetyl-coenzyme A ; KM=97 uM for glucosamine-6-phosphate ; Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2. Homodimer. Q96EK6; Q96EK6: GNPNAT1; NbExp=2; IntAct=EBI-3913338, EBI-3913338; Q96EK6; P28062-2: PSMB8; NbExp=3; IntAct=EBI-3913338, EBI-372312; Golgi apparatus membrane; Peripheral membrane protein. Endosome membrane ; Peripheral membrane protein Rhizomelic dysplasia, Ain-Naz type (RHZDAN) [MIM:619598]: An autosomal recessive skeletal dysplasia characterized by short stature, marked rhizomelic shortening of the limbs, platyspondyly, hip dysplasia, and large hands and feet relative to height. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the acetyltransferase family. GNA1 subfamily. Golgi membrane liver development glucosamine 6-phosphate N-acetyltransferase activity endosome late endosome endoplasmic reticulum endoplasmic reticulum-Golgi intermediate compartment Golgi apparatus cytosol glucosamine metabolic process N-acetylglucosamine metabolic process UDP-N-acetylglucosamine biosynthetic process N-acetyltransferase activity endosome membrane membrane transferase activity transferase activity, transferring acyl groups identical protein binding monosaccharide binding cellular response to leukemia inhibitory factor uc001xab.1 uc001xab.2 uc001xab.3 uc001xab.4 uc001xab.5 
ENST00000216416.9 CNIH1 ENST00000216416.9 cornichon family AMPA receptor auxiliary protein 1 (from RefSeq NM_005776.3) CNIH CNIH1_HUMAN CNIL ENST00000216416.1 ENST00000216416.2 ENST00000216416.3 ENST00000216416.4 ENST00000216416.5 ENST00000216416.6 ENST00000216416.7 ENST00000216416.8 NM_005776 O95406 Q3SYM7 UNQ155/PRO181 uc001xat.1 uc001xat.2 uc001xat.3 Involved in the selective transport and maturation of TGF- alpha family proteins. Interacts with AREG immature precursor and with immature TGFA, i.e. with a prosegment and lacking full N-glycosylation, but not with the fully N-glycosylated form. In the Golgi apparatus, may form a complex with GORASP55 and transmembrane TGFA. O95406; Q13520: AQP6; NbExp=3; IntAct=EBI-12172273, EBI-13059134; O95406; Q13323: BIK; NbExp=3; IntAct=EBI-12172273, EBI-700794; O95406; P19397: CD53; NbExp=3; IntAct=EBI-12172273, EBI-6657396; O95406; P11912: CD79A; NbExp=3; IntAct=EBI-12172273, EBI-7797864; O95406; O95471: CLDN7; NbExp=3; IntAct=EBI-12172273, EBI-740744; O95406; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-12172273, EBI-18013275; O95406; P00387: CYB5R3; NbExp=3; IntAct=EBI-12172273, EBI-1046040; O95406; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12172273, EBI-781551; O95406; P34910-2: EVI2B; NbExp=3; IntAct=EBI-12172273, EBI-17640610; O95406; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12172273, EBI-18304435; O95406; O15552: FFAR2; NbExp=3; IntAct=EBI-12172273, EBI-2833872; O95406; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12172273, EBI-13345167; O95406; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12172273, EBI-11721746; O95406; P28335: HTR2C; NbExp=3; IntAct=EBI-12172273, EBI-994141; O95406; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12172273, EBI-17490413; O95406; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-12172273, EBI-358888; O95406; Q8IX19: MCEMP1; NbExp=3; IntAct=EBI-12172273, EBI-2816356; O95406; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12172273, EBI-11956541; O95406; Q6IN84: MRM1; NbExp=3; IntAct=EBI-12172273, EBI-5454865; O95406; P35372-10: OPRM1; NbExp=3; IntAct=EBI-12172273, EBI-12807478; O95406; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-12172273, EBI-13044680; O95406; Q96DD7: SHISA4; NbExp=3; IntAct=EBI-12172273, EBI-18035902; O95406; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12172273, EBI-18159983; O95406; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-12172273, EBI-17595455; O95406; A1A5C7-2: SLC22A23; NbExp=3; IntAct=EBI-12172273, EBI-12081840; O95406; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-12172273, EBI-17295964; O95406; Q9BZL3: SMIM3; NbExp=6; IntAct=EBI-12172273, EBI-741850; O95406; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12172273, EBI-18178701; Endoplasmic reticulum membrane ; Multi-pass membrane protein Golgi apparatus membrane Note=Located primarily in the ER; may cycle between the ER and the Golgi apparatus. Highly expressed in heart, liver, skeletal muscle, pancreas, adrenal medulla and cortex, thyroid, testis, spleen, appendix, peripheral blood lymphocytes and bone marrow. Lower expression found in brain, placenta, lung, kidney, ovary, small intestine, stomach, lymph node, thymus and fetal liver. Expression is up-regulated in dorsolateral prefrontal cortex of patients with schizophrenia (postmortem brain study). Belongs to the cornichon family. Golgi membrane endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus ER to Golgi vesicle-mediated transport immune response signal transduction ER to Golgi transport vesicle membrane membrane integral component of membrane vesicle-mediated transport endoplasmic reticulum-Golgi intermediate compartment membrane COPII vesicle coating uc001xat.1 uc001xat.2 uc001xat.3 
ENST00000216420.12 CGRRF1 ENST00000216420.12 cell growth regulator with ring finger domain 1 (from RefSeq NM_006568.3) CGR19 CGRF1_HUMAN ENST00000216420.1 ENST00000216420.10 ENST00000216420.11 ENST00000216420.2 ENST00000216420.3 ENST00000216420.4 ENST00000216420.5 ENST00000216420.6 ENST00000216420.7 ENST00000216420.8 ENST00000216420.9 NM_006568 Q96BX2 Q99675 RNF197 uc001xay.1 uc001xay.2 uc001xay.3 uc001xay.4 uc001xay.5 Able to inhibit growth in several cell lines. Q99675; Q8TD06: AGR3; NbExp=3; IntAct=EBI-2130213, EBI-3925742; Q99675; O15155: BET1; NbExp=3; IntAct=EBI-2130213, EBI-749204; Q99675; P21854: CD72; NbExp=3; IntAct=EBI-2130213, EBI-307924; Q99675; O14735: CDIPT; NbExp=3; IntAct=EBI-2130213, EBI-358858; Q99675; O43169: CYB5B; NbExp=3; IntAct=EBI-2130213, EBI-1058710; Q99675; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-2130213, EBI-12118888; Q99675; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-2130213, EBI-12142299; Q99675; O15552: FFAR2; NbExp=3; IntAct=EBI-2130213, EBI-2833872; Q99675; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-2130213, EBI-11955647; Q99675; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2130213, EBI-13345167; Q99675; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2130213, EBI-10266796; Q99675; P26715: KLRC1; NbExp=3; IntAct=EBI-2130213, EBI-9018187; Q99675; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-2130213, EBI-3267258; Q99675; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-2130213, EBI-12133176; Q99675; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-2130213, EBI-2341610; Q99675; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-2130213, EBI-3923617; Q99675; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-2130213, EBI-12092917; Q99675; Q8TEB9: RHBDD1; NbExp=3; IntAct=EBI-2130213, EBI-9916444; Q99675; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-2130213, EBI-4403649; Q99675; Q99726: SLC30A3; NbExp=3; IntAct=EBI-2130213, EBI-10294651; Q99675; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-2130213, EBI-10262251; Q99675; Q96L08: SUSD3; NbExp=3; IntAct=EBI-2130213, EBI-18194029; Q99675; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-2130213, EBI-2844246; Q99675; Q14656: TMEM187; NbExp=3; IntAct=EBI-2130213, EBI-13046724; Q99675; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-2130213, EBI-12111910; Q99675; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-2130213, EBI-17249488; Q99675; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-2130213, EBI-751210; Q99675; O95159: ZFPL1; NbExp=3; IntAct=EBI-2130213, EBI-718439; Nucleus Endoplasmic reticulum Ubiquitously expressed with high expression in testis and the cerebellum. Up-regulated by endoplasmic reticulum (ER) stress triggered by thapsigargin or tunicamycin. nucleus nucleoplasm endoplasmic reticulum cell cycle cell cycle arrest negative regulation of cell proliferation intracellular membrane-bounded organelle metal ion binding uc001xay.1 uc001xay.2 uc001xay.3 uc001xay.4 uc001xay.5 
ENST00000216442.12 ATP6V1D ENST00000216442.12 ATPase H+ transporting V1 subunit D (from RefSeq NM_015994.4) ATP6M B2RE33 ENST00000216442.1 ENST00000216442.10 ENST00000216442.11 ENST00000216442.2 ENST00000216442.3 ENST00000216442.4 ENST00000216442.5 ENST00000216442.6 ENST00000216442.7 ENST00000216442.8 ENST00000216442.9 NM_015994 Q9Y5K8 Q9Y688 VATD VATD_HUMAN uc001xjf.1 uc001xjf.2 uc001xjf.3 uc001xjf.4 uc001xjf.5 This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes the V1 domain D subunit protein. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.236310.1, SRR1803613.130608.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216442.12/ ENSP00000216442.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (PubMed:21844891). V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (PubMed:33065002). The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (PubMed:33065002). The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002). Interacts with SNX10 (PubMed:21844891). Q9Y5K8; Q16864: ATP6V1F; NbExp=3; IntAct=EBI-2684998, EBI-714690; Q9Y5K8; Q9BUW7: BBLN; NbExp=5; IntAct=EBI-2684998, EBI-752084; Q9Y5K8; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-2684998, EBI-2514791; Q9Y5K8; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2684998, EBI-3044087; Q9Y5K8; O14777: NDC80; NbExp=3; IntAct=EBI-2684998, EBI-715849; Q9Y5K8; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-2684998, EBI-2799833; Membrane ; Peripheral membrane protein ; Cytoplasmic side Cytoplasmic vesicle, clathrin- coated vesicle membrane ; Peripheral membrane protein Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium Note=Localizes to centrosome and the base of the cilium. Belongs to the V-ATPase D subunit family. protein binding lysosomal membrane cytosol plasma membrane ion transport insulin receptor signaling pathway membrane regulation of macroautophagy cell projection organization proton-transporting V-type ATPase complex transferrin transport ion transmembrane transport specific granule membrane ATPase activity, coupled to transmembrane movement of substances neutrophil degranulation proton-transporting ATPase activity, rotational mechanism cilium assembly protein localization to cilium extracellular exosome phagosome acidification hydrogen ion transmembrane transport centrosome cilium uc001xjf.1 uc001xjf.2 uc001xjf.3 uc001xjf.4 uc001xjf.5 
ENST00000216445.8 CCDC198 ENST00000216445.8 coiled-coil domain containing 198, transcript variant 2 (from RefSeq NM_018168.4) C14orf105 CCDC198 ENST00000216445.1 ENST00000216445.2 ENST00000216445.3 ENST00000216445.4 ENST00000216445.5 ENST00000216445.6 ENST00000216445.7 FAME FAME_HUMAN NM_018168 Q17R99 Q53G04 Q9NVL8 uc001xcy.1 uc001xcy.2 uc001xcy.3 uc001xcy.4 uc001xcy.5 May be involved in tuning the metabolism, energy expenditure, and excretion processes. Q9NVL8; Q8NA61: CBY2; NbExp=3; IntAct=EBI-10238351, EBI-741724; Q9NVL8; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-10238351, EBI-10175124; Q9NVL8; Q13643: FHL3; NbExp=3; IntAct=EBI-10238351, EBI-741101; Q9NVL8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10238351, EBI-618309; Q9NVL8; Q6A162: KRT40; NbExp=3; IntAct=EBI-10238351, EBI-10171697; Q9NVL8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10238351, EBI-741037; Q9NVL8; Q99750: MDFI; NbExp=3; IntAct=EBI-10238351, EBI-724076; Q9NVL8; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10238351, EBI-742948; Q9NVL8; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-10238351, EBI-1105124; Q9NVL8; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10238351, EBI-302345; Q9NVL8; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-10238351, EBI-747107; Q9NVL8; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-10238351, EBI-2212028; Q9NVL8; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-10238351, EBI-742397; Q9NVL8; Q13077: TRAF1; NbExp=3; IntAct=EBI-10238351, EBI-359224; Q9NVL8; Q12933: TRAF2; NbExp=3; IntAct=EBI-10238351, EBI-355744; Q9NVL8; P14373: TRIM27; NbExp=3; IntAct=EBI-10238351, EBI-719493; Cell membrane ; Peripheral membrane protein Cytoplasmic vesicle Note=The localization of CCDC198 changes from membranous to vesicle-forming structures in the malignant tissue. protein binding uc001xcy.1 uc001xcy.2 uc001xcy.3 uc001xcy.4 uc001xcy.5 
ENST00000216446.9 PLEK2 ENST00000216446.9 pleckstrin 2 (from RefSeq NM_016445.3) ENST00000216446.1 ENST00000216446.2 ENST00000216446.3 ENST00000216446.4 ENST00000216446.5 ENST00000216446.6 ENST00000216446.7 ENST00000216446.8 NM_016445 PLEK2_HUMAN Q96JT0 Q9NYT0 uc001xjh.1 uc001xjh.2 uc001xjh.3 The protein encoded by this gene associates with membrane-bound phosphatidylinositols generated by phosphatidylinositol 3-kinase. The encoded protein then interacts with the actin cytoskeleton to induce cell spreading. In conjunction with complement component 1, q subcomponent, B chain (C1QB), this gene shows an increase in expression in melanoma cells and may serve as an accurate biomarker for the disease. [provided by RefSeq, Dec 2015]. ##Evidence-Data-START## Transcript exon combination :: SRR5189658.122977.1, BC001226.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145893, SAMEA2146411 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216446.9/ ENSP00000216446.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May help orchestrate cytoskeletal arrangement. Contribute to lamellipodia formation. Cell projection, lamellipodium membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. cytoplasm cytoskeleton plasma membrane membrane actin cytoskeleton organization lamellipodium membrane positive regulation of cell projection organization actin cytoskeleton reorganization phosphatidylinositol-3-phosphate binding intracellular signal transduction cell projection phosphatidylinositol-3,4-bisphosphate binding phosphatidylinositol-3,5-bisphosphate binding uc001xjh.1 uc001xjh.2 uc001xjh.3 
ENST00000216452.9 PIGH ENST00000216452.9 phosphatidylinositol glycan anchor biosynthesis class H, transcript variant 1 (from RefSeq NM_004569.5) B2RAA4 ENST00000216452.1 ENST00000216452.2 ENST00000216452.3 ENST00000216452.4 ENST00000216452.5 ENST00000216452.6 ENST00000216452.7 ENST00000216452.8 NM_004569 PIGH PIGH_HUMAN Q14442 uc001xjr.1 uc001xjr.2 uc001xjr.3 This gene encodes an endoplasmic reticulum associated protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI anchor is a glycolipid found on many blood cells and which serves to anchor proteins to the cell surface. The protein encoded by this gene is a subunit of the GPI N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to phosphatidylinositol (PI) on the cytoplasmic side of the endoplasmic reticulum. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.5166.1, SRR1803613.53054.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216452.9/ ENSP00000216452.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Part of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. Component of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex composed at least by PIGA, PIGC, PIGH, PIGP, PIGQ, PIGY and DPM2 (PubMed:16162815, PubMed:9463366). Interacts with PIGQ (PubMed:9463366). Q14442; P37287: PIGA; NbExp=5; IntAct=EBI-2803676, EBI-26643054; Cytoplasm. Glycosylphosphatidylinositol biosynthesis defect 17 (GPIBD17) [MIM:618010]: An autosomal recessive disorder characterized by variable neurologic deficits that become apparent in infancy or early childhood. Clinical features include learning disabilities, mild-to-moderate developmental delay, seizures of variable severity, aggressive or over- friendly behavior, and autistic features. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the PIGH family. Name=Functional Glycomics Gateway - GTase; Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit H; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_557"; glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex catalytic activity cytoplasm endoplasmic reticulum endoplasmic reticulum membrane cellular protein modification process GPI anchor biosynthetic process preassembly of GPI anchor in ER membrane transferase activity transferase activity, transferring glycosyl groups phosphatidylinositol N-acetylglucosaminyltransferase activity uc001xjr.1 uc001xjr.2 uc001xjr.3 
ENST00000216455.9 PSMA3 ENST00000216455.9 proteasome 20S subunit alpha 3, transcript variant 1 (from RefSeq NM_002788.4) B2RCK6 ENST00000216455.1 ENST00000216455.2 ENST00000216455.3 ENST00000216455.4 ENST00000216455.5 ENST00000216455.6 ENST00000216455.7 ENST00000216455.8 HC8 NM_002788 P25788 PSA3_HUMAN PSC8 Q86U83 Q8N1D8 Q9BS70 uc001xdj.1 uc001xdj.2 uc001xdj.3 uc001xdj.4 The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Two alternative transcripts encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]. Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP- dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin- independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits (PubMed:25599644, PubMed:26133119, PubMed:26657688, PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951). The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings (PubMed:25599644, PubMed:26133119, PubMed:26657688, PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951). The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits (PubMed:25599644, PubMed:26133119, PubMed:26657688, PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951). The proteolytic activity is exerted by three beta- subunits PSMB5, PSMB6 and PSMB7 (PubMed:25599644, PubMed:26133119, PubMed:26657688, PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951). Interacts with AURKB (PubMed:14674694). Interacts with CDKN1A (PubMed:11350925). Interacts with MDM2 and RB1 (PubMed:16337594). Interacts with the C-terminus of TBXA2R isoform 2 (PubMed:17499743). Interacts with DNAJB2 (PubMed:15936278). (Microbial infection) Interacts with HIV-1 Tat protein. (Microbial infection) Interacts with hepatitis C virus (HCV) F protein. (Microbial infection) Interacts with Epstein-Barr virus EBNA3 proteins. P25788; P27449: ATP6V0C; NbExp=3; IntAct=EBI-348380, EBI-721179; P25788; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-348380, EBI-8648738; P25788; O95561: C1orf105; NbExp=3; IntAct=EBI-348380, EBI-10191951; P25788; Q96CW7: C4orf42; NbExp=3; IntAct=EBI-348380, EBI-752053; P25788; Q9NRJ3: CCL28; NbExp=3; IntAct=EBI-348380, EBI-7783254; P25788; Q9BUF7: CRB3; NbExp=3; IntAct=EBI-348380, EBI-9844372; P25788; P09228: CST2; NbExp=3; IntAct=EBI-348380, EBI-8832659; P25788; Q7Z3D6: DGLUCY; NbExp=3; IntAct=EBI-348380, EBI-2807872; P25788; Q14565: DMC1; NbExp=7; IntAct=EBI-348380, EBI-930865; P25788; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-348380, EBI-9679045; P25788; Q8N0U1: FAM171A2; NbExp=3; IntAct=EBI-348380, EBI-10264767; P25788; Q96MZ4: FAM218A; NbExp=3; IntAct=EBI-348380, EBI-10291578; P25788; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-348380, EBI-1384254; P25788; Q96D16: FBXL18; NbExp=3; IntAct=EBI-348380, EBI-744419; P25788; Q9Y3I1: FBXO7; NbExp=6; IntAct=EBI-348380, EBI-1161222; P25788; P23769: GATA2; NbExp=4; IntAct=EBI-348380, EBI-2806671; P25788; P23771: GATA3; NbExp=3; IntAct=EBI-348380, EBI-6664760; P25788; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-348380, EBI-739467; P25788; Q8N779: hCG_1998195; NbExp=3; IntAct=EBI-348380, EBI-10267476; P25788; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-348380, EBI-10188461; P25788; Q6IPM2: IQCE; NbExp=4; IntAct=EBI-348380, EBI-3893098; P25788; Q6UWL6: KIRREL2; NbExp=3; IntAct=EBI-348380, EBI-10254473; P25788; Q8N7Y1: KIRREL3-AS3; NbExp=3; IntAct=EBI-348380, EBI-10267656; P25788; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-348380, EBI-1048945; P25788; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-348380, EBI-3957672; P25788; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-348380, EBI-10261141; P25788; Q14847: LASP1; NbExp=3; IntAct=EBI-348380, EBI-742828; P25788; O95202: LETM1; NbExp=3; IntAct=EBI-348380, EBI-1052895; P25788; Q8NAJ2: LINC02913; NbExp=3; IntAct=EBI-348380, EBI-10173129; P25788; Q00987: MDM2; NbExp=2; IntAct=EBI-348380, EBI-389668; P25788; Q96PC5: MIA2; NbExp=3; IntAct=EBI-348380, EBI-1050253; P25788; Q9H6H2: MUM1; NbExp=3; IntAct=EBI-348380, EBI-10307610; P25788; P48146: NPBWR2; NbExp=3; IntAct=EBI-348380, EBI-10210114; P25788; P16860: NPPB; NbExp=3; IntAct=EBI-348380, EBI-747044; P25788; Q8N2R0: OSR2; NbExp=3; IntAct=EBI-348380, EBI-5660512; P25788; Q86TB9: PATL1; NbExp=3; IntAct=EBI-348380, EBI-2562092; P25788; Q58A44: PCOTH; NbExp=3; IntAct=EBI-348380, EBI-10243387; P25788; P29590: PML; NbExp=2; IntAct=EBI-348380, EBI-295890; P25788; Q14CW7: PRR10; NbExp=3; IntAct=EBI-348380, EBI-10234793; P25788; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-348380, EBI-740924; P25788; P79522: PRR3; NbExp=3; IntAct=EBI-348380, EBI-2803328; P25788; P25786: PSMA1; NbExp=14; IntAct=EBI-348380, EBI-359352; P25788; P25789: PSMA4; NbExp=4; IntAct=EBI-348380, EBI-359310; P25788; P60900: PSMA6; NbExp=10; IntAct=EBI-348380, EBI-357793; P25788; O14818: PSMA7; NbExp=6; IntAct=EBI-348380, EBI-603272; P25788; P28070: PSMB4; NbExp=3; IntAct=EBI-348380, EBI-603350; P25788; Q9H3S7: PTPN23; NbExp=3; IntAct=EBI-348380, EBI-724478; P25788; Q6NUJ5: PWWP2B; NbExp=3; IntAct=EBI-348380, EBI-10251192; P25788; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-348380, EBI-743796; P25788; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-348380, EBI-948156; P25788; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-348380, EBI-744023; P25788; O43251: RBFOX2; NbExp=3; IntAct=EBI-348380, EBI-746056; P25788; Q9BTD8: RBM42; NbExp=3; IntAct=EBI-348380, EBI-746862; P25788; Q14D33: RTP5; NbExp=3; IntAct=EBI-348380, EBI-10217913; P25788; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-348380, EBI-10248967; P25788; Q15637: SF1; NbExp=3; IntAct=EBI-348380, EBI-744603; P25788; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-348380, EBI-10269374; P25788; Q7L9D0: SLC22A23; NbExp=3; IntAct=EBI-348380, EBI-10256583; P25788; P14678-2: SNRPB; NbExp=3; IntAct=EBI-348380, EBI-372475; P25788; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-348380, EBI-10246938; P25788; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-348380, EBI-8635958; P25788; Q12846: STX4; NbExp=3; IntAct=EBI-348380, EBI-744942; P25788; O43752: STX6; NbExp=3; IntAct=EBI-348380, EBI-2695795; P25788; Q96HZ7: URB1-AS1; NbExp=3; IntAct=EBI-348380, EBI-10288943; P25788; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-348380, EBI-2559305; P25788; Q8N895: ZNF366; NbExp=5; IntAct=EBI-348380, EBI-2813661; P25788; Q66K41: ZNF385C; NbExp=4; IntAct=EBI-348380, EBI-8651919; P25788; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-348380, EBI-16429014; P25788; B2R550; NbExp=3; IntAct=EBI-348380, EBI-10175488; P25788; Q5JPT6; NbExp=3; IntAct=EBI-348380, EBI-10244213; P25788; Q5W150; NbExp=3; IntAct=EBI-348380, EBI-10248148; P25788; Q7KZQ1; NbExp=3; IntAct=EBI-348380, EBI-10255941; P25788; Q9H8E5; NbExp=3; IntAct=EBI-348380, EBI-10309031; P25788; Q9HAA0; NbExp=3; IntAct=EBI-348380, EBI-10309885; P25788; Q9NWL9; NbExp=3; IntAct=EBI-348380, EBI-10315054; P25788-2; P49821: NDUFV1; NbExp=3; IntAct=EBI-348394, EBI-748312; P25788-2; O76024: WFS1; NbExp=3; IntAct=EBI-348394, EBI-720609; Cytoplasm cleus te=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P25788-1; Sequence=Displayed; Name=2; IsoId=P25788-2; Sequence=VSP_005280; Down-regulated by antioxidants BO-653 and probucol. Up- regulated by bacterial lipopolysaccharides (LPS) and TNF. Belongs to the peptidase T1A family. MAPK cascade protein polyubiquitination proteasome complex stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent endopeptidase activity threonine-type endopeptidase activity protein binding nucleus nucleoplasm cytoplasm cytosol proteasome core complex proteolysis ubiquitin-dependent protein catabolic process regulation of cellular amino acid metabolic process peptidase activity proteasomal protein catabolic process proteasomal ubiquitin-independent protein catabolic process negative regulation of G2/M transition of mitotic cell cycle viral process protein deubiquitination hydrolase activity proteasome core complex, alpha-subunit complex anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process ubiquitin protein ligase binding tumor necrosis factor-mediated signaling pathway NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process regulation of mRNA stability post-translational protein modification synapse T cell receptor signaling pathway proteolysis involved in cellular protein catabolic process regulation of endopeptidase activity transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia extracellular exosome interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation uc001xdj.1 uc001xdj.2 uc001xdj.3 uc001xdj.4 
ENST00000216465.10 GSTZ1 ENST00000216465.10 glutathione S-transferase zeta 1, transcript variant 1 (from RefSeq NM_145870.3) A0A0C4DFM0 A0A0C4DFM0_HUMAN ENST00000216465.1 ENST00000216465.2 ENST00000216465.3 ENST00000216465.4 ENST00000216465.5 ENST00000216465.6 ENST00000216465.7 ENST00000216465.8 ENST00000216465.9 GSTZ1 NM_145870 hCG_22265 uc001xtj.1 uc001xtj.2 uc001xtj.3 uc001xtj.4 uc001xtj.5 This gene is a member of the glutathione S-transferase (GSTs) super-family which encodes multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme catalyzes the conversion of maleylacetoacetate to fumarylacetoacatate, which is one of the steps in the phenylalanine/tyrosine degradation pathway. Deficiency of a similar gene in mouse causes oxidative stress. Several transcript variants of this gene encode multiple protein isoforms. [provided by RefSeq, Jul 2015]. Reaction=4-maleylacetoacetate = 4-fumarylacetoacetate; Xref=Rhea:RHEA:14817, ChEBI:CHEBI:17105, ChEBI:CHEBI:18034; EC=5.2.1.2; Evidence=; Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence=; Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6. Belongs to the GST superfamily. Zeta family. catalytic activity cytoplasm aromatic amino acid family metabolic process transferase activity isomerase activity uc001xtj.1 uc001xtj.2 uc001xtj.3 uc001xtj.4 uc001xtj.5 
ENST00000216468.8 TMED8 ENST00000216468.8 transmembrane p24 trafficking protein family member 8, transcript variant 2 (from RefSeq NM_213601.3) B3KTI6 ENST00000216468.1 ENST00000216468.2 ENST00000216468.3 ENST00000216468.4 ENST00000216468.5 ENST00000216468.6 ENST00000216468.7 FAM15B L10 NM_213601 Q3MJB0 Q6PL24 Q9P1V9 TMED8_HUMAN uc001xto.1 uc001xto.2 uc001xto.3 Q6PL24; Q96IZ2: ADTRP; NbExp=3; IntAct=EBI-11603430, EBI-3921528; Q6PL24; Q86SJ2: AMIGO2; NbExp=3; IntAct=EBI-11603430, EBI-3866830; Q6PL24; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-11603430, EBI-4290634; Q6PL24; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-11603430, EBI-714543; Q6PL24; Q8IYJ2-2: C10orf67; NbExp=3; IntAct=EBI-11603430, EBI-13381098; Q6PL24; Q9H5X1: CIAO2A; NbExp=6; IntAct=EBI-11603430, EBI-752069; Q6PL24; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-11603430, EBI-11522780; Q6PL24; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-11603430, EBI-1054315; Q6PL24; Q8N8Q1: CYB561D1; NbExp=3; IntAct=EBI-11603430, EBI-12873482; Q6PL24; Q9H1M3: DEFB129; NbExp=3; IntAct=EBI-11603430, EBI-23712762; Q6PL24; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-11603430, EBI-398977; Q6PL24; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-11603430, EBI-12831978; Q6PL24; O14681: EI24; NbExp=3; IntAct=EBI-11603430, EBI-2339413; Q6PL24; Q99525: H4C7; NbExp=3; IntAct=EBI-11603430, EBI-10294329; Q6PL24; Q15012: LAPTM4A; NbExp=3; IntAct=EBI-11603430, EBI-723416; Q6PL24; P21741: MDK; NbExp=3; IntAct=EBI-11603430, EBI-722444; Q6PL24; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-11603430, EBI-6163737; Q6PL24; Q8IXM3: MRPL41; NbExp=3; IntAct=EBI-11603430, EBI-912501; Q6PL24; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-11603430, EBI-750085; Q6PL24; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-11603430, EBI-3923617; Q6PL24; Q9UI09: NDUFA12; NbExp=3; IntAct=EBI-11603430, EBI-1246332; Q6PL24; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-11603430, EBI-14065960; Q6PL24; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-11603430, EBI-749270; Q6PL24; Q9UNK0: STX8; NbExp=4; IntAct=EBI-11603430, EBI-727240; Q6PL24; Q96L08: SUSD3; NbExp=3; IntAct=EBI-11603430, EBI-18194029; Q6PL24; Q12893: TMEM115; NbExp=3; IntAct=EBI-11603430, EBI-8633987; Q6PL24; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-11603430, EBI-12155101; Q6PL24; A2RU14: TMEM218; NbExp=3; IntAct=EBI-11603430, EBI-10173151; Q6PL24; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-11603430, EBI-11956809; Q6PL24; Q8N609: TRAM1L1; NbExp=5; IntAct=EBI-11603430, EBI-11996766; Q6PL24; Q53HI1: UNC50; NbExp=3; IntAct=EBI-11603430, EBI-7601760; Q6PL24; Q969W1: ZDHHC16; NbExp=3; IntAct=EBI-11603430, EBI-11572692; Sequence=AAF62560.1; Type=Erroneous gene model prediction; Evidence=; uc001xto.1 uc001xto.2 uc001xto.3 
ENST00000216471.5 SAMD15 ENST00000216471.5 sterile alpha motif domain containing 15 (from RefSeq NM_001010860.4) C14orf174 ENST00000216471.1 ENST00000216471.2 ENST00000216471.3 ENST00000216471.4 FAM15A NM_001010860 Q2M3P3 Q9P1V8 SAM15_HUMAN uc001xtq.1 uc001xtq.2 uc001xtq.3 Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9P1V8-1; Sequence=Displayed; Name=2; IsoId=Q9P1V8-2; Sequence=VSP_023431, VSP_023432; uc001xtq.1 uc001xtq.2 uc001xtq.3 
ENST00000216479.8 AHSA1 ENST00000216479.8 activator of HSP90 ATPase activity 1, transcript variant 1 (from RefSeq NM_012111.3) AHSA1_HUMAN B2R9L2 B4DUR9 C14orf3 ENST00000216479.1 ENST00000216479.2 ENST00000216479.3 ENST00000216479.4 ENST00000216479.5 ENST00000216479.6 ENST00000216479.7 HSPC322 NM_012111 O95433 Q96IL6 Q9P060 uc001xtw.1 uc001xtw.2 uc001xtw.3 uc001xtw.4 uc001xtw.5 Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co- chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Interacts with HSPCA/HSP90 (PubMed:12504007, PubMed:12604615). Interacts (phosphorylated on Tyr-223) with HSP90AA1; the interaction activates HSP90AA1 ATPase activity (PubMed:27353360, PubMed:29127155). Interacts with HSP90AB1 (By similarity). Interacts with GCH1 (PubMed:16696853). Interacts with SRPK1 (PubMed:19240134). Interacts with FLCN (PubMed:27353360). (Microbial infection) Interacts with vesicular stomatitis virus glycoprotein (VSV G) (via cytoplasmic tail). O95433; P30793: GCH1; NbExp=3; IntAct=EBI-448610, EBI-958183; O95433; P07900: HSP90AA1; NbExp=4; IntAct=EBI-448610, EBI-296047; O95433; P08238: HSP90AB1; NbExp=4; IntAct=EBI-448610, EBI-352572; Cytoplasm, cytosol Endoplasmic reticulum Note=May transiently interact with the endoplasmic reticulum. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95433-1; Sequence=Displayed; Name=2; IsoId=O95433-2; Sequence=VSP_055797; Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta. By heat shock and treatment with the HSP90 inhibitor 17- demethoxygeldanamycin (17AAG). Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1. Belongs to the AHA1 family. ATPase activator activity protein binding cytoplasm endoplasmic reticulum cytosol positive regulation of ATPase activity cadherin binding chaperone binding Hsp90 protein binding extracellular exosome uc001xtw.1 uc001xtw.2 uc001xtw.3 uc001xtw.4 uc001xtw.5 
ENST00000216484.7 SPTLC2 ENST00000216484.7 serine palmitoyltransferase long chain base subunit 2 (from RefSeq NM_004863.4) ENST00000216484.1 ENST00000216484.2 ENST00000216484.3 ENST00000216484.4 ENST00000216484.5 ENST00000216484.6 KIAA0526 LCB2 NM_004863 O15270 Q16685 SPTC2_HUMAN SPTLC2 uc001xub.1 uc001xub.2 uc001xub.3 uc001xub.4 uc001xub.5 This gene encodes a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I. [provided by RefSeq, Mar 2011]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB011098.1, SRR1660809.78040.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19648650, PubMed:19416851, PubMed:20920666, PubMed:20504773). The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core (PubMed:19416851). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851). The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA (PubMed:19648650, PubMed:19416851). The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (PubMed:19648650, PubMed:19416851). Crucial for adipogenesis (By similarity). Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence=; Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine + CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:65073; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684; Evidence=; Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence=; SPT complex catalytic activity is negatively regulated by ORMDL proteins, including ORMDL3, in the presence of ceramides (PubMed:37308477). This mechanism allows to maintain ceramide levels at sufficient concentrations for the production of complex sphingolipids, but which prevents the accumulation of ceramides to levels that trigger apoptosis (Probable). Kinetic parameters: KM=0.75 mM for L-serine ; KM=0.3 mM for L-serine ; Vmax=1350 pmol/min/mg enzyme ; Lipid metabolism; sphingolipid metabolism. Component of the serine palmitoyltransferase (SPT) complex, which is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB (PubMed:19416851). The heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core of the enzyme, while SPTSSA or SPTSSB subunits determine substrate specificity (PubMed:33558762, PubMed:37308477). SPT also interacts with ORMDL proteins, especially ORMDL3, which negatively regulate SPT activity in the presence of ceramides (PubMed:30700557, PubMed:33558762, PubMed:37308477). Forms dimers of heterodimers with SPTLC1 (PubMed:33558761, PubMed:33558762). Endoplasmic reticulum membrane ; Single-pass membrane protein Widely expressed. Expression at protein level is highly increased in brains of patients with Alzheimer disease. No changes are observed at mRNA level. Neuropathy, hereditary sensory and autonomic, 1C (HSAN1C) [MIM:613640]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by prominent sensory abnormalities with a variable degree of motor and autonomic dysfunction. The neurological phenotype is often complicated by severe infections, osteomyelitis, and amputations. HSAN1C symptoms include loss of touch and vibration in the feet, dysesthesia and severe panmodal sensory loss in the upper and lower limbs, distal lower limb sensory loss with ulceration and osteomyelitis, and distal muscle weakness. te=The disease is caused by variants affecting the gene represented in this entry. SPTLC2 disease mutations cause a shift in the substrate specificity of SPT resulting in the alternative use of L-alanine and L-glycine over its canonical substrate L-serine. This leads to the production of 1-deoxysphingolipids that cannot be correctly metabolized (PubMed:23658386). Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Sequence=BAA25452.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; catalytic activity serine C-palmitoyltransferase activity endoplasmic reticulum endoplasmic reticulum membrane lipid metabolic process sphingolipid metabolic process sphingomyelin biosynthetic process biosynthetic process membrane integral component of membrane transferase activity transferase activity, transferring acyl groups serine C-palmitoyltransferase complex sphingolipid biosynthetic process pyridoxal phosphate binding sphinganine biosynthetic process sphingosine biosynthetic process ceramide biosynthetic process adipose tissue development positive regulation of lipophagy uc001xub.1 uc001xub.2 uc001xub.3 uc001xub.4 uc001xub.5 
ENST00000216487.12 RIN3 ENST00000216487.12 Ras and Rab interactor 3, transcript variant 1 (from RefSeq NM_024832.5) ENST00000216487.1 ENST00000216487.10 ENST00000216487.11 ENST00000216487.2 ENST00000216487.3 ENST00000216487.4 ENST00000216487.5 ENST00000216487.6 ENST00000216487.7 ENST00000216487.8 ENST00000216487.9 NM_024832 Q76LB3 Q8NF30 Q8TB24 Q8TEE8 Q8WYP4 Q9H6A5 Q9HAG1 RIN3_HUMAN uc001yap.1 uc001yap.2 uc001yap.3 uc001yap.4 uc001yap.5 This protein encoded by this gene is a member of the RIN family of Ras interaction-interference proteins, which are binding partners to the RAB5 small GTPases. The protein functions as a guanine nucleotide exchange for RAB5B and RAB31. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]. Ras effector protein that functions as a guanine nucleotide exchange (GEF) for RAB5B and RAB31, by exchanging bound GDP for free GTP. Required for normal RAB31 function. Interacts with CD2AP, RAB5B, RAB31 and BIN1. Q8TB24; O00499: BIN1; NbExp=2; IntAct=EBI-1570523, EBI-719094; Q8TB24; Q9Y5K6: CD2AP; NbExp=3; IntAct=EBI-1570523, EBI-298152; Q8TB24; P46108: CRK; NbExp=2; IntAct=EBI-1570523, EBI-886; Q8TB24; P16333: NCK1; NbExp=2; IntAct=EBI-1570523, EBI-389883; Q8TB24; P19174: PLCG1; NbExp=3; IntAct=EBI-1570523, EBI-79387; Cytoplasm toplasmic vesicle rly endosome Note=Activation of tyrosine phosphorylation signaling induces translocation to cytoplasmic vesicles. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8TB24-1; Sequence=Displayed; Name=4; IsoId=Q8TB24-4; Sequence=VSP_007587, VSP_007588; Widely expressed. Belongs to the RIN (Ras interaction/interference) family. Sequence=BAB13888.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence=; Sequence=BAB15357.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAC03432.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence=; GTPase activator activity protein binding cytoplasm endosome early endosome cytosol endocytosis signal transduction Rab guanyl-nucleotide exchange factor activity Rab GTPase binding cytoplasmic vesicle positive regulation of GTPase activity uc001yap.1 uc001yap.2 uc001yap.3 uc001yap.4 uc001yap.5 
ENST00000216489.8 ALKBH1 ENST00000216489.8 alkB homolog 1, histone H2A dioxygenase (from RefSeq NM_006020.3) ABH ABH1 ALKB1_HUMAN ALKBH ALKBH1 ENST00000216489.1 ENST00000216489.2 ENST00000216489.3 ENST00000216489.4 ENST00000216489.5 ENST00000216489.6 ENST00000216489.7 NM_006020 Q13686 Q8TAU1 Q9ULA7 uc001xuc.1 uc001xuc.2 uc001xuc.3 This gene encodes a homolog to the E. coli alkB gene product. The E. coli alkB protein is part of the adaptive response mechanism of DNA alkylation damage repair. It is involved in damage reversal by oxidative demethylation of 1-methyladenine and 3-methylcytosine. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803616.180648.1, SRR1660805.27277.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2467144, SAMN03267755 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216489.8/ ENSP00000216489.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Dioxygenase that acts as on nucleic acids, such as DNA and tRNA (PubMed:18603530, PubMed:27745969, PubMed:27497299). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:18603530, PubMed:27497299). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment (PubMed:27745969, PubMed:27497299). Mainly acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs, with a preference for N(1)-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs (PubMed:27745969). Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N(1)- methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation (PubMed:27745969). In mitochondrion, specifically interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5- formylcytosine (f(5)c) at this position (PubMed:27497299). mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation (PubMed:27497299). Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:30392959, PubMed:30017583). N(6)- methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (By similarity). Demethylates mRNAs containing N(3)-methylcytidine modification (PubMed:31188562). Also able to repair alkylated single-stranded DNA by oxidative demethylation, but with low activity (PubMed:18603530). Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites (PubMed:19959401). DNA lyase activity does not require alpha-ketboglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product (PubMed:19959401, PubMed:23577621). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation. May play a role in placental trophoblast lineage differentiation (By similarity). Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'- deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3- dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho- 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA- COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence=; Reaction=2-oxoglutarate + a methylated nucleobase within DNA + O2 = a nucleobase within DNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:30299, Rhea:RHEA-COMP:12192, Rhea:RHEA-COMP:12193, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:32875, ChEBI:CHEBI:64428; EC=1.14.11.33; Evidence=; Reaction=2-oxoglutarate + an N(6)-methyl-2'-deoxyadenosine in DNA + O2 = a 2'-deoxyadenosine in DNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49524, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=1.14.11.51; Evidence=; Reaction=2-oxoglutarate + an N(1)-methyladenosine in tRNA + O2 = an adenosine in tRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:54576, Rhea:RHEA-COMP:10242, Rhea:RHEA-COMP:12312, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; Evidence=; Reaction=2 2-oxoglutarate + 5-methylcytidine(34) in mitochondrial tRNA(Met) + 2 O2 = 5-formylcytidine(34) in mitochondrial tRNA(Met) + 2 CO2 + H2O + 2 succinate; Xref=Rhea:RHEA:54144, Rhea:RHEA- COMP:13808, Rhea:RHEA-COMP:13809, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:74483, ChEBI:CHEBI:138075; Evidence=; Reaction=2-oxoglutarate + an N(3)-methylcytidine in mRNA + O2 = a cytidine in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:60920, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15713, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60921; Evidence=; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence= Note=Binds 1 Fe(2+) ion per subunit. Monomer (PubMed:19959401). Interacts with DNAJB6 (By similarity). Nucleus Mitochondrion te=Mainly localizes in euchromatin, largely excluded from heterochromatin and nucleoli (By similarity). Ubiquitous. Belongs to the alkB family. The DNA N6-methyl adenine demethylase activity is subject to discussion. According to a report, biochemical assays do not reveal clear DNA N6-methyl adenine demethylase activity in vivo (PubMed:27745969). According to another study, has clear DNA N6-methyl adenine demethylase activity (PubMed:30017583). Sequence=CAA63047.1; Type=Frameshift; Evidence=; tRNA binding in utero embryonic development neuron migration placenta development tRNA wobble cytosine modification catalytic activity nucleus nuclear euchromatin mitochondrion DNA repair DNA dealkylation involved in DNA repair regulation of translation regulation of translational initiation regulation of translational elongation cellular response to DNA damage stimulus metabolic process ferrous iron binding regulation of gene expression oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors lyase activity cell differentiation neuron projection development oxidative DNA demethylation oxidative DNA demethylase activity chemoattractant activity RNA repair negative regulation of neuron apoptotic process metal ion binding developmental growth positive chemotaxis dioxygenase activity oxidation-reduction process regulation of mitochondrial translation methylcytosine dioxygenase activity oxidative demethylation DNA demethylation 1-ethyladenine demethylase activity tRNA demethylation tRNA demethylase activity uc001xuc.1 uc001xuc.2 uc001xuc.3 
ENST00000216492.10 CHGA ENST00000216492.10 chromogranin A, transcript variant 1 (from RefSeq NM_001275.4) B2R9E9 CMGA_HUMAN ENST00000216492.1 ENST00000216492.2 ENST00000216492.3 ENST00000216492.4 ENST00000216492.5 ENST00000216492.6 ENST00000216492.7 ENST00000216492.8 ENST00000216492.9 NM_001275 P10645 Q53FA8 Q6NR84 Q96E84 Q96GL7 Q9BQB5 uc001ybc.1 uc001ybc.2 uc001ybc.3 uc001ybc.4 uc001ybc.5 uc001ybc.6 uc001ybc.7 The protein encoded by this gene is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. It is found in secretory vesicles of neurons and endocrine cells. This gene product is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Two other peptides, catestatin and chromofungin, have antimicrobial activity and antifungal activity, respectively. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2014]. [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas. [Catestatin]: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:15326220). Displays antibacterial activity against Gram-positive bacteria S.aureus and M.luteus, and Gram-negative bacteria E.coli and P.aeruginosa (PubMed:15723172, PubMed:24723458). Can induce mast cell migration, degranulation and production of cytokines and chemokines (PubMed:21214543). Acts as a potent scavenger of free radicals in vitro (PubMed:24723458). May play a role in the regulation of cardiac function and blood pressure (PubMed:18541522). [Serpinin]: Regulates granule biogenesis in endocrine cells by up-regulating the transcription of protease nexin 1 (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein degradation in the Golgi complex which in turn promotes granule formation. Self-interacts; self-assembly is promoted in vitro by chondroitin sulfate attachment which occurs at mildly acidic pH conditions (PubMed:25326458). Interacts with SCG3 (By similarity). [Serpinin]: Secreted Cytoplasmic vesicle, secretory vesicle Note=Pyroglutaminated serpinin localizes to secretory vesicle. Cytoplasmic vesicle, secretory vesicle Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle Secreted Note=Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions. In pituitary gonadotropes, located in large secretory granules. Detected in cerebrospinal fluid (at protein level) (PubMed:25326458). Detected in urine (at protein level) (PubMed:37453717). [GE-25]: Found in the brain. Sulfated on tyrosine residues and/or contains sulfated glycans. O-glycosylated with core 1 or possibly core 8 glycans (PubMed:9852066, PubMed:19838169, PubMed:23234360). Contains chondroitin sulfate (CS); CS attachment is pH-dependent, being observed at mildly acidic conditions of pH 5 but not at neutral pH, and promotes self-assembly in vitro (PubMed:25326458). Proteolytic processing gives rise to an additional longer form of catestatin (residues 358-390) which displays a less potent catecholamine release-inhibitory activity (PubMed:10781584). Plasmin- mediated proteolytic processing can give rise to additional shorter and longer forms of catestatin peptides (PubMed:17991725). Binds calcium with a low-affinity. Belongs to the chromogranin/secretogranin protein family. regulation of the force of heart contraction mast cell chemotaxis extracellular region extracellular space organelle organization regulation of blood pressure membrane antimicrobial humoral response transport vesicle secretory granule transport vesicle membrane cytoplasmic vesicle killing of cells of other organism mast cell cytokine production protein localization to secretory granule negative regulation of catecholamine secretion chromaffin granule mast cell granule defense response to bacterium mast cell degranulation innate immune response mast cell activation perinuclear region of cytoplasm defense response to Gram-negative bacterium defense response to Gram-positive bacterium defense response to fungus positive regulation of cardiac muscle contraction adrenergic receptor signaling pathway involved in cardiac muscle relaxation positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway negative regulation of neuron death positive regulation of relaxation of cardiac muscle positive regulation of dense core granule biogenesis uc001ybc.1 uc001ybc.2 uc001ybc.3 uc001ybc.4 uc001ybc.5 uc001ybc.6 uc001ybc.7 
ENST00000216513.5 SIX4 ENST00000216513.5 SIX homeobox 4 (from RefSeq NM_017420.5) ENST00000216513.1 ENST00000216513.2 ENST00000216513.3 ENST00000216513.4 NM_017420 Q4QQH5 Q4V764 Q9UIU6 SIX4_HUMAN uc001xfc.1 uc001xfc.2 uc001xfc.3 uc001xfc.4 uc001xfc.5 This gene encodes a member of the homeobox family, subfamily SIX. The drosophila homolog is a nuclear homeoprotein required for eye development. Studies in mouse show that this gene product functions as a transcription factor, and may have a role in the differentiation or maturation of neuronal cells. [provided by RefSeq, May 2010]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.140483.1, BC098135.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2467146 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216513.5/ ENSP00000216513.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a DNA sequence on these target genes and is involved in processes like cell differentiation, cell migration and cell survival. Transactivates gene expression by binding a 5'-[CAT]A[CT][CT][CTG]GA[GAT]-3' motif present in the Trex site and a 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 site of the muscle-specific genes enhancer. Acts cooperatively with EYA proteins to transactivate their target genes through interaction and nuclear translocation of EYA protein. Acts synergistically with SIX1 to regulate target genes involved in formation of various organs, including muscle, kidney, gonad, ganglia, olfactory epithelium and cranial skeleton. Plays a role in several important steps of muscle development. Controls the genesis of hypaxial myogenic progenitors in the dermomyotome by transactivating PAX3 and the delamination and migration of the hypaxial precursors from the ventral lip to the limb buds through the transactivation of PAX3, MET and LBX1. Controls myoblast determination by transactivating MYF5, MYOD1 and MYF6. Controls somitic differentiation in myocyte through MYOG transactivation. Plays a role in synaptogenesis and sarcomere organization by participating in myofiber specialization during embryogenesis by activating fast muscle program in the primary myotome resulting in an up-regulation of fast muscle genes, including ATP2A1, MYL1 and TNNT3. Simultaneously, is also able to activate inhibitors of slow muscle genes, such as SOX6, HRASLS, and HDAC4, thereby restricting the activation of the slow muscle genes. During muscle regeneration, negatively regulates differentiation of muscle satellite cells through down-regulation of MYOG expression. During kidney development regulates the early stages of metanephros development and ureteric bud formation through regulation of GDNF, SALL1, PAX8 and PAX2 expression. Plays a role in gonad development by regulating both testis determination and size determination. In gonadal sex determination, transactivates ZFPM2 by binding a MEF3 consensus sequence, resulting in SRY up-regulation. In gonadal size determination, transactivates NR5A1 by binding a MEF3 consensus sequence resulting in gonadal precursor cell formation regulation. During olfactory development mediates the specification and patterning of olfactory placode through fibroblast growth factor and BMP4 signaling pathways and also regulates epithelial cell proliferation during placode formation. Promotes survival of sensory neurons during early trigeminal gangliogenesis. In the developing dorsal root ganglia, up-regulates SLC12A2 transcription. Regulates early thymus/parathyroid organogenesis through regulation of GCM2 and FOXN1 expression. Forms gustatory papillae during development of the tongue. Also plays a role during embryonic cranial skeleton morphogenesis. Interacts with EYA3; acts cooperatively with EYA3 to transactivate target genes through interaction and nuclear translocation of EYA3 protein. Nucleus Cytoplasm Belongs to the SIX/Sine oculis homeobox family. Sequence=BAA86223.1; Type=Erroneous initiation; Evidence=; Sequence=EAW80786.1; Type=Erroneous initiation; Evidence=; nuclear chromatin transcription regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus transcription factor complex cytoplasm regulation of transcription, DNA-templated multicellular organism development skeletal muscle tissue development regulation of synaptic growth at neuromuscular junction male gonad development anatomical structure morphogenesis regulation of gene expression male sex determination olfactory placode formation regulation of protein localization protein localization to nucleus inner ear morphogenesis negative regulation of apoptotic process negative regulation of neuron apoptotic process sequence-specific DNA binding tongue development sarcomere organization negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter male sex differentiation thymus development generation of neurons embryonic cranial skeleton morphogenesis embryonic skeletal system morphogenesis anatomical structure development regulation of epithelial cell proliferation myoblast migration pharyngeal system development myotome development fungiform papilla morphogenesis trigeminal ganglion development metanephric mesenchyme development regulation of branch elongation involved in ureteric bud branching positive regulation of ureteric bud formation positive regulation of branching involved in ureteric bud morphogenesis skeletal muscle fiber differentiation negative regulation of satellite cell differentiation uc001xfc.1 uc001xfc.2 uc001xfc.3 uc001xfc.4 uc001xfc.5 
ENST00000216540.5 SLC10A1 ENST00000216540.5 solute carrier family 10 member 1 (from RefSeq NM_003049.4) B9EGB6 ENST00000216540.1 ENST00000216540.2 ENST00000216540.3 ENST00000216540.4 GIG29 NM_003049 NTCP NTCP_HUMAN Q14973 Q2TU29 uc001xlr.1 uc001xlr.2 uc001xlr.3 uc001xlr.4 The protein encoded by this gene belongs to the sodium/bile acid cotransporter family, which are integral membrane glycoproteins that participate in the enterohepatic circulation of bile acids. Two homologous transporters are involved in the reabsorption of bile acids; the ileal sodium/bile acid cotransporter with an apical cell localization that absorbs bile acids from the intestinal lumen, bile duct and kidney, and the liver-specific sodium/bile acid cotransporter, represented by this protein, that is found in the basolateral membranes of hepatocytes. Bile acids are the catabolic product of cholesterol metabolism, hence this protein is important for cholesterol homeostasis. [provided by RefSeq, Oct 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189664.103981.1, SRR5189664.104510.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145122, SAMEA2155590 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216540.5/ ENSP00000216540.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## As a major transporter of conjugated bile salts from plasma into the hepatocyte, it plays a key role in the enterohepatic circulation of bile salts necessary for the solubilization and absorption of dietary fat and fat-soluble vitamins (PubMed:8132774, PubMed:14660639, PubMed:24867799, PubMed:34060352). It is strictly dependent on the extracellular presence of sodium (PubMed:8132774, PubMed:14660639, PubMed:24867799, PubMed:34060352). It exhibits broad substrate specificity and transports various bile acids, such as taurocholate, cholate, as well as non-bile acid organic compounds, such as estrone sulfate (PubMed:14660639, PubMed:34060352). Works collaboratively with the ileal transporter (NTCP2), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation (PubMed:33222321). (Microbial infection) Acts as a receptor for hepatitis B virus. Reaction=2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + taurocholate(in); Xref=Rhea:RHEA:71875, ChEBI:CHEBI:29101, ChEBI:CHEBI:36257; Evidence= Reaction=cholate(out) + 2 Na(+)(out) = cholate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71911, ChEBI:CHEBI:29101, ChEBI:CHEBI:29747; Evidence=; Reaction=estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71083, ChEBI:CHEBI:29101, ChEBI:CHEBI:60050; Evidence= Reaction=2 Na(+)(out) + taurochenodeoxycholate(out) = 2 Na(+)(in) + taurochenodeoxycholate(in); Xref=Rhea:RHEA:71923, ChEBI:CHEBI:9407, ChEBI:CHEBI:29101; Evidence=; Reaction=2 Na(+)(out) + tauroursodeoxycholate(out) = 2 Na(+)(in) + tauroursodeoxycholate(in); Xref=Rhea:RHEA:71927, ChEBI:CHEBI:29101, ChEBI:CHEBI:132028; Evidence=; Reaction=glycocholate(out) + 2 Na(+)(out) = glycocholate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71935, ChEBI:CHEBI:29101, ChEBI:CHEBI:29746; Evidence=; Reaction=2 Na(+)(out) + tauronorcholate(out) = 2 Na(+)(in) + tauronorcholate(in); Xref=Rhea:RHEA:71915, ChEBI:CHEBI:29101, ChEBI:CHEBI:191405; Evidence=; Reaction=2 Na(+)(out) + taurodeoxycholate(out) = 2 Na(+)(in) + taurodeoxycholate(in); Xref=Rhea:RHEA:72087, ChEBI:CHEBI:29101, ChEBI:CHEBI:36261; Evidence=; Reaction=2 Na(+)(out) + tauroallocholate(out) = 2 Na(+)(in) + tauroallocholate(in); Xref=Rhea:RHEA:51840, ChEBI:CHEBI:29101, ChEBI:CHEBI:191406; Evidence=; Reaction=2 Na(+)(out) + taurohyodeoxycholate(out) = 2 Na(+)(in) + taurohyodeoxycholate(in); Xref=Rhea:RHEA:72167, ChEBI:CHEBI:29101, ChEBI:CHEBI:191407; Evidence=; Reaction=2 Na(+)(out) + taurohyocholate(out) = 2 Na(+)(in) + taurohyocholate(in); Xref=Rhea:RHEA:72171, ChEBI:CHEBI:29101, ChEBI:CHEBI:58874; Evidence=; Reaction=2 Na(+)(out) + tauro-beta-muricholate(out) = 2 Na(+)(in) + tauro-beta-muricholate(in); Xref=Rhea:RHEA:72179, ChEBI:CHEBI:29101, ChEBI:CHEBI:133064; Evidence=; Kinetic parameters: KM=6.3 uM for taurocholate ; KM=10 uM for taurocholate ; KM=7.5 uM for taurocholate ; KM=15 uM for taurocholate ; KM=12 uM for cholate ; KM=60 uM for estrone 3-sulfate ; KM=27 uM for estrone 3-sulfate ; KM=67 uM for estrone 3-sulfate ; Vmax=333 pmol/min/mg enzyme with taurocholate as substrate ; Vmax=415 pmol/min/mg enzyme with taurocholate as substrate ; Vmax=139 pmol/min/mg enzyme with cholate as substrate ; Vmax=111 pmol/min/mg enzyme with estrone 3-sulfate as substrate ; Vmax=68 pmol/min/mg enzyme with estrone 3-sulfate as substrate ; Vmax=1060 pmol/min/mg enzyme with estrone 3-sulfate as substrate ; Vmax=130 pmol/min/mg enzyme with taurocholate as substrate ; (Microbial infection) Interacts with hepatitis B virus large envelope protein. Q14973; O95870: ABHD16A; NbExp=3; IntAct=EBI-3923031, EBI-348517; Q14973; Q9ULC5: ACSL5; NbExp=3; IntAct=EBI-3923031, EBI-2876927; Q14973; Q9NRZ7: AGPAT3; NbExp=3; IntAct=EBI-3923031, EBI-2803601; Q14973; Q8N6S5: ARL6IP6; NbExp=3; IntAct=EBI-3923031, EBI-2808844; Q14973; P07306: ASGR1; NbExp=3; IntAct=EBI-3923031, EBI-1172335; Q14973; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-3923031, EBI-3904417; Q14973; O95393: BMP10; NbExp=3; IntAct=EBI-3923031, EBI-3922513; Q14973; P06681: C2; NbExp=3; IntAct=EBI-3923031, EBI-2835920; Q14973; P07357: C8A; NbExp=3; IntAct=EBI-3923031, EBI-9021639; Q14973; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-3923031, EBI-11579371; Q14973; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-3923031, EBI-12256978; Q14973; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-3923031, EBI-7247651; Q14973; Q5RI15: COX20; NbExp=3; IntAct=EBI-3923031, EBI-2834035; Q14973; Q07325: CXCL9; NbExp=3; IntAct=EBI-3923031, EBI-3911467; Q14973; P00387: CYB5R3; NbExp=3; IntAct=EBI-3923031, EBI-1046040; Q14973; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-3923031, EBI-398977; Q14973; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-3923031, EBI-12831978; Q14973; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-3923031, EBI-11337888; Q14973; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-3923031, EBI-12118888; Q14973; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-3923031, EBI-12142299; Q14973; P37268: FDFT1; NbExp=3; IntAct=EBI-3923031, EBI-714550; Q14973; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-3923031, EBI-12175685; Q14973; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-3923031, EBI-713304; Q14973; P01350: GAST; NbExp=3; IntAct=EBI-3923031, EBI-3436637; Q14973; Q9NZC3: GDE1; NbExp=3; IntAct=EBI-3923031, EBI-2833330; Q14973; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-3923031, EBI-6166686; Q14973; O14653: GOSR2; NbExp=3; IntAct=EBI-3923031, EBI-4401517; Q14973; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-3923031, EBI-11955647; Q14973; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-3923031, EBI-13345167; Q14973; Q6IBB0: IFITM2; NbExp=3; IntAct=EBI-3923031, EBI-12167419; Q14973; Q01628: IFITM3; NbExp=3; IntAct=EBI-3923031, EBI-7932862; Q14973; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-3923031, EBI-2830349; Q14973; P48449: LSS; NbExp=3; IntAct=EBI-3923031, EBI-3930711; Q14973; P21145: MAL; NbExp=3; IntAct=EBI-3923031, EBI-3932027; Q14973; Q13021: MALL; NbExp=3; IntAct=EBI-3923031, EBI-750078; Q14973; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-3923031, EBI-2858252; Q14973; P11836: MS4A1; NbExp=3; IntAct=EBI-3923031, EBI-2808234; Q14973; A6NDP7: MYADML2; NbExp=3; IntAct=EBI-3923031, EBI-17641390; Q14973; Q99519: NEU1; NbExp=3; IntAct=EBI-3923031, EBI-721517; Q14973; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-3923031, EBI-10317425; Q14973; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-3923031, EBI-1054848; Q14973; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-3923031, EBI-11075081; Q14973; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-3923031, EBI-721750; Q14973; Q7RTS5: OTOP3; NbExp=3; IntAct=EBI-3923031, EBI-12853910; Q14973; I3L0A0: PEDS1-UBE2V1; NbExp=3; IntAct=EBI-3923031, EBI-12213001; Q14973; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-3923031, EBI-981985; Q14973; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-3923031, EBI-12257782; Q14973; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-3923031, EBI-8636004; Q14973; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-3923031, EBI-3917235; Q14973; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-3923031, EBI-4403649; Q14973; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-3923031, EBI-9679163; Q14973; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-3923031, EBI-2854842; Q14973; O95562: SFT2D2; NbExp=3; IntAct=EBI-3923031, EBI-4402330; Q14973; Q9H9B4: SFXN1; NbExp=3; IntAct=EBI-3923031, EBI-355861; Q14973; Q9Y666-2: SLC12A7; NbExp=3; IntAct=EBI-3923031, EBI-12854384; Q14973; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-3923031, EBI-12243266; Q14973; Q96AG3: SLC25A46; NbExp=3; IntAct=EBI-3923031, EBI-10281975; Q14973; Q6ICL7: SLC35E4; NbExp=3; IntAct=EBI-3923031, EBI-12867720; Q14973; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-3923031, EBI-9978441; Q14973; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-3923031, EBI-10314552; Q14973; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-3923031, EBI-12266234; Q14973; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-3923031, EBI-3907610; Q14973; Q8WY07: SLC7A3; NbExp=3; IntAct=EBI-3923031, EBI-13066314; Q14973; O60906: SMPD2; NbExp=3; IntAct=EBI-3923031, EBI-12828299; Q14973; O15400: STX7; NbExp=3; IntAct=EBI-3923031, EBI-3221827; Q14973; Q03518: TAP1; NbExp=3; IntAct=EBI-3923031, EBI-747259; Q14973; P02786: TFRC; NbExp=3; IntAct=EBI-3923031, EBI-355727; Q14973; Q969X1: TMBIM1; NbExp=3; IntAct=EBI-3923031, EBI-2820569; Q14973; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-3923031, EBI-10171534; Q14973; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-3923031, EBI-12155101; Q14973; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-3923031, EBI-348587; Q14973; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-3923031, EBI-347385; Q14973; Q8WY98: TMEM234; NbExp=3; IntAct=EBI-3923031, EBI-8642211; Q14973; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-3923031, EBI-11528917; Q14973; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-3923031, EBI-10315004; Q14973; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-3923031, EBI-2852148; Q14973; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-3923031, EBI-2820477; Q14973; Q96B49: TOMM6; NbExp=3; IntAct=EBI-3923031, EBI-10826510; Q14973; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-3923031, EBI-12195249; Q14973; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-3923031, EBI-11988865; Q14973; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-3923031, EBI-11343401; Q14973; Q53HI1: UNC50; NbExp=3; IntAct=EBI-3923031, EBI-7601760; Q14973; Q15836: VAMP3; NbExp=3; IntAct=EBI-3923031, EBI-722343; Q14973; O95070: YIF1A; NbExp=3; IntAct=EBI-3923031, EBI-2799703; Q14973; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-3923031, EBI-751253; Q14973; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-3923031, EBI-751210; Q14973; Q96FB2; NbExp=3; IntAct=EBI-3923031, EBI-2857623; Cell membrane ulti-pass membrane protein. Expressed in liver (PubMed:11031103, PubMed:12409283). Expressed in placental trophoblasts (PubMed:12409283). Hypercholanemia, familial, 2 (FHCA2) [MIM:619256]: An autosomal recessive inborn error of metabolism characterized by persistently increased plasma levels of conjugated bile salts apparent from infancy, fat malabsorption and impaired absorption of fat-soluble vitamins, including D and K. Most patients are asymptomatic. Some neonates may have transient jaundice or transiently elevated liver enzymes. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family. virus receptor activity plasma membrane integral component of plasma membrane ion transport sodium ion transport bile acid:sodium symporter activity bile acid transmembrane transporter activity symporter activity bile acid and bile salt transport membrane integral component of membrane viral process basolateral plasma membrane viral entry into host cell transmembrane transport uc001xlr.1 uc001xlr.2 uc001xlr.3 uc001xlr.4 
ENST00000216554.8 EIF5 ENST00000216554.8 eukaryotic translation initiation factor 5, transcript variant 1 (from RefSeq NM_001969.5) ENST00000216554.1 ENST00000216554.2 ENST00000216554.3 ENST00000216554.4 ENST00000216554.5 ENST00000216554.6 ENST00000216554.7 IF5_HUMAN NM_001969 P55010 Q53XB3 Q9H5N2 Q9UG48 uc001ymq.1 uc001ymq.2 uc001ymq.3 uc001ymq.4 uc001ymq.5 uc001ymq.6 Eukaryotic translation initiation factor-5 (EIF5) interacts with the 40S initiation complex to promote hydrolysis of bound GTP with concomitant joining of the 60S ribosomal subunit to the 40S initiation complex. The resulting functional 80S ribosomal initiation complex is then active in peptidyl transfer and chain elongations (summary by Si et al., 1996 [PubMed 8663286]).[supplied by OMIM, May 2010]. Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:11166181, PubMed:22813744, PubMed:24319994). In this complex, acts as a GTPase- activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181). During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744). This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181). Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744). This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744). Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744). Component of the 43S pre-initiation complex (43S PIC), which is composed of the 40S ribosomal subunit, EIF1, eIF1A (EIF1AX), eIF3 complex, EIF5 and eIF2-GTP-initiator tRNA complex (eIF2 ternary complex). Interacts with eIF1A (EIF1AX) during scanning (PubMed:24319994). Interacts through its C-terminal domain (CTD) with EIF1 or with eIF2-beta (EIF2S2) (mutually exclusive) through a common binding site (PubMed:21745818, PubMed:22813744). Interacts through its C-terminal domain (CTD) with the CTD of EIF5B (PubMed:30211544). Interacts with FMR1 isoform 6; this interaction occurs in a RNA- dependent manner (PubMed:24658146). P55010; Q9UNI6: DUSP12; NbExp=6; IntAct=EBI-286450, EBI-715161; P55010; P42858: HTT; NbExp=3; IntAct=EBI-286450, EBI-466029; Cytoplasm Belongs to the eIF-2-beta/eIF-5 family. nucleotide binding formation of translation preinitiation complex formation of cytoplasmic translation initiation complex RNA binding translation initiation factor activity GTPase activity GDP-dissociation inhibitor activity protein binding GTP binding cytoplasm cytosol plasma membrane translation translational initiation regulation of translational initiation translation factor activity, RNA binding cadherin binding eukaryotic initiation factor eIF2 binding activation of GTPase activity nucleus uc001ymq.1 uc001ymq.2 uc001ymq.3 uc001ymq.4 uc001ymq.5 uc001ymq.6 
ENST00000216629.11 BDKRB1 ENST00000216629.11 bradykinin receptor B1, transcript variant 2 (from RefSeq NM_001386007.1) A8K7F5 BKRB1_HUMAN BRADYB1 ENST00000216629.1 ENST00000216629.10 ENST00000216629.2 ENST00000216629.3 ENST00000216629.4 ENST00000216629.5 ENST00000216629.6 ENST00000216629.7 ENST00000216629.8 ENST00000216629.9 NM_001386007 P46663 Q546S7 Q8N0Y8 uc001yfh.1 uc001yfh.2 uc001yfh.3 uc001yfh.4 uc001yfh.5 This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation. P46663; PRO_0000006687 [P01042]: KNG1; NbExp=2; IntAct=EBI-6623218, EBI-6623250; Cell membrane ; Multi-pass membrane protein Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. Name=Wikipedia; Note=Bradykinin receptor entry; URL="https://en.wikipedia.org/wiki/Bradykinin_receptor"; negative regulation of protein phosphorylation positive regulation of leukocyte migration G-protein coupled receptor activity bradykinin receptor activity protein binding endoplasmic reticulum plasma membrane integral component of plasma membrane inflammatory response signal transduction G-protein coupled receptor signaling pathway positive regulation of cytosolic calcium ion concentration protein kinase C-activating G-protein coupled receptor signaling pathway response to mechanical stimulus membrane integral component of membrane cell migration sensory perception of pain negative regulation of cell growth response to lipopolysaccharide peptide binding neuron projection negative regulation of blood pressure positive regulation of release of sequestered calcium ion into cytosol uc001yfh.1 uc001yfh.2 uc001yfh.3 uc001yfh.4 uc001yfh.5 
ENST00000216639.8 VRK1 ENST00000216639.8 VRK serine/threonine kinase 1, transcript variant 1 (from RefSeq NM_003384.3) ENST00000216639.1 ENST00000216639.2 ENST00000216639.3 ENST00000216639.4 ENST00000216639.5 ENST00000216639.6 ENST00000216639.7 NM_003384 Q3SYL2 Q99986 VRK1 VRK1_HUMAN uc001yft.1 uc001yft.2 uc001yft.3 uc001yft.4 uc001yft.5 This gene encodes a member of the vaccinia-related kinase (VRK) family of serine/threonine protein kinases. This gene is widely expressed in human tissues and has increased expression in actively dividing cells, such as those in testis, thymus, fetal liver, and carcinomas. Its protein localizes to the nucleus and has been shown to promote the stability and nuclear accumulation of a transcriptionally active p53 molecule and, in vitro, to phosphorylate Thr18 of p53 and reduce p53 ubiquitination. This gene, therefore, may regulate cell proliferation. This protein also phosphorylates histone, casein, and the transcription factors ATF2 (activating transcription factor 2) and c-JUN. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC103761.1, SRR1803611.253760.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216639.8/ ENSP00000216639.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Serine/threonine kinase involved in cell cycle, nuclear condensation and transcription regulation (PubMed:14645249, PubMed:18617507, PubMed:19103756). Involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation (PubMed:19103756). Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2 (PubMed:10951572). Phosphorylates KAT5 in response to DNA damage, promoting KAT5 association with chromatin and histone acetyltransferase activity (PubMed:33076429). Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm (PubMed:16495336). Phosphorylates ATF2 which activates its transcriptional activity (PubMed:15105425). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Active in presence of Mn(2+), Mg(2+) and Zn(2+), but is not functional with Ca(2+) or Cu(2+) (PubMed:11883897). Has a higher affinity for Mn(2+) than for Mg(2+) (PubMed:11883897). RAN inhibits its autophosphorylation and its ability to phosphorylate histone H3 (PubMed:18617507). (Microbial infection) Interacts with vaccinia protein B12; this interaction inhibits the repressive activity of the vaccinia virus B12 pseudokinase on viral replication factory formation. Q99986; P15336: ATF2; NbExp=5; IntAct=EBI-1769146, EBI-1170906; Q99986; Q96GD4: AURKB; NbExp=14; IntAct=EBI-1769146, EBI-624291; Q99986; P38432: COIL; NbExp=9; IntAct=EBI-1769146, EBI-945751; Q99986; P16104: H2AX; NbExp=3; IntAct=EBI-1769146, EBI-494830; Q99986; P05412: JUN; NbExp=5; IntAct=EBI-1769146, EBI-852823; Q99986; Q92993: KAT5; NbExp=6; IntAct=EBI-1769146, EBI-399080; Q99986; O60934: NBN; NbExp=13; IntAct=EBI-1769146, EBI-494844; Q99986; Q9H4B4: PLK3; NbExp=12; IntAct=EBI-1769146, EBI-751877; Q99986; P62826: RAN; NbExp=12; IntAct=EBI-1769146, EBI-286642; Q99986; O76064: RNF8; NbExp=2; IntAct=EBI-1769146, EBI-373337; Q99986; P48431: SOX2; NbExp=14; IntAct=EBI-1769146, EBI-6124081; Q99986; P04637: TP53; NbExp=11; IntAct=EBI-1769146, EBI-366083; Q99986; Q12888: TP53BP1; NbExp=8; IntAct=EBI-1769146, EBI-396540; Nucleus toplasm Note=Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis. Widely expressed. Highly expressed in fetal liver, testis and thymus. Autophosphorylated at various serine and threonine residues (PubMed:11883897, PubMed:14645249, PubMed:19103756, PubMed:21543316). Autophosphorylation does not impair its ability to phosphorylate p53/TP53 (PubMed:11883897). Phosphorylation by PLK3 leads to induction of Golgi fragmentation during mitosis (PubMed:19103756). Pontocerebellar hypoplasia 1A (PCH1A) [MIM:607596]: A disorder characterized by an abnormally small cerebellum and brainstem, central and peripheral motor dysfunction from birth, gliosis and spinal cord anterior horn cells degeneration resembling infantile spinal muscular atrophy. Additional features include muscle hypotonia, congenital contractures and respiratory insufficiency that is evident at birth. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. VRK subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/43556/VRK1"; nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding nucleus nucleoplasm nucleolus cytoplasm Golgi stack spindle cytosol cytoskeleton protein phosphorylation cell cycle mitotic nuclear envelope disassembly mitotic nuclear envelope reassembly kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation protein kinase binding nucleosomal histone binding histone kinase activity (H3-S10 specific) histone H3-S10 phosphorylation protein autophosphorylation cell division histone kinase activity (H3-T3 specific) histone H3-T3 phosphorylation Golgi disassembly uc001yft.1 uc001yft.2 uc001yft.3 uc001yft.4 uc001yft.5 
ENST00000216714.8 APEX1 ENST00000216714.8 apurinic/apyrimidinic endodeoxyribonuclease 1, transcript variant 1 (from RefSeq NM_001641.4) APEX1 ENST00000216714.1 ENST00000216714.2 ENST00000216714.3 ENST00000216714.4 ENST00000216714.5 ENST00000216714.6 ENST00000216714.7 NM_001641 Q5TZP7 Q5TZP7_HUMAN hCG_40473 uc001vxg.1 uc001vxg.2 uc001vxg.3 uc001vxg.4 uc001vxg.5 The APEX gene encodes the major AP endonuclease in human cells. It encodes the APEX endonuclease, a DNA repair enzyme with apurinic/apyrimidinic (AP) activity. Such AP activity sites occur frequently in DNA molecules by spontaneous hydrolysis, by DNA damaging agents or by DNA glycosylases that remove specific abnormal bases. The AP sites are the most frequent pre-mutagenic lesions that can prevent normal DNA replication. Splice variants have been found for this gene; all encode the same protein. Disruptions in the biological functions related to APEX are associated with many various malignancies and neurodegenerative diseases.[provided by RefSeq, Dec 2019]. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence= Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence= Note=Probably binds two magnesium or manganese ions per subunit. ; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Nucleus Cytoplasm Mitochondrion Belongs to the DNA repair enzymes AP/ExoA family. DNA binding nuclease activity endonuclease activity endoribonuclease activity nucleus transcription factor complex cytoplasm mitochondrion centrosome DNA repair cellular response to DNA damage stimulus aging response to organonitrogen compound negative regulation of smooth muscle cell migration hydrolase activity lyase activity response to drug macromolecular complex binding cell redox homeostasis metal ion binding NF-kappaB binding cellular response to hydrogen peroxide cellular response to cAMP cellular response to peptide hormone stimulus cellular response to organonitrogen compound nucleic acid phosphodiester bond hydrolysis RNA phosphodiester bond hydrolysis, endonucleolytic positive regulation of G1/S transition of mitotic cell cycle uc001vxg.1 uc001vxg.2 uc001vxg.3 uc001vxg.4 uc001vxg.5 
ENST00000216727.9 PABPN1 ENST00000216727.9 poly(A) binding protein nuclear 1, transcript variant 1 (from RefSeq NM_004643.4) D3DS49 ENST00000216727.1 ENST00000216727.2 ENST00000216727.3 ENST00000216727.4 ENST00000216727.5 ENST00000216727.6 ENST00000216727.7 ENST00000216727.8 NM_004643 O43484 PAB2 PABP2 PABP2_HUMAN PABPN1 Q86U42 uc001wjk.1 uc001wjk.2 uc001wjk.3 uc001wjk.4 uc001wjk.5 This gene encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. The protein is required for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and controls the size of the poly(A) tail to about 250 nt. At steady-state, this protein is localized in the nucleus whereas a different poly(A) binding protein is localized in the cytoplasm. This gene contains a GCG trinucleotide repeat at the 5' end of the coding region, and expansion of this repeat from the normal 6 copies to 8-13 copies leads to autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Related pseudogenes have been identified on chromosomes 19 and X. Read-through transcription also exists between this gene and the neighboring upstream BCL2-like 2 (BCL2L2) gene. [provided by RefSeq, Dec 2010]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.332773.1, SRR1163655.418336.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Involved in the 3'-end formation of mRNA precursors (pre- mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product (By similarity). Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length (By similarity). Increases the affinity of poly(A) polymerase for RNA (By similarity). Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle- specific genes (PubMed:11371506). Binds to poly(A) and to poly(G) with high affinity (By similarity). May protect the poly(A) tail from degradation (By similarity). Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters (PubMed:27871484). May interact with SETX (PubMed:21700224). Monomer and homooligomer. Binds RNA as a monomer and oligomerizes when bound to poly(A). Interacts with PAPOLA, but only in presence of oligo(A) RNA. Interacts with transportin. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Association in a ternary complex with CPSF4 and influenza A virus NS1 blocks pre-mRNAs processing, thereby preventing nuclear export of host cell mRNAs. Associates in a single complex with SKIP and MYOD1 and interacts with SKIP in differentiated myocytes. Interacts with NUDT21/CPSF5. Interacts (via RRM domain and C-terminal arginine-rich region) with ZFP36 (via hypophosphorylated form); this interaction occurs in the nucleus in a RNA-independent manner, decreases in presence of single-stranded poly(A) RNA-oligomer and in a p38-dependent-manner and may down- regulated RNA poly(A) polymerase activity (By similarity). Component of the poly(A) tail exosome targeting (PAXT) complex made of accessory factors, such as PABPN1, ZFC3H1 and MTREX (PubMed:27871484). Interacts with ZFC3H1 in a RNase-insensitive manner (PubMed:27871484). Interacts with FRG1 (PubMed:17103222). Q86U42; P11940: PABPC1; NbExp=2; IntAct=EBI-1226435, EBI-81531; Q86U42; Q13573: SNW1; NbExp=5; IntAct=EBI-1226435, EBI-632715; Nucleus toplasm cleus speckle Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus (PubMed:10688363). Its nuclear import may involve the nucleocytoplasmic transport receptor transportin and a RAN-GTP- sensitive import mechanism (By similarity). Is exported to the cytoplasm by a carrier-mediated pathway that is independent of mRNA traffic. Colocalizes with SKIP and poly(A) RNA in nuclear speckles (By similarity). Intranuclear filamentous inclusions or 'aggregates' are detected in the myocytes of patients; these inclusions contain PABPN1, ubiquitin, subunits of the proteasome and poly(A) RNA. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q86U42-1; Sequence=Displayed; Name=2; IsoId=Q86U42-2; Sequence=VSP_009847, VSP_009848; Name=3; Synonyms=BCL2L2-PABPN1; IsoId=Q92843-2; Sequence=External; Ubiquitous. The RRM domain is essential for specific adenine bases recognition in the poly(A) tail but not sufficient for poly(A) binding. Arginine dimethylation is asymmetric and involves PRMT1 and PRMT3. It does not influence the RNA binding properties (By similarity). The poly-Ala region of PABPN1 is polymorphic (6-7 repeats) in the population and is expanded to 8-13 repeats in OPMD patients. Compound heterozygotes for (GCG)9 mutation and a (GCG)7 allele result in earlier onset and more severe clinical manifestations of the disease. Oculopharyngeal muscular dystrophy (OPMD) [MIM:164300]: A form of late-onset slowly progressive myopathy characterized by eyelid ptosis, dysphagia and, sometimes by other cranial and limb-muscle involvement. Note=The disease is caused by variants affecting the gene represented in this entry. The association of the expanded polyalanine mutations together with the capability to oligomerize may induce intranuclear inclusions and cell death. Expanded polyalanine mutations may either result from unequal crossing over during germ cell homologous recombination or from DNA slippage. The pathogenic mechanisms mediated by polyalanine expansion mutations may be either a general disruption of cellular RNA metabolism due to the trapping by the inclusions of PABPN1, mRNAs and/or nuclear proteins, resulting in the induction of cell death; or may change the normal muscle cell differentiation. [Isoform 2]: May be due to a competing donor splice site. Sequence=CAD62310.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; MAPK cascade mRNA splicing, via spliceosome nucleic acid binding RNA binding protein binding nucleus nucleoplasm cytoplasm termination of RNA polymerase II transcription RNA processing mRNA processing muscle contraction nuclear speck poly(A)+ mRNA export from nucleus mRNA 3'-end processing nuclear inclusion body modification by virus of host mRNA processing RNA polymerase binding cellular response to lipopolysaccharide positive regulation of polynucleotide adenylyltransferase activity ribonucleoprotein complex uc001wjk.1 uc001wjk.2 uc001wjk.3 uc001wjk.4 uc001wjk.5 
ENST00000216733.8 EFS ENST00000216733.8 embryonal Fyn-associated substrate, transcript variant 1 (from RefSeq NM_005864.4) B2RAJ7 B4DJ56 CASS3 E9PGU2 EFS_HUMAN ENST00000216733.1 ENST00000216733.2 ENST00000216733.3 ENST00000216733.4 ENST00000216733.5 ENST00000216733.6 ENST00000216733.7 NM_005864 O43281 O43282 uc001wjo.1 uc001wjo.2 uc001wjo.3 uc001wjo.4 uc001wjo.5 uc001wjo.6 The protein encoded by this gene is a member of the CAS (CRK-associated substrate) family of adaptor proteins which typically serve as scaffolds for the assembly of larger signaling complexes. These complexes form at the cell surface where integrin binding leads to the subsequent phosphorylation of a CAS protein. Additional binding of SRC family kinases leads to CAS hyperphosphorylation and the creation of binding sites for CRK and other proteins that cause actin cytoskeleton reorganization. This gene plays a role in integrin-mediated cell attachment, spreading, and migration and also plays a role in both normal and malignant cellular transformation. This broadly expressed gene has been shown to play a role in neurite outgrowth and its expression in the thymus and lymphocytes is important for T cell maturation and the development of immunological self-tolerance. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2020]. Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES (By similarity). O43281; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-718488, EBI-743598; O43281; P51451: BLK; NbExp=5; IntAct=EBI-718488, EBI-2105445; O43281; P06241: FYN; NbExp=4; IntAct=EBI-718488, EBI-515315; O43281; O75694: NUP155; NbExp=3; IntAct=EBI-718488, EBI-1050769; O43281; Q92882: OSTF1; NbExp=3; IntAct=EBI-718488, EBI-1051152; O43281; O94875: SORBS2; NbExp=3; IntAct=EBI-718488, EBI-311323; O43281; Q9BXA7: TSSK1B; NbExp=3; IntAct=EBI-718488, EBI-6423734; O43281; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-718488, EBI-740727; O43281-2; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-11525448, EBI-11096309; O43281-2; P21549: AGXT; NbExp=3; IntAct=EBI-11525448, EBI-727098; O43281-2; P51451: BLK; NbExp=3; IntAct=EBI-11525448, EBI-2105445; O43281-2; P06241-3: FYN; NbExp=5; IntAct=EBI-11525448, EBI-10691738; O43281-2; Q92990: GLMN; NbExp=3; IntAct=EBI-11525448, EBI-726150; O43281-2; O95872: GPANK1; NbExp=3; IntAct=EBI-11525448, EBI-751540; O43281-2; Q68G74: LHX8; NbExp=3; IntAct=EBI-11525448, EBI-8474075; O43281-2; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-11525448, EBI-14086479; O43281-2; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-11525448, EBI-5662487; O43281-2; A0A0S2Z4D7: NCK1; NbExp=3; IntAct=EBI-11525448, EBI-16429340; O43281-2; A0A0S2Z4E4: NCK1; NbExp=3; IntAct=EBI-11525448, EBI-16432934; O43281-2; E7ERP6: NCK2; NbExp=3; IntAct=EBI-11525448, EBI-16429362; O43281-2; Q13526: PIN1; NbExp=3; IntAct=EBI-11525448, EBI-714158; O43281-2; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-11525448, EBI-2130111; O43281-2; O94875-10: SORBS2; NbExp=3; IntAct=EBI-11525448, EBI-12037893; O43281-2; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-11525448, EBI-8451480; O43281-2; Q9BXA7: TSSK1B; NbExp=3; IntAct=EBI-11525448, EBI-6423734; O43281-2; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-11525448, EBI-1380492; O43281-2; P07947: YES1; NbExp=5; IntAct=EBI-11525448, EBI-515331; Event=Alternative splicing; Named isoforms=3; Name=Efs1; IsoId=O43281-1; Sequence=Displayed; Name=Efs2; IsoId=O43281-2; Sequence=VSP_004232; Name=3; IsoId=O43281-3; Sequence=VSP_004232, VSP_054584; The protein has been detected in lung and placenta. Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains. The SH3-binding sites that bind to the SRC SH3 domain are required for interaction with CRK and are implicated in promotion of serum response element (SRE) activation. The SH3 domain interacts with PTK2/FAK1. Phosphorylated on multiple tyrosine residues. Phosphorylated on tyrosines by FYN and SRC (By similarity). Belongs to the CAS family. protein binding cytoplasm cell adhesion cell migration SH3 domain binding protein domain specific binding intracellular signal transduction actin filament reorganization plasma membrane uc001wjo.1 uc001wjo.2 uc001wjo.3 uc001wjo.4 uc001wjo.5 uc001wjo.6 
ENST00000216756.11 CINP ENST00000216756.11 cyclin dependent kinase 2 interacting protein, transcript variant 1 (from RefSeq NM_032630.3) CINP CINP_HUMAN ENST00000216756.1 ENST00000216756.10 ENST00000216756.2 ENST00000216756.3 ENST00000216756.4 ENST00000216756.5 ENST00000216756.6 ENST00000216756.7 ENST00000216756.8 ENST00000216756.9 F5H7P3 F5H8A7 NM_032630 Q9BW66 Q9NPF9 uc059fna.1 uc059fna.2 The protein encoded by this gene is reported to be a component of the DNA replication complex as well as a genome-maintenance protein. It may interact with proteins important for replication initiation and has been shown to bind chromatin at the G1 phase of the cell cycle and dissociate from chromatin with replication initiation. It may also serve to regulate checkpoint signaling as part of the DNA damage response. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]. ##Evidence-Data-START## Transcript exon combination :: SRR5189658.143715.1, SRR1660803.130635.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216756.11/ ENSP00000216756.6 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the DNA replication complex, which interacts with two kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication (PubMed:16082200, PubMed:19889979). Regulates ATR-mediated checkpoint signaling in response to DNA damage (PubMed:19889979). Also involved in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles (PubMed:35354024). Promotes maturation of pre-60S ribosome together with AFG2A, AFG2B and AIRIM (PubMed:35354024). Homodimer (PubMed:16082200). Interacts with CDK2 and CDC7 (PubMed:16082200). Interacts with the components of the replication complex, MCM2, MCM3, MCM4, MCM5, MCM6, MCM7 and with ORC2-containing complexes (PubMed:16082200). Interacts with ATRIP (PubMed:19889979). Interacts with CEP152 (PubMed:21131973). Associates with pre-60S ribosomal particles (PubMed:35354024). Interacts with AIRIM (PubMed:35354024). Q9BW66; Q9NX04: AIRIM; NbExp=9; IntAct=EBI-739784, EBI-8643161; Q9BW66; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-739784, EBI-746752; Q9BW66; Q13535: ATR; NbExp=5; IntAct=EBI-739784, EBI-968983; Q9BW66; Q8WXE1: ATRIP; NbExp=9; IntAct=EBI-739784, EBI-747353; Q9BW66; Q9H2G9: BLZF1; NbExp=7; IntAct=EBI-739784, EBI-2548012; Q9BW66; Q9BX70: BTBD2; NbExp=3; IntAct=EBI-739784, EBI-710091; Q9BW66; Q8NEF3-2: CCDC112; NbExp=3; IntAct=EBI-739784, EBI-12095166; Q9BW66; Q6P656: CFAP161; NbExp=3; IntAct=EBI-739784, EBI-11901329; Q9BW66; Q96AJ1: CLUAP1; NbExp=5; IntAct=EBI-739784, EBI-739780; Q9BW66; Q96JB2-2: COG3; NbExp=3; IntAct=EBI-739784, EBI-9091495; Q9BW66; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-739784, EBI-7225287; Q9BW66; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-739784, EBI-10244131; Q9BW66; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-739784, EBI-744935; Q9BW66; O95995: GAS8; NbExp=3; IntAct=EBI-739784, EBI-1052570; Q9BW66; Q08379: GOLGA2; NbExp=6; IntAct=EBI-739784, EBI-618309; Q9BW66; A5PKX9: INADL; NbExp=3; IntAct=EBI-739784, EBI-12035052; Q9BW66; Q0VD86: INCA1; NbExp=3; IntAct=EBI-739784, EBI-6509505; Q9BW66; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-739784, EBI-2556193; Q9BW66; P43357: MAGEA3; NbExp=3; IntAct=EBI-739784, EBI-5651459; Q9BW66; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-739784, EBI-16439278; Q9BW66; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-739784, EBI-11977115; Q9BW66; Q9H3L0: MMADHC; NbExp=3; IntAct=EBI-739784, EBI-11111575; Q9BW66; Q08AG7: MZT1; NbExp=5; IntAct=EBI-739784, EBI-2637198; Q9BW66; P17568: NDUFB7; NbExp=3; IntAct=EBI-739784, EBI-1246238; Q9BW66; P26367: PAX6; NbExp=3; IntAct=EBI-739784, EBI-747278; Q9BW66; P78424: POU6F2; NbExp=3; IntAct=EBI-739784, EBI-12029004; Q9BW66; O43663: PRC1; NbExp=3; IntAct=EBI-739784, EBI-741137; Q9BW66; P54821: PRRX1; NbExp=3; IntAct=EBI-739784, EBI-12828023; Q9BW66; P25786: PSMA1; NbExp=3; IntAct=EBI-739784, EBI-359352; Q9BW66; Q04864: REL; NbExp=3; IntAct=EBI-739784, EBI-307352; Q9BW66; Q04864-2: REL; NbExp=3; IntAct=EBI-739784, EBI-10829018; Q9BW66; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-739784, EBI-748601; Q9BW66; P62316: SNRPD2; NbExp=3; IntAct=EBI-739784, EBI-297993; Q9BW66; Q02086-2: SP2; NbExp=3; IntAct=EBI-739784, EBI-9088579; Q9BW66; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-739784, EBI-6872807; Q9BW66; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-739784, EBI-11139477; Q9BW66; Q6F5E7: TXNRD3NB; NbExp=3; IntAct=EBI-739784, EBI-18122152; Q9BW66; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-739784, EBI-12287587; Q9BW66; P17023: ZNF19; NbExp=3; IntAct=EBI-739784, EBI-12884200; Q9BW66; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-739784, EBI-4395669; Nucleus Note=Binds to nuclear under G1 conditions, and dissociates from chromatin with the start of DNA replication. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9BW66-1; Sequence=Displayed; Name=2; IsoId=Q9BW66-2; Sequence=VSP_045342, VSP_045343; Name=3; IsoId=Q9BW66-3; Sequence=VSP_046386; Phosphorylated by CDC7 but not by CDK2. Belongs to the CINP family. Sequence=BU174070; Type=Frameshift; Evidence=; protein binding nucleus DNA replication DNA repair cellular response to DNA damage stimulus cell cycle cell division uc059fna.1 uc059fna.2 
ENST00000216774.11 SRP54 ENST00000216774.11 signal recognition particle 54, transcript variant 1 (from RefSeq NM_003136.4) B2R759 B4DUW6 ENST00000216774.1 ENST00000216774.10 ENST00000216774.2 ENST00000216774.3 ENST00000216774.4 ENST00000216774.5 ENST00000216774.6 ENST00000216774.7 ENST00000216774.8 ENST00000216774.9 NM_003136 P13624 P61011 SRP54 SRP54_HUMAN uc059asx.1 uc059asx.2 Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (PubMed:34020957). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (PubMed:34020957). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (PubMed:28972538, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (PubMed:34020957). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (PubMed:28972538, PubMed:29914977). Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence=; Component of a signal recognition particle (SRP) complex that consists of a 7SL RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:12244299). Interacts with RNPS1 (PubMed:14729963). Interacts with the SRP receptor subunit SRPRA (PubMed:34020957). Nucleus speckle Cytoplasm Endoplasmic reticulum Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P61011-1; Sequence=Displayed; Name=2; IsoId=P61011-2; Sequence=VSP_043696; up-regulated during granulocytic differentiation. The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit SRPRA (PubMed:34020957). The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another (PubMed:34020957). SRP receptor compaction upon binding with cargo- loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957). The M domain binds the 7SL RNA in presence of SRP19 and binds the signal sequence of presecretory proteins. Neutropenia, severe congenital 8, autosomal dominant (SCN8) [MIM:618752]: A form of severe congenital neutropenia, a disorder of hematopoiesis characterized by maturation arrest of granulopoiesis at the level of promyelocytes with peripheral blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of severe bacterial infections. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the GTP-binding SRP family. SRP54 subfamily. Name=Wikipedia; Note=Signal recognition particle entry; URL="https://en.wikipedia.org/wiki/Signal_recognition_particle"; nucleotide binding RNA binding GTPase activity protein binding GTP binding nucleus cytoplasm signal recognition particle, endoplasmic reticulum targeting cytosol SRP-dependent cotranslational protein targeting to membrane SRP-dependent cotranslational protein targeting to membrane, translocation SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition drug binding 7S RNA binding nuclear speck GDP binding endoplasmic reticulum signal peptide binding response to drug ribonucleoprotein complex binding protein targeting to ER signal recognition particle nucleolus uc059asx.1 uc059asx.2 
ENST00000216780.9 PCK2 ENST00000216780.9 phosphoenolpyruvate carboxykinase 2, mitochondrial, transcript variant 1 (from RefSeq NM_004563.4) B4DW73 ENST00000216780.1 ENST00000216780.2 ENST00000216780.3 ENST00000216780.4 ENST00000216780.5 ENST00000216780.6 ENST00000216780.7 ENST00000216780.8 NM_004563 O43253 PCK2 PCKGM_HUMAN PEPCK2 Q16822 Q86U01 Q9BV62 uc001wlt.1 uc001wlt.2 uc001wlt.3 uc001wlt.4 uc001wlt.5 This gene encodes a mitochondrial enzyme that catalyzes the conversion of oxaloacetate to phosphoenolpyruvate in the presence of guanosine triphosphate (GTP). A cytosolic form of this protein is encoded by a different gene and is the key enzyme of gluconeogenesis in the liver. Alternatively spliced transcript variants have been described. [provided by RefSeq, Apr 2014]. Mitochondrial phosphoenolpyruvate carboxykinase that catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed:28955899). Can play an active role in glyceroneogenesis and gluconeogenesis (PubMed:28955899). Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Binds 1 Mn(2+) ion per subunit. ; Kinetic parameters: KM=585 uM for phosphoenolpyruvate ; KM=8.7 uM for oxaloacetate ; KM=29 uM for GTP ; KM=200 uM for Mn(2+) ; KM=3.5 uM for Mn(2+) (in presence of Mg(2+)) ; Note=kcat is 32 sec(-1) with oxaloacetate as substrate. kcat is 585 sec(-1) with phosphoenolpyruvate as substrate. ; Carbohydrate biosynthesis; gluconeogenesis. Monomer. Q16822; P84022: SMAD3; NbExp=2; IntAct=EBI-2825219, EBI-347161; Mitochondrion Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q16822-1; Sequence=Displayed; Name=2; IsoId=Q16822-2; Sequence=VSP_038783; Name=3; IsoId=Q16822-3; Sequence=VSP_059389; Widely expressed. Mitochondrial phosphoenolpyruvate carboxykinase deficiency (M- PEPCKD) [MIM:261650]: Metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autopsy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait. Note=The gene represented in this entry may be involved in disease pathogenesis. In eukaryotes there are two isozymes: a cytoplasmic one and a mitochondrial one. Belongs to the phosphoenolpyruvate carboxykinase [GTP] family. Sequence=CAD62600.1; Type=Erroneous initiation; Evidence=; nucleotide binding phosphoenolpyruvate carboxykinase activity phosphoenolpyruvate carboxykinase (GTP) activity protein binding GTP binding mitochondrion mitochondrial matrix cytosol pyruvate metabolic process gluconeogenesis lyase activity carboxy-lyase activity purine nucleotide binding propionate catabolic process manganese ion binding cellular response to insulin stimulus response to lipid response to starvation glycerol biosynthetic process from pyruvate metal ion binding hepatocyte differentiation cellular response to glucose stimulus cellular response to dexamethasone stimulus uc001wlt.1 uc001wlt.2 uc001wlt.3 uc001wlt.4 uc001wlt.5 
ENST00000216797.10 NFKBIA ENST00000216797.10 NFKB inhibitor alpha (from RefSeq NM_020529.3) B2R8L6 ENST00000216797.1 ENST00000216797.2 ENST00000216797.3 ENST00000216797.4 ENST00000216797.5 ENST00000216797.6 ENST00000216797.7 ENST00000216797.8 ENST00000216797.9 IKBA IKBA_HUMAN MAD3 NFKBI NM_020529 P25963 uc001wtf.1 uc001wtf.2 uc001wtf.3 uc001wtf.4 uc001wtf.5 uc001wtf.6 This gene encodes a member of the NF-kappa-B inhibitor family, which contain multiple ankrin repeat domains. The encoded protein interacts with REL dimers to inhibit NF-kappa-B/REL complexes which are involved in inflammatory responses. The encoded protein moves between the cytoplasm and the nucleus via a nuclear localization signal and CRM1-mediated nuclear export. Mutations in this gene have been found in ectodermal dysplasia anhidrotic with T-cell immunodeficiency autosomal dominant disease. [provided by RefSeq, Aug 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC004983.1, M69043.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216797.10/ ENSP00000216797.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL (RELA/p65 and NFKB1/p50) dimers in the cytoplasm by masking their nuclear localization signals (PubMed:1493333, PubMed:7479976, PubMed:36651806). On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription (PubMed:7796813, PubMed:7628694, PubMed:7878466, PubMed:7479976). Interacts with RELA; the interaction requires the nuclear import signal (PubMed:1493333). Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14 (PubMed:9751059). Interacts with NKIRAS1 and NKIRAS2 (PubMed:10657303). Interacts with isoform 1 and isoform 2 of RWDD3; the interaction enhances sumoylation (PubMed:17956732, PubMed:23469069). Interacts with PRMT2 (PubMed:16648481). Interacts with PRKACA in platelets; this interaction is disrupted by thrombin and collagen (PubMed:20356841). Interacts with MEFV (PubMed:18577712). Interacts with DDRGK1; positively regulates NFKBIA phosphorylation and degradation (PubMed:23675531). (Microbial infection) Interacts with HBV protein X. P25963; O15111: CHUK; NbExp=15; IntAct=EBI-307386, EBI-81249; P25963; Q8N668: COMMD1; NbExp=3; IntAct=EBI-307386, EBI-1550112; P25963; P35221: CTNNA1; NbExp=5; IntAct=EBI-307386, EBI-701918; P25963; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-307386, EBI-744099; P25963; Q9UKB1: FBXW11; NbExp=2; IntAct=EBI-307386, EBI-355189; P25963; P25098: GRK2; NbExp=2; IntAct=EBI-307386, EBI-3904795; P25963; P34947: GRK5; NbExp=2; IntAct=EBI-307386, EBI-7149314; P25963; Q9NWT6: HIF1AN; NbExp=6; IntAct=EBI-307386, EBI-745632; P25963; O14920: IKBKB; NbExp=27; IntAct=EBI-307386, EBI-81266; P25963; Q9Y6K9: IKBKG; NbExp=6; IntAct=EBI-307386, EBI-81279; P25963; Q14511: NEDD9; NbExp=3; IntAct=EBI-307386, EBI-2108053; P25963; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-307386, EBI-11746523; P25963; P19838: NFKB1; NbExp=8; IntAct=EBI-307386, EBI-300010; P25963; Q00653: NFKB2; NbExp=2; IntAct=EBI-307386, EBI-307326; P25963; P25963: NFKBIA; NbExp=2; IntAct=EBI-307386, EBI-307386; P25963; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-307386, EBI-11956563; P25963; O43242: PSMD3; NbExp=3; IntAct=EBI-307386, EBI-357622; P25963; Q04864: REL; NbExp=3; IntAct=EBI-307386, EBI-307352; P25963; Q04206: RELA; NbExp=25; IntAct=EBI-307386, EBI-73886; P25963; Q04206-2: RELA; NbExp=2; IntAct=EBI-307386, EBI-289947; P25963; P23396: RPS3; NbExp=6; IntAct=EBI-307386, EBI-351193; P25963; P56279: TCL1A; NbExp=3; IntAct=EBI-307386, EBI-749995; P25963; P0CG48: UBC; NbExp=3; IntAct=EBI-307386, EBI-3390054; P25963; Q60680-2: Chuk; Xeno; NbExp=2; IntAct=EBI-307386, EBI-646264; P25963; Q9J0X9: UL54; Xeno; NbExp=3; IntAct=EBI-307386, EBI-7967856; P25963; P14340; Xeno; NbExp=2; IntAct=EBI-307386, EBI-465733; P25963; PRO_0000037965 [P14340]; Xeno; NbExp=2; IntAct=EBI-307386, EBI-9825968; P25963; PRO_0000038062 [P21530]; Xeno; NbExp=4; IntAct=EBI-307386, EBI-12558622; P25963; Q9E7P0; Xeno; NbExp=2; IntAct=EBI-307386, EBI-11361108; Cytoplasm Nucleus te=Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export. Induced in adherent monocytes. Phosphorylated at Ser-32 and Ser-36 by IKKA/CHUK and IKKB/IKBKB; disables inhibition of NF-kappa-B DNA-binding activity (PubMed:7796813, PubMed:7628694, PubMed:7878466, PubMed:8631829, PubMed:9701247, PubMed:10329681, PubMed:10882136). Phosphorylation at positions 32 and 36 is prerequisite to recognition by the SCF(FBXW11) and SCF(BTRC) complexes, leading to polyubiquitination and subsequent degradation (PubMed:7628694, PubMed:8631829, PubMed:9701247, PubMed:10329681). Phosphorylated at Ser-32 in response to FK506 treatment: phosphorylation is independent of IKKA/CHUK and IKKB/IKBKB and promotes NFKBIA degradation, followed by NF-kappa-B activation (PubMed:10574930). Phosphorylated at Tyr-42: its effect is however unclear (PubMed:8797825, PubMed:8940099). According to a report, phosphorylation at Tyr-42 activates NF-kappa-B without triggering proteolytic degradation of NFKBIA (PubMed:8797825). According to another publication, phosphorylation at Tyr-42 inhibits NF-kappa-B activity by preventing phosphorylation at Ser-32 and Ser-36 and subsequent ubiquitination and degradation (PubMed:8940099). Polyubiquitinated at Lys-21 and/or Lys-22 following phosphorylation at Ser-32 and Ser-36 (PubMed:7479976, PubMed:8631829, PubMed:9701247, PubMed:10329681, PubMed:20347421). Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3 (PubMed:7479976, PubMed:10329681, PubMed:20347421). Ubiquitin chain elongation is then performed by CDC34 in cooperation with the SCF(FBXW11) E3 ligase complex, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin (PubMed:10437795, PubMed:20347421). The resulting polyubiquitination leads to protein degradation (PubMed:7628694, PubMed:7479976, PubMed:20347421). Also ubiquitinated by the SCF(BTRC) complex following stimulus-dependent phosphorylation at Ser-32 and Ser-36 (PubMed:10644755). Deubiquitinated by USP38, leading to NF-kappa-B inhibition (PubMed:36651806). Sumoylated; sumoylation requires the presence of the nuclear import signal. Sumoylation blocks ubiquitination and proteasome- mediated degradation of the protein thereby increasing the protein stability. Hydroxylated by HIF1AN. (Microbial infection) Deubiquitinated by porcine reproductive and respiratory syndrome virus Nsp2 protein, which thereby interferes with NFKBIA degradation and impairs subsequent NF-kappa-B activation. Ectodermal dysplasia and immunodeficiency 2 (EDAID2) [MIM:612132]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. This form of ectodermal dysplasia is associated with decreased production of pro-inflammatory cytokines and certain interferons, rendering patients susceptible to infection. EDAID2 inheritance is autosomal dominant. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the NF-kappa-B inhibitor family. Name=NFKBIAbase; Note=NFKBIA mutation db; URL="http://structure.bmc.lu.se/idbase/NFKBIAbase/"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/nfkbia/"; protein binding nucleus nucleoplasm cytoplasm cytosol plasma membrane protein import into nucleus apoptotic process I-kappaB kinase/NF-kappaB signaling cytoplasmic sequestering of NF-kappaB transcription factor binding nuclear localization sequence binding regulation of gene expression negative regulation of macrophage derived foam cell differentiation positive regulation of cholesterol efflux negative regulation of lipid storage viral process protein deubiquitination enzyme binding ubiquitin protein ligase binding lipopolysaccharide-mediated signaling pathway negative regulation of NF-kappaB transcription factor activity positive regulation of cellular protein metabolic process response to muramyl dipeptide response to lipopolysaccharide tumor necrosis factor-mediated signaling pathway I-kappaB/NF-kappaB complex toll-like receptor 4 signaling pathway response to muscle stretch regulation of cell proliferation identical protein binding cytoplasmic sequestering of transcription factor negative regulation of apoptotic process response to exogenous dsRNA negative regulation of DNA binding negative regulation of myeloid cell differentiation negative regulation of Notch signaling pathway positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter positive regulation of inflammatory response NF-kappaB binding cellular response to cold nucleotide-binding oligomerization domain containing 1 signaling pathway nucleotide-binding oligomerization domain containing 2 signaling pathway interleukin-1-mediated signaling pathway cellular response to tumor necrosis factor regulation of NIK/NF-kappaB signaling uc001wtf.1 uc001wtf.2 uc001wtf.3 uc001wtf.4 uc001wtf.5 uc001wtf.6 
ENST00000216799.9 EMC9 ENST00000216799.9 ER membrane protein complex subunit 9, transcript variant 1 (from RefSeq NM_016049.4) C14orf122 CGI-112 D3DS60 EMC9_HUMAN ENST00000216799.1 ENST00000216799.2 ENST00000216799.3 ENST00000216799.4 ENST00000216799.5 ENST00000216799.6 ENST00000216799.7 ENST00000216799.8 FAM158A NM_016049 Q9BUM3 Q9Y3B6 uc001wmi.1 uc001wmi.2 uc001wmi.3 uc001wmi.4 Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:30415835, PubMed:29809151, PubMed:29242231). Involved in the cotranslational insertion of multi- pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:30415835, PubMed:29809151). It is also required for the post-translational insertion of tail- anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N- exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable). Component of the ER membrane protein complex (EMC) (PubMed:22119785, PubMed:29242231, PubMed:32459176). EMC8 and EMC9 are mutually exclusive subunits of the EMC complex (PubMed:32459176). Q9Y3B6; Q15006: EMC2; NbExp=10; IntAct=EBI-748366, EBI-359031; Q9Y3B6; Q14524-3: SCN5A; NbExp=3; IntAct=EBI-748366, EBI-14276801; Endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side Belongs to the EMC8/EMC9 family. protein binding cytoplasm ER membrane protein complex uc001wmi.1 uc001wmi.2 uc001wmi.3 uc001wmi.4 
ENST00000216802.10 PSME2 ENST00000216802.10 proteasome activator subunit 2 (from RefSeq NM_002818.3) ENST00000216802.1 ENST00000216802.2 ENST00000216802.3 ENST00000216802.4 ENST00000216802.5 ENST00000216802.6 ENST00000216802.7 ENST00000216802.8 ENST00000216802.9 NM_002818 PSME2_HUMAN Q15129 Q9UL46 uc001wmj.1 uc001wmj.2 uc001wmj.3 uc001wmj.4 uc001wmj.5 The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the beta subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three beta and three alpha subunits combine to form a heterohexameric ring. Six pseudogenes have been identified on chromosomes 4, 5, 8, 10 and 13. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK026580.1, SRR1163655.105740.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216802.10/ ENSP00000216802.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome. Heterodimer of PSME1 and PSME2, which forms a hexameric ring. Q9UL46; Q9BVJ7: DUSP23; NbExp=3; IntAct=EBI-741630, EBI-724940; Q9UL46; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-741630, EBI-739832; Q9UL46; Q06323: PSME1; NbExp=6; IntAct=EBI-741630, EBI-712149; Q9UL46; Q9UL46: PSME2; NbExp=6; IntAct=EBI-741630, EBI-741630; Q9UL46; O00560: SDCBP; NbExp=3; IntAct=EBI-741630, EBI-727004; Q9UL46; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-741630, EBI-607755; By IFNG/IFN-gamma. Belongs to the PA28 family. MAPK cascade protein polyubiquitination proteasome complex stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent protein binding nucleoplasm cytoplasm cytosol regulation of cellular amino acid metabolic process proteasome activator complex positive regulation of endopeptidase activity negative regulation of G2/M transition of mitotic cell cycle membrane protein deubiquitination anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway interleukin-12-mediated signaling pathway NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway identical protein binding proteasome-mediated ubiquitin-dependent protein catabolic process regulation of mRNA stability post-translational protein modification T cell receptor signaling pathway transmembrane transport Wnt signaling pathway, planar cell polarity pathway endopeptidase activator activity regulation of proteasomal protein catabolic process regulation of transcription from RNA polymerase II promoter in response to hypoxia extracellular exosome interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation regulation of G1/S transition of mitotic cell cycle uc001wmj.1 uc001wmj.2 uc001wmj.3 uc001wmj.4 uc001wmj.5 
ENST00000216807.12 BRMS1L ENST00000216807.12 BRMS1 like transcriptional repressor (from RefSeq NM_032352.4) A6NFW5 A6NH45 B2RD65 BRM1L_HUMAN ENST00000216807.1 ENST00000216807.10 ENST00000216807.11 ENST00000216807.2 ENST00000216807.3 ENST00000216807.4 ENST00000216807.5 ENST00000216807.6 ENST00000216807.7 ENST00000216807.8 ENST00000216807.9 NM_032352 Q5PSV4 Q9BRI4 uc001wtl.1 uc001wtl.2 uc001wtl.3 uc001wtl.4 uc001wtl.5 The protein encoded by this gene shows sequence similarity to the human breast carcinoma metastasis suppressor (BRMS1) protein and the mammalian Sds3 (suppressor of defective silencing 3) proteins. This protein is a component of the mSin3a family of histone deacetylase complexes (HDAC). [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.414428.1, SRR3476690.829117.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216807.12/ ENSP00000216807.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Involved in the histone deacetylase (HDAC1)-dependent transcriptional repression activity. When overexpressed in lung cancer cell line that lacks p53/TP53 expression, inhibits cell growth. Component of the Sin3/HDAC1 corepressor complex at least composed of BRMS1, BRMS1L and ING2/ING1L. Interacts with HDAC and SIN3A. Q5PSV4; P35609: ACTN2; NbExp=7; IntAct=EBI-5666615, EBI-77797; Q5PSV4; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-5666615, EBI-746752; Q5PSV4; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-5666615, EBI-10187270; Q5PSV4; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-5666615, EBI-739624; Q5PSV4; Q05D60: DEUP1; NbExp=3; IntAct=EBI-5666615, EBI-748597; Q5PSV4; O00471: EXOC5; NbExp=3; IntAct=EBI-5666615, EBI-949824; Q5PSV4; P22607: FGFR3; NbExp=3; IntAct=EBI-5666615, EBI-348399; Q5PSV4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-5666615, EBI-8285963; Q5PSV4; P01112: HRAS; NbExp=3; IntAct=EBI-5666615, EBI-350145; Q5PSV4; Q96EZ8: MCRS1; NbExp=5; IntAct=EBI-5666615, EBI-348259; Q5PSV4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-5666615, EBI-10172526; Q5PSV4; P40424: PBX1; NbExp=3; IntAct=EBI-5666615, EBI-301611; Q5PSV4; P40425: PBX2; NbExp=3; IntAct=EBI-5666615, EBI-348489; Q5PSV4; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-5666615, EBI-11523345; Q5PSV4; P40222: TXLNA; NbExp=3; IntAct=EBI-5666615, EBI-359793; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q5PSV4-1; Sequence=Displayed; Name=2; IsoId=Q5PSV4-2; Sequence=VSP_055547; Belongs to the BRMS1 family. negative regulation of transcription from RNA polymerase II promoter protein binding nucleus histone deacetylation regulation of growth histone deacetylase binding Sin3-type complex histone deacetylase activity uc001wtl.1 uc001wtl.2 uc001wtl.3 uc001wtl.4 uc001wtl.5 
ENST00000216832.9 PNN ENST00000216832.9 pinin, desmosome associated protein (from RefSeq NM_002687.4) B4DZX8 DRS ENST00000216832.1 ENST00000216832.2 ENST00000216832.3 ENST00000216832.4 ENST00000216832.5 ENST00000216832.6 ENST00000216832.7 ENST00000216832.8 MEMA NM_002687 O60899 PININ_HUMAN Q53EM7 Q6P5X4 Q7KYL1 Q99738 Q9H307 Q9UHZ9 Q9UQR9 uc001wuw.1 uc001wuw.2 uc001wuw.3 uc001wuw.4 uc001wuw.5 uc001wuw.6 Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma. Found in a mRNA splicing-dependent exon junction complex (EJC). Found in a complex with SR proteins. Found in a mRNP complex with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18 and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19, PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome C complex. Q9H307; Q9UKV3: ACIN1; NbExp=2; IntAct=EBI-681904, EBI-396258; Q9H307; P68400: CSNK2A1; NbExp=2; IntAct=EBI-681904, EBI-347804; Q9H307; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-681904, EBI-3044087; Q9H307; Q15287-1: RNPS1; NbExp=3; IntAct=EBI-681904, EBI-15972541; Q9H307; O00422: SAP18; NbExp=2; IntAct=EBI-681904, EBI-1044156; Q9H307; Q13573: SNW1; NbExp=3; IntAct=EBI-681904, EBI-632715; Nucleus speckle. Cell junction, desmosome. Note=Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein. Expressed in placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon, heart, epidermis, esophagus, brain and smooth and skeletal muscle. Expressed strongly in melanoma metastasis lesions and advanced primary tumors. Belongs to the pinin family. Sequence=CAA70874.1; Type=Frameshift; Evidence=; mRNA splicing, via spliceosome DNA binding RNA binding structural molecule activity protein binding nucleus spliceosomal complex intermediate filament plasma membrane cell-cell junction mRNA processing cell adhesion RNA splicing membrane nuclear speck cell junction desmosome exon-exon junction complex catalytic step 2 spliceosome uc001wuw.1 uc001wuw.2 uc001wuw.3 uc001wuw.4 uc001wuw.5 uc001wuw.6 
ENST00000216840.11 RABGGTA ENST00000216840.11 Rab geranylgeranyltransferase subunit alpha, transcript variant 1 (from RefSeq NM_182836.3) A8K5N2 D3DS69 ENST00000216840.1 ENST00000216840.10 ENST00000216840.2 ENST00000216840.3 ENST00000216840.4 ENST00000216840.5 ENST00000216840.6 ENST00000216840.7 ENST00000216840.8 ENST00000216840.9 NM_182836 PGTA_HUMAN Q92696 uc001wog.1 uc001wog.2 uc001wog.3 uc001wog.4 uc001wog.5 uc001wog.6 Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.60; Evidence=; The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM. Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding (PubMed:7991565). The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp (PubMed:18532927). Interacts with non-phosphorylated form of RAB8A; phosphorylation of RAB8A at 'Thr-72' disrupts this interaction (PubMed:26824392). Q92696; P24386: CHM; NbExp=2; IntAct=EBI-9104196, EBI-2515129; Q92696; P53611: RABGGTB; NbExp=4; IntAct=EBI-9104196, EBI-536715; Belongs to the protein prenyltransferase subunit alpha family. prenyltransferase activity Rab geranylgeranyltransferase activity protein binding nucleoplasm cytoplasm cytosol plasma membrane Rab-protein geranylgeranyltransferase complex cellular protein modification process visual perception zinc ion binding protein prenyltransferase activity transferase activity Rab GTPase binding protein prenylation protein geranylgeranylation regulation of apoptotic process post-translational protein modification protein heterodimerization activity macromolecular complex assembly uc001wog.1 uc001wog.2 uc001wog.3 uc001wog.4 uc001wog.5 uc001wog.6 
ENST00000216862.8 CYP24A1 ENST00000216862.8 cytochrome P450 family 24 subfamily A member 1, transcript variant 5 (from RefSeq NM_001424341.1) CP24A_HUMAN CYP24 CYP24A1 ENST00000216862.1 ENST00000216862.2 ENST00000216862.3 ENST00000216862.4 ENST00000216862.5 ENST00000216862.6 ENST00000216862.7 NM_001424341 Q07973 Q15807 Q32ML3 Q5I2W7 uc002xwv.1 uc002xwv.2 uc002xwv.3 uc002xwv.4 A cytochrome P450 monooxygenase with a key role in vitamin D catabolism and calcium homeostasis. Via C24- and C23-oxidation pathways, catalyzes the inactivation of both the vitamin D precursor calcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3)) (PubMed:24893882, PubMed:15574355, PubMed:8679605, PubMed:11012668, PubMed:16617161, PubMed:29461981). With initial hydroxylation at C-24 (via C24-oxidation pathway), performs a sequential 6-step oxidation of calcitriol leading to the formation of the biliary metabolite calcitroic acid (PubMed:24893882, PubMed:15574355). With initial hydroxylation at C-23 (via C23-oxidation pathway), catalyzes sequential oxidation of calcidiol leading to the formation of 25(OH)D3-26,23-lactone as end product (PubMed:11012668, PubMed:8679605). Preferentially hydroxylates at C-25 other vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S- hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol (PubMed:25727742). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin (PubMed:8679605). Reaction=calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitetrol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24964, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799; EC=1.14.15.16; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24965; Evidence=; Reaction=calcitetrol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)- 1,25-dihydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24972, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799, ChEBI:CHEBI:47812; EC=1.14.15.16; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24973; Evidence=; Reaction=(1S)-1,25-dihydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,23,25-trihydroxy-24-oxocalciol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24976, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47812, ChEBI:CHEBI:47813; EC=1.14.15.16; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24977; Evidence=; Reaction=(1S)-1,23-dihydroxy-24,25,26,27-tetranorcalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1-hydroxy-23-oxo-24,25,26,27- tetranorcalciol + 2 H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24984, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47818, ChEBI:CHEBI:47820; EC=1.14.15.16; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24985; Evidence=; Reaction=(1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + H(+) + O2 + 2 reduced [adrenodoxin] = calcitroate + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24988, Rhea:RHEA-COMP:9998, Rhea:RHEA- COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47820, ChEBI:CHEBI:58715; EC=1.14.15.16; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24989; Evidence=; Reaction=calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 1alpha,23S,25-trihydroxycholecalciferol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49192, Rhea:RHEA-COMP:9998, Rhea:RHEA- COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90970; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49193; Evidence=; Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2 oxidized [adrenodoxin] + secalciferol; Xref=Rhea:RHEA:24968, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933, ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.16; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24969; Evidence=; Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = 25- hydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49196, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47805; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49197; Evidence=; Reaction=25-hydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 23S,25-dihydroxy-24-oxocholecalciferol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49268, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47805, ChEBI:CHEBI:90980; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49269; Evidence=; Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (23S)- 23,25-dihydroxycalciol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:46616, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47214; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46617; Evidence=; Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 20S,25-dihydroxycholecalciferol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49212, Rhea:RHEA-COMP:9998, Rhea:RHEA- COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983, ChEBI:CHEBI:90984; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49213; Evidence=; Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 20S,24R-dihydroxycholecalciferol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49204, Rhea:RHEA-COMP:9998, Rhea:RHEA- COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983, ChEBI:CHEBI:90985; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49205; Evidence=; Reaction=20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 20S,23,25-trihydroxycholecalciferol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49396, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:91306, ChEBI:CHEBI:91308; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49397; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Kinetic parameters: KM=0.16 uM for calcidiol ; KM=0.072 uM for calcitriol ; KM=0.35 uM for calcitriol ; Vmax=0.088 mol/min/mol enzyme toward calcidiol ; Vmax=0.066 mol/min/mol enzyme toward calcitriol ; Mitochondrion Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q07973-1; Sequence=Displayed; Name=2; IsoId=Q07973-2; Sequence=VSP_043101; Name=3; Synonyms=CYP24-SV; IsoId=Q07973-3; Sequence=VSP_053367, VSP_053368; Hypercalcemia, infantile, 1 (HCINF1) [MIM:143880]: A disorder characterized by abnormally high level of calcium in the blood, failure to thrive, vomiting, dehydration, and nephrocalcinosis. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 3]: Specifically expressed in macrophages. Lacks the transit peptide. May be a dominant negative-acting isoform possibly by sequestering vitamin D metabolites. Belongs to the cytochrome P450 family. osteoblast differentiation monooxygenase activity iron ion binding nucleus nucleoplasm mitochondrion mitochondrial outer membrane plasma membrane vitamin metabolic process 25-hydroxycholecalciferol-24-hydroxylase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen heme binding 1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity response to vitamin D vitamin D metabolic process vitamin D catabolic process metal ion binding oxidation-reduction process vitamin D receptor signaling pathway uc002xwv.1 uc002xwv.2 uc002xwv.3 uc002xwv.4 
ENST00000216879.9 NSFL1C ENST00000216879.9 NSFL1 cofactor, transcript variant 1 (from RefSeq NM_016143.5) A2A2L1 B2RD74 ENST00000216879.1 ENST00000216879.2 ENST00000216879.3 ENST00000216879.4 ENST00000216879.5 ENST00000216879.6 ENST00000216879.7 ENST00000216879.8 NM_016143 NSF1C_HUMAN Q5JXA4 Q5JXA5 Q7Z533 Q9H102 Q9NVL9 Q9UI06 Q9UNZ2 UBXN2C uc002wfc.1 uc002wfc.2 uc002wfc.3 uc002wfc.4 N-ethylmaleimide-sensitive factor (NSF) and valosin-containing protein (p97) are two ATPases known to be involved in transport vesicle/target membrane fusion and fusions between membrane compartments. A trimer of the protein encoded by this gene binds a hexamer of cytosolic p97 and is required for p97-mediated regrowth of Golgi cisternae from mitotic Golgi fragments. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 8. [provided by RefSeq, May 2011]. Reduces the ATPase activity of VCP (By similarity). Necessary for the fragmentation of Golgi stacks during mitosis and for VCP- mediated reassembly of Golgi stacks after mitosis (By similarity). May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro) (PubMed:15498563). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase (PubMed:23649807). Also, regulates spindle orientation during mitosis (PubMed:23649807). Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine- containing lipids and promotes Golgi membrane fusion. Interaction with VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP. Binds ubiquitin and mono-ubiquitinated proteins via its N-terminal UBA- like domain when bound to VCP (By similarity). Q9UNZ2; Q13148: TARDBP; NbExp=4; IntAct=EBI-721577, EBI-372899; Q9UNZ2; P55072: VCP; NbExp=23; IntAct=EBI-721577, EBI-355164; Nucleus Golgi apparatus, Golgi stack Chromosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Predominantly nuclear in interphase cells. Bound to the axial elements of sex chromosomes in pachytene spermatocytes. A small proportion of the protein is cytoplasmic, associated with Golgi stacks. Localizes to centrosome during mitotic prophase and metaphase. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9UNZ2-1; Sequence=Displayed; Name=2; IsoId=Q9UNZ2-4; Sequence=VSP_009263; Name=3; IsoId=Q9UNZ2-5; Sequence=VSP_009262; Name=4; IsoId=Q9UNZ2-6; Sequence=VSP_041062; Phosphorylated during mitosis. Phosphorylation inhibits interaction with Golgi membranes and is required for the fragmentation of the Golgi stacks during mitosis (By similarity). Belongs to the NSFL1C family. Sequence=AAF17199.1; Type=Frameshift; Evidence=; Sequence=AAF17199.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence=; autophagosome assembly establishment of mitotic spindle orientation protein binding phospholipid binding nucleus nucleoplasm chromosome cytoplasm Golgi apparatus Golgi stack microtubule organizing center cytosol cytoskeleton plasma membrane Golgi organization lipid binding nuclear envelope reassembly spindle pole centrosome ubiquitin binding proteasome-mediated ubiquitin-dependent protein catabolic process intermediate filament cytoskeleton positive regulation of mitotic centrosome separation ATPase binding membrane fusion negative regulation of protein localization to centrosome VCP-NSFL1C complex uc002wfc.1 uc002wfc.2 uc002wfc.3 uc002wfc.4 
ENST00000216923.5 ZFP64 ENST00000216923.5 ZFP64 zinc finger protein, transcript variant 1 (from RefSeq NM_018197.3) A2A2N4 ENST00000216923.1 ENST00000216923.2 ENST00000216923.3 ENST00000216923.4 NM_018197 Q53H69 Q53XQ1 Q5JWM0 Q5JWM1 Q8WU98 Q9H9P1 Q9NPA5 Q9NTS7 Q9NTW7 Q9NVH4 ZF64B_HUMAN ZFP64 ZNF338 uc002xwl.1 uc002xwl.2 uc002xwl.3 uc002xwl.4 uc002xwl.5 May be involved in the regulation of mesenchymal cell differentiation through transactivation of NOTCH1 target genes. Interacts with ZNF70; this interaction promote the transactivation of the HES1 gene (PubMed:27353377). Interacts with NOTCH1 (PubMed:27353377). Q9NTW7; Q8WTP8: AEN; NbExp=7; IntAct=EBI-711679, EBI-8637627; Q9NTW7; Q13895: BYSL; NbExp=5; IntAct=EBI-711679, EBI-358049; Q9NTW7; P50402: EMD; NbExp=3; IntAct=EBI-711679, EBI-489887; Q9NTW7; Q86V42: FAM124A; NbExp=6; IntAct=EBI-711679, EBI-744506; Q9NTW7; Q14192: FHL2; NbExp=8; IntAct=EBI-711679, EBI-701903; Q9NTW7; P28799: GRN; NbExp=3; IntAct=EBI-711679, EBI-747754; Q9NTW7; V9HWH0: HEL164; NbExp=6; IntAct=EBI-711679, EBI-10330301; Q9NTW7; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-711679, EBI-739909; Q9NTW7; P25791: LMO2; NbExp=3; IntAct=EBI-711679, EBI-739696; Q9NTW7; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-711679, EBI-739832; Q9NTW7; P55081: MFAP1; NbExp=3; IntAct=EBI-711679, EBI-1048159; Q9NTW7; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-711679, EBI-1567797; Q9NTW7; P98175: RBM10; NbExp=3; IntAct=EBI-711679, EBI-721525; Q9NTW7; Q8WV44: TRIM41; NbExp=7; IntAct=EBI-711679, EBI-725997; Q9NTW7; O76024: WFS1; NbExp=3; IntAct=EBI-711679, EBI-720609; Q9NTW7-5; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-23201521, EBI-358708; Nucleus Event=Alternative splicing; Named isoforms=6; Name=3; IsoId=Q9NTW7-1; Sequence=Displayed; Name=4; Synonyms=ZNF338; IsoId=Q9NTW7-2; Sequence=VSP_007285, VSP_007286; Name=5; IsoId=Q9NTW7-3; Sequence=VSP_038213, VSP_038214; Name=6; IsoId=Q9NTW7-4; Sequence=VSP_046896, VSP_046897, VSP_046898; Name=1; IsoId=Q9NTW7-5; Sequence=VSP_046897, VSP_046898; Name=2; IsoId=Q9NTW7-6; Sequence=VSP_060092, VSP_046897, VSP_046898; Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=BAD96432.1; Type=Erroneous translation; Note=Translation C-terminally extended.; Evidence=; nucleic acid binding DNA binding protein binding nucleus metal ion binding uc002xwl.1 uc002xwl.2 uc002xwl.3 uc002xwl.4 uc002xwl.5 
ENST00000216962.9 PYGB ENST00000216962.9 glycogen phosphorylase B (from RefSeq NM_002862.4) ENST00000216962.1 ENST00000216962.2 ENST00000216962.3 ENST00000216962.4 ENST00000216962.5 ENST00000216962.6 ENST00000216962.7 ENST00000216962.8 NM_002862 P11216 PYGB PYGB_HUMAN Q96AK1 Q9NPX8 uc002wup.1 uc002wup.2 uc002wup.3 uc002wup.4 uc002wup.5 The protein encoded by this gene is a glycogen phosphorylase found predominantly in the brain. The encoded protein forms homodimers which can associate into homotetramers, the enzymatically active form of glycogen phosphorylase. The activity of this enzyme is positively regulated by AMP and negatively regulated by ATP, ADP, and glucose-6-phosphate. This enzyme catalyzes the rate-determining step in glycogen degradation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803617.211977.1, SRR1660807.231969.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216962.9/ ENSP00000216962.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Glycogen phosphorylase that regulates glycogen mobilization (PubMed:27402852). Phosphorylase is an important allosteric enzyme in carbohydrate metabolism (PubMed:3346228). Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates (PubMed:3346228). However, all known phosphorylases share catalytic and structural properties (PubMed:3346228). Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; Evidence=; Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Activity of phosphorylase is controlled both by allosteric means (through the non-covalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B. Activated upon phosphorylation. Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. P11216; Q86XI6: PPP1R3B; NbExp=3; IntAct=EBI-1047231, EBI-3918864; P11216; P06737: PYGL; NbExp=9; IntAct=EBI-1047231, EBI-2511865; P11216; P11217: PYGM; NbExp=3; IntAct=EBI-1047231, EBI-357469; P11216; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-1047231, EBI-747107; Phosphorylated (PubMed:27402852). Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A (By similarity). Belongs to the glycogen phosphorylase family. catalytic activity phosphorylase activity protein binding extracellular region cytoplasm carbohydrate metabolic process glycogen metabolic process glycogen catabolic process metabolic process glycogen phosphorylase activity membrane transferase activity transferase activity, transferring glycosyl groups pyridoxal phosphate binding azurophil granule lumen neutrophil degranulation extracellular exosome uc002wup.1 uc002wup.2 uc002wup.3 uc002wup.4 uc002wup.5 
ENST00000216968.5 PROCR ENST00000216968.5 protein C receptor (from RefSeq NM_006404.5) B2RC04 ENST00000216968.1 ENST00000216968.2 ENST00000216968.3 ENST00000216968.4 EPCR EPCR_HUMAN NM_006404 Q14218 Q6IB56 Q96CB3 Q9ULX1 Q9UNN8 uc002xbt.1 uc002xbt.2 uc002xbt.3 uc002xbt.4 uc002xbt.5 uc002xbt.6 The protein encoded by this gene is a receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The encoded protein is an N-glycosylated type I membrane protein that enhances the activation of protein C. Mutations in this gene have been associated with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy. The encoded protein may also play a role in malarial infection and has been associated with cancer. [provided by RefSeq, Jul 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC014451.1, SRR5189652.204729.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000216968.5/ ENSP00000216968.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation. Q9UNN8; P25116: F2R; NbExp=5; IntAct=EBI-719705, EBI-2803960; Membrane; Single-pass type I membrane protein. Expressed strongly in the endothelial cells of arteries and veins in heart and lung, less intensely in capillaries in the lung and skin, and not at all in the endothelium of small vessels of the liver and kidney. N-glycosylated. A soluble form exists; probably released by a metalloprotease. Seems to have the same activity as the membrane-bound form. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/procr/"; protein binding extracellular region extracellular space centrosome plasma membrane integral component of plasma membrane focal adhesion blood coagulation hemostasis cell surface membrane integral component of membrane signaling receptor activity perinuclear region of cytoplasm negative regulation of coagulation extracellular exosome uc002xbt.1 uc002xbt.2 uc002xbt.3 uc002xbt.4 uc002xbt.5 uc002xbt.6 
ENST00000217026.5 MYBL2 ENST00000217026.5 MYB proto-oncogene like 2, transcript variant 1 (from RefSeq NM_002466.4) B2RBS5 B7Z8D9 BMYB ENST00000217026.1 ENST00000217026.2 ENST00000217026.3 ENST00000217026.4 F8W6N6 MYBB_HUMAN NM_002466 P10244 Q53F07 uc002xlb.1 uc002xlb.2 uc002xlb.3 uc002xlb.4 The protein encoded by this gene, a member of the MYB family of transcription factor genes, is a nuclear protein involved in cell cycle progression. The encoded protein is phosphorylated by cyclin A/cyclin-dependent kinase 2 during the S-phase of the cell cycle and possesses both activator and repressor activities. It has been shown to activate the cell division cycle 2, cyclin D1, and insulin-like growth factor-binding protein 5 genes. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2013]. Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL22. Interacts with CCNF (via the Cyclin N-terminal domain) (PubMed:25557911). P10244; Q6MZP7: LIN54; NbExp=4; IntAct=EBI-1389468, EBI-1389411; P10244; Q5TKA1: LIN9; NbExp=7; IntAct=EBI-1389468, EBI-1389424; Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P10244-1; Sequence=Displayed; Name=2; IsoId=P10244-2; Sequence=VSP_053987; Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at Thr-520 is probably involved in transcriptional activity. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41469/MYBL2"; mitotic cell cycle RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm regulation of transcription from RNA polymerase II promoter Myb complex positive regulation of neuron apoptotic process positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter regulation of cell cycle mitotic spindle assembly cellular response to leukemia inhibitory factor uc002xlb.1 uc002xlb.2 uc002xlb.3 uc002xlb.4 
ENST00000217043.4 R3HDML ENST00000217043.4 R3H domain containing like (from RefSeq NM_178491.4) CRSPL_HUMAN ENST00000217043.1 ENST00000217043.2 ENST00000217043.3 NM_178491 Q9H3Y0 uc002xls.1 uc002xls.2 uc002xls.3 uc002xls.4 uc002xls.5 Putative serine protease inhibitor. Secreted Belongs to the CRISP family. Despite its name, it does not contain a R3H domain. extracellular region extracellular space negative regulation of peptidase activity peptidase inhibitor activity uc002xls.1 uc002xls.2 uc002xls.3 uc002xls.4 uc002xls.5 
ENST00000217073.7 PABPC1L ENST00000217073.7 poly(A) binding protein cytoplasmic 1 like, transcript variant 5 (from RefSeq NR_134987.2) A0A6Q8JFT6 A0A6Q8JFT6_HUMAN ENST00000217073.1 ENST00000217073.2 ENST00000217073.3 ENST00000217073.4 ENST00000217073.5 ENST00000217073.6 NR_134987 PABPC1L uc061xgi.1 uc061xgi.2 This gene belongs to the polyadenylate-binding protein type-1 family of proteins. Members of this family bind to the polyA tails of mRNAs to regulate mRNA stability and translation. The mouse ortholog of this gene is required for female fertility. In human, expression of a functional protein is regulated by alternative splicing. The protein-coding splice variant for this gene is abundantly expressed in human oocytes, while a noncoding splice variant subject to nonsense-mediated decay is the predominant splice variant expressed in somatic tissues. [provided by RefSeq, Aug 2019]. Binds the poly(A) tail of mRNA. Cytoplasm Belongs to the polyadenylate-binding protein type-1 family. uc061xgi.1 uc061xgi.2 
ENST00000217086.9 SALL4 ENST00000217086.9 spalt like transcription factor 4, transcript variant 1 (from RefSeq NM_020436.5) A2A2D8 ENST00000217086.1 ENST00000217086.2 ENST00000217086.3 ENST00000217086.4 ENST00000217086.5 ENST00000217086.6 ENST00000217086.7 ENST00000217086.8 NM_020436 Q540H3 Q6Y8G6 Q9UJQ4 SALL4_HUMAN ZNF797 uc002xwh.1 uc002xwh.2 uc002xwh.3 uc002xwh.4 uc002xwh.5 uc002xwh.6 uc002xwh.7 This gene encodes a zinc finger transcription factor thought to play a role in the development of abducens motor neurons. Defects in this gene are a cause of Duane-radial ray syndrome (DRRS). Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2015]. Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells. Interacts with POU5F1/OCT4 (PubMed:23012367). Interacts with NANOG (By similarity). Interacts with BEND3 (PubMed:21914818). Interacts with NSD2 (via PHD-type zinc fingers 1, 2 and 3) (By similarity). Interacts with NRBP1 (PubMed:22510880). Cytoplasm. Nucleus. Event=Alternative splicing; Named isoforms=2; Name=SALL4A; IsoId=Q9UJQ4-1; Sequence=Displayed; Name=SALL4B; IsoId=Q9UJQ4-2; Sequence=VSP_046525; Expressed in testis. Constitutively expressed in acute myeloid leukemia (AML). Isoform SALL4B exists primarily as a ubiquitinated form. Sumoylation with both SUMO1 and SUMO2 regulates the stability, subcellular localization, transcriptional activity, and may reduce interaction with POU5F1/OCT4. Duane-radial ray syndrome (DRRS) [MIM:607323]: Disorder characterized by the association of forearm malformations with Duane retraction syndrome. te=The disease is caused by variants affecting the gene represented in this entry. IVIC syndrome (IVIC) [MIM:147750]: An autosomal dominant condition characterized by upper limbs anomalies (radial ray defects, carpal bones fusion), extraocular motor disturbances, congenital bilateral non-progressive mixed hearing loss. Other less consistent malformations include heart involvement, mild thrombocytopenia and leukocytosis (before age 50), shoulder girdle hypoplasia, imperforate anus, kidney malrotation or rectovaginal fistula. The IVIC syndrome is an allelic disorder of Duane-radial ray syndrome with a similar phenotype. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the sal C2H2-type zinc-finger protein family. negative regulation of transcription from RNA polymerase II promoter heterochromatin in utero embryonic development inner cell mass cell proliferation neural tube closure ventricular septum development nucleic acid binding DNA binding protein binding nucleus nucleoplasm cytoplasm regulation of transcription, DNA-templated heart development transcription factor binding tissue development stem cell population maintenance neural tube development embryonic limb morphogenesis macromolecular complex somatic stem cell population maintenance intracellular membrane-bounded organelle positive regulation of transcription from RNA polymerase II promoter metal ion binding uc002xwh.1 uc002xwh.2 uc002xwh.3 uc002xwh.4 uc002xwh.5 uc002xwh.6 uc002xwh.7 
ENST00000217109.9 CSTF1 ENST00000217109.9 cleavage stimulation factor subunit 1, transcript variant 2 (from RefSeq NM_001324.3) CSTF1_HUMAN ENST00000217109.1 ENST00000217109.2 ENST00000217109.3 ENST00000217109.4 ENST00000217109.5 ENST00000217109.6 ENST00000217109.7 ENST00000217109.8 NM_001324 Q05048 Q5QPD8 uc002xxm.1 uc002xxm.2 uc002xxm.3 This gene encodes one of three subunits which combine to form cleavage stimulation factor (CSTF). CSTF is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. Similar to mammalian G protein beta subunits, this protein contains transducin-like repeats. Several transcript variants with different 5' UTR, but encoding the same protein, have been found for this gene. [provided by RefSeq, Jul 2008]. One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs (PubMed:10669729). May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA (PubMed:10669729). Homodimer (PubMed:10669729). The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit) (PubMed:10669729). Interacts (via repeats WD) directly with CSTF3 (PubMed:10669729). Interacts (via repeat WD6) with BARD1 (PubMed:10477523). Interacts with ERCC6 (PubMed:26030138). Q05048; Q99728: BARD1; NbExp=4; IntAct=EBI-1789619, EBI-473181; Q05048; Q9H0E2: TOLLIP; NbExp=2; IntAct=EBI-1789619, EBI-74615; Nucleus N-terminus mediates homodimerization. The N-terminus is blocked. mRNA splicing, via spliceosome RNA binding protein binding nucleus nucleoplasm mRNA cleavage stimulating factor complex termination of RNA polymerase II transcription mRNA processing mRNA 3'-end processing uc002xxm.1 uc002xxm.2 uc002xxm.3 
ENST00000217131.6 CTSZ ENST00000217131.6 cathepsin Z (from RefSeq NM_001336.4) B2RC40 CATZ_HUMAN ENST00000217131.1 ENST00000217131.2 ENST00000217131.3 ENST00000217131.4 ENST00000217131.5 NM_001336 O75331 Q9UBR2 Q9UQV5 Q9UQV6 uc002yai.1 uc002yai.2 uc002yai.3 uc002yai.4 The protein encoded by this gene is a lysosomal cysteine proteinase and member of the peptidase C1 family. It exhibits both carboxy-monopeptidase and carboxy-dipeptidase activities. The encoded protein has also been known as cathepsin X and cathepsin P. This gene is expressed ubiquitously in cancer cell lines and primary tumors and, like other members of this family, may be involved in tumorigenesis. [provided by RefSeq, Oct 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.203888.1, AF136273.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN04284274 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217131.6/ ENSP00000217131.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (PubMed:10504234). Capable of producing kinin potentiating peptides (By similarity). Reaction=Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.; EC=3.4.18.1; Evidence=; The disulfide bridge formed between Cys-33 in the propeptide and the active site residue Cys-92 may prevent activation of the zymogen through formation of a reversible covalent bond with the active site residue. Q9UBR2; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-8636823, EBI-1642333; Q9UBR2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-8636823, EBI-11524452; Q9UBR2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-8636823, EBI-3867333; Q9UBR2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-8636823, EBI-750641; Q9UBR2; O75031: HSF2BP; NbExp=3; IntAct=EBI-8636823, EBI-7116203; Q9UBR2; Q92764: KRT35; NbExp=3; IntAct=EBI-8636823, EBI-1058674; Q9UBR2; Q6A162: KRT40; NbExp=3; IntAct=EBI-8636823, EBI-10171697; Q9UBR2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-8636823, EBI-11959885; Q9UBR2; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-8636823, EBI-11955579; Q9UBR2; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-8636823, EBI-14065470; Q9UBR2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-8636823, EBI-3957694; Q9UBR2; P26371: KRTAP5-9; NbExp=8; IntAct=EBI-8636823, EBI-3958099; Q9UBR2; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-8636823, EBI-10172526; Q9UBR2; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-8636823, EBI-742948; Q9UBR2; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-8636823, EBI-945833; Q9UBR2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-8636823, EBI-22310682; Q9UBR2; O15162: PLSCR1; NbExp=3; IntAct=EBI-8636823, EBI-740019; Q9UBR2; Q63HR2: TNS2; NbExp=3; IntAct=EBI-8636823, EBI-949753; Lysosome. Widely expressed. Belongs to the peptidase C1 family. Golgi membrane angiotensin maturation carboxypeptidase activity cysteine-type endopeptidase activity protein binding extracellular region extracellular space lysosome endoplasmic reticulum endoplasmic reticulum lumen plasma membrane proteolysis ER to Golgi vesicle-mediated transport peptidase activity cysteine-type peptidase activity cell surface negative regulation of plasminogen activation negative regulation of neuron projection development hydrolase activity ER to Golgi transport vesicle growth cone cytoplasmic vesicle negative regulation of protein binding endoplasmic reticulum-Golgi intermediate compartment membrane specific granule lumen intracellular membrane-bounded organelle neutrophil degranulation positive regulation of neuron apoptotic process COPII vesicle coating proteolysis involved in cellular protein catabolic process epithelial tube branching involved in lung morphogenesis extracellular exosome cell cortex region regulation of neuron death ficolin-1-rich granule lumen positive regulation of neural precursor cell proliferation uc002yai.1 uc002yai.2 uc002yai.3 uc002yai.4 
ENST00000217133.2 TUBB1 ENST00000217133.2 tubulin beta 1 class VI (from RefSeq NM_030773.4) ENST00000217133.1 NM_030773 Q9H4B7 TBB1_HUMAN uc002yak.1 uc002yak.2 uc002yak.3 uc002yak.4 This gene encodes a member of the beta tubulin protein family. Beta tubulins are one of two core protein families (alpha and beta tubulins) that heterodimerize and assemble to form microtubules. This protein is specifically expressed in platelets and megakaryocytes and may be involved in proplatelet production and platelet release. A mutations in this gene is associated with autosomal dominant macrothrombocytopenia. Two pseudogenes of this gene are found on chromosome Y.[provided by RefSeq, Jul 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AJ292757.1, BC033679.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217133.2/ ENSP00000217133.1 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with RANBP10. Cytoplasm, cytoskeleton Hematopoietic cell-specific. Major isotype in leukocytes, where it represents 50% of all beta-tubulins. The MREI motif is common among all beta-tubulin isoforms and may be critical for tubulin autoregulation. Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Glutamylation is also involved in cilia motility (By similarity). Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into cilia and flagella axonemes, which is required for their stability and maintenance. Flagella glycylation controls sperm motility. Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. Macrothrombocytopenia, isolated, 1, autosomal dominant (MACTHC1) [MIM:613112]: A congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the tubulin family. nucleotide binding microtubule cytoskeleton organization mitotic cell cycle GTPase activity structural constituent of cytoskeleton GTP binding cytoplasm cytoskeleton microtubule microtubule-based process spindle assembly extracellular exosome uc002yak.1 uc002yak.2 uc002yak.3 uc002yak.4 
ENST00000217159.6 SLCO4A1 ENST00000217159.6 solute carrier organic anion transporter family member 4A1 (from RefSeq NM_016354.4) ENST00000217159.1 ENST00000217159.2 ENST00000217159.3 ENST00000217159.4 ENST00000217159.5 NM_016354 OATP1 OATP4A1 OATPE Q96BD0 Q9H4T7 Q9H4T8 Q9H8P2 Q9NWX8 Q9UI35 Q9UIG7 SLC21A12 SO4A1_HUMAN uc002ydb.1 uc002ydb.2 Organic anion antiporter with apparent broad substrate specificity. Recognizes various substrates including thyroid hormones 3,3',5-triiodo-L-thyronine (T3), L-thyroxine (T4) and 3,3',5'-triiodo- L-thyronine (rT3), conjugated steroids such as estrone 3-sulfate and estradiol 17-beta glucuronide, bile acids such as taurocholate and prostanoids such as prostaglandin E2, likely operating in a tissue- specific manner (PubMed:10873595, PubMed:19129463, PubMed:30343886). May be involved in uptake of metabolites from the circulation into organs such as kidney, liver or placenta. Possibly drives the selective transport of thyroid hormones and estrogens coupled to an outward glutamate gradient across the microvillous membrane of the placenta (PubMed:30343886). The transport mechanism, its electrogenicity and potential tissue-specific counterions remain to be elucidated (Probable). Reaction=3,3',5-triiodo-L-thyronine(out) + L-glutamate(in) = 3,3',5- triiodo-L-thyronine(in) + L-glutamate(out); Xref=Rhea:RHEA:72299, ChEBI:CHEBI:29985, ChEBI:CHEBI:533015; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72300; Evidence=; Reaction=L-glutamate(in) + L-thyroxine(out) = L-glutamate(out) + L- thyroxine(in); Xref=Rhea:RHEA:72303, ChEBI:CHEBI:29985, ChEBI:CHEBI:58448; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72304; Evidence=; Reaction=estrone 3-sulfate(out) + L-glutamate(in) = estrone 3- sulfate(in) + L-glutamate(out); Xref=Rhea:RHEA:72239, ChEBI:CHEBI:29985, ChEBI:CHEBI:60050; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72240; Evidence=; Reaction=L-glutamate(in) + taurocholate(out) = L-glutamate(out) + taurocholate(in); Xref=Rhea:RHEA:72307, ChEBI:CHEBI:29985, ChEBI:CHEBI:36257; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72308; Evidence=; Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L- thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812; Evidence=; Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819, ChEBI:CHEBI:58448; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71820; Evidence=; Reaction=3,3',5'-triiodo-L-thyronine(out) = 3,3',5'-triiodo-L- thyronine(in); Xref=Rhea:RHEA:71815, ChEBI:CHEBI:57261; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71816; Evidence=; Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in); Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71836; Evidence=; Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(out) = 17beta- estradiol 17-O-(beta-D-glucuronate)(in); Xref=Rhea:RHEA:72691, ChEBI:CHEBI:82961; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72692; Evidence=; Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71704; Evidence=; Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50985; Evidence=; pH dependence: Optimum pH is 6.5 with estrone 3-sulfate and L-thyroxine (T4) as substrates. ; Q96BD0; O00155: GPR25; NbExp=3; IntAct=EBI-2822217, EBI-10178951; Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=4; Comment=Experimental confirmation may be lacking for some isoforms.; Name=1; IsoId=Q96BD0-1; Sequence=Displayed; Name=2; IsoId=Q96BD0-2; Sequence=VSP_006152, VSP_006156; Name=3; IsoId=Q96BD0-3; Sequence=VSP_006153, VSP_006155; Name=4; IsoId=Q96BD0-4; Sequence=VSP_006154; Widely expressed (PubMed:10873595, PubMed:11316767). Expressed in placental trophoblasts (PubMed:10873595, PubMed:12409283). Expressed in pancreas, kidney, skeletal muscle, liver, lung, brain, heart, colon, small intestine, ovary, testis, prostate, thymus and spleen. In testis, primarily localized to Leydig cells (PubMed:35307651). Expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and pancreas (PubMed:10873595). A conserved histidine residue in the third TMD (His-191) may play an essential role in the pH sensitivity of SLCO4A1/OATP4A1- mediated substrate transport. Belongs to the organo anion transporter (TC 2.A.60) family. Sequence=BAA91247.1; Type=Erroneous initiation; Evidence=; plasma membrane integral component of plasma membrane ion transport sodium-independent organic anion transmembrane transporter activity thyroid hormone transmembrane transporter activity membrane integral component of membrane sodium-independent organic anion transport transmembrane transport thyroid hormone transport uc002ydb.1 uc002ydb.2 
ENST00000217169.8 BIRC7 ENST00000217169.8 baculoviral IAP repeat containing 7, transcript variant 1 (from RefSeq NM_139317.3) BIRC7_HUMAN ENST00000217169.1 ENST00000217169.2 ENST00000217169.3 ENST00000217169.4 ENST00000217169.5 ENST00000217169.6 ENST00000217169.7 KIAP LIVIN MLIAP NM_139317 Q96CA5 Q9BQV0 Q9H2A8 Q9HAP7 RNF50 UNQ5800/PRO19607/PRO21344 uc002yej.1 uc002yej.2 uc002yej.3 uc002yej.4 uc002yej.5 This gene encodes a member of the inhibitor of apoptosis protein (IAP) family, and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is essential for inhibitory activity and interacts with caspases, while the RING finger domain sometimes enhances antiapoptotic activity but does not inhibit apoptosis alone. Elevated levels of the encoded protein may be associated with cancer progression and play a role in chemotherapy sensitivity. Alternative splicing results in multiple transcript variants [provided by RefSeq, Jul 2013]. Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control (PubMed:11162435, PubMed:11024045, PubMed:11084335, PubMed:16729033, PubMed:17294084). Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity (PubMed:11024045, PubMed:16729033). As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival (PubMed:16729033). May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions (PubMed:16729033). Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine (PubMed:11162435, PubMed:11084335, PubMed:11865055). Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2 (PubMed:11865055). This activation depends on TAB1 and MAP3K7/TAK1 (PubMed:11865055). In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9 (PubMed:11024045). [Isoform 1]: Blocks staurosporine-induced apoptosis (PubMed:11322947). Promotes natural killer (NK) cell-mediated killing (PubMed:18034418). [Isoform 2]: Blocks etoposide-induced apoptosis (PubMed:11162435, PubMed:11322947). Protects against natural killer (NK) cell-mediated killing (PubMed:18034418). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence=; Binds to CASP9. Interaction with DIABLO/SMAC via the BIR domain disrupts binding to CASP9 and apoptotic suppressor activity. Interacts with TAB1. In vitro, interacts with CASP3 and CASP7 via its BIR domain. Q96CA5; Q9UQB9: AURKC; NbExp=3; IntAct=EBI-517623, EBI-3926851; Q96CA5; Q13490: BIRC2; NbExp=6; IntAct=EBI-517623, EBI-514538; Q96CA5; Q9Y3E2: BOLA1; NbExp=3; IntAct=EBI-517623, EBI-1049556; Q96CA5; A0A087WZT3: BOLA2-SMG1P6; NbExp=5; IntAct=EBI-517623, EBI-12006120; Q96CA5; P55211: CASP9; NbExp=12; IntAct=EBI-517623, EBI-516799; Q96CA5; P26196: DDX6; NbExp=7; IntAct=EBI-517623, EBI-351257; Q96CA5; Q9NR28: DIABLO; NbExp=6; IntAct=EBI-517623, EBI-517508; Q96CA5; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-517623, EBI-741626; Q96CA5; P52655: GTF2A1; NbExp=3; IntAct=EBI-517623, EBI-389518; Q96CA5; O43464: HTRA2; NbExp=2; IntAct=EBI-517623, EBI-517086; Q96CA5; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-517623, EBI-2556193; Q96CA5; Q96JN0-2: LCOR; NbExp=3; IntAct=EBI-517623, EBI-10961483; Q96CA5; P61968: LMO4; NbExp=3; IntAct=EBI-517623, EBI-2798728; Q96CA5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-517623, EBI-741158; Q96CA5; O43189: PHF1; NbExp=4; IntAct=EBI-517623, EBI-530034; Q96CA5; O15160: POLR1C; NbExp=6; IntAct=EBI-517623, EBI-1055079; Q96CA5; P0CG20: PRR35; NbExp=3; IntAct=EBI-517623, EBI-11986293; Q96CA5; P20618: PSMB1; NbExp=5; IntAct=EBI-517623, EBI-372273; Q96CA5; P47897: QARS1; NbExp=3; IntAct=EBI-517623, EBI-347462; Q96CA5; P35711-4: SOX5; NbExp=3; IntAct=EBI-517623, EBI-11954419; Q96CA5; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-517623, EBI-11139477; Q96CA5; Q08117: TLE5; NbExp=4; IntAct=EBI-517623, EBI-717810; Q96CA5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-517623, EBI-11741437; Q96CA5; O14787-2: TNPO2; NbExp=3; IntAct=EBI-517623, EBI-12076664; Q96CA5; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-517623, EBI-10241197; Q96CA5; P49638: TTPA; NbExp=3; IntAct=EBI-517623, EBI-10210710; Q96CA5; P61086: UBE2K; NbExp=3; IntAct=EBI-517623, EBI-473850; Q96CA5; O75604: USP2; NbExp=3; IntAct=EBI-517623, EBI-743272; Q96CA5; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-517623, EBI-2559305; Q96CA5; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-517623, EBI-2815120; Nucleus Cytoplasm Golgi apparatus Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively in the cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis. Event=Alternative splicing; Named isoforms=2; Name=2; Synonyms=Livin alpha; IsoId=Q96CA5-1; Sequence=Displayed; Name=1; Synonyms=Livin beta; IsoId=Q96CA5-2; Sequence=VSP_002459; Isoform 1 and isoform 2 are expressed at very low levels or not detectable in most adult tissues. Detected in adult heart, placenta, lung, lymph node, spleen and ovary, and in several carcinoma cell lines. Isoform 2 is detected in fetal kidney, heart and spleen, and at lower levels in adult brain, skeletal muscle and peripheral blood leukocytes. The RING domain is essential for autoubiquitination. Autoubiquitinated and undergoes proteasome-mediated degradation. The truncated protein (tLivin) not only loses its anti-apoptotic effect but also acquires a pro-apoptotic effect. Belongs to the IAP family. ubiquitin-protein transferase activity cysteine-type endopeptidase inhibitor activity protein binding nucleus cytoplasm Golgi apparatus microtubule organizing center cytosol apoptotic process activation of JUN kinase activity negative regulation of peptidase activity protein ubiquitination transferase activity enzyme binding peptidase inhibitor activity positive regulation of protein ubiquitination regulation of cell proliferation cysteine-type endopeptidase inhibitor activity involved in apoptotic process negative regulation of apoptotic process negative regulation of cysteine-type endopeptidase activity involved in apoptotic process metal ion binding ubiquitin protein ligase activity regulation of natural killer cell apoptotic process inhibition of cysteine-type endopeptidase activity involved in apoptotic process uc002yej.1 uc002yej.2 uc002yej.3 uc002yej.4 uc002yej.5 
ENST00000217173.7 UBOX5 ENST00000217173.7 U-box domain containing 5, transcript variant 1 (from RefSeq NM_014948.4) ENST00000217173.1 ENST00000217173.2 ENST00000217173.3 ENST00000217173.4 ENST00000217173.5 ENST00000217173.6 KIAA0860 NM_014948 O94941 Q6IAR5 Q86X87 Q9H4J2 RNF37 RNF37_HUMAN UBCE7IP5 UBOX5 UIP5 uc002whw.1 uc002whw.2 uc002whw.3 uc002whw.4 uc002whw.5 uc002whw.6 This gene encodes a U-box domain containing protein. The encoded protein interacts with E2 enzymes and may play a role in the ubiquitination pathway. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jun 2012]. May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence=; Protein modification; protein ubiquitination. Interacts with UBE2L3. Interacts with VCP. O94941; P54253: ATXN1; NbExp=6; IntAct=EBI-751901, EBI-930964; O94941; P40692: MLH1; NbExp=7; IntAct=EBI-751901, EBI-744248; O94941; Q13148: TARDBP; NbExp=3; IntAct=EBI-751901, EBI-372899; O94941; P55072: VCP; NbExp=6; IntAct=EBI-751901, EBI-355164; Nucleus te=Enriched in nuclear bodies. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O94941-1; Sequence=Displayed; Name=2; IsoId=O94941-2; Sequence=VSP_042899; Expressed in liver, heart, brain, kidney and testis. The U-box domain mediates interaction with E2 ubiquitin ligases and is required for the ubiquitin-protein ligase activity. Sequence=BAA74883.2; Type=Erroneous initiation; Evidence=; protein polyubiquitination ubiquitin-protein transferase activity protein binding nucleus nucleoplasm focal adhesion protein ubiquitination nuclear body transferase activity ubiquitin protein ligase binding ubiquitin-ubiquitin ligase activity metal ion binding ubiquitin protein ligase activity uc002whw.1 uc002whw.2 uc002whw.3 uc002whw.4 uc002whw.5 uc002whw.6 
ENST00000217182.6 EEF1A2 ENST00000217182.6 eukaryotic translation elongation factor 1 alpha 2 (from RefSeq NM_001958.5) B5BUF3 E1P5J1 EEF1AL EF1A2_HUMAN ENST00000217182.1 ENST00000217182.2 ENST00000217182.3 ENST00000217182.4 ENST00000217182.5 NM_001958 P54266 Q05639 Q0VGC7 STN uc002yfe.1 uc002yfe.2 uc002yfe.3 uc002yfe.4 uc002yfe.5 This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 2) is expressed in brain, heart and skeletal muscle, and the other isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas. This gene may be critical in the development of ovarian cancer. [provided by RefSeq, Mar 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC110409.1, X70940.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217182.6/ ENSP00000217182.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Monomer. Q05639; Q969K4: ABTB1; NbExp=9; IntAct=EBI-354943, EBI-7223971; Q05639; P42858: HTT; NbExp=3; IntAct=EBI-354943, EBI-466029; Q05639; Q5S007: LRRK2; NbExp=3; IntAct=EBI-354943, EBI-5323863; Q05639; Q14166: TTLL12; NbExp=4; IntAct=EBI-354943, EBI-923010; Q05639; P59595: N; Xeno; NbExp=10; IntAct=EBI-354943, EBI-7602718; Nucleus Brain, heart, and skeletal muscle. Trimethylated at Lys-165 by EEF1AKMT3 (PubMed:28108655). Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs (PubMed:28520920). Trimethylated at the N-terminus by METTL13 (PubMed:30143613). Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant (PubMed:30143613, PubMed:30612740). Developmental and epileptic encephalopathy 33 (DEE33) [MIM:616409]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. te=The disease is caused by variants affecting the gene represented in this entry. Intellectual developmental disorder, autosomal dominant 38 (MRD38) [MIM:616393]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD38 common features are severe intellectual disability, autistic behavior, absent speech, neonatal hypotonia, epilepsy and progressive microcephaly. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40408/EEF1A2"; nucleotide binding translation elongation factor activity GTPase activity protein binding GTP binding cytoplasm eukaryotic translation elongation factor 1 complex translation translational elongation translation factor activity, RNA binding response to inorganic substance protein kinase binding neuronal cell body positive regulation of apoptotic process synapse response to electrical stimulus positive regulation of lipid kinase activity cytoplasmic side of lysosomal membrane regulation of chaperone-mediated autophagy nucleus uc002yfe.1 uc002yfe.2 uc002yfe.3 uc002yfe.4 uc002yfe.5 
ENST00000217188.2 SRMS ENST00000217188.2 src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (from RefSeq NM_080823.4) C20orf148 ENST00000217188.1 NM_080823 Q9H3Y6 SRMS_HUMAN uc002yfi.1 uc002yfi.2 uc002yfi.3 uc002yfi.4 Non-receptor tyrosine-protein kinase which phosphorylates DOK1 on tyrosine residues (PubMed:23822091). Also phosphorylates KHDRBS1/SAM68 and VIM on tyrosine residues (PubMed:29496907). Phosphorylation of KHDRBS1 is EGF-dependent (PubMed:29496907). Phosphorylates OTUB1, promoting deubiquitination of RPTOR (PubMed:35927303). Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence= Interacts (via the SH2 and SH3 domains) with DOK1 (PubMed:23822091). Interacts with KHDRBS1/SAM68 and VIM (PubMed:29496907). Q9H3Y6; Q99704: DOK1; NbExp=7; IntAct=EBI-8541270, EBI-1384360; Q9H3Y6; O43639: NCK2; NbExp=3; IntAct=EBI-8541270, EBI-713635; Cytoplasm te=Localizes to punctate cytoplasmic structures. Highly expressed in most breast cancers (at protein level). The N-terminal region regulates its kinase activity. Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. nucleotide binding protein kinase activity protein tyrosine kinase activity non-membrane spanning protein tyrosine kinase activity receptor binding protein binding ATP binding cytoplasm cytosol protein phosphorylation transmembrane receptor protein tyrosine kinase signaling pathway negative regulation of signal transduction kinase activity phosphorylation cell migration transferase activity peptidyl-tyrosine phosphorylation cell differentiation extrinsic component of cytoplasmic side of plasma membrane peptidyl-tyrosine autophosphorylation regulation of cell proliferation uc002yfi.1 uc002yfi.2 uc002yfi.3 uc002yfi.4 
ENST00000217233.9 TRIB3 ENST00000217233.9 tribbles pseudokinase 3, transcript variant 1, also known as 1A (from RefSeq NM_021158.5) C20orf97 ENST00000217233.1 ENST00000217233.2 ENST00000217233.3 ENST00000217233.4 ENST00000217233.5 ENST00000217233.6 ENST00000217233.7 ENST00000217233.8 NIPK NM_021158 Q53GU4 Q53ZW7 Q6I9Y9 Q8TAI6 Q96RU7 Q9H5M8 Q9NUD2 SKIP3 TRB3 TRIB3_HUMAN uc002wdm.1 uc002wdm.2 uc002wdm.3 uc002wdm.4 uc002wdm.5 uc002wdm.6 The protein encoded by this gene is a putative protein kinase that is induced by the transcription factor NF-kappaB. The encoded protein is a negative regulator of NF-kappaB and can also sensitize cells to TNF- and TRAIL-induced apoptosis. In addition, this protein can negatively regulate the cell survival serine-threonine kinase AKT1. Differential promoter usage and alternate splicing result in multiple transcript variants. [provided by RefSeq, Jul 2014]. Inactive protein kinase which acts as a regulator of the integrated stress response (ISR), a process for adaptation to various stress (PubMed:15781252, PubMed:15775988). Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress (PubMed:15781252, PubMed:15775988). May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells (PubMed:15781252, PubMed:15775988). Acts as a negative feedback regulator of the ATF4-dependent transcription during the ISR: while TRIB3 expression is promoted by ATF4, TRIB3 protein interacts with ATF4 and inhibits ATF4 transcription activity (By similarity). Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation (By similarity). May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1 (By similarity). Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity (PubMed:12736262). Interacts with MAPK kinases and regulates activation of MAP kinases (PubMed:15299019). Can inhibit APOBEC3A editing of nuclear DNA (PubMed:22977230). Interacts with AKT1, AKT2, MAP2K1 and MAP2K7 (PubMed:15299019). Interacts with ATF4 (PubMed:12743605). Interacts with DDIT3/CHOP and inhibits its interaction with EP300/P300 (PubMed:15775988, PubMed:17872950). Interacts with APOBEC3C (PubMed:22977230). Interacts (via N-terminus) with APOBEC3A (PubMed:22977230). Interacts with RELA (PubMed:12736262). Q96RU7; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-492476, EBI-357530; Q96RU7; Q9NRW3: APOBEC3C; NbExp=5; IntAct=EBI-492476, EBI-1044593; Q96RU7; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-492476, EBI-742909; Q96RU7; P18848: ATF4; NbExp=16; IntAct=EBI-492476, EBI-492498; Q96RU7; O95817: BAG3; NbExp=3; IntAct=EBI-492476, EBI-747185; Q96RU7; P41182: BCL6; NbExp=4; IntAct=EBI-492476, EBI-765407; Q96RU7; Q13515: BFSP2; NbExp=3; IntAct=EBI-492476, EBI-10229433; Q96RU7; Q0VAL7: C21orf58; NbExp=3; IntAct=EBI-492476, EBI-10226774; Q96RU7; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-492476, EBI-7317823; Q96RU7; Q9HC52: CBX8; NbExp=3; IntAct=EBI-492476, EBI-712912; Q96RU7; Q13111: CHAF1A; NbExp=5; IntAct=EBI-492476, EBI-1020839; Q96RU7; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-492476, EBI-11980535; Q96RU7; P78358: CTAG1B; NbExp=3; IntAct=EBI-492476, EBI-1188472; Q96RU7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-492476, EBI-10976677; Q96RU7; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-492476, EBI-12082590; Q96RU7; Q86UW9: DTX2; NbExp=3; IntAct=EBI-492476, EBI-740376; Q96RU7; O95967: EFEMP2; NbExp=3; IntAct=EBI-492476, EBI-743414; Q96RU7; O15197-2: EPHB6; NbExp=3; IntAct=EBI-492476, EBI-10182490; Q96RU7; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-492476, EBI-371876; Q96RU7; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-492476, EBI-12013806; Q96RU7; Q3B820: FAM161A; NbExp=3; IntAct=EBI-492476, EBI-719941; Q96RU7; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-492476, EBI-6658203; Q96RU7; Q8NEA6-2: GLIS3; NbExp=3; IntAct=EBI-492476, EBI-12232117; Q96RU7; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-492476, EBI-11959863; Q96RU7; P62993: GRB2; NbExp=3; IntAct=EBI-492476, EBI-401755; Q96RU7; O14929: HAT1; NbExp=3; IntAct=EBI-492476, EBI-2339359; Q96RU7; P56524-2: HDAC4; NbExp=3; IntAct=EBI-492476, EBI-11953488; Q96RU7; P52597: HNRNPF; NbExp=3; IntAct=EBI-492476, EBI-352986; Q96RU7; P09067: HOXB5; NbExp=3; IntAct=EBI-492476, EBI-3893317; Q96RU7; P31273: HOXC8; NbExp=3; IntAct=EBI-492476, EBI-1752118; Q96RU7; Q14005-2: IL16; NbExp=3; IntAct=EBI-492476, EBI-17178971; Q96RU7; Q0VD86: INCA1; NbExp=3; IntAct=EBI-492476, EBI-6509505; Q96RU7; Q9C086: INO80B; NbExp=3; IntAct=EBI-492476, EBI-715611; Q96RU7; P78412: IRX6; NbExp=3; IntAct=EBI-492476, EBI-12100506; Q96RU7; Q63ZY3: KANK2; NbExp=5; IntAct=EBI-492476, EBI-2556193; Q96RU7; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-492476, EBI-6426443; Q96RU7; Q7Z3Y9: KRT26; NbExp=3; IntAct=EBI-492476, EBI-12084444; Q96RU7; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-492476, EBI-726510; Q96RU7; P25791-3: LMO2; NbExp=3; IntAct=EBI-492476, EBI-11959475; Q96RU7; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-492476, EBI-11742507; Q96RU7; Q99750: MDFI; NbExp=3; IntAct=EBI-492476, EBI-724076; Q96RU7; Q8IVT2: MISP; NbExp=3; IntAct=EBI-492476, EBI-2555085; Q96RU7; O43482: OIP5; NbExp=3; IntAct=EBI-492476, EBI-536879; Q96RU7; Q9UM07: PADI4; NbExp=3; IntAct=EBI-492476, EBI-1042511; Q96RU7; Q9BYG5: PARD6B; NbExp=3; IntAct=EBI-492476, EBI-295391; Q96RU7; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-492476, EBI-11956269; Q96RU7; Q99697-2: PITX2; NbExp=3; IntAct=EBI-492476, EBI-12138495; Q96RU7; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-492476, EBI-2692890; Q96RU7; Q5T8A7: PPP1R26; NbExp=3; IntAct=EBI-492476, EBI-308500; Q96RU7; O43741: PRKAB2; NbExp=3; IntAct=EBI-492476, EBI-1053424; Q96RU7; O14744: PRMT5; NbExp=2; IntAct=EBI-492476, EBI-351098; Q96RU7; A6NJB7-2: PRR19; NbExp=3; IntAct=EBI-492476, EBI-11998870; Q96RU7; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-492476, EBI-1050213; Q96RU7; Q96KN7-4: RPGRIP1; NbExp=3; IntAct=EBI-492476, EBI-11525164; Q96RU7; Q96NU1: SAMD11; NbExp=3; IntAct=EBI-492476, EBI-14067109; Q96RU7; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-492476, EBI-3957636; Q96RU7; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-492476, EBI-12000762; Q96RU7; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-492476, EBI-748391; Q96RU7; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-492476, EBI-11955083; Q96RU7; P09234: SNRPC; NbExp=3; IntAct=EBI-492476, EBI-766589; Q96RU7; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-492476, EBI-11959123; Q96RU7; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-492476, EBI-742688; Q96RU7; Q7Z699: SPRED1; NbExp=4; IntAct=EBI-492476, EBI-5235340; Q96RU7; P51687: SUOX; NbExp=3; IntAct=EBI-492476, EBI-3921347; Q96RU7; Q9Y242: TCF19; NbExp=3; IntAct=EBI-492476, EBI-7413767; Q96RU7; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-492476, EBI-8644516; Q96RU7; Q8WW24: TEKT4; NbExp=5; IntAct=EBI-492476, EBI-750487; Q96RU7; Q08117-2: TLE5; NbExp=3; IntAct=EBI-492476, EBI-11741437; Q96RU7; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-492476, EBI-9090990; Q96RU7; Q8WUN7: UBTD2; NbExp=3; IntAct=EBI-492476, EBI-12867288; Q96RU7; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-492476, EBI-14096082; Q96RU7; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-492476, EBI-5457544; Q96RU7; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-492476, EBI-740727; Q96RU7; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-492476, EBI-6427977; Nucleus Highest expression in liver, pancreas, peripheral blood leukocytes and bone marrow. Also highly expressed in a number of primary lung, colon and breast tumors. Expressed in spleen, thymus, and prostate and is undetectable in other examined tissues, including testis, ovary, small intestine, colon, leukocyte, heart, brain, placenta, lung, skeletal muscle, and kidney. By hypoxia, TNF, and by nutrient starvation. Expression is PI 3-kinase and/or NF-kappa-B-dependent. Induced by ER stress via ATF4- DDIT3/CHOP pathway and can down-regulate its own induction by repression of ATF4-DDIT3/CHOP functions. The protein kinase domain is predicted to be catalytically inactive. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Tribbles subfamily. The role of this protein in Akt activation has been demonstrated by Du et al (PubMed:12791994) for the mouse ortholog but Iynedjian (PubMed:15469416) has not been able to reproduce the result in rat hepatocytes. negative regulation of transcription from RNA polymerase II promoter transcription corepressor activity protein kinase inhibitor activity protein binding ATP binding nucleus cytosol plasma membrane protein phosphorylation negative regulation of protein kinase activity apoptotic process regulation of autophagy regulation of glucose transport regulation of lipid metabolic process protein kinase binding mitogen-activated protein kinase kinase binding ubiquitin protein ligase binding positive regulation of protein binding positive regulation of proteasomal ubiquitin-dependent protein catabolic process cellular response to insulin stimulus response to endoplasmic reticulum stress regulation of MAP kinase activity negative regulation of fat cell differentiation negative regulation of fatty acid biosynthetic process negative regulation of transcription, DNA-templated positive regulation of ubiquitin-protein transferase activity negative regulation of protein kinase B signaling ubiquitin-protein transferase regulator activity intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress kinase activity uc002wdm.1 uc002wdm.2 uc002wdm.3 uc002wdm.4 uc002wdm.5 uc002wdm.6 
ENST00000217244.9 CSNK2A1 ENST00000217244.9 casein kinase 2 alpha 1, transcript variant 1 (from RefSeq NM_177559.3) B4DYS6 CK2A1 CSK21_HUMAN D3DVV8 ENST00000217244.1 ENST00000217244.2 ENST00000217244.3 ENST00000217244.4 ENST00000217244.5 ENST00000217244.6 ENST00000217244.7 ENST00000217244.8 NM_177559 P19138 P20426 P68400 Q14013 Q5U065 uc002wdw.1 uc002wdw.2 uc002wdw.3 uc002wdw.4 Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. It is involved in various cellular processes, including cell cycle control, apoptosis, and circadian rhythm. The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. The protein encoded by this gene represents the alpha subunit. Multiple transcript variants encoding different protein isoforms have been found for this gene. [provided by RefSeq, Apr 2018]. Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20545769, PubMed:20625391, PubMed:22406621, PubMed:24962073, PubMed:30898438, PubMed:31439799). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (PubMed:12631575, PubMed:19387552, PubMed:19387551). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (PubMed:12631575, PubMed:19387552, PubMed:19387551). During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage (PubMed:11704824, PubMed:19188443). Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation (PubMed:11239457). Phosphorylates a number of DNA repair proteins in response to DNA damage, such as MDC1, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites (PubMed:20545769, PubMed:21482717, PubMed:22325354, PubMed:26811421, PubMed:30898438, PubMed:35597237). Can also negatively regulate apoptosis (PubMed:16193064, PubMed:22184066). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:16193064). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:16193064). Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis (PubMed:22184066). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551, PubMed:23123191). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551, PubMed:23123191). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (PubMed:19387550). Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (PubMed:30699359). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (PubMed:19387549). Acts as an ectokinase that phosphorylates several extracellular proteins (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551). During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551). Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (PubMed:20625391, PubMed:22406621). Plays an important role in the circadian clock function by phosphorylating BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (By similarity). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073). Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment (PubMed:30765518, PubMed:31439799). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence= Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence=; Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization. Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1. Interacts with SNAI1. Interacts with PML (isoform PML-12). Interacts with CCAR2. P68400; P78563: ADARB1; NbExp=3; IntAct=EBI-347804, EBI-2967304; P68400; P05067: APP; NbExp=3; IntAct=EBI-347804, EBI-77613; P68400; Q86V38: ATN1; NbExp=6; IntAct=EBI-347804, EBI-11954292; P68400; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-347804, EBI-10181188; P68400; P35226: BMI1; NbExp=2; IntAct=EBI-347804, EBI-2341576; P68400; O00257-3: CBX4; NbExp=2; IntAct=EBI-347804, EBI-4392727; P68400; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-347804, EBI-744311; P68400; P68400: CSNK2A1; NbExp=4; IntAct=EBI-347804, EBI-347804; P68400; P19784: CSNK2A2; NbExp=10; IntAct=EBI-347804, EBI-347451; P68400; P67870: CSNK2B; NbExp=27; IntAct=EBI-347804, EBI-348169; P68400; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-347804, EBI-12051833; P68400; Q9GZR7: DDX24; NbExp=2; IntAct=EBI-347804, EBI-713081; P68400; P35659: DEK; NbExp=2; IntAct=EBI-347804, EBI-301977; P68400; Q92997: DVL3; NbExp=4; IntAct=EBI-347804, EBI-739789; P68400; O75822: EIF3J; NbExp=3; IntAct=EBI-347804, EBI-366647; P68400; Q8N9E0: FAM133A; NbExp=5; IntAct=EBI-347804, EBI-10268158; P68400; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-347804, EBI-11977403; P68400; Q9NW75-2: GPATCH2; NbExp=3; IntAct=EBI-347804, EBI-12068108; P68400; Q9NWQ4-1: GPATCH2L; NbExp=6; IntAct=EBI-347804, EBI-11959863; P68400; O15499: GSC2; NbExp=3; IntAct=EBI-347804, EBI-19954058; P68400; Q13547: HDAC1; NbExp=3; IntAct=EBI-347804, EBI-301834; P68400; P09017: HOXC4; NbExp=3; IntAct=EBI-347804, EBI-3923226; P68400; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-347804, EBI-12094820; P68400; Q14145: KEAP1; NbExp=3; IntAct=EBI-347804, EBI-751001; P68400; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-347804, EBI-10213781; P68400; O60282: KIF5C; NbExp=4; IntAct=EBI-347804, EBI-717170; P68400; Q92876: KLK6; NbExp=3; IntAct=EBI-347804, EBI-2432309; P68400; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-347804, EBI-12039345; P68400; Q68G74: LHX8; NbExp=3; IntAct=EBI-347804, EBI-8474075; P68400; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-347804, EBI-10175218; P68400; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-347804, EBI-10178634; P68400; P50221: MEOX1; NbExp=3; IntAct=EBI-347804, EBI-2864512; P68400; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-347804, EBI-16439278; P68400; Q9BU76: MMTAG2; NbExp=4; IntAct=EBI-347804, EBI-742459; P68400; P23511: NFYA; NbExp=4; IntAct=EBI-347804, EBI-389739; P68400; P23511-2: NFYA; NbExp=3; IntAct=EBI-347804, EBI-11061759; P68400; Q02548: PAX5; NbExp=3; IntAct=EBI-347804, EBI-296331; P68400; P26367: PAX6; NbExp=5; IntAct=EBI-347804, EBI-747278; P68400; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-347804, EBI-2339674; P68400; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-347804, EBI-11532361; P68400; P29590: PML; NbExp=2; IntAct=EBI-347804, EBI-295890; P68400; Q9H307: PNN; NbExp=2; IntAct=EBI-347804, EBI-681904; P68400; P78424: POU6F2; NbExp=3; IntAct=EBI-347804, EBI-12029004; P68400; O75400-2: PRPF40A; NbExp=2; IntAct=EBI-347804, EBI-5280197; P68400; Q14498: RBM39; NbExp=3; IntAct=EBI-347804, EBI-395290; P68400; Q04864-2: REL; NbExp=3; IntAct=EBI-347804, EBI-10829018; P68400; Q6ZNA4: RNF111; NbExp=6; IntAct=EBI-347804, EBI-2129175; P68400; Q99496: RNF2; NbExp=4; IntAct=EBI-347804, EBI-722416; P68400; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-347804, EBI-1802965; P68400; Q92504: SLC39A7; NbExp=4; IntAct=EBI-347804, EBI-1051105; P68400; O43623: SNAI2; NbExp=3; IntAct=EBI-347804, EBI-9876238; P68400; P12931: SRC; NbExp=2; IntAct=EBI-347804, EBI-621482; P68400; Q08945: SSRP1; NbExp=3; IntAct=EBI-347804, EBI-353771; P68400; Q96MF2: STAC3; NbExp=7; IntAct=EBI-347804, EBI-745680; P68400; O75683: SURF6; NbExp=2; IntAct=EBI-347804, EBI-2691252; P68400; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-347804, EBI-11139477; P68400; Q9NVV9: THAP1; NbExp=7; IntAct=EBI-347804, EBI-741515; P68400; Q9Y2W1: THRAP3; NbExp=2; IntAct=EBI-347804, EBI-352039; P68400; Q08117-2: TLE5; NbExp=3; IntAct=EBI-347804, EBI-11741437; P68400; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-347804, EBI-725997; P68400; Q9H2G4: TSPYL2; NbExp=4; IntAct=EBI-347804, EBI-947459; P68400; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-347804, EBI-12272076; P68400; Q8IYI8: ZNF440; NbExp=3; IntAct=EBI-347804, EBI-726439; P68400; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-347804, EBI-373363; P68400; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-347804, EBI-745276; P68400; Q6NSZ9-2: ZSCAN25; NbExp=3; IntAct=EBI-347804, EBI-14650477; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P68400-1; Sequence=Displayed; Name=2; IsoId=P68400-2; Sequence=VSP_041925; Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level). Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase. Phosphorylation does not directly affect casein kinase 2 activity, but may contribute to its regulation by forming binding sites for interacting proteins and/or targeting it to different compartments. Okur-Chung neurodevelopmental syndrome (OCNDS) [MIM:617062]: An autosomal dominant neurodevelopmental disorder characterized by developmental delay, intellectual disability, behavioral problems, hypotonia, speech problems, microcephaly, pachygyria and variable dysmorphic features. Note=The disease is caused by variants affecting the gene represented in this entry. Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome. Casein kinase 2 has been found to be increased at protein level and up-regulated at the level of enzyme activity in the majority of cancers. However, elevated levels of casein kinase 2 are present in certain normal organs such as brain and testes. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily. nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding nucleus nucleoplasm cytosol plasma membrane protein kinase CK2 complex protein folding protein phosphorylation phosphatidylcholine biosynthetic process apoptotic process cell cycle signal transduction positive regulation of cell proliferation Wnt signaling pathway macroautophagy kinase activity phosphorylation Sin3 complex NuRD complex transferase activity peptidyl-serine phosphorylation peptidyl-threonine phosphorylation positive regulation of Wnt signaling pathway positive regulation of cell growth identical protein binding negative regulation of cysteine-type endopeptidase activity involved in apoptotic process positive regulation of protein catabolic process protein N-terminus binding rhythmic process regulation of cell cycle Hsp90 protein binding chaperone-mediated protein folding regulation of signal transduction by p53 class mediator negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process negative regulation of apoptotic signaling pathway PcG protein complex uc002wdw.1 uc002wdw.2 uc002wdw.3 uc002wdw.4 
ENST00000217260.9 RSPO4 ENST00000217260.9 R-spondin 4, transcript variant 1 (from RefSeq NM_001029871.4) A2A2I6 C20orf182 ENST00000217260.1 ENST00000217260.2 ENST00000217260.3 ENST00000217260.4 ENST00000217260.5 ENST00000217260.6 ENST00000217260.7 ENST00000217260.8 NM_001029871 Q2I0M5 Q9UGB2 RSPO4_HUMAN uc002wej.1 uc002wej.2 uc002wej.3 uc002wej.4 uc002wej.5 This gene encodes a member of the R-spondin family of proteins that share a common domain organization consisting of a signal peptide, cysteine-rich/furin-like domain, thrombospondin domain and a C-terminal basic region. The encoded protein may be involved in activation of Wnt/beta-catenin signaling pathways. Mutations in this gene are associated with anonychia congenital. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Sep 2009]. Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors (PubMed:29769720). Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin- dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway (PubMed:21727895, PubMed:21909076). Binds heparin (By similarity). Interacts with LGR4, LGR5 and LGR6. Q2I0M5; X5D778: ANKRD11; NbExp=3; IntAct=EBI-12821217, EBI-17183751; Q2I0M5; Q6P158: DHX57; NbExp=3; IntAct=EBI-12821217, EBI-1051531; Q2I0M5; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-12821217, EBI-11427343; Q2I0M5; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-12821217, EBI-347538; Q2I0M5; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-12821217, EBI-11978177; Q2I0M5; O14964: HGS; NbExp=3; IntAct=EBI-12821217, EBI-740220; Q2I0M5; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-12821217, EBI-6426443; Q2I0M5; P45984: MAPK9; NbExp=3; IntAct=EBI-12821217, EBI-713568; Q2I0M5; Q13064: MKRN3; NbExp=3; IntAct=EBI-12821217, EBI-2340269; Q2I0M5; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-12821217, EBI-10232538; Q2I0M5; O75716: STK16; NbExp=3; IntAct=EBI-12821217, EBI-749295; Q2I0M5; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-12821217, EBI-14096082; Q2I0M5; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-12821217, EBI-373456; Q2I0M5; Q15935: ZNF77; NbExp=3; IntAct=EBI-12821217, EBI-12840750; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q2I0M5-1; Sequence=Displayed; Name=2; IsoId=Q2I0M5-2; Sequence=VSP_018325; The FU repeat is required for activation and stabilization of beta-catenin. Tyr-112 may be phosphorylated; however as this position is probably extracellular, the vivo relevance is not proven. Nail disorder, non-syndromic congenital, 4 (NDNC4) [MIM:206800]: A nail disorder characterized by congenital anonychia or its milder phenotypic variant hyponychia. Anonychia/hyponychia is the absence or severe hypoplasia of all fingernails and toenails without significant bone anomalies. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the R-spondin family. extracellular region heparin binding Wnt signaling pathway positive regulation of Wnt signaling pathway nail development response to stimulus uc002wej.1 uc002wej.2 uc002wej.3 uc002wej.4 uc002wej.5 
ENST00000217289.9 FERMT1 ENST00000217289.9 FERM domain containing kindlin 1 (from RefSeq NM_017671.5) C20orf42 D3DW10 ENST00000217289.1 ENST00000217289.2 ENST00000217289.3 ENST00000217289.4 ENST00000217289.5 ENST00000217289.6 ENST00000217289.7 ENST00000217289.8 FERM1_HUMAN KIND1 NM_017671 Q8IX34 Q8IYH2 Q9BQL6 Q9NWM2 Q9NXQ3 URP1 uc002wmr.1 uc002wmr.2 uc002wmr.3 uc002wmr.4 This gene encodes a member of the fermitin family, and contains a FERM domain and a pleckstrin homology domain. The encoded protein is involved in integrin signaling and linkage of the actin cytoskeleton to the extracellular matrix. Mutations in this gene have been linked to Kindler syndrome. [provided by RefSeq, Dec 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB105105.1, AF443278.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites. May mediate TGF-beta 1 signaling in tumor progression. Interacts with the cytoplasmic domain of integrins ITGB1 and ITGB3. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Constituent of focal adhesions. Localized at the basal aspect of skin keratinocytes, close to the cell membrane. Colocalizes with filamentous actin. Upon TGFB1 treatment, it localizes to membrane ruffles. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9BQL6-1; Sequence=Displayed; Name=2; IsoId=Q9BQL6-2; Sequence=VSP_003810, VSP_003811; Name=3; IsoId=Q9BQL6-3; Sequence=VSP_003809; Name=4; IsoId=Q9BQL6-4; Sequence=VSP_009224, VSP_009225; Expressed in brain, skeletal muscle, kidney, colon, adrenal gland, prostate, and placenta. Weakly or not expressed in heart, thymus, spleen, liver, small intestine, bone marrow, lung and peripheral blood leukocytes. Overexpressed in some colon and lung tumors. In skin, it is localized within the epidermis and particularly in basal keratocytes. Not detected in epidermal melanocytes and dermal fibroblasts. By TGFB1. The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain. The FERM domain contains the subdomains F1, F2 and F3. It is preceded by a F0 domain with a ubiquitin-like fold. The F0 domain is required for integrin activation and for localization at focal adhesions. Kindler syndrome (KNDLRS) [MIM:173650]: An autosomal recessive skin disorder characterized by skin blistering, photosensitivity, progressive poikiloderma, and extensive skin atrophy. Additional clinical features include gingival erosions, ocular, esophageal, gastrointestinal and urogenital involvement, and an increased risk of mucocutaneous malignancy. te=The disease is caused by variants affecting the gene represented in this entry. Although most FERMT1 mutations are predicted to lead to premature termination of translation, and to loss of FERMT1 function, significant clinical variability is observed among patients. There is an association of FERMT1 missense and in-frame deletion mutations with milder disease phenotypes, and later onset of complications (PubMed:21936020). Belongs to the kindlin family. Sequence=BAA91358.1; Type=Erroneous initiation; Evidence=; Sequence=BAC03826.1; Type=Erroneous initiation; Evidence=; positive regulation of cell-matrix adhesion cytoplasm cytosol cytoskeleton plasma membrane focal adhesion cell adhesion integrin-mediated signaling pathway negative regulation of gene expression membrane cell junction positive regulation of transforming growth factor beta receptor signaling pathway ruffle membrane positive regulation of cell adhesion mediated by integrin negative regulation of protein import into nucleus cell projection keratinocyte proliferation actin filament binding keratinocyte migration negative regulation of anagen basement membrane organization negative regulation of canonical Wnt signaling pathway establishment of epithelial cell polarity negative regulation of stem cell proliferation positive regulation of transforming growth factor-beta secretion uc002wmr.1 uc002wmr.2 uc002wmr.3 uc002wmr.4 
ENST00000217305.3 PDYN ENST00000217305.3 prodynorphin, transcript variant 1 (from RefSeq NM_024411.5) A8K0Q3 ENST00000217305.1 ENST00000217305.2 NM_024411 P01213 PDYN_HUMAN uc002wfv.1 uc002wfv.2 uc002wfv.3 uc002wfv.4 uc002wfv.5 The protein encoded by this gene is a preproprotein that is proteolytically processed to form the secreted opioid peptides beta-neoendorphin, dynorphin, leu-enkephalin, rimorphin, and leumorphin. These peptides are ligands for the kappa-type of opioid receptor. Dynorphin is involved in modulating responses to several psychoactive substances, including cocaine. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2010]. Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 times more potent than Leu-enkephalin (By similarity). Leumorphin has a typical opioid activity and may have anti- apoptotic effect. Secreted. The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. Spinocerebellar ataxia 23 (SCA23) [MIM:610245]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA23 is an adult-onset autosomal dominant form characterized by slowly progressive gait and limb ataxia, with variable additional features, including peripheral neuropathy and dysarthria. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the opioid neuropeptide precursor family. opioid peptide activity extracellular region plasma membrane G-protein coupled receptor signaling pathway neuropeptide signaling pathway chemical synaptic transmission dendrite opioid receptor binding neuronal cell body axon terminus uc002wfv.1 uc002wfv.2 uc002wfv.3 uc002wfv.4 uc002wfv.5 
ENST00000217320.8 TLDC2 ENST00000217320.8 TBC/LysM-associated domain containing 2, transcript variant 1 (from RefSeq NM_080628.3) A0PJX2 B3KVU8 ENST00000217320.1 ENST00000217320.2 ENST00000217320.3 ENST00000217320.4 ENST00000217320.5 ENST00000217320.6 ENST00000217320.7 NM_080628 TLDC2_HUMAN uc002xgg.1 uc002xgg.2 uc002xgg.3 Belongs to the OXR1 family. uc002xgg.1 uc002xgg.2 uc002xgg.3 
ENST00000217381.3 SNTA1 ENST00000217381.3 syntrophin alpha 1, transcript variant 1 (from RefSeq NM_003098.3) A8K7H9 B4DX40 E1P5N1 ENST00000217381.1 ENST00000217381.2 NM_003098 Q13424 Q16438 SNT1 SNTA1_HUMAN uc002wzd.1 uc002wzd.2 uc002wzd.3 Syntrophins are cytoplasmic peripheral membrane scaffold proteins that are components of the dystrophin-associated protein complex. This gene is a member of the syntrophin gene family and encodes the most common syntrophin isoform found in cardiac tissues. The N-terminal PDZ domain of this syntrophin protein interacts with the C-terminus of the pore-forming alpha subunit (SCN5A) of the cardiac sodium channel Nav1.5. This protein also associates cardiac sodium channels with the nitric oxide synthase-PMCA4b (plasma membrane Ca-ATPase subtype 4b) complex in cardiomyocytes. This gene is a susceptibility locus for Long-QT syndrome (LQT) - an inherited disorder associated with sudden cardiac death from arrhythmia - and sudden infant death syndrome (SIDS). This protein also associates with dystrophin and dystrophin-related proteins at the neuromuscular junction and alters intracellular calcium ion levels in muscle tissue. [provided by RefSeq, Jan 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK291994.1, BC026215.2 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217381.3/ ENSP00000217381.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate (By similarity). Monomer and homodimer. Interacts with the other members of the syntrophin family SNTB1 and SNTB2; SGCG and SGCA of the dystrophin glycoprotein complex; NOS1; GRB2; the sodium channel proteins SCN4A and SCN5A; F-actin and calmodulin (By similarity). Interacts with dystrophin protein DMD and related proteins DTNA and UTRN and with MAPK12, TGFA and GA. Interacts with MYOC; regulates muscle hypertrophy (By similarity). Interacts with DTNB (By similarity). Q13424; O95477: ABCA1; NbExp=2; IntAct=EBI-717191, EBI-784112; Q13424; P25100: ADRA1D; NbExp=11; IntAct=EBI-717191, EBI-489993; Q13424; P11532: DMD; NbExp=3; IntAct=EBI-717191, EBI-295827; Q13424; Q63538: Mapk12; Xeno; NbExp=5; IntAct=EBI-717191, EBI-783937; Cell membrane, sarcolemma ; Peripheral membrane protein ; Cytoplasmic side Cell junction Cytoplasm, cytoskeleton Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13424-1; Sequence=Displayed; Name=2; IsoId=Q13424-2; Sequence=VSP_056827; High expression in skeletal muscle and heart. Low expression in brain, pancreas, liver, kidney and lung. Not detected in placenta. The PH 1 domain mediates the oligomerization in a calcium dependent manner, and the association with the phosphatidylinositol 4,5-bisphosphate. The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane (By similarity). The SU domain binds calmodulin in a calcium-dependent manner. Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD (By similarity). Long QT syndrome 12 (LQT12) [MIM:612955]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the syntrophin family. regulation of heart rate actin binding structural molecule activity protein binding calmodulin binding cytoplasm cytoskeleton plasma membrane muscle contraction dystrophin-associated glycoprotein complex syntrophin complex membrane cell junction PDZ domain binding neuromuscular junction macromolecular complex sarcolemma ion channel binding synapse nitric-oxide synthase binding ATPase binding regulation of ventricular cardiac muscle cell membrane repolarization ventricular cardiac muscle cell action potential negative regulation of peptidyl-cysteine S-nitrosylation regulation of sodium ion transmembrane transport lateral plasma membrane sodium channel regulator activity uc002wzd.1 uc002wzd.2 uc002wzd.3 
ENST00000217386.2 OXT ENST00000217386.2 oxytocin/neurophysin I prepropeptide (from RefSeq NM_000915.4) ENST00000217386.1 NM_000915 OXT X5D7M6 X5D7M6_HUMAN hCG_39619 uc002wht.1 uc002wht.2 This gene encodes a precursor protein that is processed to produce oxytocin and neurophysin I. Oxytocin is a posterior pituitary hormone which is synthesized as an inactive precursor in the hypothalamus along with its carrier protein neurophysin I. Together with neurophysin, it is packaged into neurosecretory vesicles and transported axonally to the nerve endings in the neurohypophysis, where it is either stored or secreted into the bloodstream. The precursor seems to be activated while it is being transported along the axon to the posterior pituitary. This hormone contracts smooth muscle during parturition and lactation. It is also involved in cognition, tolerance, adaptation and complex sexual and maternal behaviour, as well as in the regulation of water excretion and cardiovascular functions. [provided by RefSeq, Dec 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC069144.1, M25650.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145774, SAMEA2148874 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217386.2/ ENSP00000217386.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Neurophysin 1 specifically binds oxytocin. Belongs to the vasopressin/oxytocin family. response to amphetamine regulation of heart rate maternal aggressive behavior neuropeptide hormone activity neurohypophyseal hormone activity extracellular region extracellular space cytoplasm signal transduction positive regulation of cytosolic calcium ion concentration heart development female pregnancy memory grooming behavior response to sucrose positive regulation of norepinephrine secretion response to organic cyclic compound response to activity secretory granule sleep oxytocin receptor binding response to food positive regulation of prostaglandin secretion response to estradiol response to retinoic acid response to progesterone response to prostaglandin E social behavior negative regulation of urine volume positive regulation of renal sodium excretion response to cocaine hyperosmotic salinity response maternal behavior sperm ejaculation eating behavior drinking behavior terminal bouton response to peptide hormone regulation of digestive system process response to ether negative regulation of blood pressure positive regulation of blood pressure positive regulation of ossification positive regulation of female receptivity response to steroid hormone positive regulation of synaptic transmission response to glucocorticoid response to cAMP response to electrical stimulus regulation of sensory perception of pain positive regulation of synapse assembly male mating behavior positive regulation of penile erection positive regulation of hindgut contraction negative regulation of gastric acid secretion positive regulation of uterine smooth muscle contraction uc002wht.1 uc002wht.2 
ENST00000217402.3 CHMP4B ENST00000217402.3 charged multivesicular body protein 4B (from RefSeq NM_176812.5) C20orf178 CHM4B_HUMAN E1P5N4 ENST00000217402.1 ENST00000217402.2 NM_176812 Q53ZD6 Q9H444 SHAX1 uc002xaa.1 uc002xaa.2 uc002xaa.3 uc002xaa.4 uc002xaa.5 This gene encodes a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) protein family. The protein is part of the endosomal sorting complex required for transport (ESCRT) complex III (ESCRT-III), which functions in the sorting of endocytosed cell-surface receptors into multivesicular endosomes. The ESCRT machinery also functions in the final abscisson stage of cytokinesis and in the budding of enveloped viruses such as HIV-1. The three proteins of the CHMP4 subfamily interact with programmed cell death 6 interacting protein (PDCD6IP, also known as ALIX), which also functions in the ESCRT pathway. The CHMP4 proteins assemble into membrane-attached 5-nm filaments that form circular scaffolds and promote or stabilize outward budding. These polymers are proposed to help generate the luminal vesicles of multivesicular bodies. Mutations in this gene result in autosomal dominant posterior polar cataracts.[provided by RefSeq, Oct 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.522347.1, SRR3476690.263413.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217402.3/ ENSP00000217402.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released (PubMed:12860994, PubMed:18209100). The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). (Microbial infection) The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with CHMP6 and CHMP4C. Interacts with PDCD6IP; the interaction is direct. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with CHMP7. Interacts with CFTR; the interaction requires misfolded CFTR. Interacts with PTPN23. Q9H444; Q5VW32: BROX; NbExp=5; IntAct=EBI-749627, EBI-6286053; Q9H444; Q6P1N0: CC2D1A; NbExp=3; IntAct=EBI-749627, EBI-7112364; Q9H444; O43633: CHMP2A; NbExp=3; IntAct=EBI-749627, EBI-2692789; Q9H444; Q9UQN3: CHMP2B; NbExp=2; IntAct=EBI-749627, EBI-718324; Q9H444; Q9Y3E7: CHMP3; NbExp=5; IntAct=EBI-749627, EBI-2118119; Q9H444; Q9BY43: CHMP4A; NbExp=4; IntAct=EBI-749627, EBI-747981; Q9H444; Q9BY43-2: CHMP4A; NbExp=3; IntAct=EBI-749627, EBI-12178895; Q9H444; Q9H444: CHMP4B; NbExp=7; IntAct=EBI-749627, EBI-749627; Q9H444; Q9NZZ3: CHMP5; NbExp=4; IntAct=EBI-749627, EBI-751303; Q9H444; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-749627, EBI-749253; Q9H444; P42858: HTT; NbExp=7; IntAct=EBI-749627, EBI-466029; Q9H444; Q8WUM4: PDCD6IP; NbExp=6; IntAct=EBI-749627, EBI-310624; Q9H444; O60664: PLIN3; NbExp=3; IntAct=EBI-749627, EBI-725795; Q9H444; Q9H3S7: PTPN23; NbExp=4; IntAct=EBI-749627, EBI-724478; Q9H444; O95630: STAMBP; NbExp=3; IntAct=EBI-749627, EBI-396676; Q9H444; P63279: UBE2I; NbExp=3; IntAct=EBI-749627, EBI-80168; Q9H444; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-749627, EBI-10180829; Q9H444; Q9WU78-1: Pdcd6ip; Xeno; NbExp=2; IntAct=EBI-749627, EBI-15788421; Cytoplasm, cytosol Late endosome membrane eripheral membrane protein Midbody cleus envelope Note=Recruited to the nuclear envelope by CHMP7 during late anaphase (PubMed:26040712). Localizes transiently to the midbody arms immediately before abscission (PubMed:22422861). Widely expressed. Expressed at higher level in heart and skeletal muscle. Also expressed in brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes. The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components. ISGylated. Isgylation weakens its interaction with VPS4A. Cataract 31, multiple types (CTRCT31) [MIM:605387]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT31 includes posterior polar, progressive posterior subcapsular, nuclear, and anterior subcapsular cataracts. Note=The disease is caused by variants affecting the gene represented in this entry. Its overexpression strongly inhibits HIV-1 release. Belongs to the SNF7 family. mitotic cytokinesis ESCRT III complex protein binding nucleus nuclear envelope cytoplasm endosome cytosol posttranslational protein targeting to membrane autophagy nucleus organization vacuolar transport mitotic metaphase plate congression cytoplasmic side of plasma membrane exit from mitosis regulation of autophagy regulation of centrosome duplication protein transport membrane endosomal transport macroautophagy viral life cycle membrane coat midbody nuclear envelope reassembly late endosome membrane vesicle multivesicular body assembly maintenance of lens transparency viral budding via host ESCRT complex identical protein binding protein homodimerization activity cadherin binding viral budding regulation of viral process protein homooligomerization negative regulation of cell death extracellular exosome membrane fission ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway negative regulation of neuron death regulation of mitotic spindle assembly positive regulation of viral release from host cell negative regulation of autophagosome assembly uc002xaa.1 uc002xaa.2 uc002xaa.3 uc002xaa.4 uc002xaa.5 
ENST00000217407.3 LBP ENST00000217407.3 lipopolysaccharide binding protein (from RefSeq NM_004139.5) B2R938 ENST00000217407.1 ENST00000217407.2 LBP_HUMAN NM_004139 O43438 P18428 Q92672 Q9H403 Q9UD66 uc002xic.1 uc002xic.2 uc002xic.3 uc002xic.4 The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. Gram-negative bacteria contain a glycolipid, lipopolysaccharide (LPS), on their outer cell wall. Together with bactericidal permeability-increasing protein (BPI), the encoded protein binds LPS and interacts with the CD14 receptor, probably playing a role in regulating LPS-dependent monocyte responses. Studies in mice suggest that the encoded protein is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. This protein is part of a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). [provided by RefSeq, Apr 2012]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189652.89550.1, SRR5189664.106705.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217407.3/ ENSP00000217407.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:7517398, PubMed:24120359). Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:7517398, PubMed:24120359). When bound to LPS, interacts (via C-terminus) with soluble and membrane-bound CD14. P18428; P23560-2: BDNF; NbExp=3; IntAct=EBI-3927059, EBI-12275524; P18428; Q13162: PRDX4; NbExp=4; IntAct=EBI-3927059, EBI-2211957; Secreted toplasmic granule membrane Note=Membrane- associated in polymorphonuclear Leukocytes (PMN) granules. Detected in blood serum (at protein level). Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. lipopolysaccharide binding toll-like receptor signaling pathway leukocyte chemotaxis involved in inflammatory response macrophage activation involved in immune response immune system process receptor binding protein binding extracellular region extracellular space lipid transport acute-phase response cellular defense response opsonization lipid binding cell surface lipopolysaccharide transport membrane cytokine-mediated signaling pathway lipopolysaccharide-mediated signaling pathway detection of molecule of bacterial origin response to lipopolysaccharide negative regulation of tumor necrosis factor production positive regulation of chemokine production positive regulation of interleukin-6 production positive regulation of interleukin-8 production positive regulation of tumor necrosis factor production macromolecule localization toll-like receptor 4 signaling pathway positive regulation of toll-like receptor 4 signaling pathway positive regulation of tumor necrosis factor biosynthetic process defense response to bacterium positive regulation of macrophage activation innate immune response positive regulation of cytolysis defense response to Gram-negative bacterium defense response to Gram-positive bacterium positive regulation of respiratory burst involved in inflammatory response extracellular exosome lipoteichoic acid binding cellular response to lipopolysaccharide cellular response to lipoteichoic acid lipopeptide binding positive regulation of neutrophil chemotaxis uc002xic.1 uc002xic.2 uc002xic.3 uc002xic.4 
ENST00000217420.2 SLC32A1 ENST00000217420.2 solute carrier family 32 member 1 (from RefSeq NM_080552.3) ENST00000217420.1 NM_080552 Q8N489 Q9H598 SLC32A1 VGAT VIAAT VIAAT_HUMAN uc002xjc.1 uc002xjc.2 uc002xjc.3 uc002xjc.4 The protein encoded by this gene is an integral membrane protein involved in gamma-aminobutyric acid (GABA) and glycine uptake into synaptic vesicles. The encoded protein is a member of amino acid/polyamine transporter family II. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK055051.1, SRR3476690.433362.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145743, SAMEA2153733 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217420.2/ ENSP00000217420.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Antiporter that exchanges vesicular protons for cytosolic 4- aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals. The transport is equally dependent on the chemical and electrical components of the proton gradient (By similarity). May also transport beta-alanine (By similarity). Acidification of GABAergic synaptic vesicles is a prerequisite for 4- aminobutanoate uptake (By similarity). Reaction=4-aminobutanoate(out) + n H(+)(in) = 4-aminobutanoate(in) + n H(+)(out); Xref=Rhea:RHEA:70979, ChEBI:CHEBI:15378, ChEBI:CHEBI:59888; Evidence=; Reaction=glycine(out) + n H(+)(in) = glycine(in) + n H(+)(out); Xref=Rhea:RHEA:70983, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305; Evidence=; Reaction=beta-alanine(out) + n H(+)(in) = beta-alanine(in) + n H(+)(out); Xref=Rhea:RHEA:70987, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966; Evidence=; Cytoplasmic vesicle membrane ; Multi-pass membrane protein Presynapse Note=Presents in glycine-, GABA- or GABA- and glycine-containing boutons. Retina. Expressed throughout the horizontal cells or more specifically at the terminals. Belongs to the amino acid/polyamine transporter 2 family. Juge et al. shows that SLC32A1 is a symporter of both 4- aminobutanoate or glycine or beta-alanine with Cl(-) that operates according an electrical gradient without the need for a chemical gradient (By similarity). However Farsi et al. and Egashira et al. confirm that SLC32A1 is an antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or glycine and exclude any coupling with chloride (By similarity). Sequence=AAH36458.2; Type=Erroneous initiation; Evidence=; amino acid transmembrane transport plasma membrane ion transport neurotransmitter transport neurotransmitter secretion aging synaptic vesicle amino acid transmembrane transporter activity glycine transmembrane transporter activity gamma-aminobutyric acid:proton symporter activity gamma-aminobutyric acid transport glycine transport membrane integral component of membrane hippocampus development integral component of synaptic vesicle membrane dendrite cytoplasmic vesicle membrane synaptic vesicle membrane cytoplasmic vesicle neuron projection intracellular organelle dendrite terminus neuron projection terminus cone cell pedicle synapse presynaptic active zone cell tip inhibitory synapse clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane neurotransmitter loading into synaptic vesicle GABA-ergic synapse uc002xjc.1 uc002xjc.2 uc002xjc.3 uc002xjc.4 
ENST00000217423.4 CST4 ENST00000217423.4 cystatin S (from RefSeq NM_001899.3) CYTS_HUMAN ENST00000217423.1 ENST00000217423.2 ENST00000217423.3 NM_001899 P01036 Q9UBI5 Q9UCS9 uc002wto.1 uc002wto.2 uc002wto.3 The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes a type 2 salivary cysteine peptidase inhibitor. The protein is an S-type cystatin, based on its high level of expression in saliva, tears and seminal plasma. The specific role in these fluids is unclear but antibacterial and antiviral activity is present, consistent with a protective function. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X54667.1, BP333642.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non- competitively. P01036; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1049999, EBI-947187; Secreted Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in saliva, tears, urine and seminal fluid. Phosphorylated at both its N- and C-terminal regions. Mass=14175.8569; Mass_error=0.0564; Method=Electrospray; Evidence=; Mass=14255.8567; Mass_error=0.0899; Method=Electrospray; Note=Monophosphorylated at Ser-23, also called form S1.; Evidence=; Mass=14335.811; Mass_error=0.0775; Method=Electrospray; Note=Diphosphorylated at Ser-21 and Ser-23, also called form S2.; Evidence=; Belongs to the cystatin family. detection of chemical stimulus involved in sensory perception of bitter taste retina homeostasis cysteine-type endopeptidase inhibitor activity extracellular region extracellular space negative regulation of peptidase activity negative regulation of endopeptidase activity peptidase inhibitor activity negative regulation of proteolysis extracellular exosome uc002wto.1 uc002wto.2 uc002wto.3 
ENST00000217426.7 AHCY ENST00000217426.7 adenosylhomocysteinase, transcript variant 6 (from RefSeq NM_001362750.2) A8K307 B3KUN3 E1P5P2 ENST00000217426.1 ENST00000217426.2 ENST00000217426.3 ENST00000217426.4 ENST00000217426.5 ENST00000217426.6 F5H737 NM_001362750 P23526 Q96A36 SAHH SAHH_HUMAN uc002xai.1 uc002xai.2 uc002xai.3 uc002xai.4 uc002xai.5 S-adenosylhomocysteine hydrolase belongs to the adenosylhomocysteinase family. It catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). Thus, it regulates the intracellular S-adenosylhomocysteine (SAH) concentration thought to be important for transmethylation reactions. Deficiency in this protein is one of the different causes of hypermethioninemia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2009]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DRR138525.461807.1, SRR1163658.64733.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form adenosine and homocysteine (PubMed:10933798). Binds copper ions (By similarity). Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709; Evidence=; Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence=; Note=Binds 1 NAD(+) per subunit. Amino-acid biosynthesis; L-homocysteine biosynthesis; L- homocysteine from S-adenosyl-L-homocysteine: step 1/1. Homotetramer (PubMed:9586999, PubMed:28647132, PubMed:19177456). Interaction with AHCYL1 (PubMed:28647132). P23526; Q6AI12: ANKRD40; NbExp=8; IntAct=EBI-1053240, EBI-2838246; P23526; Q92624: APPBP2; NbExp=3; IntAct=EBI-1053240, EBI-743771; P23526; Q9BV19: C1orf50; NbExp=12; IntAct=EBI-1053240, EBI-2874661; Cytoplasm Melanosome Nucleus Endoplasmic reticulum Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P23526-1; Sequence=Displayed; Name=2; IsoId=P23526-2; Sequence=VSP_045404; Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:613752]: A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the adenosylhomocysteinase family. sulfur amino acid metabolic process response to hypoxia chronic inflammatory response to antigenic stimulus adenosylhomocysteinase activity protein binding nucleus cytoplasm cytosol one-carbon metabolic process response to nutrient hydrolase activity S-adenosylhomocysteine catabolic process adenyl nucleotide binding methylation S-adenosylmethionine cycle melanosome circadian sleep/wake cycle identical protein binding neuron projection NAD binding extracellular exosome uc002xai.1 uc002xai.2 uc002xai.3 uc002xai.4 uc002xai.5 
ENST00000217428.7 SPINT3 ENST00000217428.7 serine peptidase inhibitor, Kunitz type 3 (from RefSeq NM_006652.2) A6NCQ6 ENST00000217428.1 ENST00000217428.2 ENST00000217428.3 ENST00000217428.4 ENST00000217428.5 ENST00000217428.6 NM_006652 P49223 Q6UDR8 Q96KK2 SPIT3_HUMAN uc010ghg.1 uc010ghg.2 Secreted serine-type endopeptidase inhibitor activity extracellular region negative regulation of peptidase activity negative regulation of endopeptidase activity peptidase inhibitor activity negative regulation of transforming growth factor beta receptor signaling pathway receptor antagonist activity transforming growth factor beta binding negative regulation of receptor activity uc010ghg.1 uc010ghg.2 
ENST00000217446.8 PIGU ENST00000217446.8 phosphatidylinositol glycan anchor biosynthesis class U (from RefSeq NM_080476.5) CDC91L1 ENST00000217446.1 ENST00000217446.2 ENST00000217446.3 ENST00000217446.4 ENST00000217446.5 ENST00000217446.6 ENST00000217446.7 NM_080476 PIGU_HUMAN PSEC0205 Q7Z489 Q8N2F2 Q9H490 UNQ3055/PRO9875 uc002xas.1 uc002xas.2 uc002xas.3 uc002xas.4 uc002xas.5 The protein encoded by this gene shares similarity with Saccharomyces cerevisiae Cdc91, a predicted integral membrane protein that may function in cell division control. The protein encoded by this gene is the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY422169.1, BC030512.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the GPI transamidase complex, necessary for transfer of GPI to proteins (PubMed:34576938). May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. Forms a complex with PIGK/GPI8, PIGS, PIGT and GPAA1/GAA1. Q9H490; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-11290294, EBI-749265; Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H490-1; Sequence=Displayed; Name=2; IsoId=Q9H490-2; Sequence=VSP_009543; Neurodevelopmental disorder with brain anomalies, seizures, and scoliosis (NEDBSS) [MIM:618590]: An autosomal recessive disorder characterized by global developmental delay, severe-to-profound intellectual disability, muscular hypotonia, seizures, brain anomalies, including thin corpus callosum and cerebellar atrophy, scoliosis, and mild facial dysmorphism. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the PIGU family. endoplasmic reticulum endoplasmic reticulum membrane plasma membrane GPI anchor biosynthetic process membrane integral component of membrane attachment of GPI anchor to protein integral component of endoplasmic reticulum membrane protein localization to cell surface GPI-anchor transamidase complex regulation of JAK-STAT cascade GPI-anchor transamidase activity GPI anchor binding uc002xas.1 uc002xas.2 uc002xas.3 uc002xas.4 uc002xas.5 
ENST00000217455.9 ACOT8 ENST00000217455.9 acyl-CoA thioesterase 8 (from RefSeq NM_005469.4) ACOT8_HUMAN ACTEIII ENST00000217455.1 ENST00000217455.2 ENST00000217455.3 ENST00000217455.4 ENST00000217455.5 ENST00000217455.6 ENST00000217455.7 ENST00000217455.8 NM_005469 O14734 O15261 PTE1 Q17RX4 uc002xqa.1 uc002xqa.2 uc002xqa.3 uc002xqa.4 The protein encoded by this gene is a peroxisomal thioesterase that appears to be involved more in the oxidation of fatty acids rather than in their formation. The encoded protein can bind to the human immunodeficiency virus-1 protein Nef, and mediate Nef-induced down-regulation of CD4 in T-cells. [provided by RefSeq, Oct 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163658.330817.1, SRR5189667.88385.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2152474, SAMEA2152798 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217455.9/ ENSP00000217455.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:9299485, PubMed:9153233, PubMed:15194431). Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:9299485, PubMed:9153233). Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (PubMed:15194431). (Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression (PubMed:9153233). Reaction=choloyl-CoA + H2O = cholate + CoA + H(+); Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373; EC=3.1.2.27; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542; Evidence=; Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+); Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989; EC=3.1.2.27; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512; Evidence=; Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290; Evidence=; Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+); Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; Evidence=; Reaction=2-methylpropanoyl-CoA + H2O = 2-methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:40799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40800; Evidence=; Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; Evidence=; Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate; Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence=; Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence=; Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence=; Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence=; Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence=; Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence=; Reaction=H2O + malonyl-CoA = CoA + H(+) + malonate; Xref=Rhea:RHEA:40219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15792, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40220; Evidence=; Reaction=acetoacetyl-CoA + H2O = acetoacetate + CoA + H(+); Xref=Rhea:RHEA:15673, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287; EC=3.1.2.11; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15674; Evidence=; Reaction=H2O + propanoyl-CoA = CoA + H(+) + propanoate; Xref=Rhea:RHEA:40103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104; Evidence=; Reaction=H2O + succinyl-CoA = CoA + H(+) + succinate; Xref=Rhea:RHEA:11516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=3.1.2.3; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11517; Evidence=; Reaction=glutaryl-CoA + H2O = CoA + glutarate + H(+); Xref=Rhea:RHEA:40575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30921, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40576; Evidence=; Reaction=H2O + hexanedioyl-CoA = CoA + H(+) + hexanedioate; Xref=Rhea:RHEA:40583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17128, ChEBI:CHEBI:57287, ChEBI:CHEBI:76327; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40584; Evidence=; Reaction=H2O + octanedioyl-CoA = CoA + H(+) + octanedioate; Xref=Rhea:RHEA:40587, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:76282, ChEBI:CHEBI:76317; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40588; Evidence=; Reaction=decanedioyl-CoA + H2O = CoA + decanedioate + H(+); Xref=Rhea:RHEA:40591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:76283, ChEBI:CHEBI:76316; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40592; Evidence=; Reaction=dodecanedioyl-CoA + H2O = CoA + dodecanedioate + H(+); Xref=Rhea:RHEA:40595, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:76273, ChEBI:CHEBI:76315; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40596; Evidence=; Reaction=(9Z)-tetradecenoyl-CoA + H2O = (9Z)-tetradecenoate + CoA + H(+); Xref=Rhea:RHEA:40135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32370, ChEBI:CHEBI:57287, ChEBI:CHEBI:65060; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40136; Evidence=; Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence=; Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence=; Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence=; Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)- eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence=; Reaction=4,8-dimethylnonanoyl-CoA + H2O = 4,8-dimethylnonanoate + CoA + H(+); Xref=Rhea:RHEA:40223, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061, ChEBI:CHEBI:77063; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40224; Evidence=; Reaction=2,6-dimethylheptanoyl-CoA + H2O = 2,6-dimethylheptanoate + CoA + H(+); Xref=Rhea:RHEA:59952, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:84847, ChEBI:CHEBI:143533; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59953; Evidence=; Reaction=(3S)-hydroxy-3-methylglutaryl-CoA + H2O = 3-hydroxy-3- methylglutarate + CoA + H(+); Xref=Rhea:RHEA:16305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17325, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287; EC=3.1.2.5; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16306; Evidence=; Reaction=3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA + H(+); Xref=Rhea:RHEA:59936, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:63001, ChEBI:CHEBI:85674; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59937; Evidence=; Reaction=2-methyloctadecanoyl-CoA + H2O = 2-methyloctadecanoate + CoA + H(+); Xref=Rhea:RHEA:59940, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:143530, ChEBI:CHEBI:143531; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59941; Evidence=; Reaction=H2O + prostaglandin F2alpha-CoA = CoA + H(+) + prostaglandin F2alpha; Xref=Rhea:RHEA:59948, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57404, ChEBI:CHEBI:143532; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59949; Evidence=; Inhibited by CoASH (IC(50)=10-15 uM). Also inhibited by cysteine-reactive agents. Kinetic parameters: KM=10.1 uM for decanoyl-CoA ; Vmax=7.1 umol/min/mg enzyme ; Lipid metabolism; fatty acid metabolism. Homodimer (By similarity). (Microbial infection) Interacts with human immunodeficiency virus (HIV-1) Nef (via middle region); this interaction enhances ACOT8 Acyl-CoA thioesterase activity and occurs in a Nef myristoylation- independent manner (PubMed:9299485). According to a second report, the interaction with HIV-1 Nef occurs in a Nef myristoylation-independent manner but does not enhance ACOT8 Acyl-CoA thioesterase activity (PubMed:9153233). O14734; P13569: CFTR; NbExp=3; IntAct=EBI-1237371, EBI-349854; O14734; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-1237371, EBI-10181968; O14734; P50542: PEX5; NbExp=3; IntAct=EBI-1237371, EBI-597835; O14734; Q04864: REL; NbExp=3; IntAct=EBI-1237371, EBI-307352; O14734; Q04864-2: REL; NbExp=3; IntAct=EBI-1237371, EBI-10829018; O14734; P04601: nef; Xeno; NbExp=7; IntAct=EBI-1237371, EBI-6164028; Peroxisome matrix te=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. Detected in a T-cell line (at protein level). Ubiquitous (PubMed:9153233, PubMed:9299485). Regulated by peroxisome proliferator (such as Clofibrate), via the peroxisome proliferator-activated receptors (PPARs). Belongs to the C/M/P thioester hydrolase family. acetyl-CoA hydrolase activity succinyl-CoA hydrolase activity protein binding peroxisome peroxisomal matrix cytosol protein targeting to peroxisome lipid metabolic process fatty acid metabolic process acyl-CoA metabolic process bile acid biosynthetic process peroxisome organization fatty acid catabolic process viral process CoA hydrolase activity palmitoyl-CoA hydrolase activity peroxisome fission hydrolase activity fatty acid beta-oxidation using acyl-CoA oxidase choloyl-CoA hydrolase activity alpha-linolenic acid metabolic process dicarboxylic acid catabolic process negative regulation of CD4 biosynthetic process acetoacetyl-CoA hydrolase activity acyl-CoA hydrolase activity hydroxymethylglutaryl-CoA hydrolase activity carboxylic ester hydrolase activity medium-chain acyl-CoA hydrolase activity long-chain acyl-CoA hydrolase activity uc002xqa.1 uc002xqa.2 uc002xqa.3 uc002xqa.4 
ENST00000217456.3 APMAP ENST00000217456.3 adipocyte plasma membrane associated protein (from RefSeq NM_020531.3) A8K514 APMAP_HUMAN B4DXG1 C20orf3 ENST00000217456.1 ENST00000217456.2 NM_020531 Q6UVZ8 Q9GZS8 Q9HDC9 Q9NUB2 UNQ1869/PRO4305 uc002wty.1 uc002wty.2 uc002wty.3 uc002wty.4 uc002wty.5 Exhibits strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. May play a role in adipocyte differentiation. Q9HDC9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-723950, EBI-18304435; Membrane ; Single- pass type II membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9HDC9-1; Sequence=Displayed; Name=2; IsoId=Q9HDC9-2; Sequence=VSP_036992, VSP_036993; Liver, glomerular and tubular structures of the kidney, endothelial cells, arterial wall and pancreatic islets of Langerhans (at protein level). Found ubiquitously in adult as well as in embryonic tissues. In adult tissue, the highest expression is found in the liver, placenta and heart. Found on the cell surface of monocytes. In embryonic tissue, the highest expression levels is found in the liver and the kidney. Belongs to the strictosidine synthase family. Sequence=AAQ89435.1; Type=Erroneous initiation; Evidence=; Sequence=BAB11885.1; Type=Erroneous initiation; Evidence=; Sequence=BAB15253.1; Type=Erroneous initiation; Evidence=; Sequence=BAB15578.1; Type=Erroneous initiation; Evidence=; arylesterase activity endoplasmic reticulum biological_process biosynthetic process cell surface membrane integral component of membrane strictosidine synthase activity uc002wty.1 uc002wty.2 uc002wty.3 uc002wty.4 uc002wty.5 
ENST00000217515.11 TXNL1 ENST00000217515.11 thioredoxin like 1, transcript variant 2 (from RefSeq NR_024546.2) ENST00000217515.1 ENST00000217515.10 ENST00000217515.2 ENST00000217515.3 ENST00000217515.4 ENST00000217515.5 ENST00000217515.6 ENST00000217515.7 ENST00000217515.8 ENST00000217515.9 HEL-S-114 NR_024546 TXNL1 V9HW51 V9HW51_HUMAN hCG_23140 uc002lgg.1 uc002lgg.2 uc002lgg.3 uc002lgg.4 uc002lgg.5 cytosol cell redox homeostasis uc002lgg.1 uc002lgg.2 uc002lgg.3 uc002lgg.4 uc002lgg.5 
ENST00000217652.8 MYL12A ENST00000217652.8 myosin light chain 12A, transcript variant 1 (from RefSeq NM_006471.4) ENST00000217652.1 ENST00000217652.2 ENST00000217652.3 ENST00000217652.4 ENST00000217652.5 ENST00000217652.6 ENST00000217652.7 ML12A_HUMAN MLCB MRLC3 NM_006471 P19105 Q53X45 RLC uc002klr.1 uc002klr.2 uc002klr.3 uc002klr.4 This gene encodes a nonsarcomeric myosin regulatory light chain. This protein is activated by phosphorylation and regulates smooth muscle and non-muscle cell contraction. This protein may also be involved in DNA damage repair by sequestering the transcriptional regulator apoptosis-antagonizing transcription factor (AATF)/Che-1 which functions as a repressor of p53-driven apoptosis. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome 8.[provided by RefSeq, Dec 2014]. Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). Myosin is a hexamer of 2 heavy chains and 4 light chains. P19105; Q62868: Rock2; Xeno; NbExp=2; IntAct=EBI-354418, EBI-1569209; Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge (By similarity). This chain binds calcium. calcium ion binding protein binding cytosol muscle contraction myosin complex metal ion binding extracellular exosome platelet aggregation uc002klr.1 uc002klr.2 uc002klr.3 uc002klr.4 
ENST00000217740.4 RNF125 ENST00000217740.4 ring finger protein 125 (from RefSeq NM_017831.4) ENST00000217740.1 ENST00000217740.2 ENST00000217740.3 NM_017831 Q96EQ8 Q9NX39 RN125_HUMAN RNF125 uc002kxf.1 uc002kxf.2 uc002kxf.3 This gene encodes a novel E3 ubiquitin ligase that contains a RING finger domain in the N-terminus and three zinc-binding and one ubiquitin-interacting motif in the C-terminus. As a result of myristoylation, this protein associates with membranes and is primarily localized to intracellular membrane systems. The encoded protein may function as a positive regulator in the T-cell receptor signaling pathway. [provided by RefSeq, Mar 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.373170.1, SRR1660809.78201.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217740.4/ ENSP00000217740.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins, such as RIGI, MAVS/IPS1, IFIH1/MDA5, JAK1 and p53/TP53 (PubMed:15843525, PubMed:17460044, PubMed:17643463, PubMed:26027934, PubMed:26471729, PubMed:25591766, PubMed:27411375). Acts as a negative regulator of type I interferon production by mediating ubiquitination of RIGI at 'Lys- 181', leading to RIGI degradation (PubMed:17460044, PubMed:26471729). Mediates ubiquitination and subsequent degradation of p53/TP53 (PubMed:25591766). Mediates ubiquitination and subsequent degradation of JAK1 (PubMed:26027934). Acts as a positive regulator of T-cell activation (PubMed:15843525). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence= Protein modification; protein ubiquitination. Interacts with UBE2D1 (PubMed:27411375). Interacts with VCP/p97; leading to recruit RNF125 to RIGI and promote ubiquitination of RIGI (PubMed:26471729). Q96EQ8; Q9BYX4: IFIH1; NbExp=2; IntAct=EBI-2339208, EBI-6115771; Q96EQ8; Q7Z434-1: MAVS; NbExp=2; IntAct=EBI-2339208, EBI-15577799; Q96EQ8; O95786: RIGI; NbExp=4; IntAct=EBI-2339208, EBI-995350; Q96EQ8; O95786-1: RIGI; NbExp=5; IntAct=EBI-2339208, EBI-15577823; Q96EQ8; Q96LR5: UBE2E2; NbExp=5; IntAct=EBI-2339208, EBI-2129763; Q96EQ8; P55072: VCP; NbExp=3; IntAct=EBI-2339208, EBI-355164; Golgi apparatus membrane ; Lipid-anchor Note=Shows a reticular staining pattern within the cell and is probably expressed at other intracellular membranes in addition to the Golgi membrane. Not detected at the plasma membrane. Predominantly expressed in lymphoid tissues, including bone marrow, spleen and thymus. Also weakly expressed in other tissues. Predominant in the CD4(+) and CD8(+) T-cells, suggesting that it is preferentially confined to T-cells. Down-regulated by miR-15b (PubMed:26202983). Down-regulated in BRAFi resistant melanomas, leading to increased levels of JAK1 and possibly promoting BRAFi resistance. The C2HC RNF-type zinc finger and the linker region stabilize the RING-type zinc finger, leading to promote binding of the RING-type zinc finger to the ubiquitin-conjugating enzyme E2 (donor ubiquitin) (PubMed:27411375). Autoubiquitinated, leading to its subsequent proteasomal degradation. Tenorio syndrome (TNORS) [MIM:616260]: A disease characterized by overgrowth, macrocephaly, and intellectual disability. Some patients may have mild hydrocephaly, hypoglycemia, and inflammatory diseases resembling Sjogren syndrome. Note=The disease is caused by variants affecting the gene represented in this entry. Golgi membrane protein polyubiquitination p53 binding adaptive immune response immune system process protein binding Golgi apparatus ubiquitin-dependent protein catabolic process zinc ion binding membrane protein ubiquitination transferase activity ubiquitin conjugating enzyme binding negative regulation of type I interferon production VCP-NPL4-UFD1 AAA ATPase complex negative regulation of RIG-I signaling pathway intracellular membrane-bounded organelle metal ion binding ubiquitin protein ligase activity uc002kxf.1 uc002kxf.2 uc002kxf.3 
ENST00000217893.10 TAF9 ENST00000217893.10 TATA-box binding protein associated factor 9, transcript variant 1 (from RefSeq NM_003187.5) D3DWA3 ENST00000217893.1 ENST00000217893.2 ENST00000217893.3 ENST00000217893.4 ENST00000217893.5 ENST00000217893.6 ENST00000217893.7 ENST00000217893.8 ENST00000217893.9 NM_003187 Q16594 Q5U0D1 Q9BTS1 TAF2G TAF9_HUMAN TAFII31 uc003jwe.1 uc003jwe.2 uc003jwe.3 Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the smaller subunits of TFIID that binds to the basal transcription factor GTF2B as well as to several transcriptional activators such as p53 and VP16. In human, TAF9 and AK6 (GeneID: 102157402) are two distinct genes that share 5' exons. A similar but distinct gene (TAF9L) has been found on the X chromosome and a pseudogene has been identified on chromosome 19. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]. The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF9 is also a component of the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex (PubMed:15899866). TAF9 and its paralog TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes (PubMed:15899866). Essential for cell viability (PubMed:15899866). May have a role in gene regulation associated with apoptosis (PubMed:15899866). Component of the TFIID basal transcription factor complex, composed of TATA-box-binding protein TBP, and a number of TBP- associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). Component of the TATA-binding protein-free TAF complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex (PubMed:11564863, PubMed:9885574). The PCAF complex consists at least of TADA2L/ADA2, SUPT3H/SPT3, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP (PubMed:9885574, PubMed:9674425). The STAGA transcription coactivator-HAT complex consists at least of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9 (PubMed:11564863). Binds N-terminal domain of p53/TP53 which is essential for transcription (PubMed:7761466). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975). Binds TFIIB and the Herpes simplex virus activator VP16 (PubMed:7761466). Forms a heterodimer with TAF6 in a complex with the TAF4B-TAF12 heterodimer (PubMed:7597030, PubMed:15601843). Also interacts with TAF5 (PubMed:15899866). Binds directly DNA (PubMed:15601843). Increased DNA binding when complexed with TAF6 (PubMed:15601843). Q16594; Q14919: DRAP1; NbExp=9; IntAct=EBI-712521, EBI-712941; Q16594; Q92831: KAT2B; NbExp=3; IntAct=EBI-712521, EBI-477430; Q16594; P52294: KPNA1; NbExp=4; IntAct=EBI-712521, EBI-358383; Q16594; O60684: KPNA6; NbExp=4; IntAct=EBI-712521, EBI-359923; Q16594; Q9Y6J9: TAF6L; NbExp=9; IntAct=EBI-712521, EBI-743984; Q16594; P46099: Klf1; Xeno; NbExp=3; IntAct=EBI-712521, EBI-15761537; Nucleus 6 to 8-fold by apoptotic signals. Belongs to the TAF9 family. AK6 and TAF9 were initially considered as products of the same gene since they share two exons. However, they are translated from different initiation codons and reading frames and encode unrelated proteins. This arrangement is conserved in some mammalian species. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/taf9/"; SAGA complex PCAF complex box C/D snoRNP assembly p53 binding DNA binding transcription coactivator activity protein binding nucleus nucleoplasm transcription factor TFIID complex DNA-templated transcription, initiation transcription from RNA polymerase II promoter transcription initiation from RNA polymerase II promoter cellular response to DNA damage stimulus transcription factor binding positive regulation of cell growth STAGA complex negative regulation of proteasomal ubiquitin-dependent protein catabolic process transcription factor TFTC complex activating transcription factor binding snRNA transcription from RNA polymerase II promoter negative regulation of apoptotic process histone H3 acetylation transcription regulatory region DNA binding positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity protein stabilization ATPase binding positive regulation of response to cytokine stimulus response to interleukin-1 C2H2 zinc finger domain binding pre-snoRNP complex MLL1 complex regulation of signal transduction by p53 class mediator negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator histone acetyltransferase activity uc003jwe.1 uc003jwe.2 uc003jwe.3 
ENST00000217901.10 IDH3G ENST00000217901.10 isocitrate dehydrogenase (NAD(+)) 3 non-catalytic subunit gamma, transcript variant 1 (from RefSeq NM_004135.4) E9PDD5 ENST00000217901.1 ENST00000217901.2 ENST00000217901.3 ENST00000217901.4 ENST00000217901.5 ENST00000217901.6 ENST00000217901.7 ENST00000217901.8 ENST00000217901.9 IDH3G_HUMAN NM_004135 P51553 Q9BUU5 uc004fip.1 uc004fip.2 uc004fip.3 uc004fip.4 uc004fip.5 Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the gamma subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. This gene is a candidate gene for periventricular heterotopia. Several alternatively spliced transcript variants of this gene have been described, but only some of their full length natures have been determined. [provided by RefSeq, Jul 2008]. Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit. ; The heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits can be allosterically activated by citrate (CIT) or/and ADP, and the two activators can act independently or synergistically. The heterodimer composed of IDH3A and IDH3B subunits cannot be allosterically regulated and the allosteric regulation of the heterotetramer is through the IDH3G subunit and not the IDH3B subunit. The IDH3G subunit contains the allosteric site which consists of a CIT- binding site and an ADP-binding site, and the binding of CIT and ADP causes conformational changes at the allosteric site which are transmitted to the active site in the catalytic subunit (IDH3A) through a cascade of conformational changes at the heterodimer interface, leading to stabilization of the isocitrate-binding at the active site and thus activation of the enzyme. ATP can activate the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits at low concentrations but inhibits their activities at high concentrations, whereas ATP exhibits only inhibitory effect on the heterodimer composed of IDH3A and IDH3B subunits. Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer containing one IDH3A and one IDH3B subunit and the heterodimer containing one IDH3A and one IDH3G subunit assemble into a heterotetramer (which contains two subunits of IDH3A, one of IDH3B and one of IDH3G) and further into the heterooctamer. P51553; P50213: IDH3A; NbExp=5; IntAct=EBI-1210876, EBI-355999; Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P51553-1; Sequence=Displayed; Name=2; IsoId=P51553-2; Sequence=VSP_046771; Belongs to the isocitrate and isopropylmalate dehydrogenases family. nucleotide binding magnesium ion binding isocitrate dehydrogenase (NAD+) activity ATP binding nucleoplasm nucleolus mitochondrion mitochondrial matrix carbohydrate metabolic process tricarboxylic acid cycle isocitrate metabolic process oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor metal ion binding NAD binding oxidation-reduction process uc004fip.1 uc004fip.2 uc004fip.3 uc004fip.4 uc004fip.5 
ENST00000217909.8 SLC25A43 ENST00000217909.8 solute carrier family 25 member 43 (from RefSeq NM_145305.3) ENST00000217909.1 ENST00000217909.2 ENST00000217909.3 ENST00000217909.4 ENST00000217909.5 ENST00000217909.6 ENST00000217909.7 NM_145305 O75854 Q8N9L5 Q8WUT9 S2543_HUMAN uc004erd.1 uc004erd.2 uc004erd.3 uc004erd.4 uc004erd.5 This gene encodes a member of the mitochondrial carrier family of proteins.[provided by RefSeq, Dec 2009]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.385473.1, BC019584.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000217909.8/ ENSP00000217909.7 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Mitochondrion inner membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8WUT9-1; Sequence=Displayed; Name=2; IsoId=Q8WUT9-2; Sequence=VSP_026245; Belongs to the mitochondrial carrier (TC 2.A.29) family. Sequence=AAC62432.1; Type=Erroneous gene model prediction; Evidence=; mitochondrion mitochondrial inner membrane membrane integral component of membrane transmembrane transporter activity transmembrane transport uc004erd.1 uc004erd.2 uc004erd.3 uc004erd.4 uc004erd.5 
ENST00000217926.7 H2BW1 ENST00000217926.7 H2B.W histone 1 (from RefSeq NM_001002916.5) B1AK72 ENST00000217926.1 ENST00000217926.2 ENST00000217926.3 ENST00000217926.4 ENST00000217926.5 ENST00000217926.6 H2BFWT H2BW1 H2BWT_HUMAN NM_001002916 Q147W3 Q7Z2G1 TH2B-175 uc004elr.1 uc004elr.2 uc004elr.3 uc004elr.4 uc004elr.5 Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene encodes a replication-independent histone that is a member of the H2B histone family that is specifically expressed in sperm nuclei. A polymorphism in the 5' UTR of this gene is associated with male infertility.[provided by RefSeq, Oct 2015]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: BC038109.2, BI459475.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148874 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript replication-independent histone :: PMID: 25731851 ##RefSeq-Attributes-END## Atypical histone H2B that can form nucleosomes structurally and dynamically indistinguishable from those containing conventional H2B. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (PubMed:15475252, PubMed:16449661). However, unlike conventional H2B, does not recruit chromosome condensation factors and does not participate in the assembly of mitotic chromosomes (PubMed:16449661). May be important for telomere function and play a role in spermatogenesis (PubMed:16449661, PubMed:19583817). Can replace the conventional histone H2B in the nucleosome (PubMed:16449661). The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA (Probable). Q7Z2G1; Q6NXS1: PPP1R2B; NbExp=3; IntAct=EBI-18200422, EBI-10251630; Nucleus membrane Chromosome Chromosome, telomere Event=Alternative initiation; Named isoforms=3; Name=2; IsoId=Q7Z2G1-2; Sequence=Displayed; Name=1; IsoId=Q7Z2G1-1; Sequence=VSP_062144; Name=3; IsoId=Q7Z2G1-3; Sequence=VSP_062143; Testis-specific (at protein level). In contrast to other H2B histones, it does not contain the conserved residue in C-terminus that is the target of monoubiquitination. [Isoform 3]: Gene prediction based on conservation. Has orthologs in primates, but not in rodents. Belongs to the histone H2B family. nucleosome DNA binding nucleus chromosome nucleosome assembly membrane nuclear membrane protein heterodimerization activity uc004elr.1 uc004elr.2 uc004elr.3 uc004elr.4 uc004elr.5 
ENST00000217939.7 MXRA5 ENST00000217939.7 matrix remodeling associated 5 (from RefSeq NM_015419.4) ENST00000217939.1 ENST00000217939.2 ENST00000217939.3 ENST00000217939.4 ENST00000217939.5 ENST00000217939.6 MXRA5_HUMAN NM_015419 Q6P1M7 Q9NR99 Q9Y3Y8 uc004crg.1 uc004crg.2 uc004crg.3 uc004crg.4 uc004crg.5 uc004crg.6 uc004crg.7 This gene encodes one of the matrix-remodelling associated proteins. This protein contains 7 leucine-rich repeats and 12 immunoglobulin-like C2-type domains related to perlecan. This gene has a pseudogene on chromosome Y. [provided by RefSeq, Mar 2010]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The extent of this transcript is supported by transcript alignments. An in-frame AUG is located 25 codons upstream of the annotated translation start site but is not being annotated as a start site since it is poorly conserved, is in a weak Kozak sequence context, and is predicted to disrupt an N-terminal signal peptide sequence. ##Evidence-Data-START## CDS exon combination :: AF245505.1 [ECO:0000331] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## CDS uses downstream in-frame AUG :: downstream AUG is associated with N-terminal localization signal MANE Ensembl match :: ENST00000217939.7/ ENSP00000217939.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## In kidney, has anti-inflammatory and anti-fibrotic properties by limiting the induction of chemokines, fibronectin and collagen expression in response to TGB1 and pro-inflammatory stimuli. Secreted Detected in placenta (at protein level) (PubMed:32337544). Detected in cerebrospinal fluid and fibroblasts (at protein level) (PubMed:25326458, PubMed:36213313). Highly expressed in kidney, also detected on liver and spleen (PubMed:27599751). Expressed by proximal tubular cells of the kidney (at protein level) (PubMed:27599751). Expression highly increases during chronic kidney disease and autosomal dominant polycystic kidney disease, where is detected in cysts (PubMed:27599751). Over-expressed in centenarians. Expression is reduced from young to old but increased from old to centenarians. Expression is induced by TGFB1, in kidney tubular cells. This induction is inhibited by the vitamin D receptor activator paricalcitol (at protein level). Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry. Sequence=AAH11846.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; Sequence=AAH64986.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; Sequence=AAH80586.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; extracellular matrix structural constituent extracellular region extracellular exosome response to transforming growth factor beta uc004crg.1 uc004crg.2 uc004crg.3 uc004crg.4 uc004crg.5 uc004crg.6 uc004crg.7 
ENST00000217957.10 VSIG1 ENST00000217957.10 V-set and immunoglobulin domain containing 1, transcript variant 2 (from RefSeq NM_182607.5) C9J4P2 ENST00000217957.1 ENST00000217957.2 ENST00000217957.3 ENST00000217957.4 ENST00000217957.5 ENST00000217957.6 ENST00000217957.7 ENST00000217957.8 ENST00000217957.9 GPA34 NM_182607 Q6MZS4 Q86XK7 VSIG1_HUMAN uc004eno.1 uc004eno.2 uc004eno.3 uc004eno.4 uc004eno.5 This gene encodes a member of the junctional adhesion molecule (JAM) family. The encoded protein contains multiple glycosylation sites at the N-terminal region, and multiple phosphorylation sites and glutamic acid/proline (EP) repeats at the C-terminal region. The gene is expressed in normal stomach and testis, as well as in gastric, esophageal and ovarian cancers. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2009]. Q86XK7; P54852: EMP3; NbExp=3; IntAct=EBI-18323486, EBI-3907816; Q86XK7; Q04756: HGFAC; NbExp=3; IntAct=EBI-18323486, EBI-1041722; Q86XK7; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-18323486, EBI-10317425; Q86XK7; O75841: UPK1B; NbExp=3; IntAct=EBI-18323486, EBI-12237619; Membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q86XK7-1; Sequence=Displayed; Name=2; IsoId=Q86XK7-2; Sequence=VSP_045475; Detected only in stomach mucosa and testis, and to a much lesser level in pancreas (at protein level). Detected in gastric cancers (31%), esophageal carcinomas (50%) and ovarian cancers (23%). Highly N-glycosylated. Appears not to contain significant amounts of O-linked carbohydrates or sialic acid in its sugar moieties. Sequence=CAE45954.1; Type=Erroneous initiation; Evidence=; epithelial cell morphogenesis plasma membrane membrane integral component of membrane basolateral plasma membrane maintenance of gastrointestinal epithelium uc004eno.1 uc004eno.2 uc004eno.3 uc004eno.4 uc004eno.5 
ENST00000217958.8 PSMD10 ENST00000217958.8 proteasome 26S subunit, non-ATPase 10, transcript variant 1 (from RefSeq NM_002814.4) ENST00000217958.1 ENST00000217958.2 ENST00000217958.3 ENST00000217958.4 ENST00000217958.5 ENST00000217958.6 ENST00000217958.7 NM_002814 O75832 PSD10_HUMAN Q5U0B2 Q8IZK9 uc004enp.1 uc004enp.2 uc004enp.3 uc004enp.4 This gene encodes a subunit of the PA700/19S complex, which is the regulatory component of the 26S proteasome. The 26S proteosome complex is required for ubiquitin-dependent protein degradation. This protein is a non-ATPase subunit that may be involved in protein-protein interactions. Aberrant expression of this gene may paly a role in tumorigenesis. Two transcripts encoding different isoforms have been described. Pseudogenes have been identified on chromosomes 3 and 20.[provided by RefSeq, Mar 2011]. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis. Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export. Part of transient complex containing PSMD10, PSMC4, PSMC5 and PAAF1 formed during the assembly of the 26S proteasome. Stays associated throughout the assembly of the PA700/19S RC and is released upon association with the 20S core. Interacts with PSMC4. Interacts with RB1. Interacts with CDK4. Interacts with MDM2. Interacts with RELA. Associates with a CDK4:CCND2 serine/threonine kinase complex. Interacts with ARHGDIA and increases the interaction between ARHGDIA and RHOA, hence promotes ARHGDIA inactivation of RHOA and ROCK. O75832; O00299: CLIC1; NbExp=9; IntAct=EBI-752185, EBI-347404; O75832; Q12849: GRSF1; NbExp=4; IntAct=EBI-752185, EBI-1054150; O75832; Q9NWT6: HIF1AN; NbExp=2; IntAct=EBI-752185, EBI-745632; O75832; P0DMV8: HSPA1A; NbExp=2; IntAct=EBI-752185, EBI-11052499; O75832; P43358: MAGEA4; NbExp=5; IntAct=EBI-752185, EBI-743122; O75832; O43639: NCK2; NbExp=2; IntAct=EBI-752185, EBI-713635; O75832; P43686: PSMC4; NbExp=23; IntAct=EBI-752185, EBI-743997; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75832-1; Sequence=Displayed; Name=2; IsoId=O75832-2; Sequence=VSP_043043; Tends to be up-regulated in cancer cells with RAS mutations, including lung cancers and adenocarconimas (at protein level). Was initially identified as a genuine component of the 26S proteasome. negative regulation of transcription from RNA polymerase II promoter MAPK cascade protein polyubiquitination proteasome complex stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent protein binding nucleus nucleoplasm cytoplasm cytosol regulation of transcription from RNA polymerase II promoter regulation of cellular amino acid metabolic process apoptotic process cytoplasmic sequestering of NF-kappaB transcription factor binding negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination positive regulation of cell growth anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process positive regulation of protein ubiquitination negative regulation of NF-kappaB transcription factor activity positive regulation of proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway negative regulation of apoptotic process proteasome-mediated ubiquitin-dependent protein catabolic process negative regulation of MAPK cascade regulation of mRNA stability negative regulation of DNA damage response, signal transduction by p53 class mediator post-translational protein modification intermediate filament cytoskeleton positive regulation of cyclin-dependent protein serine/threonine kinase activity T cell receptor signaling pathway transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia RNA polymerase II sequence-specific DNA binding transcription factor binding interleukin-1-mediated signaling pathway proteasome regulatory particle assembly negative regulation of canonical Wnt signaling pathway negative regulation of release of cytochrome c from mitochondria positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation proteasome regulatory particle, base subcomplex uc004enp.1 uc004enp.2 uc004enp.3 uc004enp.4 
ENST00000217971.8 PGRMC1 ENST00000217971.8 progesterone receptor membrane component 1, transcript variant 1 (from RefSeq NM_006667.5) ENST00000217971.1 ENST00000217971.2 ENST00000217971.3 ENST00000217971.4 ENST00000217971.5 ENST00000217971.6 ENST00000217971.7 NM_006667 PGRMC1 Q6IB11 Q6IB11_HUMAN hCG_23188 uc004erb.1 uc004erb.2 uc004erb.3 uc004erb.4 uc004erb.5 uc004erb.6 This gene encodes a putative membrane-associated progesterone steroid receptor. The protein is expressed predominantly in the liver and kidney. [provided by RefSeq, Mar 2010]. Endoplasmic reticulum membrane ; Single-pass membrane protein Membrane ; Single-pass membrane protein Microsome membrane ; Single-pass membrane protein Mitochondrion outer membrane ; Single-pass membrane protein ; Extracellular side Secreted Belongs to the cytochrome b5 family. MAPR subfamily. protein binding membrane integral component of membrane uc004erb.1 uc004erb.2 uc004erb.3 uc004erb.4 uc004erb.5 uc004erb.6 
ENST00000217999.3 RHOXF1 ENST00000217999.3 Rhox homeobox family member 1 (from RefSeq NM_139282.3) ENST00000217999.1 ENST00000217999.2 NM_139282 O95030 OTEX PEPP1 Q3SYE0 Q8NHV9 RHOXF1 RHXF1_HUMAN uc004esk.1 uc004esk.2 uc004esk.3 This gene is a member of the PEPP subfamily of paired-like homoebox genes. The gene may be regulated by androgens and epigenetic mechanisms. The encoded nuclear protein is likely a transcription factor that may play a role in human reproduction. [provided by RefSeq, Dec 2012]. ##Evidence-Data-START## Transcript exon combination :: BC069529.1, AY099086.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000217999.3/ ENSP00000217999.1 RefSeq Select criteria :: based on expression ##RefSeq-Attributes-END## Transcription factor maybe involved in reproductive processes. Modulates expression of target genes encoding proteins involved in processes relevant to spermatogenesis. Does not interact with itself. Q8NHV9; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-3923409, EBI-2603996; Nucleus Ovary, testis and epididymis. Also detected in the prostate and the mammary gland. Expressed in many tumor cell lines derived from acute lymphocytic leukemia, prostate, endometrial adenocarcinoma, melanoma, bladder carcinoma, colon carcinoma, erythroleukemia and breast carcinoma. Not expressed in placenta. In testis, mainly expressed in germ cells, but also detected in somatic cells such as Sertoli cells, Leydig cells and peritubular cells (PubMed:28171660). Predominantly expressed in late stage germ cells, pachytene spermatocytes and round spermatides. By androgen. Mutagenesis of amino acids 147 to 164 and 155 to 164 lead to a major cytoplasmic localization, with only minor localization in the nucleus. Belongs to the paired-like homeobox family. PEPP subfamily. Sequence=AAC78617.1; Type=Erroneous gene model prediction; Evidence=; nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development gamete generation positive regulation of gene expression sexual reproduction intracellular steroid hormone receptor signaling pathway sequence-specific DNA binding uc004esk.1 uc004esk.2 uc004esk.3 
ENST00000218006.3 GUCY2F ENST00000218006.3 guanylate cyclase 2F, retinal (from RefSeq NM_001522.3) ENST00000218006.1 ENST00000218006.2 GUC2F GUC2F_HUMAN NM_001522 P51841 Q9UJF1 RETGC2 uc065aqx.1 uc065aqx.2 The protein encoded by this gene is a guanylyl cyclase found predominantly in photoreceptors in the retina. The encoded protein is thought to be involved in resynthesis of cGMP after light activation of the visual signal transduction cascade, allowing a return to the dark state. This protein is a single-pass type I membrane protein. Defects in this gene may be a cause of X-linked retinitis pigmentosa. [provided by RefSeq, Dec 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no transcript sequence was available to make the entire refseq consistent with the reference genome assembly. The extent of this transcript is supported by transcript alignments. ##Evidence-Data-START## Transcript exon combination :: L37378.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA2161674 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218006.3/ ENSP00000218006.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Responsible for the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors (PubMed:7777544). Plays an essential role in phototransduction, by mediating cGMP replenishment (By similarity). May also participate in the trafficking of membrane-asociated proteins to the photoreceptor outer segment membrane (By similarity). Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence=; Activated by GUCA1B when free calcium ions concentration is low, and inhibited by GUCA1B when free calcium ions concentration is high (PubMed:15772651). Inhibited by RD3 (PubMed:29515371). Homodimer (By similarity). Interacts with RD3; promotes the exit of GUCY2F from the endoplasmic reticulum and its trafficking to the photoreceptor outer segments (By similarity). Photoreceptor outer segment membrane ; Single-pass type I membrane protein Retina. Localized exclusively in the outer nuclear layer and inner segments of the rod and cone photoreceptor cells. The protein kinase domain is predicted to be catalytically inactive. There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. nucleotide binding peptide receptor activity guanylate cyclase activity protein kinase activity ATP binding GTP binding nuclear outer membrane plasma membrane integral component of plasma membrane cGMP biosynthetic process protein phosphorylation signal transduction receptor guanylyl cyclase signaling pathway visual perception cyclic nucleotide biosynthetic process membrane integral component of membrane lyase activity phosphorus-oxygen lyase activity natriuretic peptide receptor activity peptide hormone binding cGMP-mediated signaling regulation of rhodopsin mediated signaling pathway intracellular signal transduction signaling receptor activity protein homodimerization activity protein heterodimerization activity response to stimulus detection of light stimulus involved in visual perception photoreceptor disc membrane uc065aqx.1 uc065aqx.2 
ENST00000218008.8 ATP1B4 ENST00000218008.8 ATPase Na+/K+ transporting family member beta 4, transcript variant 1 (from RefSeq NM_001142447.3) AT1B4_HUMAN ENST00000218008.1 ENST00000218008.2 ENST00000218008.3 ENST00000218008.4 ENST00000218008.5 ENST00000218008.6 ENST00000218008.7 NM_001142447 Q17RR0 Q9UN41 Q9UN42 uc004esr.1 uc004esr.2 uc004esr.3 uc004esr.4 uc004esr.5 This gene has been found in all vertebrate genomes sequenced to date. However, this gene has undergone a change in function in placental mammals compared to other species. Specifically, in fish, avian, and amphibian species, this gene encodes plasma membrane-bound beta-subunits of Na,K-ATPase. In placental mammals, the encoded protein interacts with the nuclear transcriptional coregulator SKIP and may be involved in the regulation of TGF-beta signaling. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2010]. May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit. Associates with a SMAD7-transcriptional complex. Interacts with SNW1 and TOR1AIP1 (By similarity). According to PubMed:17592128, does not associate with known Na,K-ATPase alpha-subunits. Q9UN42; P07306: ASGR1; NbExp=3; IntAct=EBI-12894731, EBI-1172335; Q9UN42; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-12894731, EBI-10267100; Q9UN42; Q07325: CXCL9; NbExp=3; IntAct=EBI-12894731, EBI-3911467; Q9UN42; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-12894731, EBI-10976398; Q9UN42; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-12894731, EBI-741850; Q9UN42; O60636: TSPAN2; NbExp=3; IntAct=EBI-12894731, EBI-3914288; Q9UN42; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-12894731, EBI-10243654; Q9UN42; Q9CSN1: Snw1; Xeno; NbExp=2; IntAct=EBI-12894731, EBI-2551848; Nucleus inner membrane ; Single-pass type II membrane protein Note=Detected in nuclear envelops. Event=Alternative splicing; Named isoforms=2; Name=A; IsoId=Q9UN42-1; Sequence=Displayed; Name=B; IsoId=Q9UN42-2; Sequence=VSP_000351; Highly expressed in skeletal muscle and at a lower level in heart. Belongs to the X(+)/potassium ATPases subunit beta family. protein binding nucleus nuclear envelope nuclear inner membrane integral component of plasma membrane sodium:potassium-exchanging ATPase complex regulation of transcription, DNA-templated monovalent inorganic cation transmembrane transporter activity monovalent inorganic cation transport membrane integral component of membrane positive regulation of transcription from RNA polymerase II promoter uc004esr.1 uc004esr.2 uc004esr.3 uc004esr.4 uc004esr.5 
ENST00000218032.7 TLR8 ENST00000218032.7 toll like receptor 8, transcript variant 2 (from RefSeq NM_138636.5) B3Y654 D1CS70 D1CS76 ENST00000218032.1 ENST00000218032.2 ENST00000218032.3 ENST00000218032.4 ENST00000218032.5 ENST00000218032.6 NM_138636 Q495P4 Q6UXL6 Q9NR97 Q9NYG9 TLR8 TLR8_HUMAN UNQ249/PRO286 uc004cve.1 uc004cve.2 uc004cve.3 uc004cve.4 The protein encoded by this gene is a member of the Toll-like receptor (TLR) family which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is predominantly expressed in lung and peripheral blood leukocytes, and lies in close proximity to another family member, TLR7, on chromosome X. [provided by RefSeq, Jul 2008]. Endosomal receptor that plays a key role in innate and adaptive immunity (PubMed:25297876, PubMed:32433612). Controls host immune response against pathogens through recognition of RNA degradation products specific to microorganisms that are initially processed by RNASET2 (PubMed:31778653). Recognizes GU-rich single- stranded RNA (GU-rich RNA) derived from SARS-CoV-2, SARS-CoV-1 and HIV- 1 viruses (PubMed:33718825). Upon binding to agonists, undergoes dimerization that brings TIR domains from the two molecules into direct contact, leading to the recruitment of TIR-containing downstream adapter MYD88 through homotypic interaction (PubMed:23520111, PubMed:25599397, PubMed:26929371, PubMed:33718825). In turn, the Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3 leading to activation of downstream transcription factors NF- kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons, respectively (PubMed:16737960, PubMed:17932028, PubMed:29155428). Activated by RNAs having enough uridines. Homodimer (PubMed:23520111, PubMed:25599397, PubMed:26929371, PubMed:29155428). Interacts with MYD88 via their respective TIR domains (Probable). Interacts with UNC93B1 (By similarity). Interacts with BTK (PubMed:17932028). Interacts with SMPDL3B (By similarity). Q9NR97-1; Q9NR97-1: TLR8; NbExp=4; IntAct=EBI-16041685, EBI-16041685; Endosome membrane ; Single-pass type I membrane protein Note=Endosomal localization confers distinctive proteolytic processing. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NR97-1; Sequence=Displayed; Name=2; IsoId=Q9NR97-2; Sequence=VSP_053412; Expressed in myeloid dendritic cells, monocytes, and monocyte-derived dendritic cells. Ubiquitinated by RNF216; leading to degradation by the proteasome. Proteolytic processing occurs in monocytes and monocyte-derived macrophages by both furin-like proprotein convertase and cathepsins (PubMed:25297876). The cleavage is necessary for dimer formation and subsequent activation (PubMed:26929371). Immunodeficiency 98 with autoinflammation, X-linked (IMD98) [MIM:301078]: An X-linked disorder characterized by onset of recurrent infections associated with lymphoproliferation and autoinflammation in the first decade of life. Mostly males are affected; carrier females may have mild symptoms. Features include mouth ulcers, fever, poor early growth, hepatosplenomegaly, lymphadenopathy, polyarthritis, and non-infectious enteritis. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the Toll-like receptor family. Golgi membrane microglial cell activation regulation of protein phosphorylation toll-like receptor signaling pathway immune system process MyD88-dependent toll-like receptor signaling pathway DNA binding RNA binding double-stranded RNA binding single-stranded RNA binding transmembrane signaling receptor activity endoplasmic reticulum membrane plasma membrane inflammatory response immune response signal transduction I-kappaB kinase/NF-kappaB signaling drug binding signaling pattern recognition receptor activity response to virus external side of plasma membrane endosome membrane membrane integral component of membrane immunoglobulin mediated immune response positive regulation of interleukin-6 production toll-like receptor 8 signaling pathway toll-like receptor 9 signaling pathway endolysosome membrane signaling receptor activity identical protein binding positive regulation of interferon-gamma biosynthetic process innate immune response positive regulation of innate immune response positive regulation of interferon-alpha biosynthetic process positive regulation of interferon-beta biosynthetic process positive regulation of interleukin-8 biosynthetic process regulation of cytokine secretion positive regulation of interleukin-1 beta secretion defense response to virus cellular response to mechanical stimulus positive regulation of interleukin-6 secretion negative regulation of interleukin-12 secretion uc004cve.1 uc004cve.2 uc004cve.3 uc004cve.4 
ENST00000218068.7 PAGE4 ENST00000218068.7 PAGE family member 4, transcript variant 1 (from RefSeq NM_007003.4) B2R529 D3DX68 ENST00000218068.1 ENST00000218068.2 ENST00000218068.3 ENST00000218068.4 ENST00000218068.5 ENST00000218068.6 GAGEC1 JM27 NM_007003 O60829 PAGE4_HUMAN Q6IBI1 uc004don.1 uc004don.2 uc004don.3 uc004don.4 This gene is a member of the GAGE family. The GAGE genes are expressed in a variety of tumors and in some fetal and reproductive tissues. This gene is strongly expressed in prostate and prostate cancer. It is also expressed in other male and female reproductive tissues including testis, fallopian tube, uterus, and placenta, as well as in testicular cancer and uterine cancer. The protein encoded by this gene shares sequence similarity with other GAGE/PAGE proteins, and also belongs to a family of CT (cancer-testis) antigens. The protein may play a role in benign and malignant prostate diseases. A related pseudogene is located on chromosome 7. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]. Intrinsically disordered protein that potentiates the transcriptional activator activity of JUN (PubMed:24263171, PubMed:28289210). Protects cells from stress-induced apoptosis by inhibiting reactive oxygen species (ROS) production and via regulation of the MAPK signaling pathway (PubMed:21357425, PubMed:25374899, PubMed:30658679). Interacts with JUN. O60829; P05412: JUN; NbExp=2; IntAct=EBI-27085632, EBI-852823; Cytoplasm cleus Mitochondrion Note=Translocates to mitochondria in response to stress. Expressed at basal lvels in the adult normal prostate gland but is highly up-regulated in the fetal prostate and prostate cancer cells (PubMed:12489849, PubMed:25374899, PubMed:24559171, PubMed:24263171). Preferentially expressed in normal male and female reproductive tissues, testis, fallopian tube, uterus, and placenta, as well as in testicular cancer, uterine cancer, cervical cancer and kidney cancer (PubMed:9724777, PubMed:12489849). Highly expressed in the earlier stages of fetal development, expression decreases dramatically by the time the pre- pubertal prostate buds are developed (36 weeks). Up-regulated in response to a variety of stress factors. HIPK1-mediated phosphorylation at Thr-51 leads to the compaction of its intrinsically disordered conformation and is critical for its ability to potentiate the transcriptional activator activity of JUN inspite of a reduced interaction with JUN (PubMed:24559171, PubMed:26242913). CLK2-mediated phosphorylation at multiple Ser and Thr residues attenuates its ability to potentiate JUN transcriptional activator activity (PubMed:28289210). Belongs to the GAGE family. molecular_function DNA binding transcription coactivator activity protein binding cellular_component nucleus cytoplasm mitochondrion response to oxidative stress biological_process regulation of stress-activated MAPK cascade response to starvation negative regulation of apoptotic process negative regulation of oxidative stress-induced cell death negative regulation of reactive oxygen species biosynthetic process positive regulation of nucleic acid-templated transcription uc004don.1 uc004don.2 uc004don.3 uc004don.4 
ENST00000218075.9 GLRA2 ENST00000218075.9 glycine receptor alpha 2, transcript variant 1 (from RefSeq NM_002063.4) A8K0J6 B2R6I8 B7Z4F5 ENST00000218075.1 ENST00000218075.2 ENST00000218075.3 ENST00000218075.4 ENST00000218075.5 ENST00000218075.6 ENST00000218075.7 ENST00000218075.8 GLRA2 GLRA2_HUMAN J3KQ59 NM_002063 P23416 Q53YX7 Q6ICQ0 Q99862 uc010neq.1 uc010neq.2 uc010neq.3 uc010neq.4 uc010neq.5 The glycine receptor consists of two subunits, alpha and beta, and acts as a pentamer. The protein encoded by this gene is an alpha subunit and can bind strychnine. Several transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Jan 2010]. Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:2155780, PubMed:15302677, PubMed:16144831, PubMed:23895467, PubMed:25445488, PubMed:26370147, PubMed:34473954). Channel opening is also triggered by taurine and beta-alanine (PubMed:15302677). Plays a role in synaptic plasticity (By similarity). Contributes to the generation of inhibitory postsynaptic currents, and is involved in the down-regulation of neuronal excitability (PubMed:25445488). Plays a role in cellular responses to ethanol (PubMed:23895467). Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence= Inhibited by strychnine (PubMed:2155780, PubMed:15302677, PubMed:34473954). Inhibited by picrotoxin (PubMed:15302677). Channel activity is potentiated by 10-100 uM Zn(2+) (PubMed:15302677, PubMed:16144831, PubMed:23895467). Channel activity is marginally increased by 50 mM ethanol; it is strongly increased by a combination of 0.5 uM Zn(2+) and 50 mM ethanol (PubMed:23895467). Channel activity is inhibited by 100-1000 uM Zn(2+) (PubMed:15302677). Kinetic parameters: Note=For isoform Alpha-2* homopentamers, a concentration of about 66 uM glycine results in half-maximal channel conductance. For isoform Alpha-2B homopentamers, a concentration of about 34 uM glycine results in half-maximal channel conductance.; Homopentamer (in vitro) (PubMed:34473954). Interacts with GLRB (PubMed:16144831). Heteropentamer composed of GLRA2 and GLRB (PubMed:34473954). Both homopentamers and heteropentamers form functional ion channels, but their characteristics are subtly different (PubMed:15302677). Postsynaptic cell membrane ; Multi-pass membrane protein Synapse Cell membrane ulti-pass membrane protein Cell projection Event=Alternative splicing; Named isoforms=3; Name=Alpha-2*; IsoId=P23416-1; Sequence=Displayed; Name=Alpha-2B; IsoId=P23416-2; Sequence=VSP_000082; Name=3; IsoId=P23416-3; Sequence=VSP_045465; Intellectual developmental disorder, X-linked, syndromic, Pilorge type (MRXSP) [MIM:301076]: A disorder characterized by global developmental delay with variably impaired intellectual development, speech delay, and behavioral abnormalities. Variable features include motor incoordination, seizures, and ocular abnormalities. Disease onset is in infancy, and severity is higly variable. te=The disease is caused by variants affecting the gene represented in this entry. The alpha subunit binds strychnine. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Glycine receptor (TC 1.A.9.3) subfamily. GLRA2 sub-subfamily. transmembrane signaling receptor activity ion channel activity extracellular ligand-gated ion channel activity chloride channel activity plasma membrane integral component of plasma membrane ion transport chloride transport signal transduction neuropeptide signaling pathway chemical synaptic transmission membrane integral component of membrane glycine binding extracellular-glycine-gated chloride channel activity transmitter-gated ion channel activity glycine-gated chloride ion channel activity cell junction ion transmembrane transport chloride channel complex regulation of membrane potential cell projection neuron projection response to amino acid synapse postsynaptic membrane metal ion binding neurological system process synaptic transmission, glycinergic regulation of postsynaptic membrane potential excitatory postsynaptic potential cellular response to amino acid stimulus cellular response to zinc ion cellular response to ethanol chloride transmembrane transport transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential uc010neq.1 uc010neq.2 uc010neq.3 uc010neq.4 uc010neq.5 
ENST00000218099.7 F9 ENST00000218099.7 coagulation factor IX, transcript variant 1 (from RefSeq NM_000133.4) A8K9N4 ENST00000218099.1 ENST00000218099.2 ENST00000218099.3 ENST00000218099.4 ENST00000218099.5 ENST00000218099.6 F2RM36 FA9_HUMAN NM_000133 P00740 Q5FBE1 Q5JYJ8 uc004fas.1 uc004fas.2 uc004fas.3 This gene encodes vitamin K-dependent coagulation factor IX that circulates in the blood as an inactive zymogen. This factor is converted to an active form by factor XIa, which excises the activation peptide and thus generates a heavy chain and a light chain held together by one or more disulfide bonds. The role of this activated factor IX in the blood coagulation cascade is to activate factor X to its active form through interactions with Ca+2 ions, membrane phospholipids, and factor VIII. Alterations of this gene, including point mutations, insertions and deletions, cause factor IX deficiency, which is a recessive X-linked disorder, also called hemophilia B or Christmas disease. Alternative splicing results in multiple transcript variants encoding different isoforms that may undergo similar proteolytic processing. [provided by RefSeq, Sep 2015]. Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence= Heterodimer of a light chain and a heavy chain; disulfide- linked (PubMed:20121198, PubMed:20121197, PubMed:20080729). Interacts with SERPINC1. P00740; PRO_0000002968 [P00451]: F8; NbExp=2; IntAct=EBI-9640450, EBI-11621603; P00740; Q3U4G3: Xxylt1; Xeno; NbExp=3; IntAct=EBI-9640450, EBI-16178491; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P00740-1; Sequence=Displayed; Name=2; IsoId=P00740-2; Sequence=VSP_047689; Detected in blood plasma (at protein level) (PubMed:3857619, PubMed:8295821, PubMed:2592373, PubMed:9169594, PubMed:19846852). Synthesized primarily in the liver and secreted in plasma. Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain (PubMed:6425296). Under physiological ion concentrations, Ca(2+) is displaced by Mg(2+) from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein (By similarity). Activated by factor XIa, which excises the activation peptide (PubMed:9169594, PubMed:1730085). The propeptide can also be removed by snake venom protease (PubMed:20004170, PubMed:20080729). The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. Hemophilia B (HEMB) [MIM:306900]: An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma. te=The disease is caused by variants affecting the gene represented in this entry. Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide (PubMed:12588353, PubMed:2738071, PubMed:3009023, PubMed:8295821, PubMed:9169594, PubMed:9600455, PubMed:25251685). Mutation in position 93 (Alabama) probably fails to bind to cell membranes (PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent cleavage of the activation peptide (PubMed:6603618, PubMed:8076946, PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493). Thrombophilia, X-linked, due to factor IX defect (THPH8) [MIM:300807]: A hemostatic disorder characterized by a tendency to thrombosis. Note=The disease is caused by variants affecting the gene represented in this entry. Warfarin sensitivity, X-linked (WARFS) [MIM:301052]: A condition characterized by sensitivity to warfarin, a drugs used as anti-coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. Warfarin sensitive individuals develop bleeding complications when they are given warfarin within the therapeutic ranges. te=The disease is caused by variants affecting the gene represented in this entry. Available under the name BeneFix (Baxter and American Home Products). Used to treat hemophilia B. In 1952, one of the earliest researchers of the disease, Dr. R.G. Macfarlane used the patient's surname, Christmas, to refer to the disease and also to refer to the clotting factor which he called the 'Christmas Factor'. At the time, Stephen Christmas was a 5-year-old boy. He died in 1993 at the age of 46 from acquired immunodeficiency syndrome contracted through treatment with blood products. Belongs to the peptidase S1 family. Name=Wikipedia; Note=Factor IX entry; URL="https://en.wikipedia.org/wiki/Factor_IX"; Name=Factor IX Mutation Database; URL="http://www.factorix.org/"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/f9/"; Name=BeneFix; Note=Clinical information on BeneFix; URL="https://www.pfizer.com/products/product-detail/benefix"; Name=Protein Spotlight; Note=The Christmas Factor - Issue 41 of December 2003; URL="https://web.expasy.org/spotlight/back_issues/041"; endopeptidase activity serine-type endopeptidase activity calcium ion binding protein binding extracellular region extracellular space endoplasmic reticulum lumen Golgi lumen plasma membrane proteolysis ER to Golgi vesicle-mediated transport blood coagulation blood coagulation, intrinsic pathway hemostasis peptidase activity serine-type peptidase activity hydrolase activity zymogen activation metal ion binding extracellular exosome uc004fas.1 uc004fas.2 uc004fas.3 
ENST00000218104.6 ABCD1 ENST00000218104.6 ATP binding cassette subfamily D member 1 (from RefSeq NM_000033.4) ABCD1 ABCD1_HUMAN ALD ENST00000218104.1 ENST00000218104.2 ENST00000218104.3 ENST00000218104.4 ENST00000218104.5 NM_000033 P33897 Q6GTZ2 uc004fif.1 uc004fif.2 uc004fif.3 The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ALD subfamily, which is involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs in the organelle. All known peroxisomal ABC transporters are half transporters which require a partner half transporter molecule to form a functional homodimeric or heterodimeric transporter. This peroxisomal membrane protein is likely involved in the peroxisomal transport or catabolism of very long chain fatty acids. Defects in this gene have been identified as the underlying cause of adrenoleukodystrophy, an X-chromosome recessively inherited demyelinating disorder of the nervous system. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC025358.1, Z21876.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218104.6/ ENSP00000218104.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)- CoA from the cytosol to the peroxisome lumen (PubMed:11248239, PubMed:15682271, PubMed:16946495, PubMed:18757502, PubMed:21145416, PubMed:23671276, PubMed:29397936, PubMed:33500543). Coupled to the ATP- dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP- dependent transport into peroxisomes, the ACOT activity is essential during this transport process (PubMed:33500543, PubMed:29397936). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (PubMed:23671276, PubMed:21145416). Involved in several processes; namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance. Controls also the cellular response to oxidative stress by regulating mitochondrial functions such as mitochondrial oxidative phosphorylation and depolarization. And finally controls the inflammatory response by positively regulating peroxisomal beta-oxidation of VLCFAs (By similarity). Reaction=a very long-chain fatty acyl-CoA + H2O = a very long-chain fatty acid + CoA + H(+); Xref=Rhea:RHEA:67072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073; Evidence=; Reaction=a very long-chain fatty acid(in) + ATP + H2O = a very long- chain fatty acid(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58950, ChEBI:CHEBI:456216; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081; Evidence=; Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate; Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788; Evidence=; Reaction=ATP + H2O + tetracosanoate(in) = ADP + H(+) + phosphate + tetracosanoate(out); Xref=Rhea:RHEA:67088, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67089; Evidence=; Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate; Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792; Evidence=; Reaction=ATP + H2O + hexacosanoate(in) = ADP + H(+) + hexacosanoate(out) + phosphate; Xref=Rhea:RHEA:67084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:31013, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67085; Evidence=; Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+); Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784; Evidence=; Reaction=ATP + docosanoate(in) + H2O = ADP + docosanoate(out) + H(+) + phosphate; Xref=Rhea:RHEA:67092, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23858, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67093; Evidence=; The cysteine-reactive reagent p- chloromercuribenzoic acid (pCMB) strongly decreased the ACOT activity. The serine esterase inhibitors phenylmethylsulfonyl fluoride (PMSF), diisopropylfluorophosphate (DFP) and bis-(4-nitrophenyl)phosphate (BNPP) moderately reduced the ACOT activity. The histidine-reacting reagent diethyl pyrocarbonate (DEPC) has no effect on the ACOT activity. Can form homodimers and heterodimers with ABCD2 and ABCD3. Dimerization is necessary to form an active transporter (PubMed:17609205, PubMed:10551832) (Probable). The minimal functional unit is a homodimer but the major oligomeric form in peroxisomal membrane is a homotetramer (By similarity). Forms heterotramers with ABCD2 (By similarity). Interacts with PEX19; facilitates ABCD1 insertion into the peroxisome membrane (PubMed:10777694, PubMed:10704444). P33897; P33897: ABCD1; NbExp=2; IntAct=EBI-81045, EBI-81045; P33897; P28288: ABCD3; NbExp=2; IntAct=EBI-81045, EBI-80992; P33897; P40855: PEX19; NbExp=3; IntAct=EBI-81045, EBI-594747; P33897; P48410: Abcd1; Xeno; NbExp=2; IntAct=EBI-81045, EBI-81118; Peroxisome membrane ulti-pass membrane protein Mitochondrion membrane ; Multi-pass membrane protein. Lysosome membrane ; Multi-pass membrane protein. Endoplasmic reticulum membrane ; Multi- pass membrane protein. Up-regulated by degradation or export of cholesterol. The NH2-terminal transmembrane domaine (TMD) is involved in the recognition of substrates, and undergoes a conformational change upon ATP binding to the COOH-terminal nucleotide binding domain (NBD). Tyrosine-phosphorylated. Adrenoleukodystrophy (ALD) [MIM:300100]: A peroxisomal metabolic disorder characterized by progressive multifocal demyelination of the central nervous system and by peripheral adrenal insufficiency (Addison disease). It results in mental deterioration, corticospinal tract dysfunction, and cortical blindness. Different clinical manifestations exist like: cerebral childhood ALD (CALD), adult cerebral ALD (ACALD), adrenomyeloneuropathy (AMN) and 'Addison disease only' (ADO) phenotype. te=The disease is caused by variants affecting the gene represented in this entry. Note=The promoter region of ABCD1 is deleted in the chromosome Xq28 deletion syndrome which involves ABCD1 and the neighboring gene BCAP31. Belongs to the ABC transporter superfamily. ABCD family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily. Variants Trp-88, Cys-152, Cys-181, Ser-343, Pro-503, Arg-514 and His-554 have original been associated with ALD. However this paper was retracted due to inconsistencies in a confirmation immunoblot that could not be validated from the originally published data. Name=X-ALD gene mutation database; URL="https://adrenoleukodystrophy.info/"; Name=ABCMdb; Note=Database for mutations in ABC proteins; URL="http://abcm2.hegelab.org/search"; very long-chain fatty acid metabolic process nucleotide binding regulation of oxidative phosphorylation long-chain fatty acid transporter activity protein binding ATP binding cytoplasm mitochondrion lysosome lysosomal membrane peroxisome peroxisomal membrane integral component of peroxisomal membrane endoplasmic reticulum endoplasmic reticulum membrane cytosol fatty acid beta-oxidation peroxisome organization fatty-acyl-CoA transporter activity peroxisomal long-chain fatty acid import fatty-acyl-CoA transport peroxisomal membrane transport membrane integral component of membrane ATPase activity enzyme binding fatty acid elongation mitochondrial membrane regulation of fatty acid beta-oxidation positive regulation of fatty acid beta-oxidation fatty acid beta-oxidation using acyl-CoA oxidase alpha-linolenic acid metabolic process very long-chain fatty-acyl-CoA catabolic process ATPase activity, coupled to transmembrane movement of substances long-chain fatty acid catabolic process very long-chain fatty acid catabolic process identical protein binding protein homodimerization activity myelin maintenance ADP binding linoleic acid metabolic process perinuclear region of cytoplasm regulation of mitochondrial depolarization transmembrane transport fatty acid homeostasis sterol homeostasis negative regulation of cytokine production involved in inflammatory response regulation of cellular response to oxidative stress negative regulation of reactive oxygen species biosynthetic process neuron projection maintenance positive regulation of unsaturated fatty acid biosynthetic process uc004fif.1 uc004fif.2 uc004fif.3 
ENST00000218176.4 KCND1 ENST00000218176.4 potassium voltage-gated channel subfamily D member 1 (from RefSeq NM_004979.6) A6NEF1 B2RCG0 ENST00000218176.1 ENST00000218176.2 ENST00000218176.3 KCND1_HUMAN NM_004979 O75671 Q9NSA2 uc004dlx.1 uc004dlx.2 uc004dlx.3 This gene encodes a multipass membrane protein that comprises the pore subunit of the voltage-gated A-type potassium channel, which functions in the repolarization of membrane action potentials. Activity of voltage-gated potassium channels is important in a number of physiological processes, among them the regulation of neurotransmitter release, heart rate, insulin secretion, and smooth muscle contraction. [provided by RefSeq, Aug 2013]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC045659.1, AB021865.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218176.4/ ENSP00000218176.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits. Homotetramer or heterotetramer with KCND2 and/or KCND3. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4 (By similarity). Interacts with DPP10 (Probable). Membrane; Multi-pass membrane protein. Cell projection, dendrite Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NSA2-1; Sequence=Displayed; Name=2; IsoId=Q9NSA2-2; Sequence=VSP_057040; Widely expressed. Highly expressed in brain, in particular in cerebellum and thalamus; detected at lower levels in the other parts of the brain. The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Belongs to the potassium channel family. D (Shal) (TC 1.A.1.2) subfamily. Kv4.1/KCND1 sub-subfamily. ion channel activity voltage-gated ion channel activity voltage-gated potassium channel activity A-type (transient outward) potassium channel activity potassium channel activity cellular_component plasma membrane ion transport potassium ion transport voltage-gated potassium channel complex membrane integral component of membrane dendrite regulation of ion transmembrane transport cell projection neuronal cell body metal ion binding protein homooligomerization transmembrane transport cardiac conduction potassium ion transmembrane transport uc004dlx.1 uc004dlx.2 uc004dlx.3 
ENST00000218230.6 PCSK1N ENST00000218230.6 proprotein convertase subtilisin/kexin type 1 inhibitor (from RefSeq NM_013271.5) ENST00000218230.1 ENST00000218230.2 ENST00000218230.3 ENST00000218230.4 ENST00000218230.5 NM_013271 PCS1N_HUMAN Q4VC04 Q9UHG2 uc004dkz.1 uc004dkz.2 uc004dkz.3 uc004dkz.4 uc004dkz.5 uc004dkz.6 uc004dkz.7 The protein encoded by this gene functions as an inhibitor of prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. The proprotein is further processed into multiple short peptides. A polymorphism within this gene may be associated with obesity. [provided by RefSeq, Aug 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC094731.1, BX459856.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218230.6/ ENSP00000218230.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May function in the control of the neuroendocrine secretory pathway. Proposed be a specific endogenous inhibitor of PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal inhibitory domain, but not the further processed peptides reduce PCSK1 activity in the endoplasmic reticulum and Golgi. It reduces the activity of the 84 kDa form but not the autocatalytically derived 66 kDa form of PCSK1. Subsequent processing of proSAAS may eliminate the inhibition. Slows down convertase-mediated processing of proopiomelanocortin and proenkephalin. May control the intracellular timing of PCSK1 rather than its total level of activity (By similarity). [Big LEN]: Endogenous ligand for GPR171. Neuropeptide involved in the regulation of feeding. [PEN]: Endogenous ligand for GPR171. Neuropeptide involved in the regulation of feeding. Interacts via the C-terminal inhibitory domain with PCSK1 66 kDa form. Secreted Golgi apparatus, trans-Golgi network Note=A N-terminal processed peptide, probably Big SAAS or Little SAAS, is accumulated in cytoplasmic protein tau deposits in frontotemporal dementia and parkinsonism linked to chromosome 17 (Pick disease), Alzheimer disease and amyotrophic lateral sclerosis- parkinsonism/dementia complex 1 (Guam disease). Expressed in brain and pancreas. ProSAAS(1-180) increases secretion of enzymatically inactive PCSK1. The C-terminal inhibitory domain is involved in inhibition of PCSK1. It corresponds to the probable processing intermediate Big PEN- LEN, binds to PCSK1 in vitro and contains the hexapeptide L-L-R-V-K-R, which, as a synthetic peptide, is sufficient for PCSK1 inhibition (By similarity). [Big LEN]: The four C-terminal amino acids of Big LEN are sufficient to bind and activate GPR171. Proteolytically cleaved in the Golgi. O-glycosylated with a core 1 or possibly core 8 glycan. response to dietary excess endopeptidase inhibitor activity serine-type endopeptidase inhibitor activity receptor binding extracellular region extracellular space Golgi apparatus trans-Golgi network neuropeptide signaling pathway response to cold negative regulation of endopeptidase activity peptide hormone processing secretory granule uc004dkz.1 uc004dkz.2 uc004dkz.3 uc004dkz.4 uc004dkz.5 uc004dkz.6 uc004dkz.7 
ENST00000218249.7 RAB40AL ENST00000218249.7 RAB40A like (from RefSeq NM_001031834.1) ENST00000218249.1 ENST00000218249.2 ENST00000218249.3 ENST00000218249.4 ENST00000218249.5 ENST00000218249.6 NM_001031834 P0C0E4 Q495H3 RB40L_HUMAN RLGP uc004ejs.1 uc004ejs.2 uc004ejs.3 uc004ejs.4 uc004ejs.5 This gene encodes a member of the Rab40 subfamily of Rab small GTP-binding proteins that contains a C-terminal suppressors of cytokine signaling box. Disruptions in this gene are associated with Duchenne muscular dystrophy. [provided by RefSeq, Apr 2010]. ##Evidence-Data-START## Transcript is intronless :: BC101169.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218249.7/ ENSP00000218249.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. Membrane ; Lipid-anchor ; Cytoplasmic side Cytoplasm Mitochondrion Expressed in brain, lung, heart, skeletal muscle, kidney and liver. Highest expression in brain. Expressed in fetal brain and kidney. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. Belongs to the small GTPase superfamily. Rab family. nucleotide binding GTPase activity GTP binding cytoplasm mitochondrion endosome plasma membrane intracellular protein transport synaptic vesicle membrane protein ubiquitination Rab protein signal transduction intracellular signal transduction protein localization to plasma membrane uc004ejs.1 uc004ejs.2 uc004ejs.3 uc004ejs.4 uc004ejs.5 
ENST00000218316.4 GPR50 ENST00000218316.4 G protein-coupled receptor 50 (from RefSeq NM_004224.3) ENST00000218316.1 ENST00000218316.2 ENST00000218316.3 MTR1L_HUMAN NM_004224 Q0VGG3 Q13585 Q3ZAR0 uc010ntg.1 uc010ntg.2 uc010ntg.3 uc010ntg.4 This gene product belongs to the G-protein coupled receptor 1 family. Even though this protein shares similarity with the melatonin receptors, it does not bind melatonin, however, it inhibits melatonin receptor 1A function through heterodimerization. Polymorphic variants of this gene have been associated with bipolar affective disorder in women. [provided by RefSeq, Jan 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U52219.1, BC103696.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142680, SAMEA2149876 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218316.4/ ENSP00000218316.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## G protein-coupled receptor that plays a role in numerous physiological processes including regulation of energy metabolism, neurite outgrowth or cell migration (PubMed:19699797). Promotes self- renewal and neuronal differentiation of neural progenitor cells through activation of the NOTCH and WNT/beta-catenin signaling pathways (By similarity). Modulates the KAT5-dependent glucocorticoid receptor signaling by modulating KAT5 subcellular compartmentalisation (PubMed:21858214). Plays also a role in the activation TGFBR1 in the absence of TGFBR2 by interfering with FKBP1A binding to TGFBR1, leading to induction of both canonical and non-canonical SMAD signaling pathways resulting in inhibition of proliferation or promotion of migration (PubMed:29572483). [C-terminal domain]: Upon cleavage by CAPN1, functions as a scaffold in the nucleus for interacting partners such as GTF2I to promote FOS promoter activation. Homodimer, and heterodimer with MTNR1A and MTNR1B. Interacts with KAT5 (PubMed:21858214). Interacts with RTN4 isoform A/NOGO-A (PubMed:19699797). Interacts with TGFBR1 (PubMed:29572483). [C-terminal domain]: Interacts with GTF2I. Q13585; P04731: MT1A; NbExp=3; IntAct=EBI-8550965, EBI-8045030; Q13585; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-8550965, EBI-10172590; Cell membrane ; Multi-pass membrane protein. Postsynaptic density [C-terminal domain]: Nucleus Hypothalamus and pituitary. By TGFB. Cleaved by CAPN1 in a calcium-dependent manner. Belongs to the G-protein coupled receptor 1 family. G-protein coupled receptor activity protein binding nucleoplasm plasma membrane integral component of plasma membrane signal transduction G-protein coupled receptor signaling pathway cell-cell signaling melatonin receptor activity membrane integral component of membrane identical protein binding uc010ntg.1 uc010ntg.2 uc010ntg.3 uc010ntg.4 
ENST00000218340.4 RP2 ENST00000218340.4 RP2 activator of ARL3 GTPase (from RefSeq NM_006915.3) ENST00000218340.1 ENST00000218340.2 ENST00000218340.3 NM_006915 O75695 Q86XJ7 Q9NU67 XRP2_HUMAN uc004dgw.1 uc004dgw.2 uc004dgw.3 uc004dgw.4 uc004dgw.5 uc004dgw.6 The RP2 locus has been implicated as one cause of X-linked retinitis pigmentosa. The predicted gene product shows homology with human cofactor C, a protein involved in the ultimate step of beta-tubulin folding. Progressive retinal degeneration may therefore be due to the accumulation of incorrectly-folded photoreceptor or neuron-specific tubulin isoforms followed by progressive cell death [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC043348.2, SRR1660803.127077.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218340.4/ ENSP00000218340.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as a guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119 (or UNC119B). Interacts with ARL3; interaction is direct and stimulated with the activated GTP-bound form of ARL3. O75695; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-7996807, EBI-11339910; O75695; Q9WUL7: Arl3; Xeno; NbExp=5; IntAct=EBI-7996807, EBI-6860857; Cell membrane ipid-anchor ; Cytoplasmic side Cell projection, cilium Note=Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. Ubiquitous. Expressed in the rod and cone photoreceptors, extending from the tips of the outer segment (OS) through the inner segment (IS) and outer nuclear layer (ONL) and into the synaptic terminals of the outer plexiform layer (ONL). Also detected in the bipolar, horizontal and amacrine cells in the inner nuclear layer (INL), extending to the inner plexiform layer (IPL) and though the ganglion cell layer (GCL) and into the nerve fiber layer (NFL) (at protein level). Myristoylated on Gly-2; which may be required for membrane targeting. Palmitoylated on Cys-3; which may be required for plasma membrane targeting (Probable). Mutation of Cys-3 targets the protein to internal membranes. Retinitis pigmentosa 2 (RP2) [MIM:312600]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TBCC family. Name=Mutations of the RP2 gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/rp2mut.htm"; nucleotide binding magnesium ion binding cell morphogenesis GTPase activator activity protein binding GTP binding nucleoplasm cytoplasm Golgi apparatus centriole plasma membrane cilium protein folding post-Golgi vesicle-mediated transport visual perception protein transport membrane nuclear body cytoplasmic vesicle ciliary basal body cell projection positive regulation of GTPase activity unfolded protein binding extracellular exosome periciliary membrane compartment post-chaperonin tubulin folding pathway uc004dgw.1 uc004dgw.2 uc004dgw.3 uc004dgw.4 uc004dgw.5 uc004dgw.6 
ENST00000218364.5 HTATSF1 ENST00000218364.5 HIV-1 Tat specific factor 1, transcript variant 2 (from RefSeq NM_014500.5) D3DWG9 ENST00000218364.1 ENST00000218364.2 ENST00000218364.3 ENST00000218364.4 HTATSF1 HTSF1_HUMAN NM_014500 O43719 Q59G06 Q99730 uc004ezx.1 uc004ezx.2 uc004ezx.3 uc004ezx.4 uc004ezx.5 The protein encoded by this gene functions as a cofactor for the stimulation of transcriptional elongation by HIV-1 Tat, which binds to the HIV-1 promoter through Tat-TAR interaction. This protein may also serve as a dual-function factor to couple transcription and splicing and to facilitate their reciprocal activation. Alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Sep 2009]. Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch- site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint- interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S- phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237). (Microbial infection) In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:11780068, PubMed:9710584, PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, interacts (via UHM region) directly with SF3B1 (PubMed:30567737). Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin (PubMed:9649438, PubMed:10393184, PubMed:10454543, PubMed:10913173, PubMed:11780068). Interacts with GTF2F2/RAP30 and POLR2A (PubMed:10454543). Interacts with TCERG1/CA150 (PubMed:15485897). Interacts with (poly-ADP-ribosylated) RPA1; promoting HTATSF1 recruitment to DNA damage sites (PubMed:35597237). Interacts (when phosphorylated) with TOPBP1; promoting recruitment of TOPBP1 to DNA damage sites during S-phase (PubMed:35597237). O43719; O75533-1: SF3B1; NbExp=6; IntAct=EBI-720468, EBI-15565798; Nucleus romosome Note=Recruited to DNA damage sites during S-phase following interaction with poly-ADP-ribosylated RPA1. Widely expressed. The RRM domains mediate interaction with U snRNPs (PubMed:11780068). The RRM domains specifically bind poly-ADP- ribosylated RPA1 (PubMed:35597237). Phosphorylation at Ser-748 by CK2 during S-phase in response to DNA damage promotes interaction with TOPBP1 and double-strand break (DSB) repair via homologous recombination. Belongs to the HTATSF1 family. Sequence=AAB18823.1; Type=Frameshift; Evidence=; Sequence=BAD92540.1; Type=Erroneous initiation; Evidence=; mRNA splicing, via spliceosome nucleic acid binding RNA binding nucleus nucleoplasm U2-type spliceosomal complex U2 snRNP regulation of transcription from RNA polymerase II promoter viral genome replication regulation of DNA-templated transcription, elongation uc004ezx.1 uc004ezx.2 uc004ezx.3 uc004ezx.4 uc004ezx.5 
ENST00000218388.9 TIMP1 ENST00000218388.9 TIMP metallopeptidase inhibitor 1 (from RefSeq NM_003254.3) ENST00000218388.1 ENST00000218388.2 ENST00000218388.3 ENST00000218388.4 ENST00000218388.5 ENST00000218388.6 ENST00000218388.7 ENST00000218388.8 NM_003254 Q6FGX5 Q6FGX5_HUMAN TIMP1 hCG_29141 uc004dif.1 uc004dif.2 uc004dif.3 uc004dif.4 uc004dif.5 This gene belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. In addition to its inhibitory role against most of the known MMPs, the encoded protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC000866.1, GQ891504.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218388.9/ ENSP00000218388.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Belongs to the protease inhibitor I35 (TIMP) family. cell activation protease binding connective tissue replacement involved in inflammatory response wound healing extracellular region collagen trimer basement membrane aging metalloendopeptidase inhibitor activity response to organic substance negative regulation of endopeptidase activity extracellular matrix response to cytokine wound healing negative regulation of apoptotic process response to peptide hormone cartilage development uc004dif.1 uc004dif.2 uc004dif.3 uc004dif.4 uc004dif.5 
ENST00000218436.7 ITIH6 ENST00000218436.7 inter-alpha-trypsin inhibitor heavy chain family member 6 (from RefSeq NM_198510.3) A6NN03 ENST00000218436.1 ENST00000218436.2 ENST00000218436.3 ENST00000218436.4 ENST00000218436.5 ENST00000218436.6 ITIH5L ITIH6_HUMAN NM_198510 Q6UXX5 UNQ6369/PRO21074 uc004dtj.1 uc004dtj.2 uc004dtj.3 The protein encoded by this gene belongs to the interalpha trypsin inhibitor heavy chain (ITIH) family. Interalpha trypsin inhibitor (ITI) is composed of two heavy chains (containing VWA domain) and one light chain. The light chain confers the protease-inhibitor function, while the heavy chains are involved in mediating protein-protein interactions with the components of the extracellular matrix. [provided by RefSeq, Sep 2009]. ##Evidence-Data-START## Transcript exon combination :: AY358170.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968832, SAMEA2142853 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218436.7/ ENSP00000218436.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Q6UXX5; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-11028396, EBI-11954519; Q6UXX5; A0A024RCZ4: C6orf1; NbExp=3; IntAct=EBI-11028396, EBI-23226736; Q6UXX5; Q03828: EVX2; NbExp=3; IntAct=EBI-11028396, EBI-17280301; Q6UXX5; Q5T749: KPRP; NbExp=3; IntAct=EBI-11028396, EBI-10981970; Q6UXX5; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-11028396, EBI-12111050; Q6UXX5; O43711: TLX3; NbExp=3; IntAct=EBI-11028396, EBI-3939165; Q6UXX5; O95231: VENTX; NbExp=3; IntAct=EBI-11028396, EBI-10191303; Q6UXX5; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-11028396, EBI-744257; Secreted Belongs to the ITIH family. serine-type endopeptidase inhibitor activity extracellular region negative regulation of peptidase activity negative regulation of endopeptidase activity hyaluronan metabolic process peptidase inhibitor activity uc004dtj.1 uc004dtj.2 uc004dtj.3 
ENST00000218516.4 GLA ENST00000218516.4 galactosidase alpha, transcript variant 1 (from RefSeq NM_000169.3) ENST00000218516.1 ENST00000218516.2 ENST00000218516.3 GLA NM_000169 Q53Y83 Q53Y83_HUMAN hCG_20401 uc004ehl.1 uc004ehl.2 uc004ehl.3 This gene encodes a homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. This enzyme predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. A variety of mutations in this gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease, a rare lysosomal storage disorder that results from a failure to catabolize alpha-D-galactosyl glycolipid moieties. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK222627.1, X05790.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218516.4/ ENSP00000218516.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Homodimer. Lysosome Belongs to the glycosyl hydrolase 27 family. catalytic activity hydrolase activity, hydrolyzing O-glycosyl compounds alpha-galactosidase activity lysosome carbohydrate metabolic process metabolic process hydrolase activity hydrolase activity, acting on glycosyl bonds galactoside binding uc004ehl.1 uc004ehl.2 uc004ehl.3 
ENST00000218652.12 NDFIP2 ENST00000218652.12 Nedd4 family interacting protein 2, transcript variant 1 (from RefSeq NM_019080.3) ENST00000218652.1 ENST00000218652.10 ENST00000218652.11 ENST00000218652.2 ENST00000218652.3 ENST00000218652.4 ENST00000218652.5 ENST00000218652.6 ENST00000218652.7 ENST00000218652.8 ENST00000218652.9 KIAA1165 N4WBP5A NFIP2_HUMAN NM_019080 Q7Z2H3 Q7Z428 Q8TAR3 Q9NV92 Q9ULQ5 uc058xra.1 uc058xra.2 Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus and multivesicular body where it mediates KCNH2 degradation (PubMed:26363003). May modulate EGFR signaling. Together with NDFIP1, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (By similarity). Forms heterodimers with NDFIP1. Interacts with HECT domain- containing E3 ubiquitin-protein ligases, including NEDD4 (PubMed:12796489). Interacts with NEDD4L (PubMed:26363003). Interacts with PTEN. When phosphorylated at Tyr-167, interacts with SRC and LYN SH2 domain. May thus act as a scaffold that recruits SRC to NDFIP1, enhancing NDFIP1 phosphorylation. Interacts with SLC11A2/DMT1 (PubMed:18776082). May interact with phosphorylated EGFR. Interacts with KCNH2 (PubMed:26363003). Q9NV92; Q16637: SMN2; NbExp=3; IntAct=EBI-2933200, EBI-395421; Q9NV92; P07919: UQCRH; NbExp=3; IntAct=EBI-2933200, EBI-1224427; Endosome membrane ; Multi-pass membrane protein Golgi apparatus membrane dosome, multivesicular body membrane Expressed in brain, lung, heart, skeletal muscle, kidney, liver and placenta. By T-cell activation. The PPxY motifs are required for E3 ubiquitin-protein ligase activation and for ubiquitination. Ubiquitinated by NEDD4 and ITCH. Also ubiquitinated by NEDD4L. Ubiquitination by NEDD4 or NEDD4L does not affect turnover (By similarity). Undergoes transient tyrosine-phosphorylation following EGF stimulation, most probably catalyzed by SRC. Phosphorylation on Tyr- 151, Tyr-171 and Tyr-177 are dependent on the phosphorylation on Tyr- 167. Also phosphorylated by LYN and FYN. Sequence=AAH21988.1; Type=Erroneous initiation; Evidence=; Sequence=AAH26126.1; Type=Erroneous initiation; Evidence=; Sequence=BAA91863.1; Type=Erroneous initiation; Evidence=; Golgi membrane protein binding cytoplasm mitochondrion endosome endoplasmic reticulum Golgi apparatus ubiquitin-dependent protein catabolic process vacuolar transport endosome membrane negative regulation of gene expression membrane integral component of membrane metal ion transport positive regulation of protein ubiquitination negative regulation of transporter activity multivesicular body membrane positive regulation of I-kappaB kinase/NF-kappaB signaling intracellular membrane-bounded organelle perinuclear region of cytoplasm WW domain binding negative regulation of protein transport uc058xra.1 uc058xra.2 
ENST00000218721.1 MLNR ENST00000218721.1 motilin receptor (from RefSeq NM_001507.1) GPR38 MTLR MTLR1 MTLR_HUMAN NM_001507 O43193 uc010tgj.1 uc010tgj.2 Motilin is a 22 amino acid peptide hormone expressed throughout the gastrointestinal (GI) tract. The protein encoded by this gene is a motilin receptor which is a member of the G-protein coupled receptor 1 family. This member is a multi-pass transmembrane protein, and is an important therapeutic target for the treatment of hypomotility disorders. [provided by RefSeq, Aug 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY603964.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145240, SAMEA2145313 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000218721.1/ ENSP00000218721.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor for motilin. Cell membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=2; Name=A; IsoId=O43193-1; Sequence=Displayed; Name=B; IsoId=O43193-2; Sequence=VSP_001894; Expressed only in thyroid, stomach, and bone marrow. Belongs to the G-protein coupled receptor 1 family. G-protein coupled receptor activity plasma membrane signal transduction G-protein coupled receptor signaling pathway G-protein coupled peptide receptor activity membrane integral component of membrane hormone binding uc010tgj.1 uc010tgj.2 
ENST00000218867.4 SGCG ENST00000218867.4 sarcoglycan gamma, transcript variant 4 (from RefSeq NM_001378246.1) ENST00000218867.1 ENST00000218867.2 ENST00000218867.3 NM_001378246 Q13326 Q32M32 Q5T9J6 SGCG_HUMAN uc001uom.1 uc001uom.2 uc001uom.3 uc001uom.4 This gene encodes gamma-sarcoglycan, one of several sarcolemmal transmembrane glycoproteins that interact with dystrophin. The dystrophin-glycoprotein complex (DGC) spans the sarcolemma and is comprised of dystrophin, syntrophin, alpha- and beta-dystroglycans and sarcoglycans. The DGC provides a structural link between the subsarcolemmal cytoskeleton and the extracellular matrix of muscle cells. Defects in the encoded protein can lead to early onset autosomal recessive muscular dystrophy, in particular limb-girdle muscular dystrophy, type 2C (LGMD2C). [provided by RefSeq, Oct 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK316579.1, SRR5189655.131113.1 [ECO:0000332] ##Evidence-Data-END## Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. Interacts with the syntrophin SNTA1. Cross-link to form 2 major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The association between SGCB and SGCG is particularly strong while SGCA is loosely associated with the other sarcoglycans (By similarity). Interacts with FLNC. Q13326; O00501: CLDN5; NbExp=3; IntAct=EBI-5357343, EBI-18400628; Q13326; O75923: DYSF; NbExp=3; IntAct=EBI-5357343, EBI-2799016; Q13326; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-5357343, EBI-17498703; Cell membrane, sarcolemma ; Single- pass type II membrane protein Cytoplasm, cytoskeleton Expressed in skeletal and heart muscle. Muscular dystrophy, limb-girdle, autosomal recessive 5 (LGMDR5) [MIM:253700]: An autosomal recessive degenerative myopathy characterized by rapidly progressive muscle wasting from early childhood with loss of independent ambulation around age 12 years, dystrophic pattern on muscle biopsy, absence of gamma-sarcoglycan and normal dystrophin immunostaining. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the sarcoglycan beta/delta/gamma/zeta family. Name=Leiden Muscular Dystrophy pages; Note=SGCG mutations in LGMD2C; URL="https://www.dmd.nl/sgcg_home.html"; protein binding nucleoplasm cytoplasm cytoskeleton plasma membrane muscle organ development dystroglycan complex sarcoglycan complex membrane integral component of membrane sarcolemma cardiac muscle tissue development heart contraction uc001uom.1 uc001uom.2 uc001uom.3 uc001uom.4 
ENST00000219022.3 OLFM4 ENST00000219022.3 olfactomedin 4 (from RefSeq NM_006418.5) ENST00000219022.1 ENST00000219022.2 GW112 NM_006418 O95362 OLFM4_HUMAN Q5VWG0 Q6UX06 Q86T22 UNQ362/PRO698 uc001vhl.1 uc001vhl.2 uc001vhl.3 uc001vhl.4 uc001vhl.5 This gene was originally cloned from human myeloblasts and found to be selectively expressed in inflammed colonic epithelium. This gene encodes a member of the olfactomedin family. The encoded protein is an antiapoptotic factor that promotes tumor growth and is an extracellular matrix glycoprotein that facilitates cell adhesion. [provided by RefSeq, Mar 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY358567.1, BC117329.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219022.3/ ENSP00000219022.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin. Homomultimer; disulfide-linked. Interacts with NDUFA13. Interacts with cell surface lectins (locutions ricinus communis agglutinin I, concanavalin-A and wheat germ agglutinin) and cadherin. Q6UX06; P41181: AQP2; NbExp=3; IntAct=EBI-2804156, EBI-12701138; Q6UX06; Q92482: AQP3; NbExp=3; IntAct=EBI-2804156, EBI-2808854; Q6UX06; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-2804156, EBI-11532900; Q6UX06; O95471: CLDN7; NbExp=3; IntAct=EBI-2804156, EBI-740744; Q6UX06; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-2804156, EBI-11977093; Q6UX06; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-2804156, EBI-11989440; Q6UX06; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-2804156, EBI-11291074; Q6UX06; Q9HBJ8: CLTRN; NbExp=3; IntAct=EBI-2804156, EBI-3924906; Q6UX06; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2804156, EBI-6942903; Q6UX06; O14944: EREG; NbExp=3; IntAct=EBI-2804156, EBI-17272224; Q6UX06; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2804156, EBI-18304435; Q6UX06; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-2804156, EBI-12142257; Q6UX06; Q14626: IL11RA; NbExp=3; IntAct=EBI-2804156, EBI-13638581; Q6UX06; Q9NQX7-3: ITM2C; NbExp=3; IntAct=EBI-2804156, EBI-12811565; Q6UX06; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2804156, EBI-749265; Q6UX06; P43628: KIR2DL3; NbExp=3; IntAct=EBI-2804156, EBI-8632435; Q6UX06; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-2804156, EBI-17272405; Q6UX06; Q5T700: LDLRAD1; NbExp=7; IntAct=EBI-2804156, EBI-10173166; Q6UX06; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-2804156, EBI-17490413; Q6UX06; Q6ZUX7: LHFPL2; NbExp=3; IntAct=EBI-2804156, EBI-17566767; Q6UX06; Q9Y239: NOD1; NbExp=2; IntAct=EBI-2804156, EBI-1051262; Q6UX06; Q9HC29: NOD2; NbExp=2; IntAct=EBI-2804156, EBI-7445625; Q6UX06; P15151: PVR; NbExp=3; IntAct=EBI-2804156, EBI-3919694; Q6UX06; Q6DKI7: PVRIG; NbExp=3; IntAct=EBI-2804156, EBI-17964309; Q6UX06; Q9NXS2-3: QPCTL; NbExp=3; IntAct=EBI-2804156, EBI-13336719; Q6UX06; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-2804156, EBI-17595455; Q6UX06; A1A5C7-2: SLC22A23; NbExp=3; IntAct=EBI-2804156, EBI-12081840; Q6UX06; Q96L08: SUSD3; NbExp=3; IntAct=EBI-2804156, EBI-18194029; Q6UX06; Q8N205: SYNE4; NbExp=3; IntAct=EBI-2804156, EBI-7131783; Q6UX06; Q9UP52: TFR2; NbExp=3; IntAct=EBI-2804156, EBI-3934135; Q6UX06; Q8N3G9: TMEM130; NbExp=3; IntAct=EBI-2804156, EBI-19763514; Q6UX06; O14788: TNFSF11; NbExp=3; IntAct=EBI-2804156, EBI-7404021; Q6UX06; O43557: TNFSF14; NbExp=3; IntAct=EBI-2804156, EBI-524131; Q6UX06; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-2804156, EBI-17670824; Secreted, extracellular space. Mitochondrion. Note=Subcellular location is not clearly defined: has been shown to be secreted (PubMed:16566923), but also in the mitochondrion (PubMed:15059901, PubMed:20724538), cytoplasm and plasma membrane (PubMed:20724538) and in the nucleus (PubMed:15059901). Expressed during myeloid lineage development. Much higher expression in bone marrow neutrophils than in peripheral blood neutrophils (at protein level). Strongly expressed in the prostate, small intestine and colon and moderately expressed in the bone marrow and stomach. Overexpressed in some pancreatic cancer tissues. Elevated expression during the early S phase of the cell cycle, followed by a gradual decrease during late S phase. By retinoic acid. This induction requires functional NFKB pathway. The olfactomedin-like domain is involved in the interaction with cadherin. N-glycosylated. Sequence=AAC72970.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAC72970.1; Type=Frameshift; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/49730/OLFM4"; catalytic activity protein binding extracellular region extracellular space mitochondrion plasma membrane cell adhesion specific granule lumen specific granule protein homodimerization activity neutrophil degranulation cadherin binding perinuclear region of cytoplasm protein homooligomerization extracellular exosome positive regulation of substrate adhesion-dependent cell spreading tertiary granule lumen regulation of necrotic cell death secretory granule azurophil granule regulation of apoptotic process regulation of phagocytosis regulation of neutrophil extravasation uc001vhl.1 uc001vhl.2 uc001vhl.3 uc001vhl.4 uc001vhl.5 
ENST00000219069.6 ZNF263 ENST00000219069.6 zinc finger protein 263, transcript variant 1 (from RefSeq NM_005741.5) B2R634 ENST00000219069.1 ENST00000219069.2 ENST00000219069.3 ENST00000219069.4 ENST00000219069.5 FPM315 NM_005741 O14978 O43387 Q96H95 ZKSCAN12 ZN263_HUMAN ZNF263 uc002cuq.1 uc002cuq.2 uc002cuq.3 uc002cuq.4 uc002cuq.5 Transcription factor that binds to the consensus sequence 5'- TCCTCCC-3' and acts as a transcriptional repressor (PubMed:32051553). Binds to the promoter region of SIX3 and recruits other proteins involved in chromatin modification and transcriptional corepression, resulting in methylation of the promoter and transcriptional repression (PubMed:32051553). Acts as a transcriptional repressor of HS3ST1 and HS3ST3A1 via binding to gene promoter regions (PubMed:32277030). Interacts with a number of proteins involved in chromatin modification and transcriptional corepression including DNMT1, DNMT3A, HDAC2, PHF8, TRIM28/KAP1, SETDB1, EZH2, UHRF1, CBX3/HP1-gamma, and CBX5/HP1-alpha; recruits these proteins to the SIX3 promoter region, leading to SIX3 transcriptional repression (PubMed:32051553). Interacts with MAPK3/ERK1 and MAPK1/ERK2 (PubMed:32051553). O14978; P49760: CLK2; NbExp=3; IntAct=EBI-744493, EBI-750020; O14978; P49761: CLK3; NbExp=3; IntAct=EBI-744493, EBI-745579; O14978; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-744493, EBI-5666657; O14978; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-744493, EBI-11959863; O14978; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-744493, EBI-752007; O14978; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-744493, EBI-739832; O14978; O60437: PPL; NbExp=3; IntAct=EBI-744493, EBI-368321; O14978; P57086: SCAND1; NbExp=5; IntAct=EBI-744493, EBI-745846; O14978; Q9Y4C2: TCAF1; NbExp=3; IntAct=EBI-744493, EBI-750484; O14978; Q8WV44: TRIM41; NbExp=5; IntAct=EBI-744493, EBI-725997; O14978; P49910: ZNF165; NbExp=3; IntAct=EBI-744493, EBI-741694; O14978; P10073: ZSCAN22; NbExp=3; IntAct=EBI-744493, EBI-10178224; Nucleus Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocyte. Ubiquitinated, leading to proteasomal degradation. May be involved in the EGFR-mediated promotion of invasion and anchorage-independent growth in glioblastomas via silencing of SIX3 (PubMed:32051553). May act as a prognostic indicator in glioblastoma patients, with increased expression correlating with poor prognosis (PubMed:32051553). Belongs to the krueppel C2H2-type zinc-finger protein family. negative regulation of transcription from RNA polymerase II promoter transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated sequence-specific DNA binding negative regulation of transcription, DNA-templated metal ion binding uc002cuq.1 uc002cuq.2 uc002cuq.3 uc002cuq.4 uc002cuq.5 
ENST00000219070.9 MMP2 ENST00000219070.9 matrix metallopeptidase 2, transcript variant 1 (from RefSeq NM_004530.6) B2R6U1 B4DWH3 CLG4A E9PE45 ENST00000219070.1 ENST00000219070.2 ENST00000219070.3 ENST00000219070.4 ENST00000219070.5 ENST00000219070.6 ENST00000219070.7 ENST00000219070.8 MMP2_HUMAN NM_004530 P08253 Q9UCJ8 uc002ehz.1 uc002ehz.2 uc002ehz.3 uc002ehz.4 uc002ehz.5 uc002ehz.6 This gene is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. The protein encoded by this gene is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. This enzyme can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. This protein is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, and metastasis. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2014]. Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta- type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14. PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels. [Isoform 2]: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial- nuclear stress signaling with activation of the pro-inflammatory NF- kappaB, NFAT and IRF transcriptional pathways. Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.; EC=3.4.24.24; Evidence= Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence= Note=Binds 4 Ca(2+) ions per subunit. Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence= Note=Binds 2 Zn(2+) ions per subunit. Inhibited by histatin-3 1/24 (histatin-5). Interacts (via the C-terminal hemopexin-like domains- containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C- terminal); the interaction inhibits the degradation activity. Interacts with GSK3B. P08253; P05067: APP; NbExp=3; IntAct=EBI-1033518, EBI-77613; P08253; PRO_0000000092 [P05067]: APP; NbExp=4; IntAct=EBI-1033518, EBI-821758; P08253; PRO_0000000093 [P05067]: APP; NbExp=2; IntAct=EBI-1033518, EBI-2431589; P08253; P20908: COL5A1; NbExp=3; IntAct=EBI-1033518, EBI-2464511; P08253; Q8NBP7: PCSK9; NbExp=4; IntAct=EBI-1033518, EBI-7539251; P08253; Q04864-2: REL; NbExp=3; IntAct=EBI-1033518, EBI-10829018; P08253; Q8IX30: SCUBE3; NbExp=2; IntAct=EBI-1033518, EBI-4479975; P08253; P16035: TIMP2; NbExp=2; IntAct=EBI-1033518, EBI-1033507; [Isoform 1]: Secreted, extracellular space, extracellular matrix Membrane. Nucleus. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes. [Isoform 2]: Cytoplasm. Mitochondrion. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P08253-1; Sequence=Displayed; Name=2; IsoId=P08253-2; Sequence=VSP_044631; Name=3; IsoId=P08253-3; Sequence=VSP_045704; Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. Aspirin appears to inhibit expression. The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation- peptide release activates the enzyme. Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro. The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT- MMP3). Autocatalytic cleavage in the C-terminal produces the anti- angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3. Multicentric osteolysis, nodulosis, and arthropathy (MONA) [MIM:259600]: An autosomal recessive syndrome characterized by severe multicentric osteolysis with predominant involvement of the hands and feet. Additional features include coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. te=The disease is caused by variants affecting the gene represented in this entry. [Isoform 2]: Induced by oxidative stress. Belongs to the peptidase M10A family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41396/MMP2"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp2/"; angiogenesis response to hypoxia blood vessel maturation intramembranous ossification metalloendopeptidase activity serine-type endopeptidase activity protein binding extracellular region extracellular space nucleus cytoplasm mitochondrion plasma membrane proteolysis embryo implantation peptidase activity metallopeptidase activity zinc ion binding membrane hydrolase activity cytokine-mediated signaling pathway extracellular matrix disassembly sarcomere extracellular matrix organization collagen catabolic process extracellular matrix cellular response to reactive oxygen species endodermal cell differentiation cellular protein metabolic process metal ion binding ephrin receptor signaling pathway positive regulation of smooth muscle cell proliferation skeletal system morphogenesis tissue remodeling face morphogenesis bone trabecula formation cellular response to amino acid stimulus response to beta-amyloid positive regulation of vascular smooth muscle cell proliferation uc002ehz.1 uc002ehz.2 uc002ehz.3 uc002ehz.4 uc002ehz.5 uc002ehz.6 
ENST00000219091.9 ZNF205 ENST00000219091.9 zinc finger protein 205, transcript variant 2 (from RefSeq NM_001042428.2) A8MZK0 D3DUB4 ENST00000219091.1 ENST00000219091.2 ENST00000219091.3 ENST00000219091.4 ENST00000219091.5 ENST00000219091.6 ENST00000219091.7 ENST00000219091.8 I0J0A3 NM_001042428 O95201 Q9BU95 RHIT RHIT_HUMAN ZNF210 uc002cub.1 uc002cub.2 uc002cub.3 uc002cub.4 uc002cub.5 Transcriptional repressor involved in regulating MPV17L expression (PubMed:22306510). By regulating MPV17L expression, contributes to the regulation of genes involved in H(2)O(2) metabolism and the mitochondrial apoptotic cascade (PubMed:22306510). O95201; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-747343, EBI-5916454; O95201; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-747343, EBI-79165; O95201; Q63HR2: TNS2; NbExp=3; IntAct=EBI-747343, EBI-949753; O95201; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-747343, EBI-744794; O95201; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-747343, EBI-947187; O95201; Q9NRR5: UBQLN4; NbExp=2; IntAct=EBI-747343, EBI-711226; Nucleus Expressed in heart, skeletal muscle, pancreas and brain. Weakly expressed in placenta, lung, liver, kidney and thymus. In spleen levels are lower in adult than in fetal tissue. The KRAB domain is required for transcriptional repression. Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=AAC70007.1; Type=Erroneous initiation; Evidence=; negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding nucleic acid binding DNA binding protein binding nucleus mitochondrion regulation of transcription, DNA-templated zinc ion binding positive regulation of hydrogen peroxide biosynthetic process metal ion binding positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway uc002cub.1 uc002cub.2 uc002cub.3 uc002cub.4 uc002cub.5 
ENST00000219097.7 ORC6 ENST00000219097.7 origin recognition complex subunit 6, transcript variant 2 (from RefSeq NR_037620.2) B3KN89 ENST00000219097.1 ENST00000219097.2 ENST00000219097.3 ENST00000219097.4 ENST00000219097.5 ENST00000219097.6 NR_037620 ORC6L ORC6_HUMAN Q9Y5N6 uc002eeh.1 uc002eeh.2 uc002eeh.3 uc002eeh.4 The origin recognition complex (ORC) is a highly conserved six subunit protein complex essential for the initiation of the DNA replication in eukaryotic cells. Studies in yeast demonstrated that ORC binds specifically to origins of replication and serves as a platform for the assembly of additional initiation factors such as Cdc6 and Mcm proteins. The protein encoded by this gene is a subunit of the ORC complex. Gene silencing studies with small interfering RNA demonstrated that this protein plays an essential role in coordinating chromosome replication and segregation with cytokinesis. [provided by RefSeq, Oct 2010]. Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Does not bind histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase. Interacts with DBF4 (By similarity). Q9Y5N6; P17096: HMGA1; NbExp=4; IntAct=EBI-374840, EBI-746843; Q9Y5N6; Q969G2: LHX4; NbExp=8; IntAct=EBI-374840, EBI-2865388; Q9Y5N6; Q9UBD5: ORC3; NbExp=4; IntAct=EBI-374840, EBI-374916; Q9Y5N6; O43929: ORC4; NbExp=2; IntAct=EBI-374840, EBI-374889; Q9Y5N6; Q96R06: SPAG5; NbExp=4; IntAct=EBI-374840, EBI-413317; Nucleus. Meier-Gorlin syndrome 3 (MGORS3) [MIM:613803]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the ORC6 family. G1/S transition of mitotic cell cycle origin recognition complex fibrillar center DNA binding DNA replication origin binding protein binding nucleus nucleoplasm nuclear origin of replication recognition complex DNA replication DNA replication initiation membrane negative regulation of cell division uc002eeh.1 uc002eeh.2 uc002eeh.3 uc002eeh.4 
ENST00000219139.8 PHAF1 ENST00000219139.8 phagosome assembly factor 1, transcript variant 1 (from RefSeq NM_025187.5) C16orf6 C16orf70 ENST00000219139.1 ENST00000219139.2 ENST00000219139.3 ENST00000219139.4 ENST00000219139.5 ENST00000219139.6 ENST00000219139.7 NM_025187 PHAF1 PHAF1_HUMAN Q9BSU1 Q9HA86 uc002erd.1 uc002erd.2 uc002erd.3 uc002erd.4 uc002erd.5 Plays a regulatory role in autophagic activity. In complex with BCAS3, associates with the autophagosome formation site during both non-selective and selective autophagy. Interacts with BCAS3; the interaction is requrired for the association with the phagophore. Q9BSU1; P54252: ATXN3; NbExp=4; IntAct=EBI-946080, EBI-946046; Q9BSU1; Q9H6U6-2: BCAS3; NbExp=3; IntAct=EBI-946080, EBI-10307911; Q9BSU1; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-946080, EBI-11954144; Q9BSU1; Q68D86: CCDC102B; NbExp=5; IntAct=EBI-946080, EBI-10171570; Q9BSU1; O15442-2: MPPED1; NbExp=3; IntAct=EBI-946080, EBI-12183511; Q9BSU1; P48146: NPBWR2; NbExp=3; IntAct=EBI-946080, EBI-10210114; Q9BSU1; Q6MZQ0: PRR5L; NbExp=3; IntAct=EBI-946080, EBI-1567866; Q9BSU1; Q9H0E2: TOLLIP; NbExp=5; IntAct=EBI-946080, EBI-74615; Q9BSU1; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-946080, EBI-10687282; Cytoplasm Preautophagosomal structure Note=The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BSU1-1; Sequence=Displayed; Name=2; IsoId=Q9BSU1-2; Sequence=VSP_026623, VSP_026624, VSP_026625; Belongs to the PHAF1 family. Was originally (Ref.1) thought to be a lin-10 homolog. protein binding trans-Golgi network dendrite synaptic vesicle membrane Golgi to plasma membrane protein transport uc002erd.1 uc002erd.2 uc002erd.3 uc002erd.4 uc002erd.5 
ENST00000219150.10 CORO1A ENST00000219150.10 coronin 1A, transcript variant 2 (from RefSeq NM_007074.4) B2RBL1 COR1A_HUMAN CORO1 ENST00000219150.1 ENST00000219150.2 ENST00000219150.3 ENST00000219150.4 ENST00000219150.5 ENST00000219150.6 ENST00000219150.7 ENST00000219150.8 ENST00000219150.9 NM_007074 P31146 Q2YD73 uc002dww.1 uc002dww.2 uc002dww.3 uc002dww.4 uc002dww.5 This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. Alternative splicing results in multiple transcript variants. A related pseudogene has been defined on chromosome 16. [provided by RefSeq, Sep 2010]. May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes. Binds actin. P31146; P05067: APP; NbExp=3; IntAct=EBI-1046676, EBI-77613; P31146; A1L4K1: FSD2; NbExp=7; IntAct=EBI-1046676, EBI-5661036; P31146; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1046676, EBI-618309; P31146; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-1046676, EBI-9091197; P31146; P43364: MAGEA11; NbExp=3; IntAct=EBI-1046676, EBI-739552; P31146; P40763: STAT3; NbExp=2; IntAct=EBI-1046676, EBI-518675; Cytoplasm, cytoskeleton Cytoplasm, cell cortex Cytoplasmic vesicle, phagosome membrane Note=In non-infected macrophages, associated with the cortical microtubule network. In mycobacteria-infected macrophages, becomes progressively relocalized and retained around the mycobacterial phagosomes. Retention on the phagosomal membrane is strictly dependent on mycobacterial viability and not due to impaired acidification (By similarity). Expressed in brain, thymus, spleen, bone marrow and lymph node. Low in lung and gut. phosphorylation at Thr-412 by PKC strongly down-regulates the association with actin. Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading to proteasomal degradation. Immunodeficiency 8 with lymphoproliferation (IMD8) [MIM:615401]: A disease of the immune system leading to recurrent infections, and characterized by CD4+ T-cells lymphopenia. Patients can develop B-cell lymphoproliferation associated with Epstein-Barr virus infection. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the WD repeat coronin family. immunological synapse phagolysosome assembly phagocytic cup RNA binding actin binding actin monomer binding protein binding cytoplasm early endosome cytosol cytoskeleton actin filament plasma membrane cell-cell junction cell cortex calcium ion transport phagocytosis actin filament organization protein C-terminus binding regulation of actin polymerization or depolymerization cytoskeletal protein binding regulation of cell shape actin cytoskeleton membrane cell migration lamellipodium actin cytoskeleton organization positive regulation of cell migration axon leukocyte chemotaxis phagocytic vesicle membrane regulation of actin filament polymerization cortical actin cytoskeleton cell leading edge negative regulation of vesicle fusion cytoplasmic vesicle cell-substrate adhesion myosin heavy chain binding uropod organization regulation of actin cytoskeleton organization macromolecular complex response to cytokine nerve growth factor signaling pathway positive regulation of T cell proliferation identical protein binding protein homodimerization activity T cell homeostasis natural killer cell degranulation negative regulation of neuron apoptotic process phosphatidylinositol 3-kinase binding innate immune response synapse phagocytic vesicle homeostasis of number of cells within a tissue positive regulation of T cell activation positive chemotaxis actin filament binding negative regulation of actin nucleation regulation of release of sequestered calcium ion into cytosol early endosome to recycling endosome transport extracellular exosome cellular response to interleukin-4 glutamatergic synapse immunological synapse formation nucleus uc002dww.1 uc002dww.2 uc002dww.3 uc002dww.4 uc002dww.5 
ENST00000219162.4 MT4 ENST00000219162.4 metallothionein 4 (from RefSeq NM_032935.3) ENST00000219162.1 ENST00000219162.2 ENST00000219162.3 MT4_HUMAN NM_032935 P47944 Q14DA1 uc002eje.1 uc002eje.2 Seems to bind zinc and copper. Could play a special role in regulating zinc metabolism during the differentiation of stratified epithelia. Belongs to the metallothionein superfamily. Type 1 family. nucleus cytoplasm cellular metal ion homeostasis cellular zinc ion homeostasis biological_process detoxification of copper ion metal ion binding cellular response to cadmium ion cellular response to copper ion cellular response to zinc ion uc002eje.1 uc002eje.2 
ENST00000219169.9 NUTF2 ENST00000219169.9 nuclear transport factor 2, transcript variant 1 (from RefSeq NM_005796.3) B2R4G7 ENST00000219169.1 ENST00000219169.2 ENST00000219169.3 ENST00000219169.4 ENST00000219169.5 ENST00000219169.6 ENST00000219169.7 ENST00000219169.8 NM_005796 NTF2 NTF2_HUMAN NUTF2 P13662 P61970 Q6IB67 uc002eup.1 uc002eup.2 uc002eup.3 uc002eup.4 uc002eup.5 This gene encodes a cytosolic factor that facilitates protein transport into the nucleus. The encoded protein is required for nuclear import of the small Ras-like GTPase, Ran which is involved in numerous cellular processes. This protein also interacts with the nuclear pore complex glycoprotein p62. [provided by RefSeq, Apr 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1105906.1, SRR3476690.653232.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219169.9/ ENSP00000219169.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. Homodimer (PubMed:7744965). Interacts with RAN (GDP-bound form); the interaction is direct and regulates RAN nuclear import (PubMed:10679025). Interacts with the nucleoporins NUP54, NUP58 and NUP62 (via FG repeats); recruits NUTF2 to the nuclear pore complex a step required for NUTF2-mediated GDP-bound RAN nuclear import (PubMed:7744965). Interacts with CAPG; mediates its nuclear import (PubMed:18266911). P61970; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-591778, EBI-10181188; P61970; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-591778, EBI-10693038; P61970; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-591778, EBI-12020154; P61970; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-591778, EBI-711501; P61970; Q8NCX0-3: CCDC150; NbExp=3; IntAct=EBI-591778, EBI-12235840; P61970; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-591778, EBI-743375; P61970; Q9BY43-2: CHMP4A; NbExp=3; IntAct=EBI-591778, EBI-12178895; P61970; P12532: CKMT1B; NbExp=3; IntAct=EBI-591778, EBI-1050662; P61970; Q16740: CLPP; NbExp=3; IntAct=EBI-591778, EBI-1056029; P61970; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-591778, EBI-742802; P61970; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-591778, EBI-740641; P61970; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-591778, EBI-713401; P61970; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-591778, EBI-9089060; P61970; O43790: KRT86; NbExp=3; IntAct=EBI-591778, EBI-9996498; P61970; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-591778, EBI-11958364; P61970; Q14847-2: LASP1; NbExp=3; IntAct=EBI-591778, EBI-9088686; P61970; Q5T751: LCE1C; NbExp=3; IntAct=EBI-591778, EBI-12224199; P61970; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-591778, EBI-11955689; P61970; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-591778, EBI-726510; P61970; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-591778, EBI-2857471; P61970; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-591778, EBI-5662487; P61970; P15531: NME1; NbExp=3; IntAct=EBI-591778, EBI-741141; P61970; O00746: NME4; NbExp=3; IntAct=EBI-591778, EBI-744871; P61970; Q9NQ35: NRIP3; NbExp=3; IntAct=EBI-591778, EBI-10311735; P61970; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-591778, EBI-741048; P61970; P37198: NUP62; NbExp=7; IntAct=EBI-591778, EBI-347978; P61970; P61970: NUTF2; NbExp=3; IntAct=EBI-591778, EBI-591778; P61970; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-591778, EBI-10240813; P61970; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-591778, EBI-10302990; P61970; P12004: PCNA; NbExp=3; IntAct=EBI-591778, EBI-358311; P61970; Q01813: PFKP; NbExp=3; IntAct=EBI-591778, EBI-359022; P61970; Q9UIL8: PHF11; NbExp=3; IntAct=EBI-591778, EBI-2861403; P61970; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-591778, EBI-710402; P61970; P62826: RAN; NbExp=6; IntAct=EBI-591778, EBI-286642; P61970; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-591778, EBI-747925; P61970; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-591778, EBI-11995806; P61970; Q9C004: SPRY4; NbExp=3; IntAct=EBI-591778, EBI-354861; P61970; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-591778, EBI-12833746; P61970; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-591778, EBI-17438286; P61970; Q08117-2: TLE5; NbExp=3; IntAct=EBI-591778, EBI-11741437; P61970; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-591778, EBI-2514383; P61970; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-591778, EBI-12111538; P61970; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-591778, EBI-2682299; Cytoplasm, cytosol cleus outer membrane Nucleus, nuclear pore complex Nucleus inner membrane Nucleus, nucleoplasm Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. protein binding nucleus nuclear inner membrane nuclear outer membrane nuclear pore nucleoplasm cytoplasm cytosol protein import into nucleus protein export from nucleus nucleocytoplasmic transport Ran GTPase binding protein transport membrane structural constituent of nuclear pore nuclear membrane positive regulation of protein import into nucleus identical protein binding nuclear pore central transport channel mRNA transport nuclear import signal receptor activity extracellular exosome protein localization to nuclear pore negative regulation of vascular endothelial growth factor production uc002eup.1 uc002eup.2 uc002eup.3 uc002eup.4 uc002eup.5 
ENST00000219197.11 CBLN1 ENST00000219197.11 cerebellin 1 precursor (from RefSeq NM_004352.4) B2RAN9 CBLN1_HUMAN ENST00000219197.1 ENST00000219197.10 ENST00000219197.2 ENST00000219197.3 ENST00000219197.4 ENST00000219197.5 ENST00000219197.6 ENST00000219197.7 ENST00000219197.8 ENST00000219197.9 NM_004352 P02682 P23435 Q52M09 uc002efq.1 uc002efq.2 uc002efq.3 uc002efq.4 uc002efq.5 This gene encodes a cerebellum-specific precursor protein, precerebellin, with similarity to the globular (non-collagen-like) domain of complement component C1qB. Precerebellin is processed to give rise to several derivatives, including the hexadecapeptide, cerebellin, which is highly enriched in postsynaptic structures of Purkinje cells. Cerebellin has also been found in human and rat adrenals, where it has been shown to enhance the secretory activity of this gland. [provided by RefSeq, Aug 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1141237.1, SRR3476690.238601.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968832 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219197.11/ ENSP00000219197.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber- Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post- synaptic components. On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). NRXN1-CBLN1-GRID2 complex mediates the D- Serine-dependent long term depression signals and AMPA receptor endocytosis (PubMed:27418511). Essential for long-term maintenance but not establishment of excitatory synapses (By similarity). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (By similarity). The cerebellin peptide exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release (By similarity). Homohexamer; disulfide-linked homotrimers. The trimers associate via N-terminal cysteine residues to form disulfide-linked hexamers (PubMed:27418511). May form oligomers with CBLN2, CBLN3 AND CBLN4 prior to secretion. Once secreted, does not interact with other CBLN family members. Interacts with GRID1 (By similarity). Interacts with NRXN1 and NRXN2 long (alpha) and short (beta) isoforms produced by alternative promoter usage. Competes with NLGN1 for NRXN1-binding. Weakly interacts with NRXN3 short isoform and not at all with NRXN3 long isoform (PubMed:27418511). Interacts (via C1q domain) with GRID2; GRID2-binding is calcium-independent; CBLN1 hexamers anchor GRID2 N- terminal domain dimers to monomeric NRXN1 isoform beta; promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (PubMed:27418511). Interacts with OTOL1 (By similarity). Secreted Postsynaptic cell membrane In the Purkinje cells postsynaptic structures. In the cerebellum, cerebellin is much less abundant than [des-Ser1]- cerebellin. Low at birth, the cerebellin concentration increases between day 5 and 15, and reaches peak values between day 21 and 56. The proteolytic processing to yield cerebellin seems to occur either prior to the secretion by presynaptic neurons and subsequent oligomerization or in some other location after release of the mature protein. Sialoglycoprotein. protein binding extracellular region plasma membrane heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules chemical synaptic transmission nervous system development protein secretion membrane cerebellar granule cell differentiation cell junction protein homodimerization activity synaptic cleft synapse postsynaptic membrane positive regulation of synapse assembly negative regulation of excitatory postsynaptic potential glutamatergic synapse positive regulation of long term synaptic depression regulation of presynapse assembly uc002efq.1 uc002efq.2 uc002efq.3 uc002efq.4 uc002efq.5 
ENST00000219204.8 ARL2BP ENST00000219204.8 ADP ribosylation factor like GTPase 2 binding protein (from RefSeq NM_012106.4) AR2BP_HUMAN B3KQJ5 BART BART1 ENST00000219204.1 ENST00000219204.2 ENST00000219204.3 ENST00000219204.4 ENST00000219204.5 ENST00000219204.6 ENST00000219204.7 NM_012106 Q504R0 Q9Y2Y0 uc002elf.1 uc002elf.2 uc002elf.3 ADP-ribosylation factor (ARF)-like proteins (ARLs) comprise a functionally distinct group of the ARF family of RAS-related GTPases. The protein encoded by this gene binds to ARL2.GTP with high affinity but does not interact with ARL2.GDP, activated ARF, or RHO proteins. The lack of detectable membrane association of this protein or ARL2 upon activation of ARL2 is suggestive of actions distinct from those of the ARFs. This protein is considered to be the first ARL2-specific effector identified, due to its interaction with ARL2.GTP but lack of ARL2 GTPase-activating protein activity. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660803.49844.1, SRR3476690.1049778.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219204.8/ ENSP00000219204.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2. Found in a complex with ARL2BP, ARL2 and SLC25A6. Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4. Interacts with GTP-bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to SLC25A4. Interaction with ARL2 may be required for targeting to cilia basal body. Interacts with STAT3; interaction is enhanced with ARL2. Q9Y2Y0; P36404: ARL2; NbExp=24; IntAct=EBI-3449344, EBI-752365; Q9Y2Y0; P36405: ARL3; NbExp=6; IntAct=EBI-3449344, EBI-712710; Q9Y2Y0; P46379-2: BAG6; NbExp=3; IntAct=EBI-3449344, EBI-10988864; Q9Y2Y0; Q9Y6A4: CFAP20; NbExp=4; IntAct=EBI-3449344, EBI-1046872; Q9Y2Y0; P22607: FGFR3; NbExp=3; IntAct=EBI-3449344, EBI-348399; Q9Y2Y0; P06396: GSN; NbExp=3; IntAct=EBI-3449344, EBI-351506; Q9Y2Y0; O14901: KLF11; NbExp=3; IntAct=EBI-3449344, EBI-948266; Q9Y2Y0; P17987: TCP1; NbExp=3; IntAct=EBI-3449344, EBI-356553; Q9Y2Y0; Q9Y649; NbExp=3; IntAct=EBI-3449344, EBI-25900580; Cytoplasm. Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, cilium basal body. Note=The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y2Y0-1; Sequence=Displayed; Name=2; IsoId=Q9Y2Y0-2; Sequence=VSP_025317, VSP_025318; Expressed in retina pigment epithelial cells (at protein level). Widely expressed. Retinitis pigmentosa 82 with or without situs inversus (RP82) [MIM:615434]: An autosomal recessive disorder characterized by variable association of retinitis pigmentosa with situs inversus. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Situs inversus is a congenital abnormality in which organs in the thorax and the abdomen are opposite to their normal positions due to lateral transposition. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the ARL2BP family. transcription coactivator activity protein binding nucleus cytoplasm mitochondrion mitochondrial intermembrane space mitochondrial matrix centrosome microtubule organizing center spindle cytosol cytoskeleton cilium signal transduction midbody GTPase regulator activity positive regulation of tyrosine phosphorylation of STAT protein cell projection regulation of catalytic activity regulation of insulin secretion maintenance of protein location in nucleus positive regulation of nucleic acid-templated transcription uc002elf.1 uc002elf.2 uc002elf.3 
ENST00000219207.10 PLLP ENST00000219207.10 plasmolipin (from RefSeq NM_015993.3) B2R9T6 ENST00000219207.1 ENST00000219207.2 ENST00000219207.3 ENST00000219207.4 ENST00000219207.5 ENST00000219207.6 ENST00000219207.7 ENST00000219207.8 ENST00000219207.9 NM_015993 PLLP_HUMAN PMLP Q9Y342 TM4SF11 uc002elg.1 uc002elg.2 uc002elg.3 uc002elg.4 Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective (By similarity). Hexamer arranged as a trimer of two plasmolipin subunits. Q9Y342; Q13520: AQP6; NbExp=3; IntAct=EBI-3919291, EBI-13059134; Q9Y342; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-3919291, EBI-747430; Q9Y342; Q6UWJ8-2: CD164L2; NbExp=3; IntAct=EBI-3919291, EBI-13362802; Q9Y342; O95500: CLDN14; NbExp=3; IntAct=EBI-3919291, EBI-11742599; Q9Y342; Q2HXU8-2: CLEC12B; NbExp=3; IntAct=EBI-3919291, EBI-12811991; Q9Y342; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-3919291, EBI-11749983; Q9Y342; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-3919291, EBI-17233035; Q9Y342; A8MQ03: CYSRT1; NbExp=4; IntAct=EBI-3919291, EBI-3867333; Q9Y342; Q15125: EBP; NbExp=3; IntAct=EBI-3919291, EBI-3915253; Q9Y342; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-3919291, EBI-18535450; Q9Y342; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3919291, EBI-781551; Q9Y342; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-3919291, EBI-18636064; Q9Y342; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-3919291, EBI-12142257; Q9Y342; O43559: FRS3; NbExp=3; IntAct=EBI-3919291, EBI-725515; Q9Y342; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-3919291, EBI-17231387; Q9Y342; Q8TED1: GPX8; NbExp=3; IntAct=EBI-3919291, EBI-11721746; Q9Y342; P28799: GRN; NbExp=3; IntAct=EBI-3919291, EBI-747754; Q9Y342; P49639: HOXA1; NbExp=3; IntAct=EBI-3919291, EBI-740785; Q9Y342; P48051: KCNJ6; NbExp=3; IntAct=EBI-3919291, EBI-12017638; Q9Y342; O76011: KRT34; NbExp=3; IntAct=EBI-3919291, EBI-1047093; Q9Y342; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-3919291, EBI-1044640; Q9Y342; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-3919291, EBI-2820517; Q9Y342; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-3919291, EBI-11956541; Q9Y342; Q9NXJ0: MS4A12; NbExp=6; IntAct=EBI-3919291, EBI-10227644; Q9Y342; Q9H813: PACC1; NbExp=3; IntAct=EBI-3919291, EBI-4319734; Q9Y342; O15173: PGRMC2; NbExp=3; IntAct=EBI-3919291, EBI-1050125; Q9Y342; Q9H9V4: RNF122; NbExp=3; IntAct=EBI-3919291, EBI-2129998; Q9Y342; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-3919291, EBI-3920694; Q9Y342; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3919291, EBI-18159983; Q9Y342; Q86WV6: STING1; NbExp=3; IntAct=EBI-3919291, EBI-2800345; Q9Y342; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-3919291, EBI-18196631; Q9Y342; Q495A1: TIGIT; NbExp=3; IntAct=EBI-3919291, EBI-4314807; Q9Y342; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3919291, EBI-8638294; Q9Y342; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-3919291, EBI-17684533; Q9Y342; Q8WUU8: TMEM174; NbExp=3; IntAct=EBI-3919291, EBI-10276729; Q9Y342; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-3919291, EBI-11724433; Q9Y342; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-3919291, EBI-12345267; Q9Y342; O43557: TNFSF14; NbExp=3; IntAct=EBI-3919291, EBI-524131; Q9Y342; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-3919291, EBI-10262539; Q9Y342; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-3919291, EBI-1055364; Q9Y342; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-3919291, EBI-12837904; Membrane; Multi-pass membrane protein. Belongs to the MAL family. protein binding ion transport response to wounding membrane integral component of membrane structural constituent of myelin sheath myelination compact myelin membrane raft uc002elg.1 uc002elg.2 uc002elg.3 uc002elg.4 
ENST00000219235.5 CCL22 ENST00000219235.5 C-C motif chemokine ligand 22 (from RefSeq NM_002990.5) A-152E5.1 A0N0Q6 B2R4W2 CCL22_HUMAN ENST00000219235.1 ENST00000219235.2 ENST00000219235.3 ENST00000219235.4 MDC NM_002990 O00626 SCYA22 uc002elh.1 uc002elh.2 uc002elh.3 uc002elh.4 uc002elh.5 This antimicrobial gene is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity for monocytes, dendritic cells, natural killer cells and for chronically activated T lymphocytes. It also displays a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. The product of this gene binds to chemokine receptor CCR4. This chemokine may play a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. [provided by RefSeq, Sep 2014]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.47952.1, U83171.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219235.5/ ENSP00000219235.4 Protein has antimicrobial activity :: PMID: 12949249 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May play a role in the trafficking of activated/effector T- lymphocytes to inflammatory sites and other aspects of activated T- lymphocyte physiology. Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T- lymphocytes and a potent chemoattractant for chronically activated T- lymphocytes but has no chemoattractant activity for neutrophils, eosinophils, and resting T-lymphocytes. Binds to CCR4. Processed forms MDC(3-69), MDC(5-69) and MDC(7-69) seem not be active. O00626; Q13520: AQP6; NbExp=3; IntAct=EBI-3907871, EBI-13059134; Secreted. Highly expressed in macrophage and in monocyte- derived dendritic cells, and thymus. Also found in lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression in lung and spleen. Very weak expression in small intestine. In lymph node expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+). Expressed in Langerhans' cell histiocytosis but not in dermatopathic lymphadenopathy. Expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. The N-terminal processed forms MDC(3-69), MDC(5-69) and MDC(7-69) are produced by proteolytic cleavage after secretion from monocyte derived dendrocytes. Belongs to the intercrine beta (chemokine CC) family. Name=Wikipedia; Note=CCL22 entry; URL="https://en.wikipedia.org/wiki/CCL22"; monocyte chemotaxis cytokine activity extracellular region extracellular space chemotaxis inflammatory response immune response signal transduction G-protein coupled receptor signaling pathway cell-cell signaling chemokine activity response to virus cytokine-mediated signaling pathway neutrophil chemotaxis killing of cells of other organism positive regulation of GTPase activity CCR chemokine receptor binding lymphocyte chemotaxis cell chemotaxis chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor uc002elh.1 uc002elh.2 uc002elh.3 uc002elh.4 uc002elh.5 
ENST00000219240.9 DHODH ENST00000219240.9 dihydroorotate dehydrogenase (quinone) (from RefSeq NM_001361.5) A8K8C8 ENST00000219240.1 ENST00000219240.2 ENST00000219240.3 ENST00000219240.4 ENST00000219240.5 ENST00000219240.6 ENST00000219240.7 ENST00000219240.8 NM_001361 PYRD_HUMAN Q02127 Q6P176 uc002fbp.1 uc002fbp.2 uc002fbp.3 uc002fbp.4 uc002fbp.5 The protein encoded by this gene catalyzes the fourth enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate, in de novo pyrimidine biosynthesis. This protein is a mitochondrial protein located on the outer surface of the inner mitochondrial membrane. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803616.136604.1, SRR1803617.224526.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000219240.9/ ENSP00000219240.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway. Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence=; Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence=; Note=Binds 1 FMN per subunit. ; Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. Monomer. Q02127; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-3928775, EBI-2466594; Q02127; P49638: TTPA; NbExp=3; IntAct=EBI-3928775, EBI-10210710; Mitochondrion inner membrane ; Single-pass membrane protein The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration. Postaxial acrofacial dysostosis (POADS) [MIM:263750]: POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases. Note=The disease is caused by variants affecting the gene represented in this entry. The identification of DHODH defects as the cause of postaxial acrofacial dysostosis (POADS) was obtained via exome sequencing (PubMed:19915526), demonstrating that this method is a powerful tool for identifying genes underlying rare Mendelian disorders. Exome sequencing consists of targeted resequencing of all protein-coding subsequences, which requires around 5% as much sequencing as a whole human genome. Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. catalytic activity dihydroorotate dehydrogenase activity nucleoplasm cytoplasm mitochondrion mitochondrial inner membrane cytosol 'de novo' pyrimidine nucleobase biosynthetic process pyrimidine nucleotide biosynthetic process female pregnancy lactation drug binding pyrimidine ribonucleotide biosynthetic process FMN binding response to organic cyclic compound membrane integral component of membrane oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors response to caffeine response to drug response to starvation neuronal cell body positive regulation of apoptotic process 'de novo' UMP biosynthetic process pyrimidine nucleoside biosynthetic process ubiquinone binding oxidation-reduction process regulation of mitochondrial fission response to L-arginine uc002fbp.1 uc002fbp.2 uc002fbp.3 uc002fbp.4 uc002fbp.5 
ENST00000219244.9 CCL17 ENST00000219244.9 C-C motif chemokine ligand 17 (from RefSeq NM_002987.3) A0N0Q9 CCL17_HUMAN ENST00000219244.1 ENST00000219244.2 ENST00000219244.3 ENST00000219244.4 ENST00000219244.5 ENST00000219244.6 ENST00000219244.7 ENST00000219244.8 NM_002987 Q2M287 Q92583 SCYA17 TARC uc002elj.1 uc002elj.2 This antimicrobial gene is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity for T lymphocytes, but not monocytes or granulocytes. The product of this gene binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells. [provided by RefSeq, Sep 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC069107.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2144335, SAMEA2156670 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## CDS uses downstream in-frame AUG :: upstream AUG and CDS extension is not conserved MANE Ensembl match :: ENST00000219244.9/ ENSP00000219244.4 Protein has antimicrobial activity :: PMID: 12949249 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Chemokine, which displays chemotactic activity for T lymphocytes, preferentially Th2 cells, but not monocytes or granulocytes. Therefore plays an important role in a wide range of inflammatory and immunological processes (PubMed:8702936, PubMed:9169480). Acts by binding to CCR4 at T-cell surface (PubMed:9169480, PubMed:10540332). Mediates GM-CSF/CSF2-driven pain and inflammation (PubMed:27525438). In the brain, required to maintain the typical, highly branched morphology of hippocampal microglia under homeostatic conditions. May be important for the appropriate adaptation of microglial morphology and synaptic plasticity to acute lipopolysaccharide (LPS)-induced neuroinflammation (By similarity). Plays a role in wound healing, mainly by inducing fibroblast migration into the wound (By similarity). Q92583; O00585: CCL21; NbExp=2; IntAct=EBI-16640146, EBI-953695; Q92583; O15444: CCL25; NbExp=2; IntAct=EBI-16640146, EBI-7783341; Q92583; Q9Y258: CCL26; NbExp=2; IntAct=EBI-16640146, EBI-7783416; Q92583; Q9NRJ3: CCL28; NbExp=3; IntAct=EBI-16640146, EBI-7783254; Q92583; P13501: CCL5; NbExp=9; IntAct=EBI-16640146, EBI-2848366; Q92583; PRO_0000005175 [P13501]: CCL5; NbExp=6; IntAct=EBI-16640146, EBI-11712923; Q92583; P51679: CCR4; NbExp=2; IntAct=EBI-16640146, EBI-7847466; Q92583; P51681: CCR5; NbExp=2; IntAct=EBI-16640146, EBI-489374; Q92583; P02776: PF4; NbExp=2; IntAct=EBI-16640146, EBI-2565740; Secreted Constitutively expressed in thymus. Detected at lower levels in the lung, colon and small intestine (PubMed:8702936). Expressed in stimulated peripheral blood mononuclear cells, but not in resting cells (PubMed:8702936). In monocytes, up-regulated by IL4 and by GM-CSF/CSF2 in an IRF4-dependent manner (at protein level). Belongs to the intercrine beta (chemokine CC) family. Although CCL17 was shown to bind to CCR8, additional studies demonstrated that CCR4, not CCR8, was the bona fide CCL17 receptor. Was originally thought to be a ligand for CCR8. Name=Wikipedia; Note=CCL17 entry; URL="https://en.wikipedia.org/wiki/CCL17"; monocyte chemotaxis receptor binding cytokine activity protein binding extracellular region extracellular space chemotaxis inflammatory response immune response G-protein coupled receptor signaling pathway cell-cell signaling multicellular organism development chemokine activity neutrophil chemotaxis killing of cells of other organism CCR4 chemokine receptor binding positive regulation of GTPase activity negative regulation of myoblast differentiation CCR chemokine receptor binding lymphocyte chemotaxis chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor uc002elj.1 uc002elj.2 
ENST00000219252.10 POLR2C ENST00000219252.10 RNA polymerase II subunit C (from RefSeq NM_032940.3) ENST00000219252.1 ENST00000219252.2 ENST00000219252.3 ENST00000219252.4 ENST00000219252.5 ENST00000219252.6 ENST00000219252.7 ENST00000219252.8 ENST00000219252.9 NM_032940 POLR2C Q6FGR6 Q6FGR6_HUMAN hCG_2025883 uc002elt.1 uc002elt.2 uc002elt.3 This gene encodes the third largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, POLR2J. These two subunits form a core subassembly unit of the polymerase. A pseudogene has been identified on chromosome 21. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC003159.1, SRR3476690.801283.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219252.10/ ENSP00000219252.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family. DNA binding DNA-directed 5'-3' RNA polymerase activity nucleus nucleoplasm cytoplasm cytosol transcription, DNA-templated microtubule cytoskeleton protein dimerization activity uc002elt.1 uc002elt.2 uc002elt.3 
ENST00000219271.4 MMP15 ENST00000219271.4 matrix metallopeptidase 15 (from RefSeq NM_002428.4) A0A2U6 ENST00000219271.1 ENST00000219271.2 ENST00000219271.3 MMP15_HUMAN NM_002428 P51511 Q14111 uc002ena.1 uc002ena.2 uc002ena.3 uc002ena.4 uc002ena.5 This gene encodes a member of the peptidase M10 family and membrane-type subfamily of matrix metalloproteinases (MMPs). Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Members of this subfamily contain a transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. The encoded preproprotein is proteolytically processed to generate the mature protease. This protein may play a role in cancer progression. [provided by RefSeq, Jan 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC036495.1, Z48482.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219271.4/ ENSP00000219271.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; P51511; P04070: PROC; NbExp=2; IntAct=EBI-1383043, EBI-1383018; Membrane ; Single-pass type I membrane protein ; Extracellular side Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle. The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation- peptide release activates the enzyme. The precursor is cleaved by a furin endopeptidase. Belongs to the peptidase M10A family. Sequence=BAA13071.1; Type=Erroneous initiation; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp15/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41392/MMP15"; metalloendopeptidase activity protein binding extracellular space plasma membrane integral component of plasma membrane cellular protein modification process proteolysis enzyme activator activity peptidase activity metallopeptidase activity zinc ion binding membrane integral component of membrane hydrolase activity extracellular matrix disassembly extracellular matrix organization collagen catabolic process extracellular matrix response to estradiol endodermal cell differentiation positive regulation of catalytic activity metal ion binding metalloaminopeptidase activity uc002ena.1 uc002ena.2 uc002ena.3 uc002ena.4 uc002ena.5 
ENST00000219281.8 USB1 ENST00000219281.8 U6 snRNA biogenesis phosphodiesterase 1, transcript variant 1 (from RefSeq NM_024598.4) B4DWE3 B4DZW5 C16orf57 ENST00000219281.1 ENST00000219281.2 ENST00000219281.3 ENST00000219281.4 ENST00000219281.5 ENST00000219281.6 ENST00000219281.7 Mpn1 NM_024598 Q96FZ9 Q9BQ65 Q9H8X8 USB1 USB1_HUMAN uc002emz.1 uc002emz.2 uc002emz.3 uc002emz.4 uc002emz.5 This gene encodes a protein with several conserved domains, however, its exact function is not known. Mutations in this gene are associated with poikiloderma with neutropenia (PN), which shows phenotypic overlap with Rothmund-Thomson syndrome (RTS) caused by mutations in the RECQL4 gene. It is believed that this gene product interacts with RECQL4 protein via SMAD4 proteins, explaining the partial clinical overlap between PN and RTS. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene. [provided by RefSeq, Mar 2011]. 3'-5' RNA exonuclease that trims the 3' end of oligo(U) and oligo(A) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate (PubMed:23022480, PubMed:22899009, PubMed:26213367, PubMed:31832688, PubMed:23190533, PubMed:28887445, PubMed:30215753). Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation (PubMed:23022480, PubMed:22899009, PubMed:26213367, PubMed:31832688, PubMed:23190533, PubMed:28887445, PubMed:30215753). In addition also removes uridines from the 3' end of U6atac snRNA and possibly the vault RNA VTRNA1-1 (PubMed:26213367). Reaction=a 3'-end uridylyl-uridine-RNA = a 3'-end 2',3'-cyclophospho- uridine-RNA + uridine; Xref=Rhea:RHEA:46052, Rhea:RHEA-COMP:17384, Rhea:RHEA-COMP:17385, ChEBI:CHEBI:16704, ChEBI:CHEBI:85643, ChEBI:CHEBI:85644; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46053; Evidence=; Reaction=a 3'-end uridylyl-adenosine-RNA = a 3'-end 2',3'-cyclophospho- uridine-RNA + adenosine; Xref=Rhea:RHEA:67896, Rhea:RHEA-COMP:17385, Rhea:RHEA-COMP:17386, ChEBI:CHEBI:16335, ChEBI:CHEBI:85644, ChEBI:CHEBI:176518; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67897; Evidence=; 3'-5' RNA exonuclease activity is inhibited by a 3' phosphate terminated RNA. Kinetic parameters: KM=7.58 uM for UAUUUdUUU ; KM=9.75 uM for UAUUUdUAU ; KM=3.12 uM for UAUUUdUAU ; KM=7.17 uM for UAUUUdUAA ; pH dependence: Optimum pH is 7.5. Interacts with PLRG1, CDC5L and PRPF19. Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9BQ65-1; Sequence=Displayed; Name=2; IsoId=Q9BQ65-2; Sequence=VSP_042878; Name=3; IsoId=Q9BQ65-3; Sequence=VSP_042936; Poikiloderma with neutropenia (PN) [MIM:604173]: A genodermatosis characterized by poikiloderma, pachyonychia and chronic neutropenia. The disorder starts as a papular erythematous rash on the limbs during the first year of life. It gradually spreads centripetally and, as the papular rash resolves, hypo- and hyperpigmentation result, with development of telangiectasias. Another skin manifestation is pachyonychia, but alopecia and leukoplakia are distinctively absent. Patients have recurrent pneumonias that usually result in reactive airway disease and/or chronic cough. One of the most important extracutaneous symptoms is an increased susceptibility to infections, mainly affecting the respiratory system, primarily due to a chronic neutropenia and to neutrophil functional defects. Bone marrow abnormalities account for neutropenia and may evolve into myelodysplasia associated with the risk of leukemic transformation. Poikiloderma with neutropenia shows phenotypic overlap with Rothmund- Thomson syndrome. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the 2H phosphoesterase superfamily. USB1 family. 3'-5'-exoribonuclease activity nuclease activity nucleus RNA splicing hydrolase activity U6 snRNA 3'-end processing intercellular bridge nucleic acid phosphodiester bond hydrolysis RNA phosphodiester bond hydrolysis, exonucleolytic poly(U)-specific exoribonuclease activity, producing 3' uridine cyclic phosphate ends uc002emz.1 uc002emz.2 uc002emz.3 uc002emz.4 uc002emz.5 
ENST00000219299.8 CFAP263 ENST00000219299.8 coiled-coil domain containing 113, transcript variant 1 (from RefSeq NM_014157.4) B2RAQ7 B4DR20 CC113_HUMAN CCDC113 ENST00000219299.1 ENST00000219299.2 ENST00000219299.3 ENST00000219299.4 ENST00000219299.5 ENST00000219299.6 ENST00000219299.7 HSPC065 NM_014157 Q9H0I3 Q9NZX2 uc002ene.1 uc002ene.2 uc002ene.3 uc002ene.4 Component of centriolar satellites contributing to primary cilium formation. Interacts with HAP1 and PCM1. Q9H0I3; O75031: HSF2BP; NbExp=3; IntAct=EBI-715690, EBI-7116203; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Note=Colocalized with HAP1 at centriolar satellites. Centriolar satellite localization requires PCM1. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H0I3-1; Sequence=Displayed; Name=2; IsoId=Q9H0I3-2; Sequence=VSP_042753; Sequence=AAF29037.1; Type=Frameshift; Evidence=; protein binding nucleoplasm cytoplasm microtubule organizing center cytosol cytoskeleton cell projection organization macromolecular complex centriolar satellite cilium assembly uc002ene.1 uc002ene.2 uc002ene.3 uc002ene.4 
ENST00000219302.8 NME3 ENST00000219302.8 NME/NM23 nucleoside diphosphate kinase 3 (from RefSeq NM_002513.3) ENST00000219302.1 ENST00000219302.2 ENST00000219302.3 ENST00000219302.4 ENST00000219302.5 ENST00000219302.6 ENST00000219302.7 NDK3_HUMAN NM_002513 Q13232 Q9BWH4 uc002cmm.1 uc002cmm.2 uc002cmm.3 uc002cmm.4 uc002cmm.5 Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis. Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Q13232; Q6ICB0: DESI1; NbExp=6; IntAct=EBI-713684, EBI-2806959; Q13232; P15531: NME1; NbExp=5; IntAct=EBI-713684, EBI-741141; Q13232; O43765: SGTA; NbExp=12; IntAct=EBI-713684, EBI-347996; Q13232; Q96EQ0: SGTB; NbExp=5; IntAct=EBI-713684, EBI-744081; Q13232; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-713684, EBI-741480; Q13232; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-713684, EBI-10173939; Q13232; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-713684, EBI-947187; Preferentially expressed at early stages of myeloid differentiation of highly purified CD34+ cells. Belongs to the NDK family. nucleotide binding nucleoside diphosphate kinase activity protein binding ATP binding cytosol purine nucleotide metabolic process nucleoside diphosphate phosphorylation GTP biosynthetic process pyrimidine nucleotide metabolic process UTP biosynthetic process CTP biosynthetic process apoptotic process nucleotide metabolic process nucleobase-containing small molecule interconversion kinase activity phosphorylation transferase activity metal ion binding uc002cmm.1 uc002cmm.2 uc002cmm.3 uc002cmm.4 uc002cmm.5 
ENST00000219313.9 PSMD7 ENST00000219313.9 proteasome 26S subunit, non-ATPase 7 (from RefSeq NM_002811.5) D3DWS9 ENST00000219313.1 ENST00000219313.2 ENST00000219313.3 ENST00000219313.4 ENST00000219313.5 ENST00000219313.6 ENST00000219313.7 ENST00000219313.8 MOV34L NM_002811 P51665 PSMD7_HUMAN Q6PKI2 Q96E97 uc002fcq.1 uc002fcq.2 uc002fcq.3 uc002fcq.4 The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 17. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1146516.1, SRR3476690.1155915.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219313.9/ ENSP00000219313.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD7, a base containing 6 ATPases and few additional components (PubMed:27428775, PubMed:27342858). Within the complex, PSMD7 interacts with subunit PSMD4 through their respective MPN domain. Interacts with TRIM5 (PubMed:22078707). P51665; P54252: ATXN3; NbExp=9; IntAct=EBI-357659, EBI-946046; P51665; P42858: HTT; NbExp=10; IntAct=EBI-357659, EBI-466029; P51665; O00487: PSMD14; NbExp=14; IntAct=EBI-357659, EBI-722193; Does not bind a metal ion. Belongs to the peptidase M67A family. Sequence=AAH00338.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; MAPK cascade protein polyubiquitination proteasome complex stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent protein binding extracellular region nucleus nucleoplasm cytosol proteasome regulatory particle regulation of cellular amino acid metabolic process negative regulation of G2/M transition of mitotic cell cycle membrane protein deubiquitination anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway secretory granule lumen NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway protein homodimerization activity proteasome-mediated ubiquitin-dependent protein catabolic process neutrophil degranulation regulation of mRNA stability post-translational protein modification T cell receptor signaling pathway transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia extracellular exosome interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation ficolin-1-rich granule lumen uc002fcq.1 uc002fcq.2 uc002fcq.3 uc002fcq.4 
ENST00000219315.9 SETD6 ENST00000219315.9 SET domain containing 6, protein lysine methyltransferase, transcript variant 1 (from RefSeq NM_001160305.4) A8K380 B5ME38 ENST00000219315.1 ENST00000219315.2 ENST00000219315.3 ENST00000219315.4 ENST00000219315.5 ENST00000219315.6 ENST00000219315.7 ENST00000219315.8 NM_001160305 Q8TBK2 Q9H787 SETD6 SETD6_HUMAN uc002ens.1 uc002ens.2 uc002ens.3 uc002ens.4 uc002ens.5 This gene encodes a methyltransferase that adds a methyl group to the histone H2AZ, which is involved in nuclear receptor-dependent transcription. The protein also interacts with several endogenous proteins which are involved in nuclear hormone receptor signaling. A related pseudogene is located on chromosome 2. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]. Protein-lysine N-methyltransferase. Monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulation of NF-kappa-B transcription factor activity (PubMed:21131967, PubMed:30189201, PubMed:21515635). Monomethylates 'Lys-8' of H2AZ (H2AZK8me1) (PubMed:23324626). Required for the maintenance of embryonic stem cell self-renewal (By similarity). Methylates PAK4. Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)- methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737; Evidence= Reaction=L-lysyl(8)-[histone H2AZ] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(8)-[histone H2AZ] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67808, Rhea:RHEA-COMP:17357, Rhea:RHEA-COMP:17358, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67809; Evidence=; Activated by automethylation. pH dependence: Optimum pH is 10. ; Monomer, homodimer and homotrimer; these structures are stabilized in the presence of S-adenosyl-L-methionine (SAM). Q8TBK2; Q04207: Rela; Xeno; NbExp=4; IntAct=EBI-3863032, EBI-644400; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8TBK2-1; Sequence=Displayed; Name=2; IsoId=Q8TBK2-2; Sequence=VSP_024093; Automethylated; Lys-39 and Lys-179 serve as the major automethylation sites. Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SETD6 subfamily. protein binding nucleus nucleoplasm cytosol methyltransferase activity protein-lysine N-methyltransferase activity transferase activity peptidyl-lysine monomethylation stem cell population maintenance negative regulation of NF-kappaB transcription factor activity methylation histone lysine methylation stem cell differentiation regulation of inflammatory response NF-kappaB binding uc002ens.1 uc002ens.2 uc002ens.3 uc002ens.4 uc002ens.5 
ENST00000219320.9 SLC38A7 ENST00000219320.9 solute carrier family 38 member 7, transcript variant 7 (from RefSeq NR_161424.1) ENST00000219320.1 ENST00000219320.2 ENST00000219320.3 ENST00000219320.4 ENST00000219320.5 ENST00000219320.6 ENST00000219320.7 ENST00000219320.8 NR_161424 Q53GJ9 Q9H9I5 Q9NVC3 S38A7_HUMAN SLC38A7 SNAT7 uc002eod.1 uc002eod.2 uc002eod.3 Symporter that selectively cotransports sodium ions and amino acids, such as L-glutamine and L-asparagine from the lysosome into the cytoplasm and may participates in mTORC1 activation (PubMed:28416685, PubMed:35561222). The transport activity requires an acidic lysosomal lumen (PubMed:28416685). Reaction=L-asparagine(in) + Na(+)(in) = L-asparagine(out) + Na(+)(out); Xref=Rhea:RHEA:71383, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048; Evidence=; Reaction=L-glutamine(in) + Na(+)(in) = L-glutamine(out) + Na(+)(out); Xref=Rhea:RHEA:68236, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359; Evidence=; Interacts with the mTORC1 complex; this interaction mediates the recruitment of mTORC1 to the lysosome and its subsequent activation. Q9NVC3; Q5T8D3-2: ACBD5; NbExp=3; IntAct=EBI-10314552, EBI-10961679; Q9NVC3; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-10314552, EBI-19125216; Q9NVC3; Q96BI3: APH1A; NbExp=3; IntAct=EBI-10314552, EBI-2606935; Q9NVC3; P41181: AQP2; NbExp=3; IntAct=EBI-10314552, EBI-12701138; Q9NVC3; O43315: AQP9; NbExp=3; IntAct=EBI-10314552, EBI-17444777; Q9NVC3; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-10314552, EBI-11343438; Q9NVC3; Q6UXG8-3: BTNL9; NbExp=3; IntAct=EBI-10314552, EBI-17953245; Q9NVC3; P51798: CLCN7; NbExp=3; IntAct=EBI-10314552, EBI-4402346; Q9NVC3; O95471: CLDN7; NbExp=3; IntAct=EBI-10314552, EBI-740744; Q9NVC3; Q8IUN9: CLEC10A; NbExp=3; IntAct=EBI-10314552, EBI-2873246; Q9NVC3; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-10314552, EBI-18013275; Q9NVC3; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-10314552, EBI-852194; Q9NVC3; P49447: CYB561; NbExp=3; IntAct=EBI-10314552, EBI-8646596; Q9NVC3; P00387: CYB5R3; NbExp=3; IntAct=EBI-10314552, EBI-1046040; Q9NVC3; Q15125: EBP; NbExp=3; IntAct=EBI-10314552, EBI-3915253; Q9NVC3; Q92838: EDA; NbExp=3; IntAct=EBI-10314552, EBI-529425; Q9NVC3; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-10314552, EBI-781551; Q9NVC3; P30040: ERP29; NbExp=3; IntAct=EBI-10314552, EBI-946830; Q9NVC3; P34910-2: EVI2B; NbExp=3; IntAct=EBI-10314552, EBI-17640610; Q9NVC3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10314552, EBI-18304435; Q9NVC3; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-10314552, EBI-3918971; Q9NVC3; P48165: GJA8; NbExp=3; IntAct=EBI-10314552, EBI-17458373; Q9NVC3; O95377: GJB5; NbExp=3; IntAct=EBI-10314552, EBI-3909454; Q9NVC3; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10314552, EBI-13345167; Q9NVC3; O15529: GPR42; NbExp=3; IntAct=EBI-10314552, EBI-18076404; Q9NVC3; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-10314552, EBI-2867874; Q9NVC3; Q13651: IL10RA; NbExp=3; IntAct=EBI-10314552, EBI-1031656; Q9NVC3; P43628: KIR2DL3; NbExp=3; IntAct=EBI-10314552, EBI-8632435; Q9NVC3; O95867: LY6G6C; NbExp=3; IntAct=EBI-10314552, EBI-9088345; Q9NVC3; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-10314552, EBI-10329546; Q9NVC3; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-10314552, EBI-6163737; Q9NVC3; P15941-11: MUC1; NbExp=3; IntAct=EBI-10314552, EBI-17263240; Q9NVC3; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-10314552, EBI-12382569; Q9NVC3; P35372-10: OPRM1; NbExp=3; IntAct=EBI-10314552, EBI-12807478; Q9NVC3; Q96RD7: PANX1; NbExp=3; IntAct=EBI-10314552, EBI-7037612; Q9NVC3; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-10314552, EBI-16427978; Q9NVC3; Q99942: RNF5; NbExp=8; IntAct=EBI-10314552, EBI-348482; Q9NVC3; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10314552, EBI-3920694; Q9NVC3; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-10314552, EBI-17247926; Q9NVC3; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-10314552, EBI-749270; Q9NVC3; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-10314552, EBI-18037857; Q9NVC3; Q14973: SLC10A1; NbExp=3; IntAct=EBI-10314552, EBI-3923031; Q9NVC3; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-10314552, EBI-17595455; Q9NVC3; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-10314552, EBI-8644112; Q9NVC3; Q9H2J7: SLC6A15; NbExp=3; IntAct=EBI-10314552, EBI-11343466; Q9NVC3; O43278-2: SPINT1; NbExp=3; IntAct=EBI-10314552, EBI-12078338; Q9NVC3; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10314552, EBI-17280858; Q9NVC3; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-10314552, EBI-18196631; Q9NVC3; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-10314552, EBI-10982110; Q9NVC3; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10314552, EBI-18178701; Q9NVC3; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-10314552, EBI-12345267; Q9NVC3; P19075: TSPAN8; NbExp=3; IntAct=EBI-10314552, EBI-4289938; Q9NVC3; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-10314552, EBI-751210; Lysosome membrane ulti-pass membrane protein Cell projection, axon Note=In neurons, located in soma. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NVC3-1; Sequence=Displayed; Name=2; IsoId=Q9NVC3-2; Sequence=VSP_031511; Belongs to the amino acid/polyamine transporter 2 family. amino acid transmembrane transport L-histidine transmembrane transporter activity L-glutamate transmembrane transporter activity protein binding ion transport sodium ion transport amino acid transport asparagine transport glutamine transport amino acid transmembrane transporter activity L-amino acid transmembrane transporter activity L-alanine transmembrane transporter activity L-asparagine transmembrane transporter activity L-aspartate transmembrane transporter activity L-glutamine transmembrane transporter activity L-leucine transmembrane transporter activity L-methionine transmembrane transporter activity L-serine transmembrane transporter activity branched-chain amino acid transport neutral amino acid transport L-alanine transport L-glutamate transport methionine transport L-serine transport membrane integral component of membrane axon neuronal cell body L-aspartate transport L-histidine transmembrane transport cation transmembrane transport L-alpha-amino acid transmembrane transport uc002eod.1 uc002eod.2 uc002eod.3 
ENST00000219334.10 SMPD3 ENST00000219334.10 sphingomyelin phosphodiesterase 3 (from RefSeq NM_018667.4) B7ZL82 ENST00000219334.1 ENST00000219334.2 ENST00000219334.3 ENST00000219334.4 ENST00000219334.5 ENST00000219334.6 ENST00000219334.7 ENST00000219334.8 ENST00000219334.9 NM_018667 NSMA2_HUMAN Q2M1S8 Q9NY59 SMPD3 uc002ewa.1 uc002ewa.2 uc002ewa.3 uc002ewa.4 uc002ewa.5 Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:10823942, PubMed:14741383, PubMed:15051724). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location. May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity). Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence=; Reaction=H2O + N-(15Z-tetracosenoyl)sphing-4-enine-1-phosphocholine = H(+) + N-(15Z-tetracosenoyl)-sphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74450, ChEBI:CHEBI:74535, ChEBI:CHEBI:295975; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45321; Evidence=; Reaction=H2O + N-(tetracosanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-tetracosanoyl-sphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45324, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72965, ChEBI:CHEBI:83360, ChEBI:CHEBI:295975; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45325; Evidence=; Reaction=an N-(acyl)-sphingosylphosphocholine + H2O = an N-acyl- sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64583, ChEBI:CHEBI:83273, ChEBI:CHEBI:295975; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45301; Evidence=; Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- hexadecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; Evidence=; Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + H2O = 1-O- octadecyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:39923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74001, ChEBI:CHEBI:75216, ChEBI:CHEBI:295975; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39924; Evidence=; Reaction=a sphingosylphosphocholine + H2O = a sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84410, ChEBI:CHEBI:85171, ChEBI:CHEBI:295975; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45297; Evidence=; Reaction=H2O + N-(hexadecanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-hexadecanoylsphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72959, ChEBI:CHEBI:78646, ChEBI:CHEBI:295975; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45645; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Inhibited by nSMase inhibitor GW4869 (PubMed:10823942). Binding of anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) increases enzymatic activity (By similarity). Kinetic parameters: Vmax=953 nmol/h/mg enzyme with sphingomyelin as substrate (at pH 7.5 and 37 degrees Celsius in presence of 0.1% Triton X-100) ; Vmax=152 nmol/h/mg enzyme with sphingosylphosphocholine as substrate (at pH 7.5 and 37 degrees Celsius) ; Vmax=8.6 nmol/h/mg enzyme with 1-O-octadecyl-sn-glycero-3- phosphocholine as substrate (at pH 7.5 and 37 degrees Celsius) ; Vmax=92.2 nmol/h/mg enzyme with 1-hexadecanoyl-sn-glycero-3- phosphocholine as substrate (at pH 7.5 and 37 degrees Celsius) ; pH dependence: Optimum pH is 7.5.; Lipid metabolism; sphingolipid metabolism. Q9NY59; O75530: EED; NbExp=2; IntAct=EBI-715400, EBI-923794; Golgi apparatus membrane ; Lipid-anchor Cell membrane ; Lipid-anchor Note=May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:10823942). Localizes to plasma membrane in confluent contact- inhaibited cells (PubMed:15051724). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NY59-1; Sequence=Displayed; Name=2; IsoId=Q9NY59-2; Sequence=VSP_054334; Predominantly expressed in brain. Up-regulated during G0/G1 phases. Palmitoylated, palmitoylation-deficient proteins are targeted for lysosomal degradation. Belongs to the neutral sphingomyelinase family. Golgi cis cisterna Golgi membrane skeletal system development ossification regulation of protein phosphorylation endochondral ossification chondrocyte development hematopoietic progenitor cell differentiation regulation of leukocyte migration chondrocyte development involved in endochondral bone morphogenesis phospholipase activity sphingomyelin phosphodiesterase activity protein binding cytoplasm Golgi apparatus plasma membrane lipid metabolic process sphingolipid metabolic process ceramide metabolic process sphingomyelin metabolic process sphingomyelin catabolic process glycosphingolipid metabolic process cell cycle signal transduction multicellular organism development polysaccharide transport membrane hydrolase activity peptide hormone secretion bone mineralization lung development BMP signaling pathway collagen metabolic process cellular response to reactive oxygen species multicellular organism growth identical protein binding protein kinase B signaling positive regulation of mitotic nuclear division metal ion binding platelet-derived growth factor receptor signaling pathway lung alveolus development positive regulation of smooth muscle cell proliferation cartilage development bone development respiratory system development regulation of cartilage development neutral sphingomyelin phosphodiesterase activity cellular response to hydrogen peroxide G1 to G0 transition cellular response to magnesium ion cellular response to tumor necrosis factor cellular response to redox state DNA biosynthetic process extracellular matrix assembly sphingolipid mediated signaling pathway dentinogenesis bone growth regulation of hyaluronan biosynthetic process negative regulation of hyaluronan biosynthetic process cellular response to peptide positive regulation of exosomal secretion positive regulation of ceramide biosynthetic process uc002ewa.1 uc002ewa.2 uc002ewa.3 uc002ewa.4 uc002ewa.5 
ENST00000219343.11 SLC7A6 ENST00000219343.11 solute carrier family 7 member 6, transcript variant 2 (from RefSeq NM_003983.6) ENST00000219343.1 ENST00000219343.10 ENST00000219343.2 ENST00000219343.3 ENST00000219343.4 ENST00000219343.5 ENST00000219343.6 ENST00000219343.7 ENST00000219343.8 ENST00000219343.9 KIAA0245 NM_003983 Q68DS4 Q7L1N3 Q92536 SLC7A6 YLAT2_HUMAN uc002evu.1 uc002evu.2 uc002evu.3 uc002evu.4 Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis (PubMed:9829974, PubMed:10903140, PubMed:16785209, PubMed:31705628, PubMed:15756301, PubMed:11311135, PubMed:17329401, PubMed:14603368, PubMed:19562367). Also exchanges L-arginine with L-lysine in a sodium-independent manner (PubMed:10903140). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (PubMed:10903140). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration (By similarity). May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (PubMed:17197568). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity). Reaction=L-arginine(in) + L-lysine(out) = L-arginine(out) + L- lysine(in); Xref=Rhea:RHEA:70827, ChEBI:CHEBI:32551, ChEBI:CHEBI:32682; Evidence=; Reaction=L-arginine(in) + L-leucine(out) + Na(+)(out) = L-arginine(out) + L-leucine(in) + Na(+)(in); Xref=Rhea:RHEA:70831, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57427; Evidence=; Reaction=L-arginine(in) + L-glutamine(out) + Na(+)(out) = L- arginine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70835, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:58359; Evidence=; Reaction=L-arginine(in) + L-histidine(out) + Na(+)(out) = L- arginine(out) + L-histidine(in) + Na(+)(in); Xref=Rhea:RHEA:70839, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57595; Evidence=; Reaction=L-arginine(in) + L-cysteine(out) + Na(+)(out) = L- arginine(out) + L-cysteine(in) + Na(+)(in); Xref=Rhea:RHEA:70847, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:35235; Evidence=; Reaction=L-arginine(in) + L-methionine(out) + Na(+)(out) = L- arginine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70843, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57844; Evidence=; Arginine transport is strongly inhibited by lysine, glutamate, leucine, glutamine, methionine and histidine, in the presence of Na(+) (PubMed:10903140). Also inhibited by protein kinase C (PKC) and treatment with phorbol-12-myristate-13-acetate (PMA) (PubMed:17329401). Kinetic parameters: KM=295 uM for L-glutamine (in the presence of NaCl) ; KM=236 uM for L-leucine (in the presence of NaCl) ; KM=120 uM for L-arginine (in the presence of NaCl) ; KM=138 uM for L-arginine (in the absence of NaCl) ; KM=185 uM for L-arginine ; KM=201 uM for L-leucine ; KM=5100 uM for sodium ion (in the presence of 100 mM L-leucine and with different sodium ions concentrations.) ; KM=0.145 uM for L-arginine (in fibroblasts from healthy donors) ; Vmax=1.479 nmol/min/mg enzyme toward L-arginine (in fibroblasts from healthy donors) ; Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. Q92536; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-2880595, EBI-8645574; Cell membrane ; Multi-pass membrane protein Expressed in normal fibroblasts and those from LPI patients (PubMed:11078698). Also expressed in HUVECs, monocytes, RPE cells, and various carcinoma cell lines (PubMed:11742806, PubMed:14603368, PubMed:15280038, PubMed:17197568, PubMed:17329401). Expressed in brain, heart, testis, kidney, small intestine and parotis (PubMed:10903140). Highly expressed in T lymphocytes (PubMed:31705628). Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family. Sequence=BAA13376.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; amino acid transmembrane transport plasma membrane integral component of plasma membrane amino acid transport amino acid transmembrane transporter activity L-amino acid transmembrane transporter activity antiporter activity membrane integral component of membrane basolateral plasma membrane transmembrane transporter activity intracellular membrane-bounded organelle leukocyte migration transmembrane transport L-alpha-amino acid transmembrane transport uc002evu.1 uc002evu.2 uc002evu.3 uc002evu.4 
ENST00000219345.10 PLA2G15 ENST00000219345.10 phospholipase A2 group XV, transcript variant 1 (from RefSeq NM_012320.4) B3KMF3 B4DUD1 ENST00000219345.1 ENST00000219345.2 ENST00000219345.3 ENST00000219345.4 ENST00000219345.5 ENST00000219345.6 ENST00000219345.7 ENST00000219345.8 ENST00000219345.9 LYPLA3 NM_012320 PAG15_HUMAN PLA2G15 Q53GZ1 Q8NCC3 Q9NPQ6 Q9UG04 Q9Y2B3 UNQ341/PRO540 uc002evr.1 uc002evr.2 uc002evr.3 uc002evr.4 uc002evr.5 Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene hydrolyzes lysophosphatidylcholine to glycerophosphorylcholine and a free fatty acid. This enzyme is present in the plasma and thought to be associated with high-density lipoprotein. A later paper contradicts the function of this gene. It demonstrates that this gene encodes a lysosomal enzyme instead of a lysophospholipase and has both calcium-independent phospholipase A2 and transacylase activities. [provided by RefSeq, Jul 2008]. Has dual calcium-independent phospholipase and O- acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments (PubMed:10092508, PubMed:11790796, PubMed:20410020, PubMed:23958596, PubMed:29724779, PubMed:25727495). Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity) (PubMed:10092508, PubMed:11790796, PubMed:20410020, PubMed:23958596, PubMed:29724779, PubMed:25727495). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines (PubMed:29724779). Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines and phosphatidylethanolamines (By similarity). Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide (PubMed:29724779). Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress (PubMed:30830753). Required for normal phospholipid degradation in alveolar macrophages with potential implications in pulmonary surfactant clearance (By similarity). At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (PubMed:10092508). Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784; Evidence=; Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O = 2-glutaroyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62480, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77756, ChEBI:CHEBI:145781; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62481; Evidence=; Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = 2-nonadioyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62464, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78207, ChEBI:CHEBI:145780; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62465; Evidence=; Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H2O = 2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62484, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77890, ChEBI:CHEBI:145782; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62485; Evidence=; Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62488, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61042, ChEBI:CHEBI:145783; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62489; Evidence=; Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence=; Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence=; Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N- (acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3- phosphoethanolamine; Xref=Rhea:RHEA:38827, ChEBI:CHEBI:46979, ChEBI:CHEBI:73007, ChEBI:CHEBI:76077, ChEBI:CHEBI:76088; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38828; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z- octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero- 3-phosphoethanolamine; Xref=Rhea:RHEA:38823, ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007, ChEBI:CHEBI:76054; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38824; Evidence=; Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N- (acetyl)-sphing-4-enine + 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3- phosphoethanolamine; Xref=Rhea:RHEA:38831, ChEBI:CHEBI:46979, ChEBI:CHEBI:73008, ChEBI:CHEBI:76077, ChEBI:CHEBI:76090; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38832; Evidence=; Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z- octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero- 3-phosphoethanolamine; Xref=Rhea:RHEA:38835, ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008, ChEBI:CHEBI:76086; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38836; Evidence=; Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N- (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn- glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38843, ChEBI:CHEBI:46979, ChEBI:CHEBI:73009, ChEBI:CHEBI:76077, ChEBI:CHEBI:76091; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38844; Evidence=; Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1- hexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38839, ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009, ChEBI:CHEBI:76080; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38840; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4- enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38759, ChEBI:CHEBI:46979, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071, ChEBI:CHEBI:76077; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38760; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing- 4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38755, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001, ChEBI:CHEBI:76054; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38756; Evidence=; Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N- (acetyl)-sphing-4-enine + 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphocholine; Xref=Rhea:RHEA:38811, ChEBI:CHEBI:46979, ChEBI:CHEBI:73002, ChEBI:CHEBI:76077, ChEBI:CHEBI:76084; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38812; Evidence=; Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z- octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero- 3-phosphocholine; Xref=Rhea:RHEA:38807, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:76086; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38808; Evidence=; Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N- (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn- glycero-3-phosphocholine; Xref=Rhea:RHEA:38775, ChEBI:CHEBI:46979, ChEBI:CHEBI:73003, ChEBI:CHEBI:76077, ChEBI:CHEBI:76079; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38776; Evidence=; Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)- eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn- glycero-3-phosphocholine; Xref=Rhea:RHEA:38771, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003, ChEBI:CHEBI:76080; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38772; Evidence=; Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1- hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(4Z,7Z,10Z,13Z,16Z,19Z- docosahexaenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38815, ChEBI:CHEBI:46979, ChEBI:CHEBI:74963, ChEBI:CHEBI:76077, ChEBI:CHEBI:76085; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38816; Evidence=; Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1- (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38819, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:76087; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38820; Evidence=; Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + N- (acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-nonadioyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:62472, ChEBI:CHEBI:46979, ChEBI:CHEBI:76077, ChEBI:CHEBI:78207, ChEBI:CHEBI:145780; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62473; Evidence=; Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-sphing-4- enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38799, ChEBI:CHEBI:46979, ChEBI:CHEBI:75034, ChEBI:CHEBI:76071, ChEBI:CHEBI:76074; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38800; Evidence=; Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing- 4-enine + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38795, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034, ChEBI:CHEBI:76054; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38796; Evidence=; Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3- phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z- octadecadienoyl)-N-acetylsphing-4-enine + 1-octadecanoyl-sn-glycero- 3-phosphocholine; Xref=Rhea:RHEA:57108, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858, ChEBI:CHEBI:76086, ChEBI:CHEBI:84822; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57109; Evidence=; Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N- (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn- glycero-3-phosphocholine; Xref=Rhea:RHEA:57120, ChEBI:CHEBI:46979, ChEBI:CHEBI:74965, ChEBI:CHEBI:76074, ChEBI:CHEBI:76079; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57121; Evidence=; Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)- eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-octadecanoyl-sn- glycero-3-phosphocholine; Xref=Rhea:RHEA:57116, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:76080; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57117; Evidence=; Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing- 4-enine + 2-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38767, ChEBI:CHEBI:46979, ChEBI:CHEBI:74667, ChEBI:CHEBI:76054, ChEBI:CHEBI:76078; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38768; Evidence=; Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1-hexadecanoyl-N-(acetyl)-sphing-4-enine; Xref=Rhea:RHEA:38763, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979, ChEBI:CHEBI:74667, ChEBI:CHEBI:76077; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38764; Evidence=; Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing- 4-enine + 2-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38791, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054, ChEBI:CHEBI:76073, ChEBI:CHEBI:76076; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38792; Evidence=; Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1-octadecanoyl-N-(acetyl)-sphing-4-enine; Xref=Rhea:RHEA:38803, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979, ChEBI:CHEBI:76073, ChEBI:CHEBI:76074; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38804; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N- (acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4- enine + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38703, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979, ChEBI:CHEBI:74669, ChEBI:CHEBI:76054; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38704; Evidence= Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L- serine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)- sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:57140, ChEBI:CHEBI:46979, ChEBI:CHEBI:76074, ChEBI:CHEBI:77342, ChEBI:CHEBI:78260; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57141; Evidence=; Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L- serine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)- sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phosphoserine; Xref=Rhea:RHEA:57136, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054, ChEBI:CHEBI:78260, ChEBI:CHEBI:84467; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57137; Evidence=; Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'- sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)- sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn- glycerol); Xref=Rhea:RHEA:57144, ChEBI:CHEBI:46979, ChEBI:CHEBI:72845, ChEBI:CHEBI:76074, ChEBI:CHEBI:141490; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57145; Evidence=; Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'- sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N- (acetyl)-sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phospho-(1'-sn- glycerol); Xref=Rhea:RHEA:57148, ChEBI:CHEBI:46979, ChEBI:CHEBI:72827, ChEBI:CHEBI:72845, ChEBI:CHEBI:76054; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57149; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N- (5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (9Z-octadecenoyl)-sn- glycero-3-phosphocholine + 2-[(5Z,8Z,11Z,14Z)- eicosatetraenoylamino]ethyl (9Z)-octadecenoate; Xref=Rhea:RHEA:38751, ChEBI:CHEBI:2700, ChEBI:CHEBI:74669, ChEBI:CHEBI:76070, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38752; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(9Z- octadecenoyl) ethanolamine = (9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 2-[(9Z)-octadecenoylamino]ethyl (9Z)-octadecenoate; Xref=Rhea:RHEA:38747, ChEBI:CHEBI:71466, ChEBI:CHEBI:74669, ChEBI:CHEBI:76068, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38748; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3-(9Z- octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol; Xref=Rhea:RHEA:38743, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735, ChEBI:CHEBI:75938, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38744; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z- octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol; Xref=Rhea:RHEA:38739, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735, ChEBI:CHEBI:75757, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38740; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2- hexadecanoylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z)-octadecenoyl-2-hexadecanoylglycerol; Xref=Rhea:RHEA:38735, ChEBI:CHEBI:74669, ChEBI:CHEBI:75455, ChEBI:CHEBI:76065, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38736; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3- hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol; Xref=Rhea:RHEA:38731, ChEBI:CHEBI:64757, ChEBI:CHEBI:74669, ChEBI:CHEBI:75867, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38732; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O- hexadecyl-2-acetyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1-O-hexadecyl-2-acetyl-3-(9Z)-octadecenoyl-sn- glycerol; Xref=Rhea:RHEA:38707, ChEBI:CHEBI:74669, ChEBI:CHEBI:75936, ChEBI:CHEBI:76055, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38708; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O- hexadecylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-hexadecyl-3-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:38711, ChEBI:CHEBI:74669, ChEBI:CHEBI:76061, ChEBI:CHEBI:76062, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38712; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O- hexadecyl-2-O-methyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1-O-hexadecyl-2-O-methyl-3-(9Z)-octadecenoyl-sn- glycerol; Xref=Rhea:RHEA:38723, ChEBI:CHEBI:74669, ChEBI:CHEBI:76063, ChEBI:CHEBI:76064, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38724; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1- hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3- phosphocholine + 1-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol; Xref=Rhea:RHEA:38727, ChEBI:CHEBI:74669, ChEBI:CHEBI:75542, ChEBI:CHEBI:75868, ChEBI:CHEBI:76083; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38728; Evidence=; Inhibited by zinc ions at neutral pH. Zinc ions in plasma may keep the enzyme from hydrolyzing inappropriate substrates. pH dependence: Optimum pH is 4-4.5. ; Lysosome Secreted Membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8NCC3-1; Sequence=Displayed; Name=2; IsoId=Q8NCC3-2; Sequence=VSP_056689, VSP_056690; Detected in blood plasma (at protein level) (PubMed:10092508, PubMed:20410020). Ubiquitous. Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes (PubMed:10092508). N-glycosylated (PubMed:11790796, PubMed:23958596). N-glycosylation is important for maturation of the enzyme and normal subcellular location (PubMed:23958596). Belongs to the AB hydrolase superfamily. Lipase family. Sequence=CAB53675.1; Type=Erroneous initiation; Evidence=; lysophospholipase activity phospholipid binding extracellular region extracellular space nucleoplasm lysosome lipid metabolic process fatty acid metabolic process phospholipid metabolic process glycerophospholipid metabolic process ceramide metabolic process O-acyltransferase activity fatty acid catabolic process membrane lipid catabolic process transferase activity transferase activity, transferring acyl groups hydrolase activity phosphatidylcholine catabolic process intracellular membrane-bounded organelle phosphatidylethanolamine catabolic process phosphatidylcholine metabolic process calcium-independent phospholipase A2 activity extracellular exosome uc002evr.1 uc002evr.2 uc002evr.3 uc002evr.4 uc002evr.5 
ENST00000219368.8 FA2H ENST00000219368.8 fatty acid 2-hydroxylase (from RefSeq NM_024306.5) B7Z8T6 ENST00000219368.1 ENST00000219368.2 ENST00000219368.3 ENST00000219368.4 ENST00000219368.5 ENST00000219368.6 ENST00000219368.7 FA2H FA2H_HUMAN FAAH FAXDC1 NM_024306 O75213 Q7L5A8 Q96DK1 Q9H1A5 uc002fde.1 uc002fde.2 uc002fde.3 uc002fde.4 This gene encodes a protein that catalyzes the synthesis of 2-hydroxysphingolipids, a subset of sphingolipids that contain 2-hydroxy fatty acids. Sphingolipids play roles in many cellular processes and their structural diversity arises from modification of the hydrophobic ceramide moiety, such as by 2-hydroxylation of the N-acyl chain, and the existence of many different head groups. Mutations in this gene have been associated with leukodystrophy dysmyelinating with spastic paraparesis with or without dystonia.[provided by RefSeq, Mar 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.205016.1, AK058016.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968832 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219368.8/ ENSP00000219368.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the hydroxylation of free fatty acids at the C-2 position to produce 2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis (PubMed:15337768, PubMed:15863841, PubMed:17355976, PubMed:22517924). FA2H is stereospecific for the production of (R)-2- hydroxy fatty acids (PubMed:22517924). Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath (By similarity). Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies critical for skin permeability barrier (PubMed:17355976). Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis (By similarity). Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins (By similarity). Reaction=a 1,2-saturated fatty acid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (R)-2-hydroxy fatty acid + 2 Fe(III)-[cytochrome b5] + H2O; Xref=Rhea:RHEA:38855, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:76177, ChEBI:CHEBI:83955; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38856; Evidence=; Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoate + O2 = (R)- 2-hydroxyhexadecanoate + 2 Fe(III)-[cytochrome b5] + H2O; Xref=Rhea:RHEA:38551, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:75927; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38552; Evidence=; Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoate = (R)- 2-hydroxyoctadecanoate + 2 Fe(III)-[cytochrome b5] + H2O; Xref=Rhea:RHEA:39815, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:25629, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57562; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39816; Evidence=; Reaction=docosanoate + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 2- hydroxydocosanoate + 2 Fe(III)-[cytochrome b5] + H2O; Xref=Rhea:RHEA:39819, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23858, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:76722; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39820; Evidence=; Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + tetracosanoate = (R)- 2-hydroxytetracosanoate + 2 Fe(III)-[cytochrome b5] + H2O; Xref=Rhea:RHEA:38559, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31014, ChEBI:CHEBI:75935; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38560; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center. ; Kinetic parameters: Note=KM<0.18 uM for tetracosanoic acid. ; pH dependence: Optimum pH is 7.6-7.8. ; Lipid metabolism; fatty acid metabolism. Sphingolipid metabolism; galactosylceramide biosynthesis. Q7L5A8; Q13520: AQP6; NbExp=3; IntAct=EBI-11337888, EBI-13059134; Q7L5A8; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-11337888, EBI-36513937; Q7L5A8; P07307-3: ASGR2; NbExp=3; IntAct=EBI-11337888, EBI-12808270; Q7L5A8; P11912: CD79A; NbExp=3; IntAct=EBI-11337888, EBI-7797864; Q7L5A8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-11337888, EBI-6942903; Q7L5A8; Q15700: DLG2; NbExp=3; IntAct=EBI-11337888, EBI-80426; Q7L5A8; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-11337888, EBI-356015; Q7L5A8; Q15125: EBP; NbExp=3; IntAct=EBI-11337888, EBI-3915253; Q7L5A8; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-11337888, EBI-18535450; Q7L5A8; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-11337888, EBI-781551; Q7L5A8; O75477: ERLIN1; NbExp=3; IntAct=EBI-11337888, EBI-359299; Q7L5A8; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-11337888, EBI-18304435; Q7L5A8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11337888, EBI-13345167; Q7L5A8; Q8TED1: GPX8; NbExp=3; IntAct=EBI-11337888, EBI-11721746; Q7L5A8; Q92876: KLK6; NbExp=3; IntAct=EBI-11337888, EBI-2432309; Q7L5A8; Q5T0T0: MARCHF8; NbExp=3; IntAct=EBI-11337888, EBI-14061946; Q7L5A8; P21757: MSR1; NbExp=3; IntAct=EBI-11337888, EBI-1776976; Q7L5A8; O00623: PEX12; NbExp=3; IntAct=EBI-11337888, EBI-594836; Q7L5A8; O15173: PGRMC2; NbExp=3; IntAct=EBI-11337888, EBI-1050125; Q7L5A8; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-11337888, EBI-12375429; Q7L5A8; O95470: SGPL1; NbExp=3; IntAct=EBI-11337888, EBI-1046170; Q7L5A8; Q14973: SLC10A1; NbExp=3; IntAct=EBI-11337888, EBI-3923031; Q7L5A8; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-11337888, EBI-18159983; Q7L5A8; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-11337888, EBI-8032987; Q7L5A8; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-11337888, EBI-12947623; Q7L5A8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-11337888, EBI-8638294; Q7L5A8; Q96HV5: TMEM41A; NbExp=3; IntAct=EBI-11337888, EBI-10288884; Q7L5A8; Q9Y320: TMX2; NbExp=3; IntAct=EBI-11337888, EBI-6447886; Endoplasmic reticulum membrane ; Multi-pass membrane protein Microsome membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q7L5A8-1; Sequence=Displayed; Name=2; IsoId=Q7L5A8-2; Sequence=VSP_056135; Detected in differentiating cultured keratinocytes (at protein level). Detected in epidermis and cultured keratinocytes (PubMed:17355976). Highly expressed in brain and colon. Detected at lower levels in testis, prostate, pancreas and kidney (PubMed:15337768). Up-regulated during keratinocyte differentiation. The histidine box domains may contain the active site and/or be involved in metal ion binding. The N-terminal cytochrome b5 heme-binding domain is essential for catalytic activity. Spastic paraplegia 35, autosomal recessive, with or without neurodegeneration (SPG35) [MIM:612319]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG35 is a complicated form characterized by childhood onset of gait difficulties. It has a rapid progression and many patients become wheelchair-bound as young adults. Patients manifest cognitive decline associated with leukodystrophy. Other variable neurologic features, such as dystonia, optic atrophy, and seizures may also occur. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the sterol desaturase family. SCS7 subfamily. Sequence=AAC23496.1; Type=Erroneous gene model prediction; Evidence=; sebaceous gland cell differentiation iron ion binding endoplasmic reticulum endoplasmic reticulum membrane lipid metabolic process fatty acid metabolic process fatty acid biosynthetic process glucosylceramide biosynthetic process galactosylceramide biosynthetic process lipid biosynthetic process membrane integral component of membrane oxidoreductase activity heme binding sphingolipid biosynthetic process lipid modification organelle membrane central nervous system myelin maintenance peripheral nervous system myelin maintenance regulation of cell proliferation regulation of hair cycle intracellular membrane-bounded organelle plasma membrane raft organization ceramide biosynthetic process metal ion binding oxidation-reduction process establishment of skin barrier fatty acid alpha-hydroxylase activity uc002fde.1 uc002fde.2 uc002fde.3 uc002fde.4 
ENST00000219400.8 CMC2 ENST00000219400.8 C-X9-C motif containing 2, transcript variant 10 (from RefSeq NR_147842.2) C16orf61 COXM2_HUMAN D3DUK6 DC13 ENST00000219400.1 ENST00000219400.2 ENST00000219400.3 ENST00000219400.4 ENST00000219400.5 ENST00000219400.6 ENST00000219400.7 NR_147842 Q9NRP2 uc002ffu.1 uc002ffu.2 uc002ffu.3 uc002ffu.4 uc002ffu.5 May be involved in cytochrome c oxidase biogenesis. Q9NRP2; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-16780661, EBI-747505; Q9NRP2; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-16780661, EBI-11962928; Mitochondrion Belongs to the CMC family. mitochondrion uc002ffu.1 uc002ffu.2 uc002ffu.3 uc002ffu.4 uc002ffu.5 
ENST00000219406.11 PDIA2 ENST00000219406.11 protein disulfide isomerase family A member 2 (from RefSeq NM_006849.4) A6ZJ64 B4DI27 ENST00000219406.1 ENST00000219406.10 ENST00000219406.2 ENST00000219406.3 ENST00000219406.4 ENST00000219406.5 ENST00000219406.6 ENST00000219406.7 ENST00000219406.8 ENST00000219406.9 NM_006849 PDIA2_HUMAN PDIP Q13087 Q2WGM4 Q4TT67 Q6B010 Q96KJ6 Q9BW95 uc002cgo.1 uc002cgo.2 uc002cgo.3 This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, two catalytically active thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming disulfide bonds through its thiol isomerase, oxidase, and reductase activity. The encoded protein also possesses estradiol-binding activity and can modulate intracellular estradiol levels. [provided by RefSeq, Sep 2017]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7410570.571219.1, SRR7410570.571220.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219406.11/ ENSP00000219406.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins. Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Monomer; predominantly as monomer under reducing conditions. Homodimer; disulfide-linked. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Q13087; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-1752525, EBI-10210845; Q13087; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-1752525, EBI-12111050; Q13087; P16333: NCK1; NbExp=3; IntAct=EBI-1752525, EBI-389883; Endoplasmic reticulum lumen Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13087-1; Sequence=Displayed; Name=2; IsoId=Q13087-2; Sequence=VSP_039292; Highly expressed in pancreas (at protein level). The disulfide-linked homodimer exhibits an enhanced chaperone activity. Glycosylated. Belongs to the protein disulfide isomerase family. Sequence=AAC50401.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence=; Sequence=AAH75029.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence=; Sequence=BAG58339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; protein disulfide isomerase activity steroid binding protein binding endoplasmic reticulum endoplasmic reticulum lumen protein folding protein retention in ER lumen lipid binding disulfide oxidoreductase activity peptide disulfide oxidoreductase activity isomerase activity protein folding in endoplasmic reticulum response to endoplasmic reticulum stress cell redox homeostasis oxidation-reduction process uc002cgo.1 uc002cgo.2 uc002cgo.3 
ENST00000219409.8 ARHGDIG ENST00000219409.8 Rho GDP dissociation inhibitor gamma (from RefSeq NM_001176.4) ENST00000219409.1 ENST00000219409.2 ENST00000219409.3 ENST00000219409.4 ENST00000219409.5 ENST00000219409.6 ENST00000219409.7 GDIR3_HUMAN NM_001176 Q4TT69 Q96S29 Q99819 uc002cgm.1 uc002cgm.2 uc002cgm.3 The GDP-dissociation inhibitors (GDIs) play a primary role in modulating the activation of GTPases by inhibiting the exchange of GDP for GTP. See ARHGDIB (MIM 602843).[supplied by OMIM, Nov 2010]. ##Evidence-Data-START## Transcript exon combination :: AB593111.1, ERR279844.8487.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219409.8/ ENSP00000219409.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post-translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP. Q99819; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-10295284, EBI-1012434; Q99819; Q96L14: CEP170P1; NbExp=3; IntAct=EBI-10295284, EBI-743488; Q99819; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-10295284, EBI-739657; Q99819; Q9BTT4: MED10; NbExp=3; IntAct=EBI-10295284, EBI-394354; Q99819; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-10295284, EBI-2554984; Cytoplasm. Primarily expressed in pancreas and brain. Belongs to the Rho GDI family. blastocyst hatching GDP-dissociation inhibitor activity Rho GDP-dissociation inhibitor activity GTPase activator activity protein binding cytoplasm cytosol plasma membrane negative regulation of cell adhesion Rho protein signal transduction membrane GTPase regulator activity cytoplasmic vesicle regulation of protein localization positive regulation of GTPase activity Rac GTPase binding regulation of catalytic activity regulation of small GTPase mediated signal transduction uc002cgm.1 uc002cgm.2 uc002cgm.3 
ENST00000219439.9 HSDL1 ENST00000219439.9 hydroxysteroid dehydrogenase like 1, transcript variant 1 (from RefSeq NM_031463.5) B4DSL2 D3DUL4 ENST00000219439.1 ENST00000219439.2 ENST00000219439.3 ENST00000219439.4 ENST00000219439.5 ENST00000219439.6 ENST00000219439.7 ENST00000219439.8 HSDL1_HUMAN NM_031463 Q3SXM4 Q3SXM5 Q8NC98 Q9BY22 SDR12C3 uc002fhk.1 uc002fhk.2 uc002fhk.3 uc002fhk.4 Interacts with STYXL1. Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3SXM5-1; Sequence=Displayed; Name=2; IsoId=Q3SXM5-2; Sequence=VSP_042823; Highly expressed in testis and ovary. Also detected in thyroid, spinal cord, adrenal gland, heart, placenta, skeletal muscle, small intestine, colon, spleen, prostate and pancreas. Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily. Although it belongs to the SDR family, Phe-218 is present instead of the conserved Tyr which is an active site residue. It is therefore expected that this protein lacks oxidoreductase activity. Sequence=AAK15047.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAK16927.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; protein binding mitochondrion oxidation-reduction process steroid dehydrogenase activity uc002fhk.1 uc002fhk.2 uc002fhk.3 uc002fhk.4 
ENST00000219454.10 WFDC1 ENST00000219454.10 WAP four-disulfide core domain 1, transcript variant 1 (from RefSeq NM_021197.4) D3DUL7 ENST00000219454.1 ENST00000219454.2 ENST00000219454.3 ENST00000219454.4 ENST00000219454.5 ENST00000219454.6 ENST00000219454.7 ENST00000219454.8 ENST00000219454.9 NM_021197 PS20 Q8NC27 Q9HAU1 Q9HC57 WFDC1_HUMAN uc002fhw.1 uc002fhw.2 uc002fhw.3 uc002fhw.4 uc002fhw.5 uc002fhw.6 This gene encodes a member of the WAP-type four disulfide core domain family. The WAP-type four-disulfide core domain contains eight cysteines forming four disulfide bonds at the core of the protein, and functions as a protease inhibitor in many family members. This gene is mapped to chromosome 16q24, an area of frequent loss of heterozygosity in cancers, including prostate, breast and hepatocellular cancers and Wilms' tumor. This gene is downregulated in many cancer types and may be involved in the inhibition of cell proliferation. The encoded protein may also play a role in the susceptibility of certain CD4 memory T cells to human immunodeficiency virus infection. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]. Has growth inhibitory activity. Secreted Sequence=AAG15263.1; Type=Frameshift; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/424/WFDC1"; regulation of cell growth molecular_function serine-type endopeptidase inhibitor activity extracellular region extracellular space negative regulation of peptidase activity negative regulation of endopeptidase activity negative regulation of cell growth peptidase inhibitor activity response to estradiol response to drug negative regulation of epithelial cell proliferation negative regulation of inflammatory response negative regulation of wound healing uc002fhw.1 uc002fhw.2 uc002fhw.3 uc002fhw.4 uc002fhw.5 uc002fhw.6 
ENST00000219473.12 USP10 ENST00000219473.12 ubiquitin specific peptidase 10, transcript variant 2 (from RefSeq NM_005153.3) B2RDJ8 B4DS84 ENST00000219473.1 ENST00000219473.10 ENST00000219473.11 ENST00000219473.2 ENST00000219473.3 ENST00000219473.4 ENST00000219473.5 ENST00000219473.6 ENST00000219473.7 ENST00000219473.8 ENST00000219473.9 KIAA0190 NM_005153 Q14694 Q9BWG7 Q9NSL7 UBP10_HUMAN USP10 uc002fii.1 uc002fii.2 uc002fii.3 uc002fii.4 uc002fii.5 Ubiquitin is a highly conserved protein that is covalently linked to other proteins to regulate their function and degradation. This gene encodes a member of the ubiquitin-specific protease family of cysteine proteases. The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates. The protein is found in the nucleus and cytoplasm. It functions as a co-factor of the DNA-bound androgen receptor complex, and is inhibited by a protein in the Ras-GTPase pathway. The human genome contains several pseudogenes similar to this gene. Several transcript variants, some protein-coding and others not protein-coding, have been found for this gene. [provided by RefSeq, Jan 2013]. Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 and CFTR (PubMed:11439350, PubMed:18632802, PubMed:31981475). Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53 (PubMed:20096447). Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response (PubMed:20096447). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes (PubMed:21962518). In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13 (PubMed:21962518). Does not deubiquitinate MDM2 (PubMed:20096447). Plays a key role in 40S ribosome subunit recycling when a ribosome has stalled during translation: acts both by inhibiting formation of stress granules, which store stalled translation pre-initiation complexes, and mediating deubiquitination of 40S ribosome subunits (PubMed:27022092, PubMed:31981475, PubMed:34348161, PubMed:34469731). Acts as a negative regulator of stress granules formation by lowering G3BP1 and G3BP2 valence, thereby preventing G3BP1 and G3BP2 ability to undergo liquid- liquid phase separation (LLPS) and assembly of stress granules (PubMed:11439350, PubMed:27022092, PubMed:32302570). Promotes 40S ribosome subunit recycling following ribosome dissociation in response to ribosome stalling by mediating deubiquitination of 40S ribosomal proteins RPS2/us5, RPS3/us3 and RPS10/eS10, thereby preventing their degradation by the proteasome (PubMed:31981475, PubMed:34348161, PubMed:34469731). Part of a ribosome quality control that takes place when ribosomes have stalled during translation initiation (iRQC): USP10 acts by removing monoubiquitination of RPS2/us5 and RPS3/us3, promoting 40S ribosomal subunit recycling (PubMed:34469731). Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling (PubMed:19398555). Involved in a TANK-dependent negative feedback response to attenuate NF-kappa-B activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (PubMed:25861989). Deubiquitinates TBX21 leading to its stabilization (PubMed:24845384). Plays a negative role in the RLR signaling pathway upon RNA virus infection by blocking the RIGI- mediated MAVS activation. Mechanistically, removes the unanchored 'Lys- 63'-linked polyubiquitin chains of MAVS to inhibit its aggregation, essential for its activation (PubMed:37582970). Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence= Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP10 and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34- containing complexes. Found in a deubiquitination complex with TANK, USP10 and ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta (IL1B)-mediated NF-kappa-B activation by promoting IKBKG or TRAF6 deubiquitination (PubMed:25861989). Interacts with IKBKG; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with TANK; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with TRAF6; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with ZC3H12A; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with G3BP1 (via NTF2 domain) and G3BP2 (via NTF2 domain); inhibiting stress granule formation (PubMed:11439350, PubMed:23279204, PubMed:27022092, PubMed:32302570, PubMed:31981475, PubMed:36183834, PubMed:36279435). Q14694; P13569: CFTR; NbExp=7; IntAct=EBI-2510389, EBI-349854; Q14694; Q13283: G3BP1; NbExp=13; IntAct=EBI-2510389, EBI-1047359; Q14694; Q9UN86: G3BP2; NbExp=10; IntAct=EBI-2510389, EBI-1044298; Q14694; Q9UN86-2: G3BP2; NbExp=3; IntAct=EBI-2510389, EBI-11035716; Q14694; P14136: GFAP; NbExp=3; IntAct=EBI-2510389, EBI-744302; Q14694; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2510389, EBI-1055254; Q14694; P63244: RACK1; NbExp=3; IntAct=EBI-2510389, EBI-296739; Q14694; Q5D1E8: ZC3H12A; NbExp=5; IntAct=EBI-2510389, EBI-747793; Cytoplasm cleus rly endosome Note=Cytoplasmic in normal conditions (PubMed:20096447). After DNA damage, translocates to the nucleus following phosphorylation by ATM (PubMed:20096447). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q14694-1; Sequence=Displayed; Name=2; IsoId=Q14694-2; Sequence=VSP_038869; Name=3; IsoId=Q14694-3; Sequence=VSP_038868; Widely expressed. Following DNA damage. Down-regulated in renal cell carcinomas. Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus. Ubiquitinated. Deubiquitinated by USP13. Belongs to the peptidase C19 family. USP10 subfamily. Sequence=CAD97644.1; Type=Erroneous initiation; Evidence=; p53 binding RNA binding cysteine-type endopeptidase activity thiol-dependent ubiquitin-specific protease activity protein binding nucleus nucleoplasm cytoplasm endosome early endosome cytosol DNA repair proteolysis ubiquitin-dependent protein catabolic process autophagy cellular response to DNA damage stimulus peptidase activity cysteine-type peptidase activity regulation of autophagy protein deubiquitination hydrolase activity translesion synthesis DNA damage response, signal transduction by p53 class mediator macromolecular complex thiol-dependent ubiquitinyl hydrolase activity negative regulation of I-kappaB kinase/NF-kappaB signaling ion channel binding cellular response to interleukin-1 uc002fii.1 uc002fii.2 uc002fii.3 uc002fii.4 uc002fii.5 
ENST00000219476.9 TSC2 ENST00000219476.9 TSC complex subunit 2, transcript variant 26 (from RefSeq NM_001406680.1) A7E2E2 B4DIL8 B4DIQ7 B4DRN2 B7Z2B8 C9J378 ENST00000219476.1 ENST00000219476.2 ENST00000219476.3 ENST00000219476.4 ENST00000219476.5 ENST00000219476.6 ENST00000219476.7 ENST00000219476.8 NM_001406680 O75275 P49815 Q4LE71 Q8TAZ1 TSC2 TSC2_HUMAN TSC4 uc002con.1 uc002con.2 uc002con.3 uc002con.4 uc002con.5 uc002con.6 Catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:12842888, PubMed:28215400, PubMed:35772404, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:33436626). Within the TSC-TBC complex, TSC2 acts as a GTPase- activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12172553, PubMed:12906785, PubMed:12842888, PubMed:15340059, PubMed:12820960, PubMed:22819219, PubMed:24529379, PubMed:33436626). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:12842888, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:35772404). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also stimulates the intrinsic GTPase activity of the Ras- related proteins RAP1A and RAB5 (By similarity). Component of the TSC-TBC complex (also named Rhebulator complex), composed of 2 molecules of TSC1, 2 molecules of TSC2 and 1 molecule of TBC1D7 (PubMed:10585443, PubMed:12172553, PubMed:12906785, PubMed:12842888, PubMed:28215400, PubMed:9580671, PubMed:15963462, PubMed:22795129, PubMed:24529379, PubMed:33436626). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co- chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex thereby stabilizing TSC2 (PubMed:29127155). Interacts with TSC1 and HERC1; the interaction with TSC1 stabilizes TSC2 and prevents the interaction with HERC1 (PubMed:16464865). May also interact with the adapter molecule RABEP1 (PubMed:9045618). The final complex may contain TSC2 and RABEP1 linked to RAB5 (PubMed:9045618). Interacts with HSPA1 and HSPA8 (PubMed:15963462). Interacts with NAA10 (via C-terminal domain) (PubMed:20145209). Interacts with RRAGA (polyubiquitinated) (PubMed:25936802). Interacts with WDR45B (PubMed:28561066). Interacts with RPAP3 and URI1 (PubMed:28561026). Interacts with YWHAG (PubMed:33473107). (Microbial infection) Interacts with human cytomegalovirus protein UL38; this interaction inhibits cellular stress response mediated by mTORC1. P49815; Q9NRD5: PICK1; NbExp=2; IntAct=EBI-396587, EBI-79165; P49815; P62136: PPP1CA; NbExp=2; IntAct=EBI-396587, EBI-357253; P49815; O00141: SGK1; NbExp=4; IntAct=EBI-396587, EBI-1042854; P49815; Q96EB6: SIRT1; NbExp=2; IntAct=EBI-396587, EBI-1802965; P49815; Q92574: TSC1; NbExp=13; IntAct=EBI-396587, EBI-1047085; P49815; P31946: YWHAB; NbExp=6; IntAct=EBI-396587, EBI-359815; P49815; P63104: YWHAZ; NbExp=8; IntAct=EBI-396587, EBI-347088; Lysosome membrane ; Peripheral membrane protein Cytoplasm, cytosol Note=Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients (PubMed:24529379). In response to insulin signaling and phosphorylation by PKB/AKT1, the complex dissociates from lysosomal membranes and relocalizes to the cytosol (PubMed:24529379). Event=Alternative splicing; Named isoforms=8; Name=1; IsoId=P49815-1; Sequence=Displayed; Name=2; IsoId=P49815-2; Sequence=VSP_004470; Name=3; IsoId=P49815-3; Sequence=VSP_004471; Name=4; IsoId=P49815-4; Sequence=VSP_004472; Name=5; IsoId=P49815-5; Sequence=VSP_004471, VSP_004472; Name=6; IsoId=P49815-6; Sequence=VSP_038355, VSP_004470, VSP_004472; Name=7; IsoId=P49815-7; Sequence=VSP_054163, VSP_004470, VSP_004472; Name=8; Synonyms=H, I; IsoId=P49815-8; Sequence=VSP_055896, VSP_055897; Liver, brain, heart, lymphocytes, fibroblasts, biliary epithelium, pancreas, skeletal muscle, kidney, lung and placenta. Phosphorylation at Ser-939 and Thr-1462 by PKB/AKT1 in response to insulin signaling and growth factor stimulation inhibits the ability of the TSC-TBC complex to suppress mTORC1 signaling: phosphorylation promotes dissociation of the TSC-TBC complex from lysosomal membranes, leading to activation of mTORC1 by RHEB (PubMed:12150915, PubMed:12172553, PubMed:24529379). Phosphorylation at Ser-1387, Ser- 1418 or Ser-1420 does not affect interaction with TSC1 (PubMed:15963462). Phosphorylation by AMPK activates it and leads to negative regulation of the mTORC1 complex (PubMed:14651849). Phosphorylated at Ser-1798 by RPS6KA1; phosphorylation inhibits TSC2 ability to suppress mTORC1 signaling (PubMed:15342917). Phosphorylated by DAPK1 (PubMed:18974095). Ubiquitinated by the DCX(FBXW5) E3 ubiquitin-protein ligase complex, leading to its subsequent degradation (PubMed:18381890, PubMed:27278822). Ubiquitinated by MYCBP2 independently of its phosphorylation status leading to subsequent degradation; association with TSC1 protects from ubiquitination (PubMed:18308511). Tuberous sclerosis 2 (TSC2) [MIM:613254]: An autosomal dominant multi-system disorder that affects especially the brain, kidneys, heart, and skin. It is characterized by hamartomas (benign overgrowths predominantly of a cell or tissue type that occurs normally in the organ) and hamartias (developmental abnormalities of tissue combination). Clinical manifestations include epilepsy, learning difficulties, behavioral problems, and skin lesions. Seizures can be intractable and premature death can occur from a variety of disease- associated causes. te=The disease is caused by variants affecting the gene represented in this entry. Lymphangioleiomyomatosis (LAM) [MIM:606690]: Progressive and often fatal lung disease characterized by a diffuse proliferation of abnormal smooth muscle cells in the lungs. It affects almost exclusively young women and can occur as an isolated disorder or in association with tuberous sclerosis complex. Note=The disease is caused by variants affecting the gene represented in this entry. Focal cortical dysplasia 2 (FCORD2) [MIM:607341]: A form of focal cortical dysplasia, a malformation of cortical development that results in medically refractory epilepsy in the pediatric population and in adults. FCORD2 is a severe form, with onset usually in childhood, characterized by disrupted cortical lamination and specific cytological abnormalities. It is classified in 2 subtypes: type IIA characterized by dysmorphic neurons and lack of balloon cells; type IIB with dysmorphic neurons and balloon cells. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 8]: May be due to an intron retention. Sequence=BAE06082.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/184/TSC2"; Name=Tuberous sclerosis database Tuberous sclerosis 2 (TSC2); Note=Leiden Open Variation Database (LOVD); URL="https://databases.lovd.nl/shared/genes/TSC2"; neural tube closure GTPase activator activity protein binding nucleus cytoplasm lysosome Golgi apparatus cytosol negative regulation of protein kinase activity protein import into nucleus endocytosis heart development protein localization negative regulation of cell proliferation negative regulation of phosphatidylinositol 3-kinase signaling postsynaptic density membrane viral process vesicle-mediated transport positive regulation of macroautophagy phosphatase binding regulation of endocytosis negative regulation of Wnt signaling pathway small GTPase binding negative regulation of TOR signaling TSC1-TSC2 complex protein homodimerization activity anoikis protein kinase B signaling positive regulation of GTPase activity regulation of insulin receptor signaling pathway negative regulation of insulin receptor signaling pathway insulin-like growth factor receptor signaling pathway perinuclear region of cytoplasm positive chemotaxis regulation of small GTPase mediated signal transduction regulation of cell cycle Hsp90 protein binding negative regulation of protein kinase B signaling negative regulation of macromitophagy uc002con.1 uc002con.2 uc002con.3 uc002con.4 uc002con.5 uc002con.6 
ENST00000219478.11 ZNF500 ENST00000219478.11 zinc finger protein 500, transcript variant 1 (from RefSeq NM_021646.4) A8K6X7 B4DNN9 ENST00000219478.1 ENST00000219478.10 ENST00000219478.2 ENST00000219478.3 ENST00000219478.4 ENST00000219478.5 ENST00000219478.6 ENST00000219478.7 ENST00000219478.8 ENST00000219478.9 KIAA0557 NM_021646 O60304 Q0VAL2 Q96CQ8 Q9BTG0 ZKSCAN18 ZN500_HUMAN uc002cxp.1 uc002cxp.2 uc002cxp.3 May be involved in transcriptional regulation. O60304; O95363: FARS2; NbExp=3; IntAct=EBI-18234077, EBI-2513774; O60304; P14136: GFAP; NbExp=3; IntAct=EBI-18234077, EBI-744302; O60304; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-18234077, EBI-5460660; O60304; O43464: HTRA2; NbExp=3; IntAct=EBI-18234077, EBI-517086; O60304; P42858: HTT; NbExp=6; IntAct=EBI-18234077, EBI-466029; O60304; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-18234077, EBI-1055254; O60304; O43189: PHF1; NbExp=3; IntAct=EBI-18234077, EBI-530034; O60304; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-18234077, EBI-5235340; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O60304-1; Sequence=Displayed; Name=2; IsoId=O60304-2; Sequence=VSP_055962; Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=BAA25483.1; Type=Erroneous initiation; Evidence=; nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus nucleoplasm cytosol regulation of transcription, DNA-templated metal ion binding uc002cxp.1 uc002cxp.2 uc002cxp.3 
ENST00000219479.7 NME4 ENST00000219479.7 NME/NM23 nucleoside diphosphate kinase 4, transcript variant 1 (from RefSeq NM_005009.3) A2IDD0 ENST00000219479.1 ENST00000219479.2 ENST00000219479.3 ENST00000219479.4 ENST00000219479.5 ENST00000219479.6 NDKM_HUMAN NM23D NME4 NM_005009 O00746 Q5U0M9 uc002cgz.1 uc002cgz.2 uc002cgz.3 uc002cgz.4 uc002cgz.5 The nucleoside diphosphate (NDP) kinases (EC 2.7.4.6) are ubiquitous enzymes that catalyze transfer of gamma-phosphates, via a phosphohistidine intermediate, between nucleoside and dioxynucleoside tri- and diphosphates. The enzymes are products of the nm23 gene family, which includes NME4 (Milon et al., 1997 [PubMed 9099850]).[supplied by OMIM, May 2008]. Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis (PubMed:10799505). Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity (PubMed:18635542, PubMed:23150663). Acts as a mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration (PubMed:18635542). Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria (PubMed:24970086). In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (PubMed:18635542, PubMed:17028143, PubMed:23150663). Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence=; Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence=; Reaction=a cardiolipin(in) = a cardiolipin(out); Xref=Rhea:RHEA:38695, ChEBI:CHEBI:62237; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38696; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Binding to anionic phospholipids, predominantly to cardiolipin inhibits its phosphotransfer activity. Homohexamer (PubMed:10799505). Interacts with OPA1 (PubMed:23150663). Interacts with CAPN8 (By similarity). O00746; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-744871, EBI-11096309; O00746; P01019: AGT; NbExp=3; IntAct=EBI-744871, EBI-751728; O00746; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-744871, EBI-8643161; O00746; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-744871, EBI-742909; O00746; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-744871, EBI-1166928; O00746; P54253: ATXN1; NbExp=6; IntAct=EBI-744871, EBI-930964; O00746; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-744871, EBI-2837444; O00746; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-744871, EBI-725606; O00746; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-744871, EBI-12011224; O00746; Q9NP86: CABP5; NbExp=3; IntAct=EBI-744871, EBI-10311131; O00746; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-744871, EBI-10171570; O00746; Q2TAC2-2: CCDC57; NbExp=5; IntAct=EBI-744871, EBI-10961624; O00746; P55273: CDKN2D; NbExp=3; IntAct=EBI-744871, EBI-745859; O00746; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-744871, EBI-749051; O00746; Q99828: CIB1; NbExp=3; IntAct=EBI-744871, EBI-372594; O00746; Q96Q77: CIB3; NbExp=3; IntAct=EBI-744871, EBI-10292696; O00746; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-744871, EBI-7062247; O00746; Q86UW9: DTX2; NbExp=3; IntAct=EBI-744871, EBI-740376; O00746; P02042: HBD; NbExp=3; IntAct=EBI-744871, EBI-6152722; O00746; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-744871, EBI-12094670; O00746; O75031: HSF2BP; NbExp=3; IntAct=EBI-744871, EBI-7116203; O00746; P42858: HTT; NbExp=20; IntAct=EBI-744871, EBI-466029; O00746; P03952: KLKB1; NbExp=3; IntAct=EBI-744871, EBI-10087153; O00746; P61968: LMO4; NbExp=3; IntAct=EBI-744871, EBI-2798728; O00746; P06858: LPL; NbExp=3; IntAct=EBI-744871, EBI-715909; O00746; Q13064: MKRN3; NbExp=3; IntAct=EBI-744871, EBI-2340269; O00746; P40692: MLH1; NbExp=3; IntAct=EBI-744871, EBI-744248; O00746; P15531: NME1; NbExp=11; IntAct=EBI-744871, EBI-741141; O00746; P22392: NME2; NbExp=5; IntAct=EBI-744871, EBI-713693; O00746; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-744871, EBI-744782; O00746; P61970: NUTF2; NbExp=3; IntAct=EBI-744871, EBI-591778; O00746; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-744871, EBI-398874; O00746; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-744871, EBI-721769; O00746; O15160: POLR1C; NbExp=5; IntAct=EBI-744871, EBI-1055079; O00746; P20618: PSMB1; NbExp=3; IntAct=EBI-744871, EBI-372273; O00746; P37840: SNCA; NbExp=3; IntAct=EBI-744871, EBI-985879; O00746; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-744871, EBI-742688; O00746; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-744871, EBI-740595; O00746; Q13148: TARDBP; NbExp=6; IntAct=EBI-744871, EBI-372899; O00746; O14656-2: TOR1A; NbExp=3; IntAct=EBI-744871, EBI-25847109; O00746; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-744871, EBI-11961968; O00746; Q15645: TRIP13; NbExp=4; IntAct=EBI-744871, EBI-358993; O00746; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-744871, EBI-3918381; O00746; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-744871, EBI-948354; O00746; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-744871, EBI-607755; O00746; P40337-2: VHL; NbExp=3; IntAct=EBI-744871, EBI-12157263; O00746; Q05516: ZBTB16; NbExp=3; IntAct=EBI-744871, EBI-711925; Mitochondrion intermembrane space ; Peripheral membrane protein. Mitochondrion matrix Note=Predominantly localized in the mitochondrion intermembrane space (PubMed:18635542). Colocalizes with OPA1 in mitochondria (PubMed:24970086). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O00746-1; Sequence=Displayed; Name=2; IsoId=O00746-2; Sequence=VSP_054743; Widely distributed. Found at very high levels in prostate, heart, liver, small intestine, and skeletal muscle tissues, and in low amounts in the brain and in blood leukocytes. Belongs to the NDK family. nucleotide binding nucleoside diphosphate kinase activity protein binding ATP binding mitochondrion mitochondrial inner membrane mitochondrial intermembrane space mitochondrial matrix purine nucleotide metabolic process nucleoside diphosphate phosphorylation GTP biosynthetic process pyrimidine nucleotide metabolic process UTP biosynthetic process CTP biosynthetic process lipid transport lipid binding nucleoside metabolic process nucleotide metabolic process nucleobase-containing small molecule interconversion membrane kinase activity phosphorylation transferase activity metal ion binding cardiolipin binding uc002cgz.1 uc002cgz.2 uc002cgz.3 uc002cgz.4 uc002cgz.5 
ENST00000219481.10 DECR2 ENST00000219481.10 2,4-dienoyl-CoA reductase 2 (from RefSeq NM_020664.4) DECR2_HUMAN ENST00000219481.1 ENST00000219481.2 ENST00000219481.3 ENST00000219481.4 ENST00000219481.5 ENST00000219481.6 ENST00000219481.7 ENST00000219481.8 ENST00000219481.9 NM_020664 PDCR Q6ZRS7 Q96ET0 Q9NUI1 SDR17C1 uc002chb.1 uc002chb.2 uc002chb.3 uc002chb.4 uc002chb.5 Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid. Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099, ChEBI:CHEBI:85493; EC=1.3.1.124; Evidence=; Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101, ChEBI:CHEBI:85493; EC=1.3.1.124; Evidence=; Reaction=(2E,4Z,7Z,10Z,13Z,16Z,19Z)-docosaheptaenoyl-CoA + H(+) + NADPH = (3E,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + NADP(+); Xref=Rhea:RHEA:44920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77559, ChEBI:CHEBI:84791; Evidence=; Kinetic parameters: KM=59 uM for 2,4-hexadienoyl-CoA ; KM=6 uM for 2,4-decadienoyl-CoA ; KM=102 uM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA ; KM=71.6 uM for 2,4-hexadienoyl CoA ; KM=2.4 uM for 2,4-decadienoyl CoA ; Vmax=1.75 umol/min/mg enzyme toward 2,4-hexadienoyl CoA ; Vmax=1.37 umol/min/mg enzyme toward 2,4-decadienoyl CoA ; Monomer, dimer and oligomer. Q9NUI1; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-3937367, EBI-725606; Q9NUI1; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-3937367, EBI-9057006; Q9NUI1; P51784: USP11; NbExp=3; IntAct=EBI-3937367, EBI-306876; Q9NUI1; O14972: VPS26C; NbExp=3; IntAct=EBI-3937367, EBI-7207091; Peroxisome Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NUI1-1; Sequence=Displayed; Name=2; IsoId=Q9NUI1-2; Sequence=VSP_013630, VSP_013631, VSP_013632; Name=3; IsoId=Q9NUI1-3; Sequence=VSP_013629; Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily. peroxisome peroxisomal membrane cytosol protein targeting to peroxisome lipid metabolic process fatty acid metabolic process unsaturated fatty acid biosynthetic process 2,4-dienoyl-CoA reductase (NADPH) activity oxidoreductase activity trans-2-enoyl-CoA reductase (NADPH) activity fatty acid beta-oxidation using acyl-CoA oxidase oxidation-reduction process uc002chb.1 uc002chb.2 uc002chb.3 uc002chb.4 uc002chb.5 
ENST00000219548.9 STUB1 ENST00000219548.9 STIP1 homology and U-box containing protein 1, transcript variant 1 (from RefSeq NM_005861.4) A2IDB9 CHIP CHIP_HUMAN ENST00000219548.1 ENST00000219548.2 ENST00000219548.3 ENST00000219548.4 ENST00000219548.5 ENST00000219548.6 ENST00000219548.7 ENST00000219548.8 NM_005861 O60526 PP1131 Q969U2 Q9HBT1 Q9UNE7 STUB1 uc002cit.1 uc002cit.2 uc002cit.3 uc002cit.4 uc002cit.5 This gene encodes a protein containing tetratricopeptide repeat and a U-box that functions as a ubiquitin ligase/cochaperone. The encoded protein binds to and ubiquitinates shock cognate 71 kDa protein (Hspa8) and DNA polymerase beta (Polb), among other targets. Mutations in this gene cause spinocerebellar ataxia, autosomal recessive 16. Alternative splicing results in multiple transcript variants. There is a pseudogene for this gene on chromosome 2. [provided by RefSeq, Jun 2014]. E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 (PubMed:15466472). Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 (PubMed:10330192, PubMed:11146632, PubMed:15466472). Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation (PubMed:11557750, PubMed:23990462). Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome (PubMed:19713937). Mediates polyubiquitination of CYP3A4 (PubMed:19103148). Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation (PubMed:19567782). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome (PubMed:24043303). Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD- L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity (PubMed:28813410). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed:29883609). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence= Protein modification; protein ubiquitination. Homodimer (By similarity). Interacts with BAG2 (PubMed:16169850). Interacts with E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (PubMed:11557750). Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1 (PubMed:15215316). Interacts with MKKS (PubMed:18094050). Interacts with DNAAF4 (PubMed:19423554). Interacts (when monoubiquitinated) with ATXN3. Interacts with UBE2W. Interacts (via the U-box domain) with the UBE2V2- UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity (By similarity). Interacts with DNAJB6 (PubMed:22366786). Interacts with FLCN (PubMed:27353360). Interacts with HSP90AA1 (PubMed:27353360, PubMed:24613385). Interacts with HSP90 (PubMed:11146632). Interacts with UBE2N and UBE2V1 (PubMed:16307917). Interacts (via TPR repeats) with the C-terminal domain of HSPA1A (PubMed:10330192). Interacts with the non-acetylated form of HSPA1A and HSPA1B (PubMed:27708256). Interacts (via TPR repeats) with the C- terminal domain of HSPA8 (PubMed:10330192, PubMed:11557750, PubMed:23990462, PubMed:27708256). Interacts with SMAD3 and HSP90AB1 (PubMed:24613385). Interacts with UBE4B (PubMed:17369820). Interacts with PRMT5 (PubMed:33376131). Q9UNE7; P01023: A2M; NbExp=3; IntAct=EBI-357085, EBI-640741; Q9UNE7; Q96AP0: ACD; NbExp=2; IntAct=EBI-357085, EBI-717666; Q9UNE7; P61158: ACTR3; NbExp=3; IntAct=EBI-357085, EBI-351428; Q9UNE7; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-357085, EBI-25928834; Q9UNE7; Q86WG3: ATCAY; NbExp=4; IntAct=EBI-357085, EBI-1783328; Q9UNE7; Q99933: BAG1; NbExp=2; IntAct=EBI-357085, EBI-1030678; Q9UNE7; O95816: BAG2; NbExp=4; IntAct=EBI-357085, EBI-355275; Q9UNE7; O95817: BAG3; NbExp=3; IntAct=EBI-357085, EBI-747185; Q9UNE7; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-357085, EBI-11532900; Q9UNE7; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-357085, EBI-1383687; Q9UNE7; Q9NRJ3: CCL28; NbExp=3; IntAct=EBI-357085, EBI-7783254; Q9UNE7; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-357085, EBI-1045797; Q9UNE7; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-357085, EBI-25836642; Q9UNE7; P21964-2: COMT; NbExp=3; IntAct=EBI-357085, EBI-10200977; Q9UNE7; Q15438: CYTH1; NbExp=3; IntAct=EBI-357085, EBI-997830; Q9UNE7; P53355: DAPK1; NbExp=2; IntAct=EBI-357085, EBI-358616; Q9UNE7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-357085, EBI-10976677; Q9UNE7; Q8WXU2-2: DNAAF4; NbExp=3; IntAct=EBI-357085, EBI-9381887; Q9UNE7; A0AVK6: E2F8; NbExp=3; IntAct=EBI-357085, EBI-7779316; Q9UNE7; P00533: EGFR; NbExp=4; IntAct=EBI-357085, EBI-297353; Q9UNE7; O00471: EXOC5; NbExp=3; IntAct=EBI-357085, EBI-949824; Q9UNE7; O75344: FKBP6; NbExp=3; IntAct=EBI-357085, EBI-744771; Q9UNE7; Q9BZS1: FOXP3; NbExp=7; IntAct=EBI-357085, EBI-983719; Q9UNE7; P06241: FYN; NbExp=3; IntAct=EBI-357085, EBI-515315; Q9UNE7; P22466: GAL; NbExp=3; IntAct=EBI-357085, EBI-6624768; Q9UNE7; Q53GS7: GLE1; NbExp=3; IntAct=EBI-357085, EBI-1955541; Q9UNE7; P28799: GRN; NbExp=3; IntAct=EBI-357085, EBI-747754; Q9UNE7; P07900: HSP90AA1; NbExp=9; IntAct=EBI-357085, EBI-296047; Q9UNE7; P08238: HSP90AB1; NbExp=5; IntAct=EBI-357085, EBI-352572; Q9UNE7; P08107: HSPA1B; NbExp=5; IntAct=EBI-357085, EBI-629985; Q9UNE7; P11142: HSPA8; NbExp=8; IntAct=EBI-357085, EBI-351896; Q9UNE7; P04792: HSPB1; NbExp=4; IntAct=EBI-357085, EBI-352682; Q9UNE7; P42858: HTT; NbExp=12; IntAct=EBI-357085, EBI-466029; Q9UNE7; P02545: LMNA; NbExp=3; IntAct=EBI-357085, EBI-351935; Q9UNE7; Q07954-2: LRP1; NbExp=3; IntAct=EBI-357085, EBI-25833471; Q9UNE7; Q5S007: LRRK2; NbExp=4; IntAct=EBI-357085, EBI-5323863; Q9UNE7; Q9Y2U5: MAP3K2; NbExp=9; IntAct=EBI-357085, EBI-357393; Q9UNE7; P10636: MAPT; NbExp=2; IntAct=EBI-357085, EBI-366182; Q9UNE7; Q15773: MLF2; NbExp=3; IntAct=EBI-357085, EBI-1051875; Q9UNE7; P00540: MOS; NbExp=2; IntAct=EBI-357085, EBI-1757866; Q9UNE7; P05164: MPO; NbExp=3; IntAct=EBI-357085, EBI-2556173; Q9UNE7; P13591: NCAM1; NbExp=3; IntAct=EBI-357085, EBI-2846607; Q9UNE7; P35240: NF2; NbExp=3; IntAct=EBI-357085, EBI-1014472; Q9UNE7; P08138: NGFR; NbExp=3; IntAct=EBI-357085, EBI-1387782; Q9UNE7; Q96PB7: OLFM3; NbExp=4; IntAct=EBI-357085, EBI-10292253; Q9UNE7; Q96PB7-3: OLFM3; NbExp=3; IntAct=EBI-357085, EBI-12005356; Q9UNE7; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-357085, EBI-25929070; Q9UNE7; O00628-2: PEX7; NbExp=3; IntAct=EBI-357085, EBI-25882083; Q9UNE7; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-357085, EBI-9090282; Q9UNE7; P17612: PRKACA; NbExp=3; IntAct=EBI-357085, EBI-476586; Q9UNE7; O60260-5: PRKN; NbExp=6; IntAct=EBI-357085, EBI-21251460; Q9UNE7; P51149: RAB7A; NbExp=3; IntAct=EBI-357085, EBI-1056089; Q9UNE7; P04049: RAF1; NbExp=8; IntAct=EBI-357085, EBI-365996; Q9UNE7; Q14257: RCN2; NbExp=3; IntAct=EBI-357085, EBI-356710; Q9UNE7; O95072: REC8; NbExp=2; IntAct=EBI-357085, EBI-9361206; Q9UNE7; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-357085, EBI-3918154; Q9UNE7; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-357085, EBI-6257312; Q9UNE7; Q15019-2: SEPTIN2; NbExp=3; IntAct=EBI-357085, EBI-10983222; Q9UNE7; P01011: SERPINA3; NbExp=3; IntAct=EBI-357085, EBI-296557; Q9UNE7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-357085, EBI-5235340; Q9UNE7; O15269-2: SPTLC1; NbExp=3; IntAct=EBI-357085, EBI-25912901; Q9UNE7; Q13501: SQSTM1; NbExp=3; IntAct=EBI-357085, EBI-307104; Q9UNE7; Q86WV8: TSC1; NbExp=3; IntAct=EBI-357085, EBI-12806590; Q9UNE7; Q99757: TXN2; NbExp=3; IntAct=EBI-357085, EBI-2932492; Q9UNE7; P68036: UBE2L3; NbExp=3; IntAct=EBI-357085, EBI-711173; Q9UNE7; P61088: UBE2N; NbExp=5; IntAct=EBI-357085, EBI-1052908; Q9UNE7; Q7Z7E8: UBE2Q1; NbExp=3; IntAct=EBI-357085, EBI-1783287; Q9UNE7; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-357085, EBI-11141397; Q9UNE7; O76024: WFS1; NbExp=3; IntAct=EBI-357085, EBI-720609; Q9UNE7; Q5QJC9: Bag5; Xeno; NbExp=5; IntAct=EBI-357085, EBI-1374246; Q9UNE7; P12504: vif; Xeno; NbExp=2; IntAct=EBI-357085, EBI-779991; Q9UNE7-1; P31749: AKT1; NbExp=5; IntAct=EBI-15687717, EBI-296087; Q9UNE7-1; P11142-1: HSPA8; NbExp=4; IntAct=EBI-15687717, EBI-351908; Q9UNE7-1; Q5S007: LRRK2; NbExp=2; IntAct=EBI-15687717, EBI-5323863; Q9UNE7-1; P10636: MAPT; NbExp=5; IntAct=EBI-15687717, EBI-366182; Cytoplasm cleus Note=Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UNE7-1; Sequence=Displayed; Name=2; IsoId=Q9UNE7-2; Sequence=VSP_015947; Expressed in differentiated myotubes (at protein level) (PubMed:17369820). Highly expressed in skeletal muscle, heart, pancreas, brain and placenta (PubMed:10330192, PubMed:11435423). Detected in kidney, liver and lung (PubMed:10330192, PubMed:11435423). Up-regulated by inflammatory signals in regulatory T-cells (Treg). The U-box domain is required for the ubiquitin protein ligase activity. The TPR domain is essential for ubiquitination mediated by UBE2D1. Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 (By similarity). Auto- ubiquitinated; mediated by UBE2D1 and UBE2D2. Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16) [MIM:615768]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR16 is characterized by truncal and limb ataxia resulting in gait instability. Additionally, patients may show dysarthria, nystagmus, spasticity of the lower limbs, and mild peripheral sensory neuropathy. te=The disease is caused by variants affecting the gene represented in this entry. Spinocerebellar ataxia 48 (SCA48) [MIM:618093]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA48 is an autosomal dominant neurodegenerative disease characterized by onset in mid-adulthood of progressive cognitive decline and gait ataxia, and vermian and hemispheric cerebellar atrophy. Note=The disease is caused by variants affecting the gene represented in this entry. Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients. ubiquitin ligase complex protein polyubiquitination G-protein coupled receptor binding response to ischemia ubiquitin-protein transferase activity protein binding nucleus nucleoplasm cytoplasm endoplasmic reticulum cytosol DNA repair ubiquitin-dependent protein catabolic process misfolded or incompletely synthesized protein catabolic process cellular response to DNA damage stimulus protein ubiquitination transferase activity enzyme binding kinase binding Z disc ER-associated ubiquitin-dependent protein catabolic process negative regulation of transforming growth factor beta receptor signaling pathway Hsp70 protein binding ubiquitin-dependent SMAD protein catabolic process protein binding, bridging TPR domain binding endoplasmic reticulum unfolded protein response heat shock protein binding ubiquitin conjugating enzyme complex positive regulation of protein ubiquitination ubiquitin protein ligase binding regulation of protein stability regulation of glucocorticoid metabolic process negative regulation of protein binding positive regulation of proteasomal ubiquitin-dependent protein catabolic process ubiquitin-ubiquitin ligase activity cellular response to heat ERBB2 signaling pathway nuclear inclusion body protein homodimerization activity proteasome-mediated ubiquitin-dependent protein catabolic process SMAD binding tau protein binding chaperone binding positive regulation of ubiquitin-protein transferase activity protein maturation misfolded protein binding protein autoubiquitination Hsp90 protein binding ubiquitin protein ligase activity chaperone-mediated autophagy protein K63-linked ubiquitination cellular response to misfolded protein cellular response to hypoxia positive regulation of chaperone-mediated protein complex assembly uc002cit.1 uc002cit.2 uc002cit.3 uc002cit.4 uc002cit.5 
ENST00000219596.6 MEFV ENST00000219596.6 MEFV innate immunity regulator, pyrin, transcript variant 1 (from RefSeq NM_000243.3) D3DUC0 ENST00000219596.1 ENST00000219596.2 ENST00000219596.3 ENST00000219596.4 ENST00000219596.5 F5H0Q3 MEF MEFV MEFV_HUMAN NM_000243 O15553 Q3MJ84 Q96PN4 Q96PN5 TRIM20 uc002cun.1 uc002cun.2 This gene encodes a protein, also known as pyrin or marenostrin, that is an important modulator of innate immunity. Mutations in this gene are associated with Mediterranean fever, a hereditary periodic fever syndrome. [provided by RefSeq, Jul 2008]. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923, PubMed:16037825, PubMed:27030597, PubMed:28835462, PubMed:16785446, PubMed:17431422, PubMed:26347139). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed:16785446, PubMed:17431422, PubMed:26347139). Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation (PubMed:16785446, PubMed:17431422, PubMed:26347139). However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production (PubMed:16037825, PubMed:27030597, PubMed:28835462). Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). Homotrimer. Interacts (via the B box-type zinc finger) with PSTPIP1 (PubMed:14595024, PubMed:17964261, PubMed:19109554, PubMed:28835462). Interacts (via the B30.2/SPRY domain) with several components of the inflammasome complex, including CASP1 p20 and p10 subunits, CASP5, PYCARD, NLRP1, NLRP2 and NLRP3, as well as with unprocessed IL1B; this interaction may lead to autophagic degradation of these proteins (PubMed:11498534, PubMed:16785446, PubMed:17431422, PubMed:17964261, PubMed:26347139). Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity). Interacts with NFKBIA and RELA (PubMed:18577712). Interacts weakly with VASP and ACTR3 (PubMed:19109554). Interacts with active ULK1 (phosphorylated on 'Ser- 317') and BECN1 simultaneously. Also interacts with ATG16L1 (via WD repeats), and with ATG8 family members, including GABARAP, GABARAPL1 and, to a lesser extent, GABARAPL2, MAP1LC3A/LC3A and MAP1LC3C/LC3C. Interacts with TRIM21 (PubMed:26347139, PubMed:28835462). Interacts with YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ; the interaction is required for the down-regulation of pyrin pro-inflammatory activity (PubMed:27030597, PubMed:28835462). O15553; P29466: CASP1; NbExp=2; IntAct=EBI-7644532, EBI-516667; O15553; O15553: MEFV; NbExp=8; IntAct=EBI-7644532, EBI-7644532; O15553; O43586: PSTPIP1; NbExp=4; IntAct=EBI-7644532, EBI-1050964; O15553; Q9ULZ3: PYCARD; NbExp=8; IntAct=EBI-7644532, EBI-751215; O15553-2; P29466: CASP1; NbExp=3; IntAct=EBI-15588296, EBI-516667; [Isoform 1]: Cytoplasm, cytoskeleton Cell projection, ruffle Cell projection, lamellipodium Nucleus Cytoplasm toplasmic vesicle, autophagosome Note=Associated with microtubules and with the filamentous actin of perinuclear filaments and peripheral lamellar ruffles (PubMed:11468188). In pre- apoptotic cells, colocalizes with PYCARD/ASC in large specks (inflammasomes) (PubMed:11468188). In migrating monocytes, strongly polarized at the leading edge of the cell where it colocalizes with polymerizing actin and PYCARD/ASC (PubMed:11468188). [Isoform 2]: Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=FL; IsoId=O15553-2; Sequence=Displayed; Name=2; Synonyms=D2; IsoId=O15553-1; Sequence=VSP_008223; Name=3; IsoId=O15553-3; Sequence=VSP_008223, VSP_047663; Expressed in peripheral blood leukocytes, particularly in mature granulocytes and to a lesser extent in monocytes but not in lymphocytes. Detected in spleen, lung and muscle, probably as a result of leukocyte infiltration in these tissues. Not expressed in thymus, prostate, testis, ovary, small intestine, colon, heart, brain, placenta, liver, kidney, pancreas. Expression detected in several myeloid leukemic, colon cancer, and prostate cancer cell lines. First detected in bone marrow promyelocytes. Expression increases throughout myelocyte differentiation and peaks in the mature myelomonocytic cells. In monocytes, up-regulated by treatment with colchicine and IFN-alpha, by the pro-inflammatory cytokines IFNG/IFN-gamma and TNF, by bacterial lipopolysaccharides (LPS) and by retroviral infection. Repressed in monocytes by the anti-inflammatory cytokines IL10/interleukin-10, TGFB1 and IL4/interleukin-4. In neutrophils and macrophages, up-regulated by IFNG/IFN-gamma with a peak after 8 hours of treatment. The B box-type zinc finger interacts, possibly intramolecularly, with the pyrin domain; this may be an autoinhibitory mechanism released by PSTPIP1 binding. Cleaved by CASP1 (Probable). The N-terminal cleavage product localizes to the nucleus as a filamentous network and to the cytoplasm, interacts more strongly with RELA and NFKBIA than the full-length protein, enhances the nuclear localization of RELA and induces NFKBIA proteolysis. The C-terminal cleavage product localizes to the cytoplasm (Probable). Phosphorylation at Ser-242 is required for the interaction with 14-3-3 proteins and down-regulation of pyrin pro-inflammatory activity. Degraded along with the delivery of its substrates to autolysosomal compartments (at protein level). Familial Mediterranean fever, autosomal recessive (ARFMF) [MIM:249100]: A hereditary periodic fever syndrome characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. It is frequently complicated by reactive amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. te=The disease is caused by variants affecting the gene represented in this entry. The disease-associated mutations in the B30.2/SPRY domain perturb ULK1 recruitment and autophagic degradation of inflammasome components, including NLRP3, and hence may contribute to the inflammatory phenotype associated with ARFMF. Familial Mediterranean fever, autosomal dominant (ADFMF) [MIM:134610]: A hereditary periodic fever syndrome characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with reactive renal amyloidosis and characterized by colchicine unresponsiveness. te=The disease is caused by variants affecting the gene represented in this entry. Pyrin-associated autoinflammatory disease (PAAND) [MIM:608068]: An autosomal dominant autoinflammatory disorder characterized by childhood onset of recurrent episodes of fever, neutrophilic dermatosis, myalgia and arthralgia. The neutrophilic dermatosis comprises a spectrum of clinical manifestations, including severe acne, sterile skin abscesses, pyoderma gangrenosum, and neutrophilic small-vessel vasculitis. Pathological examination of affected skin shows a dense, predominantly neutrophilic, vascular, perivascular, and interstitial infiltrate. PAAND has incomplete penetrance and variable expressivity. te=The disease is caused by variants affecting the gene represented in this entry. Name=INFEVERS; Note=Repertory of FMF and hereditary autoinflammatory disorders mutations; URL="https://infevers.umai-montpellier.fr/web/search.php?n=1"; ruffle immune system process actin binding protein binding nucleus cytoplasm autophagosome cytosol cytoskeleton microtubule microtubule associated complex inflammatory response zinc ion binding positive regulation of autophagy lamellipodium cytoplasmic vesicle negative regulation of interleukin-1 beta production negative regulation of interleukin-12 production response to interferon-gamma identical protein binding cell projection innate immune response metal ion binding negative regulation of inflammatory response negative regulation of macrophage inflammatory protein 1 alpha production negative regulation of cytokine production involved in inflammatory response negative regulation of NLRP3 inflammasome complex assembly positive regulation of cysteine-type endopeptidase activity uc002cun.1 uc002cun.2 
ENST00000219611.7 CAPN15 ENST00000219611.7 calpain 15 (from RefSeq NM_005632.3) B1B1M4 CAN15_HUMAN ENST00000219611.1 ENST00000219611.2 ENST00000219611.3 ENST00000219611.4 ENST00000219611.5 ENST00000219611.6 NM_005632 O75808 Q2KHS2 Q8WTY9 Q9BUW0 SOLH uc002chi.1 uc002chi.2 uc002chi.3 uc002chi.4 This gene encodes a protein containing zinc-finger-like repeats and a calpain-like protease domain. The encoded protein may function as a transcription factor, RNA-binding protein, or in protein-protein interactions during visual system development. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: U85647.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219611.7/ ENSP00000219611.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## O75808; Q15038: DAZAP2; NbExp=3; IntAct=EBI-6149008, EBI-724310; O75808; P28799: GRN; NbExp=3; IntAct=EBI-6149008, EBI-747754; O75808; P07686: HEXB; NbExp=3; IntAct=EBI-6149008, EBI-7133736; O75808; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-6149008, EBI-723313; O75808; Q12933: TRAF2; NbExp=3; IntAct=EBI-6149008, EBI-355744; O75808; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-6149008, EBI-947187; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75808-1; Sequence=Displayed; Name=2; IsoId=O75808-2; Sequence=VSP_023361, VSP_023362; Widely expressed with higher expression in brain. Oculogastrointestinal neurodevelopmental syndrome (OGIN) [MIM:619318]: An autosomal recessive neurodevelopmental disorder characterized by growth deficits, microcephaly, global developmental delay, hearing loss, and microphthalmia and/or coloboma. Other congenital anomalies include imperforate anus, horseshoe kidney, and structural cardiac defects. Some patients have been reported with normal motor and cognitive development. Note=The disease may be caused by variants affecting the gene represented in this entry. Belongs to the peptidase C2 family. calcium-dependent cysteine-type endopeptidase activity cytoplasm proteolysis peptidase activity cysteine-type peptidase activity hydrolase activity metal ion binding uc002chi.1 uc002chi.2 uc002chi.3 uc002chi.4 
ENST00000219660.6 AQP8 ENST00000219660.6 aquaporin 8 (from RefSeq NM_001169.3) AQP8 AQP8_HUMAN ENST00000219660.1 ENST00000219660.2 ENST00000219660.3 ENST00000219660.4 ENST00000219660.5 NM_001169 O94778 Q8IUU3 Q9UIA4 uc002doc.1 uc002doc.2 uc002doc.3 uc002doc.4 uc002doc.5 Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF067797.1, AB013456.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000219660.6/ ENSP00000219660.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Channel that allows the facilitated permeation of water and uncharged molecules, such as hydrogen peroxide and the neutral form of ammonia (NH3), through cellular membranes such as plasma membrane, inner mitochondrial membrane and endoplasmic reticulum membrane of several tissues (PubMed:26972385, PubMed:15948717, PubMed:18948439, PubMed:23541115, PubMed:29732408, PubMed:30579780). The transport of the ammonia neutral form induces a parallel transport of proton, at alkaline pH when the concentration of ammonia is high (By similarity). However, it is unclear whether the transport of proton takes place via the aquaporin or via an endogenous pathway (By similarity). Also, may transport ammonia analogs such as formamide and methylamine, a transport favourited at basic pH due to the increase of unprotonated (neutral) form, which is expected to favor diffusion (PubMed:15948717). Does not transport urea or glycerol (PubMed:15948717). The water transport mechanism is mercury- and copper-sensitive and passive in response to osmotic driving forces (PubMed:15948717). At the canicular plasma membrane, mediates the osmotic transport of water toward the bile canaliculus and facilitates the cAMP-induced bile canalicular water secretion, a process involved in bile formation (PubMed:18948439). In addition, mediates the hydrogen peroxide release from hepatocyte mitochondria that modulates the SREBF2-mediated cholesterol synthesis and facilitates the mitochondrial ammonia uptake which is metabolized into urea, mainly under glucagon stimulation (PubMed:30579780, PubMed:34292591). In B cells, transports the CYBB- generated hydrogen peroxide from the external leaflet of the plasma membrane to the cytosol to promote B cell activation and differentiation for signal amplification (By similarity). In the small intestine and colon system, mediates water transport through mitochondria and apical membrane of epithelial cells (By similarity). May play an important role in the adaptive response of proximal tubule cells to acidosis possibly by facilitating the mitochondrial ammonia transport (PubMed:22622463). Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377; Evidence= Reaction=H2O2(out) = H2O2(in); Xref=Rhea:RHEA:74375, ChEBI:CHEBI:16240; Evidence= Reaction=formamide(out) = formamide(in); Xref=Rhea:RHEA:74387, ChEBI:CHEBI:16397; Evidence=; Reaction=methylamine(out) = methylamine(in); Xref=Rhea:RHEA:74391, ChEBI:CHEBI:59338; Evidence=; Reversibly gated by a two-step sulfenylation- persulfidation process in cells undergoing diverse stresses. O94778; P46379-2: BAG6; NbExp=3; IntAct=EBI-19124986, EBI-10988864; O94778; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-19124986, EBI-2680384; O94778; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-19124986, EBI-12593112; O94778; P04792: HSPB1; NbExp=3; IntAct=EBI-19124986, EBI-352682; O94778; O60333-2: KIF1B; NbExp=3; IntAct=EBI-19124986, EBI-10975473; O94778; O14901: KLF11; NbExp=3; IntAct=EBI-19124986, EBI-948266; O94778; Q04941: PLP2; NbExp=3; IntAct=EBI-19124986, EBI-608347; O94778; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-19124986, EBI-11721828; O94778; P60891: PRPS1; NbExp=3; IntAct=EBI-19124986, EBI-749195; O94778; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-19124986, EBI-396669; O94778; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-19124986, EBI-10329948; O94778; Q86Y82: STX12; NbExp=3; IntAct=EBI-19124986, EBI-2691717; O94778; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-19124986, EBI-10171534; O94778; O76024: WFS1; NbExp=3; IntAct=EBI-19124986, EBI-720609; Cell membrane ; Multi-pass membrane protein Mitochondrion inner membrane ulti-pass membrane protein Apical cell membrane ulti-pass membrane protein Basolateral cell membrane ; Multi-pass membrane protein Smooth endoplasmic reticulum membrane ; Multi-pass membrane protein Note=Localized at the hepatocyte canalicular plasma membrane (PubMed:18948439). Localized at the apical membrane of the gall-bladder epithelial cells lining both the neck and corpus regions, the pancreatic acinar cells and mucosal epithelium of the colon and jejunum (By similarity). Trafficking from intracellular vesicles to the hepatocyte canalicular plasma membrane is induced by glucagon or the second messenger 3',5'-cyclic AMP and the translocation is protein kinase A and microtubule-dependent. Localized at the brush border membranes of epithelial cells from jejunum (By similarity). Localized at the luminal membranes of crypts in ascending colon (By similarity). Detected in the sperm midpiece (at protein level) (PubMed:28042826). Expressed only in pancreas and colon. Regulated by osmotic stress (PubMed:20144166). Up-regulated in response to metabolic acidosis (PubMed:22622463). Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Sulfenylation at Cys-53(C53-SOH) when hydrogen peroxide flows through the AQP8 channel, making it susceptible to hydrogen sulfide produced by CBS. Persulfidation at Cys-53 is required to gate AQP8 channel; under stress condition, hydrogen peroxide accumulates in the cell leading to CBS activation that produces hydrogen sulfide inducing persulfidation of oxidized Cys-53 (C53-SOH). N-glycosylated. Belongs to the MIP/aquaporin (TC 1.A.8) family. mitochondrion plasma membrane integral component of plasma membrane water transport water channel activity channel activity membrane integral component of membrane mitochondrial membrane apical part of cell transmembrane transport cellular response to cAMP uc002doc.1 uc002doc.2 uc002doc.3 uc002doc.4 uc002doc.5 
ENST00000219689.12 USP31 ENST00000219689.12 ubiquitin specific peptidase 31, transcript variant 3 (from RefSeq NR_170599.1) ENST00000219689.1 ENST00000219689.10 ENST00000219689.11 ENST00000219689.2 ENST00000219689.3 ENST00000219689.4 ENST00000219689.5 ENST00000219689.6 ENST00000219689.7 ENST00000219689.8 ENST00000219689.9 KIAA1203 NR_170599 Q6AW97 Q6ZTC0 Q6ZTN2 Q70CQ4 Q9ULL7 UBP31_HUMAN uc002dll.1 uc002dll.2 uc002dll.3 uc002dll.4 uc002dll.5 May recognize and hydrolyze the peptide bond at the C- terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q70CQ4-1; Sequence=Displayed; Name=2; IsoId=Q70CQ4-2; Sequence=VSP_020459, VSP_020460, VSP_020461, VSP_020462; Widely expressed. Belongs to the peptidase C19 family. Sequence=AK126752; Type=Frameshift; Evidence=; thiol-dependent ubiquitin-specific protease activity nucleus proteolysis ubiquitin-dependent protein catabolic process peptidase activity cysteine-type peptidase activity protein deubiquitination hydrolase activity thiol-dependent ubiquitinyl hydrolase activity uc002dll.1 uc002dll.2 uc002dll.3 uc002dll.4 uc002dll.5 
ENST00000219746.14 TOX3 ENST00000219746.14 TOX high mobility group box family member 3, transcript variant 1 (from RefSeq NM_001080430.4) B4DRD0 B5MCW4 CAGF9 ENST00000219746.1 ENST00000219746.10 ENST00000219746.11 ENST00000219746.12 ENST00000219746.13 ENST00000219746.2 ENST00000219746.3 ENST00000219746.4 ENST00000219746.5 ENST00000219746.6 ENST00000219746.7 ENST00000219746.8 ENST00000219746.9 NM_001080430 O15405 TNRC9 TOX3_HUMAN uc002egw.1 uc002egw.2 uc002egw.3 uc002egw.4 The protein encoded by this gene contains an HMG-box, indicating that it may be involved in bending and unwinding of DNA and alteration of chromatin structure. The C-terminus of the encoded protein is glutamine-rich due to CAG repeats in the coding sequence. A minor allele of this gene has been implicated in an elevated risk of breast cancer. Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Apr 2009]. Transcriptional coactivator of the p300/CBP-mediated transcription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promoters. Required for depolarization-induced transcription activation of the C-FOS promoter in neurons. Associates with chromatin to the estrogen- responsive C3 promoter region. Homodimer. Interacts with CREB1; the interaction is not depolarization dependent. Interacts with CREBBP (via C-terminus) (By similarity). Interacts (via HGM box) with CITED1 (via C-terminus); the interaction increases estrogen-response element (ERE)-dependent transcription and protection against cell death. Interacts with CREB1 (phosphorylated form). Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O15405-1; Sequence=Displayed; Name=2; IsoId=O15405-2; Sequence=VSP_043095, VSP_043096; Expressed mainly in epithelial cells. Expressed in the central nervous system (CNS), in the ileum and within the brain in the frontal and occipital lobe. Up-regulated by GPR39 in neuronal cells. the C-terminus is required for calcium responsiveness but not for transactivation activity. The N-terminus is absolutely necessary for transactivation activity. RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding chromatin binding protein binding nucleus regulation of transcription from RNA polymerase II promoter apoptotic process estrogen response element binding protein homodimerization activity regulation of apoptotic process negative regulation of neuron apoptotic process positive regulation of transcription, DNA-templated phosphoprotein binding uc002egw.1 uc002egw.2 uc002egw.3 uc002egw.4 
ENST00000219789.11 CDIPT ENST00000219789.11 CDP-diacylglycerol--inositol 3-phosphatidyltransferase, transcript variant 1 (from RefSeq NM_006319.5) B4DUV0 CDIPT CDIPT_HUMAN ENST00000219789.1 ENST00000219789.10 ENST00000219789.2 ENST00000219789.3 ENST00000219789.4 ENST00000219789.5 ENST00000219789.6 ENST00000219789.7 ENST00000219789.8 ENST00000219789.9 H3BTV1 NM_006319 O14735 PIS PIS1 Q6FGU1 Q6ZN70 uc002dum.1 uc002dum.2 uc002dum.3 uc002dum.4 uc002dum.5 uc002dum.6 Phosphatidylinositol breakdown products are ubiquitous second messengers that function downstream of many G protein-coupled receptors and tyrosine kinases regulating cell growth, calcium metabolism, and protein kinase C activity. Two enzymes, CDP-diacylglycerol synthase and phosphatidylinositol synthase, are involved in the biosynthesis of phosphatidylinositol. Phosphatidylinositol synthase, a member of the CDP-alcohol phosphatidyl transferase class-I family, is an integral membrane protein found on the cytoplasmic side of the endoplasmic reticulum and the Golgi apparatus. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2013]. Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme. Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn- glycero-3-phospho-(1D-myo-inositol) + CMP + H(+); Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11581; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11582; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Catalytic activity is higher with Mg(2+). ; Inhibited by PtdIns (product inhibition), phosphatidylinositol phosphate, and nucleoside di- and tri-phosphates. pH dependence: Optimum pH is 9.0. ; Temperature dependence: Optimum temperature is 50 degrees Celsius. ; O14735; P41181: AQP2; NbExp=3; IntAct=EBI-358858, EBI-12701138; O14735; Q13520: AQP6; NbExp=3; IntAct=EBI-358858, EBI-13059134; O14735; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-358858, EBI-11343438; O14735; O15342: ATP6V0E1; NbExp=3; IntAct=EBI-358858, EBI-12935759; O14735; Q8WZ55: BSND; NbExp=3; IntAct=EBI-358858, EBI-7996695; O14735; P11912: CD79A; NbExp=3; IntAct=EBI-358858, EBI-7797864; O14735; Q99675: CGRRF1; NbExp=3; IntAct=EBI-358858, EBI-2130213; O14735; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-358858, EBI-1045797; O14735; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-358858, EBI-18013275; O14735; P49447: CYB561; NbExp=3; IntAct=EBI-358858, EBI-8646596; O14735; P00387: CYB5R3; NbExp=3; IntAct=EBI-358858, EBI-1046040; O14735; Q6PI48: DARS2; NbExp=3; IntAct=EBI-358858, EBI-3917045; O14735; Q15125: EBP; NbExp=3; IntAct=EBI-358858, EBI-3915253; O14735; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-358858, EBI-781551; O14735; P34910-2: EVI2B; NbExp=3; IntAct=EBI-358858, EBI-17640610; O14735; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-358858, EBI-18304435; O14735; P12318-2: FCGR2A; NbExp=3; IntAct=EBI-358858, EBI-17187481; O14735; O15552: FFAR2; NbExp=3; IntAct=EBI-358858, EBI-2833872; O14735; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-358858, EBI-3918971; O14735; P08034: GJB1; NbExp=3; IntAct=EBI-358858, EBI-17565645; O14735; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-358858, EBI-712073; O14735; Q96P66: GPR101; NbExp=3; IntAct=EBI-358858, EBI-17935713; O14735; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-358858, EBI-11955647; O14735; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-358858, EBI-13345167; O14735; Q8TED1: GPX8; NbExp=3; IntAct=EBI-358858, EBI-11721746; O14735; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-358858, EBI-18053395; O14735; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-358858, EBI-725665; O14735; P24592: IGFBP6; NbExp=3; IntAct=EBI-358858, EBI-947015; O14735; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-358858, EBI-10266796; O14735; O00180: KCNK1; NbExp=3; IntAct=EBI-358858, EBI-3914675; O14735; P43628: KIR2DL3; NbExp=3; IntAct=EBI-358858, EBI-8632435; O14735; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-358858, EBI-739832; O14735; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-358858, EBI-11956541; O14735; O14880: MGST3; NbExp=3; IntAct=EBI-358858, EBI-724754; O14735; Q96JA4: MS4A14; NbExp=3; IntAct=EBI-358858, EBI-12839612; O14735; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-358858, EBI-3923617; O14735; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-358858, EBI-12382569; O14735; P60201-2: PLP1; NbExp=3; IntAct=EBI-358858, EBI-12188331; O14735; Q8NC24: RELL2; NbExp=3; IntAct=EBI-358858, EBI-10269209; O14735; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-358858, EBI-10192441; O14735; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-358858, EBI-2466594; O14735; O95197: RTN3; NbExp=3; IntAct=EBI-358858, EBI-740467; O14735; Q8N9R8: SCAI; NbExp=3; IntAct=EBI-358858, EBI-4395514; O14735; O00560: SDCBP; NbExp=3; IntAct=EBI-358858, EBI-727004; O14735; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-358858, EBI-17640454; O14735; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-358858, EBI-18159983; O14735; O60669: SLC16A7; NbExp=3; IntAct=EBI-358858, EBI-3921243; O14735; P30825: SLC7A1; NbExp=3; IntAct=EBI-358858, EBI-4289564; O14735; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-358858, EBI-12947623; O14735; Q9Y320: TMX2; NbExp=3; IntAct=EBI-358858, EBI-6447886; O14735; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-358858, EBI-13356252; O14735; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-358858, EBI-1055364; Endoplasmic reticulum membrane ; Multi-pass membrane protein Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O14735-1; Sequence=Displayed; Name=2; IsoId=O14735-2; Sequence=VSP_013618, VSP_013619, VSP_013620; Name=3; IsoId=O14735-3; Sequence=VSP_054767; Detected in placenta (at protein level). Widely expressed. Higher expression in adult liver and skeletal muscle, slightly lower levels seen in pancreas, kidney, lung, placenta, brain, heart, leukocyte, colon, small intestine, ovary, testis, prostate, thymus and spleen. In fetus, expressed in kidney, liver, lung and brain. Belongs to the CDP-alcohol phosphatidyltransferase class-I family. Golgi membrane CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity protein binding endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus plasma membrane lipid metabolic process phosphatidylinositol biosynthetic process phospholipid biosynthetic process membrane integral component of membrane transferase activity phosphotransferase activity, for other substituted phosphate groups diacylglycerol binding manganese ion binding carbohydrate binding alcohol binding CDP-diacylglycerol metabolic process uc002dum.1 uc002dum.2 uc002dum.3 uc002dum.4 uc002dum.5 uc002dum.6 
ENST00000219794.11 BCKDK ENST00000219794.11 branched chain keto acid dehydrogenase kinase, transcript variant 1 (from RefSeq NM_005881.4) A8MY43 BCKDK BCKD_HUMAN ENST00000219794.1 ENST00000219794.10 ENST00000219794.2 ENST00000219794.3 ENST00000219794.4 ENST00000219794.5 ENST00000219794.6 ENST00000219794.7 ENST00000219794.8 ENST00000219794.9 NM_005881 O14874 Q6FGL4 Q96G95 Q96IN5 uc002eaw.1 uc002eaw.2 uc002eaw.3 uc002eaw.4 uc002eaw.5 uc002eaw.6 The branched-chain alpha-ketoacid dehydrogenase complex (BCKD) is an important regulator of the valine, leucine, and isoleucine catabolic pathways. The protein encoded by this gene is found in the mitochondrion, where it phosphorylates and inactivates BCKD. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2012]. Serine/threonine-protein kinase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with PPM1K, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched- chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:24449431, PubMed:29779826, PubMed:37558654). Phosphorylates and inactivates mitochondrial BCKDH complex a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Associates with the E2 component of BCKDH complex and phosphorylates BCKDHA on Ser-337, leading to conformational changes that interrupt substrate channeling between E1 and E2 and inactivates the BCKDH complex (PubMed:29779826, PubMed:37558654). Phosphorylates ACLY on Ser-455 in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and glucogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxxE/D canonical motif (PubMed:29779826). Reaction=ATP + L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase]; Xref=Rhea:RHEA:17301, Rhea:RHEA-COMP:13695, Rhea:RHEA-COMP:13696, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.4; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17302; Evidence= Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence=; Allosterically inhibited by certain thiazoles and thiophenes: thiazoles increase interaction with DBT/BCKDH-E2, whereas thiophenes reduce this interaction. Inhibited by 3,6- dichlorobenzo[b]thiophene-2-carboxylic acid (BT2) (PubMed:37558654). The ATP binding is mediated by both potassium and magnesium ions (PubMed:37558654). Protein modification. Homodimer. Homotetramer (By similarity). Dimerizes through interaction of two opposing nucleotide-binding domains. Interacts with E2 component of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex. Competes with BCKDK for binding to the E2 component; this interaction is modulated by branched-chain alpha-keto acids. At steady state, BCKDH holoenzyme contains BCKDK and BCKDHA is phosphorylated. In response to high levels of branched-chain alpha-keto acids, the inhibitory BCKDK is replaced by activating PPM1K leading to BCKDHA dephosphorylation and BCAA degradation (PubMed:22589535, PubMed:37558654). O14874; P02549: SPTA1; NbExp=3; IntAct=EBI-1046765, EBI-375617; O14874; P40763: STAT3; NbExp=2; IntAct=EBI-1046765, EBI-518675; O14874; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-1046765, EBI-6863741; O14874-2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-25895587, EBI-2837444; Mitochondrion matrix Note=Detected in the cytosolic compartment of liver cells. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O14874-1; Sequence=Displayed; Name=2; IsoId=O14874-2; Sequence=VSP_054604, VSP_054605; Name=3; IsoId=O14874-3; Sequence=VSP_054605; Ubiquitous. Autophosphorylated. Branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD) [MIM:614923]: A metabolic disorder characterized by autism, epilepsy, intellectual disability, and reduced branched-chain amino acids. Note=The disease is caused by variants affecting the gene represented in this entry. A diet enriched in branched amino acids (BCAAs) allows to normalize plasma BCAA levels. This suggests that it may be possible to treat patients with mutations in BCKDK with BCAA supplementation. Belongs to the PDK/BCKDK protein kinase family. Name=Protein Spotlight; Note=The silence within - Issue 147 of March 2013; URL="https://web.expasy.org/spotlight/back_issues/147"; nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding mitochondrion mitochondrial matrix mitochondrial alpha-ketoglutarate dehydrogenase complex protein phosphorylation cellular amino acid catabolic process branched-chain amino acid catabolic process kinase activity phosphorylation transferase activity transferase activity, transferring phosphorus-containing groups [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity uc002eaw.1 uc002eaw.2 uc002eaw.3 uc002eaw.4 uc002eaw.5 uc002eaw.6 
ENST00000219797.9 KAT8 ENST00000219797.9 lysine acetyltransferase 8, transcript variant 1 (from RefSeq NM_032188.3) A8K4Z1 ENST00000219797.1 ENST00000219797.2 ENST00000219797.3 ENST00000219797.4 ENST00000219797.5 ENST00000219797.6 ENST00000219797.7 ENST00000219797.8 G5E9P2 KAT8_HUMAN MOF MYST1 NM_032188 PP7073 Q659G0 Q7LC17 Q8IY59 Q8WYB4 Q8WZ14 Q9H7Z6 Q9HAC5 Q9NR35 uc059tlg.1 uc059tlg.2 This gene encodes a member of the MYST histone acetylase protein family. The encoded protein has a characteristic MYST domain containing an acetyl-CoA-binding site, a chromodomain typical of proteins which bind histones, and a C2HC-type zinc finger. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2012]. Histone acetyltransferase which may be involved in transcriptional activation (PubMed:12397079, PubMed:22020126). May influence the function of ATM (PubMed:15923642). As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac (PubMed:16227571, PubMed:16543150, PubMed:21217699, PubMed:22547026, PubMed:22020126). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852, PubMed:22547026). That activity is less specific than the one of the MSL complex (PubMed:20018852, PubMed:22547026). Can also acetylate TP53/p53 at 'Lys-120'. Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; Evidence=; Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1 (PubMed:16227571, PubMed:16543150). Interacts with MSL1; the interaction is direct (PubMed:21217699, PubMed:22547026). Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:16543150, PubMed:20018852). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975). Interacts with the chromodomain of MORF4L1/MRG15 (PubMed:12397079). Interacts with ATM (via its Tudor-knot domain) (PubMed:15923642). Interacts with KANSL1; the interaction is direct (PubMed:16543150, PubMed:20620954, PubMed:21217699, PubMed:22547026). Interacts with MSL3 (PubMed:21217699, PubMed:22547026, PubMed:30224647). Interacts with NELFD (By similarity). Q9H7Z6; Q03164: KMT2A; NbExp=3; IntAct=EBI-896414, EBI-591370; Q9H7Z6; Q99496: RNF2; NbExp=2; IntAct=EBI-896414, EBI-722416; Q9H7Z6; P04637: TP53; NbExp=2; IntAct=EBI-896414, EBI-366083; Q9H7Z6; P02309: HHF2; Xeno; NbExp=2; IntAct=EBI-896414, EBI-8113; Q9H7Z6-1; Q68DK7-1: MSL1; NbExp=2; IntAct=EBI-26435386, EBI-26435399; Nucleus romosome Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H7Z6-1; Sequence=Displayed; Name=2; IsoId=Q9H7Z6-2; Sequence=VSP_014579; Autoacetylation at Lys-274 is required for binding histone H4 with high affinity and for proper function. Li-Ghorbani-Weisz-Hubshman syndrome (LIGOWS) [MIM:618974]: An autosomal dominant disorder characterized by global developmental delay, mild to moderate intellectual disability, speech and language impairment, and variable facial dysmorphism. Some patients have seizures and autistic features. Brain imaging abnormalities are observed in some patients and include decreased white matter volume, enlarged ventricles, thin corpus callosum, and gray matter nodular heterotopia. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the MYST (SAS/MOZ) family. Sequence=AAL55762.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence=; Sequence=AAL56648.1; Type=Frameshift; Evidence=; histone acetyltransferase complex kinetochore nuclear chromatin histone acetyltransferase activity protein binding nucleus nucleoplasm chromosome chromatin organization regulation of transcription, DNA-templated transcription factor binding regulation of autophagy nuclear matrix acetyltransferase activity histone acetylation transferase activity transferase activity, transferring acyl groups enzyme binding myeloid cell differentiation methylated histone binding histone binding histone H4-K5 acetylation histone H4-K8 acetylation histone H4-K16 acetylation negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter metal ion binding histone acetyltransferase activity (H4-K16 specific) MLL1 complex MSL complex histone acetyltransferase activity (H4-K5 specific) histone acetyltransferase activity (H4-K8 specific) uc059tlg.1 uc059tlg.2 
ENST00000219837.12 KNOP1 ENST00000219837.12 lysine rich nucleolar protein 1, transcript variant 12 (from RefSeq NM_001348537.2) C16orf88 ENST00000219837.1 ENST00000219837.10 ENST00000219837.11 ENST00000219837.2 ENST00000219837.3 ENST00000219837.4 ENST00000219837.5 ENST00000219837.6 ENST00000219837.7 ENST00000219837.8 ENST00000219837.9 FAM191A KNOP1_HUMAN NM_001348537 O43328 Q1ED39 Q5FWF3 TSG118 uc002dgq.1 uc002dgq.2 uc002dgq.3 uc002dgq.4 uc002dgq.5 The protein encoded by this gene is a nucleolar protein that interacts with zinc finger 106 protein. The encoded protein has several of the same characteristics as nucleostemin and may be involved in testis development. [provided by RefSeq, Feb 2017]. Interacts with ZNF106. Q1ED39; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-9977982, EBI-297683; Nucleus, nucleolus Sequence=AAC05805.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH89430.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; RNA binding nucleus nucleolus uc002dgq.1 uc002dgq.2 uc002dgq.3 uc002dgq.4 uc002dgq.5 
ENST00000219919.9 AQP9 ENST00000219919.9 aquaporin 9, transcript variant 1 (from RefSeq NM_020980.5) AQP9_HUMAN ENST00000219919.1 ENST00000219919.2 ENST00000219919.3 ENST00000219919.4 ENST00000219919.5 ENST00000219919.6 ENST00000219919.7 ENST00000219919.8 NM_020980 O43315 Q9NP32 SSC1 uc002aez.1 uc002aez.2 uc002aez.3 uc002aez.4 The aquaporins are a family of water-selective membrane channels. This gene encodes a member of a subset of aquaporins called the aquaglyceroporins. This protein allows passage of a broad range of noncharged solutes and also stimulates urea transport and osmotic water permeability. This protein may also facilitate the uptake of glycerol in hepatic tissue . The encoded protein may also play a role in specialized leukocyte functions such as immunological response and bactericidal activity. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Mar 2016]. Forms a water channel with a broad specificity. Also permeable glycerol and urea. Mediates passage of a wide variety of small, non-charged solutes including carbamides, polyols, purines, and pyrimidines. O43315; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-17444777, EBI-10225815; O43315; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-17444777, EBI-11957045; O43315; P05090: APOD; NbExp=3; IntAct=EBI-17444777, EBI-715495; O43315; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-17444777, EBI-9083477; O43315; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-17444777, EBI-12256978; O43315; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-17444777, EBI-18013275; O43315; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-17444777, EBI-12019274; O43315; Q9BV81: EMC6; NbExp=3; IntAct=EBI-17444777, EBI-2820492; O43315; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-17444777, EBI-12175685; O43315; O75084: FZD7; NbExp=3; IntAct=EBI-17444777, EBI-746917; O43315; P01350: GAST; NbExp=3; IntAct=EBI-17444777, EBI-3436637; O43315; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-17444777, EBI-2867874; O43315; P24593: IGFBP5; NbExp=3; IntAct=EBI-17444777, EBI-720480; O43315; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-17444777, EBI-2820517; O43315; P30301: MIP; NbExp=3; IntAct=EBI-17444777, EBI-8449636; O43315; P09466: PAEP; NbExp=3; IntAct=EBI-17444777, EBI-465167; O43315; Q9NRX5: SERINC1; NbExp=3; IntAct=EBI-17444777, EBI-2683145; O43315; O95470: SGPL1; NbExp=3; IntAct=EBI-17444777, EBI-1046170; O43315; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-17444777, EBI-10314552; O43315; P02787: TF; NbExp=3; IntAct=EBI-17444777, EBI-714319; O43315; Q9BVK6: TMED9; NbExp=3; IntAct=EBI-17444777, EBI-1056827; O43315; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-17444777, EBI-1057733; Cell membrane ulti-pass membrane protein Highly expressed in peripheral leukocytes. Also expressed in liver, lung, and spleen. Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Belongs to the MIP/aquaporin (TC 1.A.8) family. amine transmembrane transporter activity purine nucleobase transmembrane transporter activity pyrimidine nucleobase transmembrane transporter activity water transmembrane transporter activity plasma membrane integral component of plasma membrane water transport purine nucleobase transport response to osmotic stress excretion response to organic substance polyol transmembrane transporter activity urea transmembrane transporter activity water channel activity glycerol channel activity urea channel activity channel activity canalicular bile acid transport polyol transport glycerol transport amine transport pyrimidine nucleobase transport membrane integral component of membrane basolateral plasma membrane water homeostasis intracellular membrane-bounded organelle response to mercury ion carboxylic acid transport carboxylic acid transmembrane transporter activity transmembrane transport cellular response to cAMP urea transmembrane transport pyrimidine-containing compound transmembrane transport purine nucleobase transmembrane transport carboxylic acid transmembrane transport uc002aez.1 uc002aez.2 uc002aez.3 uc002aez.4 
ENST00000220003.14 CSK ENST00000220003.14 C-terminal Src kinase, transcript variant 14 (from RefSeq NR_170550.1) CSK_HUMAN ENST00000220003.1 ENST00000220003.10 ENST00000220003.11 ENST00000220003.12 ENST00000220003.13 ENST00000220003.2 ENST00000220003.3 ENST00000220003.4 ENST00000220003.5 ENST00000220003.6 ENST00000220003.7 ENST00000220003.8 ENST00000220003.9 NR_170550 P41240 Q2M3N2 Q6FGZ6 uc002ays.1 uc002ays.2 uc002ays.3 uc002ays.4 Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C- terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK. Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Homodimer (via SH3-domain) (PubMed:19888460). Interacts with PTPN22 (PubMed:15208781). Interacts with phosphorylated SIT1, PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK to the membrane where it can phosphorylate and inhibit Src-family kinases (PubMed:11433379, PubMed:10790433, PubMed:14610046, PubMed:10838081). Interacts with SRCIN1 (PubMed:17525734). Interacts with RHOH (PubMed:20851766). Interacts (via SH2 domain) with SCIMP; this interaction is dependent on phosphorylation of SCIMP 'Tyr-107' (PubMed:21930792). Interacts (via SH2 domain) with PRAG1 (when phosphorylated at 'Tyr-391'); this interaction prevents translocation of CSK from the cytoplasm to the membrane leading to increased activity of CSK (By similarity). Interacts with LRRK1 (PubMed:23526378). P41240; P41240: CSK; NbExp=7; IntAct=EBI-1380630, EBI-1380630; P41240; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1380630, EBI-742054; P41240; P08069: IGF1R; NbExp=5; IntAct=EBI-1380630, EBI-475981; P41240; Q5T7N3: KANK4; NbExp=3; IntAct=EBI-1380630, EBI-9355810; P41240; Q9NWQ8: PAG1; NbExp=5; IntAct=EBI-1380630, EBI-2828115; P41240; P08575: PTPRC; NbExp=3; IntAct=EBI-1380630, EBI-1341; P41240; P49023: PXN; NbExp=4; IntAct=EBI-1380630, EBI-702209; P41240; Q6UWF3: SCIMP; NbExp=3; IntAct=EBI-1380630, EBI-2872510; P41240; Q7VLE8: lspA1; Xeno; NbExp=4; IntAct=EBI-1380630, EBI-26445163; P41240; P00523: SRC; Xeno; NbExp=7; IntAct=EBI-1380630, EBI-848039; Cytoplasm Cell membrane Note=Mainly cytoplasmic, also present in lipid rafts. Expressed in lung and macrophages. The architecture of this protein is similar to that of Src- family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, and a C-terminal kinase domain. Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated. Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/csk/"; nucleotide binding adaptive immune response immune system process protein kinase activity protein tyrosine kinase activity non-membrane spanning protein tyrosine kinase activity protein binding ATP binding cytoplasm cytosol plasma membrane cell-cell junction protein phosphorylation brain development protein C-terminus binding negative regulation of cell proliferation negative regulation of low-density lipoprotein particle clearance membrane kinase activity phosphorylation transferase activity peptidyl-tyrosine phosphorylation protein phosphatase binding T cell costimulation negative regulation of interleukin-6 production negative regulation of kinase activity protein kinase A catalytic subunit binding adherens junction organization identical protein binding negative regulation of Golgi to plasma membrane protein transport positive regulation of MAP kinase activity membrane raft negative regulation of bone resorption protein autophosphorylation metal ion binding oligodendrocyte differentiation negative regulation of phagocytosis T cell receptor signaling pathway regulation of Fc receptor mediated stimulatory signaling pathway extracellular exosome proline-rich region binding negative regulation of ERK1 and ERK2 cascade cellular response to peptide hormone stimulus uc002ays.1 uc002ays.2 uc002ays.3 uc002ays.4 
ENST00000220058.9 MTFMT ENST00000220058.9 mitochondrial methionyl-tRNA formyltransferase (from RefSeq NM_139242.4) B7Z734 ENST00000220058.1 ENST00000220058.2 ENST00000220058.3 ENST00000220058.4 ENST00000220058.5 ENST00000220058.6 ENST00000220058.7 ENST00000220058.8 FMT FMT1 FMT_HUMAN NM_139242 Q96DP5 uc002aof.1 uc002aof.2 uc002aof.3 uc002aof.4 uc002aof.5 uc002aof.6 The protein encoded by this nuclear gene localizes to the mitochondrion, where it catalyzes the formylation of methionyl-tRNA. [provided by RefSeq, Jun 2011]. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.186666.1, SRR3476690.992099.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000220058.9/ ENSP00000220058.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Methionyl-tRNA formyltransferase that formylates methionyl- tRNA in mitochondria and is crucial for translation initiation. Reaction=(6R)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl- tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA- COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:78530, ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; EC=2.1.2.9; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24381; Evidence=; Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96DP5-1; Sequence=Displayed; Name=2; IsoId=Q96DP5-2; Sequence=VSP_057059, VSP_057060; Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C- terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction. Combined oxidative phosphorylation deficiency 15 (COXPD15) [MIM:614947]: An autosomal recessive, mitochondrial, neurologic disorder characterized by features of Leigh syndrome and combined oxidative phosphorylation deficiency. Clinical features include mild global developmental delay, white matter abnormalities, ataxia, incoordination, speech and reading difficulties, T2-weighted hyperintensities in the basal ganglia, corpus callosum, and brainstem. Note=The disease is caused by variants affecting the gene represented in this entry. Mitochondrial complex I deficiency, nuclear type 27 (MC1DN27) [MIM:618248]: A form of mitochondrial complex I deficiency, the most common biochemical signature of mitochondrial disorders, a group of highly heterogeneous conditions characterized by defective oxidative phosphorylation, which collectively affects 1 in 5-10000 live births. Clinical disorders have variable severity, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. MC1DN27 transmission pattern is consistent with autosomal recessive inheritance. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the Fmt family. Sequence=AAH16630.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAH33687.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=BAB70984.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; catalytic activity methionyl-tRNA formyltransferase activity mitochondrion translation translational initiation biosynthetic process transferase activity hydroxymethyl-, formyl- and related transferase activity conversion of methionyl-tRNA to N-formyl-methionyl-tRNA uc002aof.1 uc002aof.2 uc002aof.3 uc002aof.4 uc002aof.5 uc002aof.6 
ENST00000220062.9 RASL12 ENST00000220062.9 RAS like family 12, transcript variant 1 (from RefSeq NM_016563.4) B2RC29 B4DJW2 B4DU82 ENST00000220062.1 ENST00000220062.2 ENST00000220062.3 ENST00000220062.4 ENST00000220062.5 ENST00000220062.6 ENST00000220062.7 ENST00000220062.8 NM_016563 Q9NYN1 RASLC_HUMAN RIS uc002aoi.1 uc002aoi.2 uc002aoi.3 Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence=; Q9NYN1; Q14192: FHL2; NbExp=4; IntAct=EBI-12917066, EBI-701903; Q9NYN1; Q13643: FHL3; NbExp=3; IntAct=EBI-12917066, EBI-741101; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NYN1-1; Sequence=Displayed; Name=2; IsoId=Q9NYN1-2; Sequence=VSP_055845; Name=3; IsoId=Q9NYN1-3; Sequence=VSP_055846; Belongs to the small GTPase superfamily. Ras family. nucleotide binding GTPase activity calmodulin binding GTP binding plasma membrane signal transduction Ras protein signal transduction membrane GDP binding uc002aoi.1 uc002aoi.2 uc002aoi.3 
ENST00000220166.10 CTSH ENST00000220166.10 cathepsin H, transcript variant 1 (from RefSeq NM_004390.5) B2RBK0 CATH_HUMAN CPSB ENST00000220166.1 ENST00000220166.2 ENST00000220166.3 ENST00000220166.4 ENST00000220166.5 ENST00000220166.6 ENST00000220166.7 ENST00000220166.8 ENST00000220166.9 NM_004390 P09668 Q96NY6 Q9BUM7 uc021srk.1 uc021srk.2 uc021srk.3 The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Alternate splicing of this gene results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jan 2016]. Important for the overall degradation of proteins in lysosomes. Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16; Composed of a mini chain and a large chain. The large chain may be split into heavy and light chain. All chains are held together by disulfide bonds. P09668; Q86V38: ATN1; NbExp=3; IntAct=EBI-6189940, EBI-11954292; P09668; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-6189940, EBI-356015; P09668; Q92876: KLK6; NbExp=3; IntAct=EBI-6189940, EBI-2432309; Lysosome. Belongs to the peptidase C1 family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40206/CTSH"; metanephros development T cell mediated cytotoxicity adaptive immune response immune response-regulating signaling pathway endopeptidase activity aminopeptidase activity cysteine-type endopeptidase activity serine-type endopeptidase activity protein binding extracellular region extracellular space lysosome cytosol proteolysis apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process peptidase activity cysteine-type peptidase activity positive regulation of cell proliferation cysteine-type endopeptidase activator activity involved in apoptotic process positive regulation of gene expression positive regulation of epithelial cell migration neuropeptide catabolic process bradykinin catabolic process positive regulation of peptidase activity peptidase activator activity involved in apoptotic process hydrolase activity antigen processing and presentation HLA-A specific activating MHC class I receptor activity positive regulation of cell migration zymogen activation protein destabilization response to retinoic acid membrane protein proteolysis secretory granule lumen cytoplasmic ribonucleoprotein granule negative regulation of apoptotic process surfactant homeostasis intracellular membrane-bounded organelle neutrophil degranulation cellular protein metabolic process positive regulation of angiogenesis proteolysis involved in cellular protein catabolic process dichotomous subdivision of terminal units involved in lung branching extracellular exosome thyroid hormone binding ERK1 and ERK2 cascade cellular response to thyroid hormone stimulus alveolar lamellar body multivesicular body lumen tertiary granule lumen ficolin-1-rich granule lumen positive regulation of apoptotic signaling pathway uc021srk.1 uc021srk.2 uc021srk.3 
ENST00000220325.9 EHD4 ENST00000220325.9 EH domain containing 4 (from RefSeq NM_139265.4) EHD4 EHD4_HUMAN ENST00000220325.1 ENST00000220325.2 ENST00000220325.3 ENST00000220325.4 ENST00000220325.5 ENST00000220325.6 ENST00000220325.7 ENST00000220325.8 FKSG7 HCA10 HCA11 NM_139265 PAST4 Q9H223 Q9HAR1 Q9NZN2 uc001zot.1 uc001zot.2 uc001zot.3 uc001zot.4 uc001zot.5 ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport. Homooligomer, and heterooligomer with EHD1, EHD2 and EHD3. Early endosome membrane ; Peripheral membrane protein ; Cytoplasmic side Recycling endosome membrane ; Peripheral membrane protein ; Cytoplasmic side Cell membrane ; Peripheral membrane protein ; Cytoplasmic side Highly expressed in pancreas and heart. The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. EHD subfamily. nucleotide binding nucleic acid binding calcium ion binding protein binding ATP binding GTP binding nucleus endosome endoplasmic reticulum plasma membrane pinocytosis membrane regulation of endocytosis early endosome membrane endocytic recycling cadherin binding metal ion binding perinuclear region of cytoplasm positive regulation of peptidyl-tyrosine phosphorylation protein homooligomerization recycling endosome membrane extracellular exosome cellular response to growth factor stimulus uc001zot.1 uc001zot.2 uc001zot.3 uc001zot.4 uc001zot.5 
ENST00000220420.10 TGM5 ENST00000220420.10 transglutaminase 5, transcript variant 1 (from RefSeq NM_201631.4) ENST00000220420.1 ENST00000220420.2 ENST00000220420.3 ENST00000220420.4 ENST00000220420.5 ENST00000220420.6 ENST00000220420.7 ENST00000220420.8 ENST00000220420.9 NM_201631 O43548 O43549 Q0VF40 Q9UEZ4 TGM5_HUMAN TGMX uc001zrd.1 uc001zrd.2 uc001zrd.3 This gene encodes a member of the transglutaminase family. The encoded protein catalyzes formation of protein cross-links between glutamine and lysine residues, often resulting in stabilization of protein assemblies. This reaction is calcium dependent. Mutations in this gene have been associated with acral peeling skin syndrome. [provided by RefSeq, Oct 2009]. Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes. Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L- lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence= Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Note=Binds 1 Ca(2+) ion per subunit. ; O43548; P55212: CASP6; NbExp=3; IntAct=EBI-12027348, EBI-718729; O43548; Q14451-3: GRB7; NbExp=3; IntAct=EBI-12027348, EBI-11991632; O43548; O00291: HIP1; NbExp=3; IntAct=EBI-12027348, EBI-473886; O43548; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-12027348, EBI-2556193; O43548; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12027348, EBI-21591415; O43548; Q6P4E2: LARP4; NbExp=3; IntAct=EBI-12027348, EBI-12079790; O43548; P47929: LGALS7B; NbExp=3; IntAct=EBI-12027348, EBI-357504; O43548; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-12027348, EBI-5280197; O43548; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-12027348, EBI-740773; Cytoplasm Note=Associated with intermediate filaments. Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=O43548-1; Sequence=Displayed; Name=Short; IsoId=O43548-2; Sequence=VSP_006415; Expressed in foreskin keratinocytes. By 12-O-tetradecanoylphorbol-13-acetate (TPA) and calcium in NHEK cells. Peeling skin syndrome 2 (PSS2) [MIM:609796]: A non- inflammatory and localized form of peeling skin syndrome, a genodermatosis characterized by the continuous shedding of the outer layers of the epidermis. In PSS2 patients, skin peeling is painless and strictly limited to the dorsa of the hands and feet. It is accompanied by painless erythema and spontaneous non-scarring healing. Ultrastructural and histological analysis shows a level of blistering high in the epidermis at the stratum granulosum-stratum corneum junction. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the transglutaminase superfamily. Transglutaminase family. protein-glutamine gamma-glutamyltransferase activity cytoplasm plasma membrane cellular protein modification process epidermis development transferase activity transferase activity, transferring acyl groups peptide cross-linking metal ion binding cornification uc001zrd.1 uc001zrd.2 uc001zrd.3 
ENST00000220478.8 SCG3 ENST00000220478.8 secretogranin III, transcript variant 1 (from RefSeq NM_013243.4) A8K2B0 B3KQP6 B4DK99 ENST00000220478.1 ENST00000220478.2 ENST00000220478.3 ENST00000220478.4 ENST00000220478.5 ENST00000220478.6 ENST00000220478.7 F5H3R8 NM_013243 Q8WXD2 Q96C83 Q96GE8 Q9Y6G7 SCG3_HUMAN UNQ2502/PRO5990 uc002abh.1 uc002abh.2 uc002abh.3 uc002abh.4 uc002abh.5 The protein encoded by this gene is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. Granins may serve as precursors for biologically active peptides. Some granins have been shown to function as helper proteins in sorting and proteolytic processing of prohormones; however, the function of this protein is unknown. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009]. Member of the granin protein family that regulates the biogenesis of secretory granules (PubMed:19357184). Acts as a sorting receptor for intragranular proteins including chromogranin A/CHGA (By similarity). May also play a role in angiogenesis. Promotes endothelial proliferation, migration and tube formation through MEK/ERK signaling pathway (PubMed:29154827). Interacts with CHGA (PubMed:19357184) (By similarity). Interacts with secretogranin II/SCG2 (PubMed:19357184). Interacts (via C-terminus) with CPE (By similarity). Q8WXD2; O00560: SDCBP; NbExp=3; IntAct=EBI-12162999, EBI-727004; Cytoplasmic vesicle, secretory vesicle Cytoplasmic vesicle, secretory vesicle membrane ; Peripheral membrane protein Secreted te=Associated with the secretory granule membrane through direct binding to cholesterol-enriched lipid rafts. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8WXD2-1; Sequence=Displayed; Name=2; IsoId=Q8WXD2-2; Sequence=VSP_042876; Detected in urine (at protein level) (PubMed:25326458). Expressed in brain, heart, kidney, liver and skeletal muscle. O-glycosylated. Polymorphisms in the 5'-flanking region and in intron 1 may have an effect on transcriptional activity and be associated with an increase in subcutaneous, but not visceral, fat area. Hence, may influence the risk of obesity. platelet degranulation RNA binding extracellular region endoplasmic reticulum lumen membrane transport vesicle transport vesicle membrane secretory granule membrane cytoplasmic vesicle protein localization to secretory granule secretory granule lumen post-translational protein modification cellular protein metabolic process uc002abh.1 uc002abh.2 uc002abh.3 uc002abh.4 uc002abh.5 
ENST00000220496.9 DNAJC17 ENST00000220496.9 DnaJ heat shock protein family (Hsp40) member C17 (from RefSeq NM_018163.3) DJC17_HUMAN ENST00000220496.1 ENST00000220496.2 ENST00000220496.3 ENST00000220496.4 ENST00000220496.5 ENST00000220496.6 ENST00000220496.7 ENST00000220496.8 NM_018163 Q9NVM6 uc001zms.1 uc001zms.2 uc001zms.3 uc001zms.4 May negatively affect PAX8-induced thyroglobulin/TG transcription. Q9NVM6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12260682, EBI-16439278; Cytoplasm Nucleus Note=Predominantly nuclear. negative regulation of transcription from RNA polymerase II promoter nucleic acid binding RNA binding nucleus cytoplasm toxin transport uc001zms.1 uc001zms.2 uc001zms.3 uc001zms.4 
ENST00000220507.5 RHOV ENST00000220507.5 ras homolog family member V (from RefSeq NM_133639.4) ARHV ENST00000220507.1 ENST00000220507.2 ENST00000220507.3 ENST00000220507.4 NM_133639 Q2KHQ5 Q8TDW6 Q96L33 RHOV RHOV_HUMAN WRCH2 uc001znd.1 uc001znd.2 uc001znd.3 uc001znd.4 Plays a role in the control of the actin cytoskeleton via activation of the JNK pathway. Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Interacts with PAK2. Q96L33; O43639: NCK2; NbExp=4; IntAct=EBI-8538631, EBI-713635; Q96L33; Q9NQU5: PAK6; NbExp=3; IntAct=EBI-8538631, EBI-1053685; Cell membrane ; Lipid-anchor ; Cytoplasmic side Endosome membrane ; Lipid-anchor ; Cytoplasmic side Note=Treatment with TNF activates endosomal but not plasma membrane RHOV. Highly expressed in pancreas, placenta, and fetal brain. Belongs to the small GTPase superfamily. Rho family. nucleotide binding GTPase activity protein binding GTP binding cytoplasm endosome cytosol plasma membrane cell cortex endocytosis actin filament organization establishment or maintenance of cell polarity small GTPase mediated signal transduction Rho protein signal transduction regulation of cell shape endosome membrane membrane protein kinase binding cell projection assembly actin cytoskeleton organization Cdc42 protein signal transduction regulation of actin cytoskeleton organization cell projection metal ion binding regulation of small GTPase mediated signal transduction uc001znd.1 uc001znd.2 uc001znd.3 uc001znd.4 
ENST00000220509.10 VPS18 ENST00000220509.10 VPS18 core subunit of CORVET and HOPS complexes (from RefSeq NM_020857.3) ENST00000220509.1 ENST00000220509.2 ENST00000220509.3 ENST00000220509.4 ENST00000220509.5 ENST00000220509.6 ENST00000220509.7 ENST00000220509.8 ENST00000220509.9 KIAA1475 NM_020857 Q8TCG0 Q96DI3 Q9H268 Q9P253 VPS18 VPS18_HUMAN uc001zne.1 uc001zne.2 uc001zne.3 uc001zne.4 Vesicle mediated protein sorting plays an important role in segregation of intracellular molecules into distinct organelles. Genetic studies in yeast have identified more than 40 vacuolar protein sorting (VPS) genes involved in vesicle transport to vacuoles. This gene encodes the human homolog of yeast class C Vps18 protein. The mammalian class C Vps proteins are predominantly associated with late endosomes/lysosomes, and like their yeast counterparts, may mediate vesicle trafficking steps in the endosome/lysosome pathway. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AL713725.1, AB040908.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220509.10/ ENSP00000220509.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in dendrite development of Pukinje cells (By similarity). Core component of at least two putative endosomal tethering complexes, the homotypic fusion and vacuole protein sorting (HOPS) complex and the class C core vacuole/endosome tethering (CORVET) complex. Their common core is composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1 (PubMed:23351085, PubMed:25783203, PubMed:23901104). Interacts with RAB5C (By similarity). Interacts with HOOK1 (By similarity). Interacts with STX7, MON1B (PubMed:20434987, PubMed:24554770). Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes (By similarity). Interacts with SYNPO2 (PubMed:23434281). Interacts with PLEKHM1 (PubMed:28325809). Q9P253; Q7L1V2: MON1B; NbExp=2; IntAct=EBI-1053363, EBI-2655311; Q9P253; O15400: STX7; NbExp=2; IntAct=EBI-1053363, EBI-3221827; Q9P253; Q9H270: VPS11; NbExp=9; IntAct=EBI-1053363, EBI-373380; Q9P253; Q9H269: VPS16; NbExp=15; IntAct=EBI-1053363, EBI-2655929; Q9P253; Q96AX1: VPS33A; NbExp=6; IntAct=EBI-1053363, EBI-2527283; Q9P253; Q96JC1: VPS39; NbExp=2; IntAct=EBI-1053363, EBI-1050197; Q9P253; P49754: VPS41; NbExp=4; IntAct=EBI-1053363, EBI-2130459; Q9P253; Q63615: Vps33a; Xeno; NbExp=2; IntAct=EBI-1053363, EBI-918669; Late endosome membrane ; Peripheral membrane protein ; Cytoplasmic side Lysosome membrane ; Peripheral membrane protein ; Cytoplasmic side Early endosome Cytoplasmic vesicle, autophagosome Cytoplasmic vesicle, clathrin-coated vesicle Note=Cytoplasmic, peripheral membrane protein associated with early endosomes and late endosomes/lysosomes. Ubiquitous. Expression was highest in heart and low in lung. Belongs to the VPS18 family. Sequence=AAH01513.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence=; Sequence=BAA95999.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; actin binding protein binding lysosome lysosomal membrane endosome early endosome late endosome autophagosome actin filament intracellular protein transport vesicle docking involved in exocytosis autophagy endosome organization vacuole organization lysosome organization endosome to lysosome transport protein transport membrane vesicle-mediated transport syntaxin binding AP-3 adaptor complex clathrin-coated vesicle protein binding, bridging HOPS complex cytoplasmic vesicle late endosome membrane CORVET complex regulation of SNARE complex assembly viral entry into host cell metal ion binding presynapse glutamatergic synapse regulation of synaptic vesicle exocytosis uc001zne.1 uc001zne.2 uc001zne.3 uc001zne.4 
ENST00000220514.8 OIP5 ENST00000220514.8 Opa interacting protein 5, transcript variant 1 (from RefSeq NM_007280.2) ENST00000220514.1 ENST00000220514.2 ENST00000220514.3 ENST00000220514.4 ENST00000220514.5 ENST00000220514.6 ENST00000220514.7 MIS18B MS18B_HUMAN NM_007280 O43482 OIP5 Q96BX7 uc001znp.1 uc001znp.2 uc001znp.3 uc001znp.4 The protein encoded by this gene localizes to centromeres, where it is essential for recruitment of CENP-A through the mediator Holliday junction recognition protein. Expression of this gene is upregulated in several cancers, making it a putative therapeutic target. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2015]. Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. Homodimer, and heterodimer with MIS18A (PubMed:17199038, PubMed:26921242). Identified in a complex containing MIS18A, OIP5/MIS18B, MIS18BP1, RBBP7 and RBBP4 (PubMed:17199038). Binds outer membrane protein OpaP from Neisseria gonorrhoeae (in vitro) (PubMed:9466265). O43482; Q9NQ94: A1CF; NbExp=3; IntAct=EBI-536879, EBI-2809489; O43482; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-536879, EBI-11096309; O43482; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-536879, EBI-742038; O43482; P21549: AGXT; NbExp=3; IntAct=EBI-536879, EBI-727098; O43482; Q92870-2: APBB2; NbExp=3; IntAct=EBI-536879, EBI-21535880; O43482; O75934: BCAS2; NbExp=3; IntAct=EBI-536879, EBI-1050106; O43482; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-536879, EBI-745073; O43482; Q13515: BFSP2; NbExp=3; IntAct=EBI-536879, EBI-10229433; O43482; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-536879, EBI-465861; O43482; Q6P1W5: C1orf94; NbExp=6; IntAct=EBI-536879, EBI-946029; O43482; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-536879, EBI-11524851; O43482; O60826: CCDC22; NbExp=3; IntAct=EBI-536879, EBI-3943153; O43482; Q8N4L8: CCDC24; NbExp=5; IntAct=EBI-536879, EBI-1104933; O43482; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-536879, EBI-10175300; O43482; Q86X02: CDR2L; NbExp=3; IntAct=EBI-536879, EBI-11063830; O43482; Q96L14: CEP170P1; NbExp=3; IntAct=EBI-536879, EBI-743488; O43482; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-536879, EBI-11752486; O43482; Q8TCT0: CERK; NbExp=3; IntAct=EBI-536879, EBI-10274247; O43482; Q9Y6H1: CHCHD2; NbExp=3; IntAct=EBI-536879, EBI-2321769; O43482; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-536879, EBI-12155483; O43482; P10606: COX5B; NbExp=3; IntAct=EBI-536879, EBI-1053725; O43482; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-536879, EBI-739773; O43482; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-536879, EBI-11962928; O43482; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-536879, EBI-9679045; O43482; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-536879, EBI-465804; O43482; Q86UW9: DTX2; NbExp=3; IntAct=EBI-536879, EBI-740376; O43482; Q9H596: DUSP21; NbExp=3; IntAct=EBI-536879, EBI-7357329; O43482; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-536879, EBI-743105; O43482; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-536879, EBI-301024; O43482; Q96DF8: ESS2; NbExp=3; IntAct=EBI-536879, EBI-3928124; O43482; Q9NYK6-3: EURL; NbExp=3; IntAct=EBI-536879, EBI-13371226; O43482; Q96MY7: FAM161B; NbExp=4; IntAct=EBI-536879, EBI-7225287; O43482; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-536879, EBI-2807642; O43482; P22607: FGFR3; NbExp=3; IntAct=EBI-536879, EBI-348399; O43482; A1L4K1: FSD2; NbExp=3; IntAct=EBI-536879, EBI-5661036; O43482; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-536879, EBI-372506; O43482; Q96CN9: GCC1; NbExp=3; IntAct=EBI-536879, EBI-746252; O43482; P55040: GEM; NbExp=3; IntAct=EBI-536879, EBI-744104; O43482; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-536879, EBI-7251368; O43482; O95872: GPANK1; NbExp=3; IntAct=EBI-536879, EBI-751540; O43482; Q13227: GPS2; NbExp=5; IntAct=EBI-536879, EBI-713355; O43482; Q14957: GRIN2C; NbExp=3; IntAct=EBI-536879, EBI-8285963; O43482; P28799: GRN; NbExp=3; IntAct=EBI-536879, EBI-747754; O43482; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-536879, EBI-11956675; O43482; O14964: HGS; NbExp=3; IntAct=EBI-536879, EBI-740220; O43482; P09067: HOXB5; NbExp=3; IntAct=EBI-536879, EBI-3893317; O43482; P17482: HOXB9; NbExp=3; IntAct=EBI-536879, EBI-745290; O43482; P31273: HOXC8; NbExp=3; IntAct=EBI-536879, EBI-1752118; O43482; P01112: HRAS; NbExp=3; IntAct=EBI-536879, EBI-350145; O43482; Q9ULV5-2: HSF4; NbExp=5; IntAct=EBI-536879, EBI-12056251; O43482; Q14005-2: IL16; NbExp=3; IntAct=EBI-536879, EBI-17178971; O43482; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-536879, EBI-2556193; O43482; O60333-2: KIF1B; NbExp=3; IntAct=EBI-536879, EBI-10975473; O43482; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-536879, EBI-8472129; O43482; O14901: KLF11; NbExp=3; IntAct=EBI-536879, EBI-948266; O43482; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-536879, EBI-6426443; O43482; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-536879, EBI-739890; O43482; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-536879, EBI-373334; O43482; P02533: KRT14; NbExp=3; IntAct=EBI-536879, EBI-702178; O43482; P19012: KRT15; NbExp=4; IntAct=EBI-536879, EBI-739566; O43482; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-536879, EBI-3044087; O43482; P12035: KRT3; NbExp=3; IntAct=EBI-536879, EBI-2430095; O43482; Q92764: KRT35; NbExp=3; IntAct=EBI-536879, EBI-1058674; O43482; O76014: KRT37; NbExp=3; IntAct=EBI-536879, EBI-1045716; O43482; Q6A162: KRT40; NbExp=3; IntAct=EBI-536879, EBI-10171697; O43482; P04259: KRT6B; NbExp=3; IntAct=EBI-536879, EBI-740907; O43482; O95678: KRT75; NbExp=5; IntAct=EBI-536879, EBI-2949715; O43482; Q14533: KRT81; NbExp=5; IntAct=EBI-536879, EBI-739648; O43482; P78385: KRT83; NbExp=3; IntAct=EBI-536879, EBI-10221390; O43482; O43790: KRT86; NbExp=3; IntAct=EBI-536879, EBI-9996498; O43482; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-536879, EBI-11953846; O43482; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-536879, EBI-1048945; O43482; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-536879, EBI-12805508; O43482; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-536879, EBI-726510; O43482; Q9NPJ6: MED4; NbExp=3; IntAct=EBI-536879, EBI-394607; O43482; O14770-4: MEIS2; NbExp=3; IntAct=EBI-536879, EBI-8025850; O43482; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-536879, EBI-2801965; O43482; Q9NYP9: MIS18A; NbExp=23; IntAct=EBI-536879, EBI-1104552; O43482; Q6P0N0: MIS18BP1; NbExp=4; IntAct=EBI-536879, EBI-9870821; O43482; Q8IVT2: MISP; NbExp=3; IntAct=EBI-536879, EBI-2555085; O43482; Q6PF18: MORN3; NbExp=3; IntAct=EBI-536879, EBI-9675802; O43482; Q9P2K5-2: MYEF2; NbExp=5; IntAct=EBI-536879, EBI-10318831; O43482; Q8NFW9: MYRIP; NbExp=3; IntAct=EBI-536879, EBI-1759414; O43482; O14561: NDUFAB1; NbExp=3; IntAct=EBI-536879, EBI-1246261; O43482; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-536879, EBI-10172876; O43482; P07196: NEFL; NbExp=3; IntAct=EBI-536879, EBI-475646; O43482; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-536879, EBI-741048; O43482; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-536879, EBI-2811583; O43482; P37198: NUP62; NbExp=6; IntAct=EBI-536879, EBI-347978; O43482; O43482: OIP5; NbExp=4; IntAct=EBI-536879, EBI-536879; O43482; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-536879, EBI-10181968; O43482; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-536879, EBI-11022007; O43482; Q8N4B1-4: PHETA1; NbExp=3; IntAct=EBI-536879, EBI-14131832; O43482; Q99697-2: PITX2; NbExp=3; IntAct=EBI-536879, EBI-12138495; O43482; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-536879, EBI-2876622; O43482; P52435: POLR2J; NbExp=3; IntAct=EBI-536879, EBI-394753; O43482; P78424: POU6F2; NbExp=3; IntAct=EBI-536879, EBI-12029004; O43482; P60891: PRPS1; NbExp=3; IntAct=EBI-536879, EBI-749195; O43482; P0CG20: PRR35; NbExp=3; IntAct=EBI-536879, EBI-11986293; O43482; P20618: PSMB1; NbExp=3; IntAct=EBI-536879, EBI-372273; O43482; Q9ULW5: RAB26; NbExp=3; IntAct=EBI-536879, EBI-958239; O43482; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-536879, EBI-14093916; O43482; P04049: RAF1; NbExp=4; IntAct=EBI-536879, EBI-365996; O43482; Q8N443: RIBC1; NbExp=3; IntAct=EBI-536879, EBI-10265323; O43482; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-536879, EBI-11984663; O43482; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-536879, EBI-6257312; O43482; Q8WXG8: S100Z; NbExp=3; IntAct=EBI-536879, EBI-12198403; O43482; Q7Z3H4: SAMD7; NbExp=3; IntAct=EBI-536879, EBI-12148649; O43482; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-536879, EBI-3957636; O43482; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-536879, EBI-12000762; O43482; Q6ZSJ9: SHISA6; NbExp=6; IntAct=EBI-536879, EBI-12037847; O43482; P12757: SKIL; NbExp=3; IntAct=EBI-536879, EBI-2902468; O43482; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-536879, EBI-455078; O43482; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-536879, EBI-9675976; O43482; P14678-2: SNRPB; NbExp=3; IntAct=EBI-536879, EBI-372475; O43482; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-536879, EBI-12288855; O43482; O60504: SORBS3; NbExp=3; IntAct=EBI-536879, EBI-741237; O43482; Q86W54-2: SPATA24; NbExp=3; IntAct=EBI-536879, EBI-12041693; O43482; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-536879, EBI-10174456; O43482; Q9BXF9: TEKT3; NbExp=5; IntAct=EBI-536879, EBI-8644516; O43482; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-536879, EBI-12090309; O43482; Q7Z6R9: TFAP2D; NbExp=5; IntAct=EBI-536879, EBI-11952651; O43482; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-536879, EBI-1105213; O43482; O60220: TIMM8A; NbExp=3; IntAct=EBI-536879, EBI-1049822; O43482; O43711: TLX3; NbExp=3; IntAct=EBI-536879, EBI-3939165; O43482; P06753: TPM3; NbExp=12; IntAct=EBI-536879, EBI-355607; O43482; Q5VU62: TPM3; NbExp=5; IntAct=EBI-536879, EBI-10184033; O43482; Q8N7U7-2: TPRX1; NbExp=5; IntAct=EBI-536879, EBI-14115717; O43482; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-536879, EBI-492476; O43482; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-536879, EBI-10259086; O43482; Q15654: TRIP6; NbExp=4; IntAct=EBI-536879, EBI-742327; O43482; Q12815: TROAP; NbExp=3; IntAct=EBI-536879, EBI-2349743; O43482; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-536879, EBI-739895; O43482; O75604: USP2; NbExp=3; IntAct=EBI-536879, EBI-743272; O43482; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-536879, EBI-11975223; O43482; O76024: WFS1; NbExp=3; IntAct=EBI-536879, EBI-720609; O43482; Q9BYJ9: YTHDF1; NbExp=3; IntAct=EBI-536879, EBI-1051237; O43482; Q15915: ZIC1; NbExp=5; IntAct=EBI-536879, EBI-11963196; O43482; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-536879, EBI-740727; O43482; Q8N720: ZNF655; NbExp=3; IntAct=EBI-536879, EBI-625509; O43482; Q9Y649; NbExp=3; IntAct=EBI-536879, EBI-25900580; Nucleus Chromosome Chromosome, centromere Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin. Belongs to the mis18 family. Sequence=AAC39561.1; Type=Erroneous initiation; Evidence=; chromosome, centromeric region chromatin protein binding nucleus nucleoplasm chromosome cytosol cell cycle chromosome segregation cell communication chromocenter Cajal body nuclear speck CENP-A containing nucleosome assembly identical protein binding metal ion binding cell division uc001znp.1 uc001znp.2 uc001znp.3 uc001znp.4 
ENST00000220531.9 BLOC1S6 ENST00000220531.9 biogenesis of lysosomal organelles complex 1 subunit 6, transcript variant 5 (from RefSeq NR_132352.2) BL1S6_HUMAN ENST00000220531.1 ENST00000220531.2 ENST00000220531.3 ENST00000220531.4 ENST00000220531.5 ENST00000220531.6 ENST00000220531.7 ENST00000220531.8 NR_132352 PA PLDN Q9UL45 uc001zvq.1 uc001zvq.2 uc001zvq.3 uc001zvq.4 uc001zvq.5 uc001zvq.6 The protein encoded by this gene may play a role in intracellular vesicle trafficking. It interacts with Syntaxin 13 which mediates intracellular membrane fusion. Mutations in this gene cause symptoms associated with Hermansky-Pudlak syndrome-9. Alternative splicing results in multiple transcript variants. A pseudogene related to this gene is located on the X chromosome. [provided by RefSeq, Aug 2015]. Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May play a role in intracellular vesicle trafficking, particularly in the vesicle-docking and fusion process. Interacts with BLOC1S4 and DTNBP1/BLOC1S7 (By similarity). Homodimer. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Interacts with BLOC1S5, F-actin, SNAP25 isoform 1 and isoform 2, SNAP47 and STX12. Q9UL45; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-465781, EBI-743598; Q9UL45; Q9NYB9-2: ABI2; NbExp=6; IntAct=EBI-465781, EBI-11096309; Q9UL45; P78537: BLOC1S1; NbExp=17; IntAct=EBI-465781, EBI-348630; Q9UL45; Q9NUP1: BLOC1S4; NbExp=5; IntAct=EBI-465781, EBI-465852; Q9UL45; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-465781, EBI-465781; Q9UL45; Q504U0: C4orf46; NbExp=3; IntAct=EBI-465781, EBI-6657981; Q9UL45; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-465781, EBI-10171416; Q9UL45; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-465781, EBI-10175300; Q9UL45; Q8N619: CDK5R1; NbExp=3; IntAct=EBI-465781, EBI-10266998; Q9UL45; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-465781, EBI-744115; Q9UL45; Q6QEF8: CORO6; NbExp=3; IntAct=EBI-465781, EBI-10254194; Q9UL45; Q13561: DCTN2; NbExp=3; IntAct=EBI-465781, EBI-715074; Q9UL45; Q96EV8: DTNBP1; NbExp=9; IntAct=EBI-465781, EBI-465804; Q9UL45; Q8IYI6: EXOC8; NbExp=4; IntAct=EBI-465781, EBI-742102; Q9UL45; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-465781, EBI-2514791; Q9UL45; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-465781, EBI-9091197; Q9UL45; Q2T9L4: INSYN1; NbExp=7; IntAct=EBI-465781, EBI-4311436; Q9UL45; A1A4E9: KRT13; NbExp=3; IntAct=EBI-465781, EBI-10171552; Q9UL45; Q14CN4: KRT72; NbExp=3; IntAct=EBI-465781, EBI-1221280; Q9UL45; Q13503: MED21; NbExp=3; IntAct=EBI-465781, EBI-394678; Q9UL45; Q9BV36: MLPH; NbExp=3; IntAct=EBI-465781, EBI-7042162; Q9UL45; P37198: NUP62; NbExp=6; IntAct=EBI-465781, EBI-347978; Q9UL45; Q9H8W4: PLEKHF2; NbExp=4; IntAct=EBI-465781, EBI-742388; Q9UL45; Q9UJ41: RABGEF1; NbExp=3; IntAct=EBI-465781, EBI-913954; Q9UL45; Q9UJ41-4: RABGEF1; NbExp=6; IntAct=EBI-465781, EBI-14093916; Q9UL45; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-465781, EBI-726876; Q9UL45; Q96BD8: SKA1; NbExp=8; IntAct=EBI-465781, EBI-741854; Q9UL45; Q16637: SMN2; NbExp=6; IntAct=EBI-465781, EBI-395421; Q9UL45; O75558: STX11; NbExp=6; IntAct=EBI-465781, EBI-714135; Q9UL45; Q16623: STX1A; NbExp=3; IntAct=EBI-465781, EBI-712466; Q9UL45; A1L190: SYCE3; NbExp=3; IntAct=EBI-465781, EBI-10283466; Q9UL45; P09493-10: TPM1; NbExp=5; IntAct=EBI-465781, EBI-12123928; Q9UL45; Q5VU62: TPM3; NbExp=3; IntAct=EBI-465781, EBI-10184033; Q9UL45; Q9Y3C0: WASHC3; NbExp=8; IntAct=EBI-465781, EBI-712969; Cytoplasm mbrane eripheral membrane protein Note=It can exist as a soluble protein as well as a peripheral membrane protein (PubMed:12019270). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9UL45-1; Sequence=Displayed; Name=2; IsoId=Q9UL45-2; Sequence=VSP_009293, VSP_009294; Name=3; IsoId=Q9UL45-3; Sequence=Not described; Widely expressed. Phosphorylated. Hermansky-Pudlak syndrome 9 (HPS9) [MIM:614171]: A form of Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal recessive disorder characterized by oculocutaneous albinism, bleeding due to platelet storage pool deficiency, and lysosomal storage defects. This syndrome results from defects of diverse cytoplasmic organelles including melanosomes, platelet dense granules and lysosomes. Ceroid storage in the lungs is associated with pulmonary fibrosis, a common cause of premature death in individuals with HPS. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 2]: May be due to a competing acceptor splice site. [Isoform 3]: May be due to exons 2 and 3 skipping. Belongs to the BLOC1S6 family. A paper showing involvement in Hermansky-Pudlak syndrome 9 was retracted due to image duplication. protein binding cytoplasm cytosol anterograde axonal transport membrane synaptic vesicle docking extrinsic component of membrane syntaxin binding transport vesicle BLOC-1 complex neuron projection development melanosome transport melanosome organization endosome to melanosome transport identical protein binding protein homodimerization activity anterograde synaptic vesicle transport positive regulation of pigment cell differentiation actin filament binding presynapse axon cytoplasm SNARE complex uc001zvq.1 uc001zvq.2 uc001zvq.3 uc001zvq.4 uc001zvq.5 uc001zvq.6 
ENST00000220562.9 EXTL3 ENST00000220562.9 exostosin like glycosyltransferase 3, transcript variant 1 (from RefSeq NM_001440.4) D3DST8 ENST00000220562.1 ENST00000220562.2 ENST00000220562.3 ENST00000220562.4 ENST00000220562.5 ENST00000220562.6 ENST00000220562.7 ENST00000220562.8 EXTL1L EXTL3 EXTL3_HUMAN EXTR1 KIAA0519 NM_001440 O00225 O43909 Q53XT3 uc003xgz.1 uc003xgz.2 uc003xgz.3 uc003xgz.4 This gene encodes a single-pass membrane protein which functions as a glycosyltransferase. The encoded protein catalyzes the transfer of N-acetylglucosamine to glycosaminoglycan chains. This reaction is important in heparin and heparan sulfate synthesis. Alternative splicing results in the multiple transcript variants. [provided by RefSeq, Nov 2012]. Glycosyltransferase which regulates the biosynthesis of heparan sulfate (HS) (PubMed:28132690, PubMed:28148688). Initiates HS synthesis by transferring the first N-acetyl-alpha-D-glucosamine (alpha-GlcNAc) residue (GlcNAcT-I activity) to the tetrasaccharide linker (GlcA-Gal-Gal-Xyl-)Ser core linker (PubMed:11390981, PubMed:35676258). May also transfer alpha-GlcNAc residues during HS elongation (GlcNAcT-II activity) (PubMed:11390981, PubMed:35676258). Lacks glucuronyl transferase II (GlcAT-II) activity (PubMed:11390981, PubMed:35676258). Important for both skeletal development and hematopoiesis, through the formation of HS proteoglycans (HSPGs) (PubMed:28132690, PubMed:28148688, PubMed:11390981, PubMed:22727489, PubMed:35676258). Through the synthesis of HS, regulates postnatal pancreatic islet maturation and insulin secretion (By similarity). Receptor for REG3A, REG3B and REG3G, induces the activation of downstream signaling pathways such as PI3K-AKT or RAS-RAF-MEK-ERK signaling pathway (PubMed:22727489, PubMed:34099862, PubMed:27830702). Required for the function of REG3A in regulating keratinocyte proliferation and differentiation (PubMed:22727489). Required for the inhibition of skin inflammation mediated by REGA through the activation of PI3K-AKT-STAT3 pathway (PubMed:27830702). Required for the function of REGA and REG3G in glucose tolerance in pancreas (PubMed:19158046). Expressed in microglia, is activated by nociceptor-derived REG3G in response to endotoxins, leading to the inhibition of kynurenine pathway to prevent endotoxic death (By similarity). Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)- beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3- O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D- Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:16221, Rhea:RHEA-COMP:12573, Rhea:RHEA-COMP:12574, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132093, ChEBI:CHEBI:132104; EC=2.4.1.223; Evidence= Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Glycan metabolism; heparan sulfate biosynthesis. Homodimer; disulfide-linked (PubMed:29346724, PubMed:35676258). Interacts with REG3A. O43909; P54253: ATXN1; NbExp=3; IntAct=EBI-1754679, EBI-930964; Endoplasmic reticulum membrane ; Single-pass type II membrane protein Golgi apparatus Cell membrane Nucleus Note=Interaction with REG3A induces its translocation to the nucleus. Ubiquitous. Expressed in keratinocytes. Expressed in pancreas (PubMed:34099862). The N-terminal glycosyltransferase domain (GT47) does not bind UDP and is therefore unlikely to possess glycosyltransferase activity. Immunoskeletal dysplasia with neurodevelopmental abnormalities (ISDNA) [MIM:617425]: An autosomal recessive disorder characterized by variable skeletal abnormalities and neurodevelopmental defects. Neurologic manifestations include intellectual disability and motor delay. Some patients manifest hypotonia and seizures. Skeletal features include disproportionate short stature, cervical malformations, epiphyseal and metaphyseal dysplasia, and rarely premature craniosynostosis with progressive microcephaly. Severe combined immunodeficiency with a complete absence of T cells is observed in some patients. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyltransferase 47 family. It is uncertain whether Met-1, Met-6 or Met-20 is the initiator. Sequence=BAA25445.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=Functional Glycomics Gateway - GTase; Note=Exostosin-like 3; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_531"; glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus protein glycosylation heparan sulfate proteoglycan biosynthetic process membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups positive regulation of cell growth IRE1-mediated unfolded protein response metal ion binding uc003xgz.1 uc003xgz.2 uc003xgz.3 uc003xgz.4 
ENST00000220584.9 FDFT1 ENST00000220584.9 farnesyl-diphosphate farnesyltransferase 1, transcript variant 3 (from RefSeq NM_004462.5) ENST00000220584.1 ENST00000220584.2 ENST00000220584.3 ENST00000220584.4 ENST00000220584.5 ENST00000220584.6 ENST00000220584.7 ENST00000220584.8 FDFT1 NM_004462 Q6IAX1 Q6IAX1_HUMAN hCG_17749 uc003wui.1 uc003wui.2 uc003wui.3 uc003wui.4 uc003wui.5 This gene encodes a membrane-associated enzyme located at a branch point in the mevalonate pathway. The encoded protein is the first specific enzyme in cholesterol biosynthesis, catalyzing the dimerization of two molecules of farnesyl diphosphate in a two-step reaction to form squalene. [provided by RefSeq, Jul 2008]. Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene. Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence=; Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence=; Reaction=2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate; Xref=Rhea:RHEA:22672, ChEBI:CHEBI:33019, ChEBI:CHEBI:57310, ChEBI:CHEBI:175763; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22673; Evidence= Reaction=H(+) + NADH + presqualene diphosphate = diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:22228, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57310, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22229; Evidence= Reaction=H(+) + NADPH + presqualene diphosphate = diphosphate + NADP(+) + squalene; Xref=Rhea:RHEA:22232, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22233; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence= Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3. Belongs to the phytoene/squalene synthase family. farnesyl-diphosphate farnesyltransferase activity endoplasmic reticulum ergosterol biosynthetic process lipid biosynthetic process biosynthetic process integral component of membrane transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups squalene synthase activity uc003wui.1 uc003wui.2 uc003wui.3 uc003wui.4 uc003wui.5 
ENST00000220592.10 AGO2 ENST00000220592.10 argonaute RISC catalytic component 2, transcript variant 1 (from RefSeq NM_012154.5) AGO2 AGO2_HUMAN EIF2C2 ENST00000220592.1 ENST00000220592.2 ENST00000220592.3 ENST00000220592.4 ENST00000220592.5 ENST00000220592.6 ENST00000220592.7 ENST00000220592.8 ENST00000220592.9 NM_012154 Q8TCZ5 Q8WV58 Q96ID1 Q9UKV8 uc003yvm.1 uc003yvm.2 uc003yvm.3 uc003yvm.4 uc003yvm.5 uc003yvm.6 This gene encodes a member of the Argonaute family of proteins which play a role in RNA interference. The encoded protein is highly basic, and contains a PAZ domain and a PIWI domain. It may interact with dicer1 and play a role in short-interfering-RNA-mediated gene silencing. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009]. Required for RNA-mediated gene silencing (RNAi) by the RNA- induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7- methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P- bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up- regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF- alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. (Microbial infection) Upon Sars-CoV-2 infection, associates with viral miRNA-like small RNA, CoV2-miR-O7a, and may repress mRNAs, such as BATF2, to evade the IFN response. Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.n2; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Inhibited by EDTA. Kinetic parameters: KM=1.1 nM for a synthetic 21-nucleotide single-stranded RNA ; Interacts with DICER1 through its Piwi domain and with TARBP2 during assembly of the RNA-induced silencing complex (RISC)(PubMed:14749716, PubMed:16271387, PubMed:16289642, PubMed:16357216, PubMed:15973356, PubMed:17507929, PubMed:18690212, PubMed:18178619, PubMed:33199684). Together, DICER1, AGO2 and TARBP2 constitute the trimeric RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Note however that the term RISC has also been used to describe the trimeric RLC/miRLC. The formation of RISC complexes containing siRNAs rather than miRNAs appears to occur independently of DICER1. Interacts with AGO1. Also interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9, ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, PABPC1, PRMT5, P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with the P-body components DCP1A and XRN1. Associates with polysomes and messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the interaction is modulated under stress-induced conditions, occurs under both cell proliferation and differentiation conditions and in an RNA- and phosphorylation- independent manner. Interacts with LIMD1, WTIP and AJUBA. Interacts with TRIM71; the interaction increases in presence of RNA (PubMed:23125361). Interacts with APOBEC3G in an RNA-dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F and APOBEC3H. Interacts with DICER1, TARBP2, EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a large RNA-induced silencing complex (RISC) (PubMed:17507929, PubMed:24726324). Interacts with FMR1 (PubMed:14703574). Interacts with ZFP36 (PubMed:15766526). Found in a complex, composed of AGO2, CHD7 and ARB2A (By similarity). Interacts with RC3H1; the interaction is RNA independent (PubMed:25697406). Interacts with SND1 (PubMed:14508492, PubMed:28546213). Interacts with SYT11 (By similarity). Interacts with CLNK (PubMed:26009488). Interacts with GARRE1 (PubMed:29395067). (Microbial infection) Interacts with Epstein-Barr virus (EBV) tegument protein BGLF2; this interaction participates in the regulation of cellular miRNA by the virus, leading to enhanced SUMOylation. (Microbial infection) Interacts with rotavirus A non- structural protein 5; this interaction probably plays a role in the sequestration of AGO2 in viral factories. Q9UKV8; Q9UL18: AGO1; NbExp=3; IntAct=EBI-528269, EBI-527363; Q9UKV8; Q9UIV1: CNOT7; NbExp=2; IntAct=EBI-528269, EBI-2105113; Q9UKV8; P26196: DDX6; NbExp=14; IntAct=EBI-528269, EBI-351257; Q9UKV8; Q96C10: DHX58; NbExp=2; IntAct=EBI-528269, EBI-744193; Q9UKV8; Q9UPY3: DICER1; NbExp=20; IntAct=EBI-528269, EBI-395506; Q9UKV8; Q9UPY3-1: DICER1; NbExp=14; IntAct=EBI-528269, EBI-15569571; Q9UKV8; G5E9A7: DMWD; NbExp=3; IntAct=EBI-528269, EBI-10976677; Q9UKV8; P00533: EGFR; NbExp=11; IntAct=EBI-528269, EBI-297353; Q9UKV8; Q13541: EIF4EBP1; NbExp=2; IntAct=EBI-528269, EBI-74090; Q9UKV8; P22607: FGFR3; NbExp=3; IntAct=EBI-528269, EBI-348399; Q9UKV8; Q02790: FKBP4; NbExp=2; IntAct=EBI-528269, EBI-1047444; Q9UKV8; Q9BVP2: GNL3; NbExp=3; IntAct=EBI-528269, EBI-641642; Q9UKV8; O15397: IPO8; NbExp=4; IntAct=EBI-528269, EBI-358808; Q9UKV8; Q9UGP4: LIMD1; NbExp=11; IntAct=EBI-528269, EBI-2652871; Q9UKV8; Q5S007: LRRK2; NbExp=3; IntAct=EBI-528269, EBI-5323863; Q9UKV8; Q86UE4: MTDH; NbExp=3; IntAct=EBI-528269, EBI-1046588; Q9UKV8; Q6IQ23: PLEKHA7; NbExp=7; IntAct=EBI-528269, EBI-2125301; Q9UKV8; O75569: PRKRA; NbExp=5; IntAct=EBI-528269, EBI-713955; Q9UKV8; P04156: PRNP; NbExp=4; IntAct=EBI-528269, EBI-977302; Q9UKV8; Q15185: PTGES3; NbExp=3; IntAct=EBI-528269, EBI-1049387; Q9UKV8; P63244: RACK1; NbExp=2; IntAct=EBI-528269, EBI-296739; Q9UKV8; P06400: RB1; NbExp=3; IntAct=EBI-528269, EBI-491274; Q9UKV8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-528269, EBI-5235340; Q9UKV8; Q15633: TARBP2; NbExp=12; IntAct=EBI-528269, EBI-978581; Q9UKV8; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-528269, EBI-356402; Q9UKV8; A7MCY6: TBKBP1; NbExp=2; IntAct=EBI-528269, EBI-359969; Q9UKV8; Q8NDV7: TNRC6A; NbExp=22; IntAct=EBI-528269, EBI-2269715; Q9UKV8; Q9UPQ9: TNRC6B; NbExp=13; IntAct=EBI-528269, EBI-947158; Q9UKV8; Q9UPQ9-2: TNRC6B; NbExp=4; IntAct=EBI-528269, EBI-6514011; Q9UKV8; Q9HCJ0: TNRC6C; NbExp=4; IntAct=EBI-528269, EBI-6507625; Q9UKV8; Q9HA38: ZMAT3; NbExp=5; IntAct=EBI-528269, EBI-2548480; Cytoplasm, P-body cleus Note=Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UKV8-1; Sequence=Displayed; Name=2; IsoId=Q9UKV8-2; Sequence=VSP_037001; The Piwi domain may perform RNA cleavage by a mechanism similar to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp- Glu (DDE) for metal ion coordination, this protein appears to utilize a triad of Asp-Asp-His (DDH). Hydroxylated. 4-hydroxylation appears to enhance protein stability but is not required for miRNA-binding or endonuclease activity. Ubiquitinated on surface-exposed lysines by a SCF-like E3 ubiquitin-protein ligase complex containing ZSWIM8 during target- directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs) (PubMed:33184234, PubMed:33184237). Ubiquitination by the SCF-like E3 ubiquitin-protein ligase complex containing ZSWIM8 leads to its subsequent degradation, thereby exposing miRNAs for degradation (PubMed:33184234, PubMed:33184237). ZSWIM8 recognizes and binds AGO2 when it is engaged with a TDMD target (PubMed:33184237). Phosphorylated. A phosphorylation cycle of C-terminal serine cluster (Ser-824-Ser-834) regulates the release of target mRNAs. Target-binding leads to phosphorylation of these residues by CSNK1A1, which reduces the affinity of AGO2 for mRNA and enables target release. The ANKRD52-PPP6C phosphatase complex dephosphorylates the residues, which primes AGO2 for binding a new target. Phosphorylation at Ser-387 by AKT3; leads to up-regulate translational repression of microRNA target and down-regulate endonucleolytic cleavage. Lessel-Kreienkamp syndrome (LESKRES) [MIM:619149]: An autosomal dominant disorder characterized by global developmental delay, intellectual disability of variable degree, and speech and language delay apparent from infancy or early childhood. Behavioral disorders are observed in most patients. Additional variable features include seizures, hypotonia, gait abnormalities, visual and cardiac defects, and non-specific facial dysmorphism. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the argonaute family. Ago subfamily. Sequence=AAH07633.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAL76093.1; Type=Miscellaneous discrepancy; Note=cDNA contains a duplication of an internal sequence at the 5' end.; Evidence=; RNA 7-methylguanosine cap binding P-body RNA polymerase II core binding core promoter binding nucleic acid binding RNA binding double-stranded RNA binding single-stranded RNA binding mRNA binding translation initiation factor activity nuclease activity endonuclease activity endoribonuclease activity protein binding nucleus nucleoplasm cytoplasm cytosol polysome mRNA cap binding complex regulation of transcription, DNA-templated translation translational initiation regulation of translation Wnt signaling pathway, calcium modulating pathway protein C-terminus binding post-embryonic development RNA secondary structure unwinding miRNA metabolic process positive regulation of gene expression negative regulation of gene expression membrane RISC complex hydrolase activity endoribonuclease activity, producing 5'-phosphomonoesters cell junction production of siRNA involved in RNA interference dendrite gene silencing by RNA pre-miRNA processing siRNA loading onto RISC involved in RNA interference posttranscriptional gene silencing by RNA production of miRNAs involved in gene silencing by miRNA siRNA binding miRNA binding miRNA mediated inhibition of translation mRNA cleavage involved in gene silencing by miRNA miRNA loading onto RISC involved in gene silencing by miRNA negative regulation of amyloid precursor protein biosynthetic process positive regulation of angiogenesis positive regulation of transcription from RNA polymerase II promoter negative regulation of translational initiation metal ion binding positive regulation of nuclear-transcribed mRNA poly(A) tail shortening regulation of gene silencing by miRNA extracellular exosome endoribonuclease activity, cleaving siRNA-paired mRNA RISC-loading complex RNA phosphodiester bond hydrolysis, endonucleolytic endoribonuclease activity, cleaving miRNA-paired mRNA mRNA cleavage involved in gene silencing by siRNA mRNA cap binding positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay positive regulation of trophoblast cell migration positive regulation of miRNA mediated inhibition of translation ribonucleoprotein complex uc003yvm.1 uc003yvm.2 uc003yvm.3 uc003yvm.4 uc003yvm.5 uc003yvm.6 
ENST00000220597.4 PAG1 ENST00000220597.4 phosphoprotein membrane anchor with glycosphingolipid microdomains 1 (from RefSeq NM_018440.4) A8K1A3 CBP ENST00000220597.1 ENST00000220597.2 ENST00000220597.3 NM_018440 PAG PHAG1_HUMAN Q2M1Z9 Q5BKU4 Q9NWQ8 Q9NYK0 uc003ybz.1 uc003ybz.2 uc003ybz.3 uc003ybz.4 The protein encoded by this gene is a type III transmembrane adaptor protein that binds to the tyrosine kinase csk protein. It is thought to be involved in the regulation of T cell activation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK289818.1, SRR1660805.105152.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220597.4/ ENSP00000220597.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell adhesion signaling. Interacts with FYN. When phosphorylated, interacts with CSK. Interacts with NHERF1/EBP50. In resting T-cells, part of a PAG1-NHERF1- MSN complex which is disrupted upon TCR activation. Interacts with LYN on plasma membrane lipid rafts. Identified in a complex with LYN and STAT3. Q9NWQ8; P41240: CSK; NbExp=5; IntAct=EBI-2828115, EBI-1380630; Q9NWQ8; P06241: FYN; NbExp=5; IntAct=EBI-2828115, EBI-515315; Q9NWQ8; P07948: LYN; NbExp=16; IntAct=EBI-2828115, EBI-79452; Q9NWQ8; P63244: RACK1; NbExp=2; IntAct=EBI-2828115, EBI-296739; Cell membrane ingle-pass type III membrane protein Note=Present in lipid rafts. Ubiquitously expressed. Present in germinal center B-cells, plasma cells, T-cells, monocytes and platelets (at protein level). Palmitoylated. Phosphorylated by FYN on Tyr-317 in resting T-cells; which promotes interaction with CSK. Dephosphorylated by PTPRC/CD45 upon TCR activation; which leads to CSK dissociation. May also be dephosphorylated by PTPN11. Hyperphosphorylated in mast cells upon FCER1 activation. Phosphorylated by LYN. adaptive immune response immune system process SH3/SH2 adaptor activity protein binding plasma membrane signal transduction positive regulation of signal transduction membrane integral component of membrane intracellular signal transduction SH2 domain binding membrane raft T cell receptor signaling pathway regulation of T cell activation negative regulation of T cell activation uc003ybz.1 uc003ybz.2 uc003ybz.3 uc003ybz.4 
ENST00000220616.9 TG ENST00000220616.9 thyroglobulin (from RefSeq NM_003235.5) ENST00000220616.1 ENST00000220616.2 ENST00000220616.3 ENST00000220616.4 ENST00000220616.5 ENST00000220616.6 ENST00000220616.7 ENST00000220616.8 NM_003235 O15274 O43899 P01266 Q15593 Q15948 Q9NYR1 Q9NYR2 Q9UMZ0 Q9UNY3 TG THYG_HUMAN uc003ytw.1 uc003ytw.2 uc003ytw.3 uc003ytw.4 uc003ytw.5 Thyroglobulin (Tg) is a glycoprotein homodimer produced predominantly by the thryroid gland. It acts as a substrate for the synthesis of thyroxine and triiodothyronine as well as the storage of the inactive forms of thyroid hormone and iodine. Thyroglobulin is secreted from the endoplasmic reticulum to its site of iodination, and subsequent thyroxine biosynthesis, in the follicular lumen. Mutations in this gene cause thyroid dyshormonogenesis, manifested as goiter, and are associated with moderate to severe congenital hypothyroidism. Polymorphisms in this gene are associated with susceptibility to autoimmune thyroid diseases (AITD) such as Graves disease and Hashimoto thryoiditis. [provided by RefSeq, Nov 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X05615.1, U93033.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA2144120 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220616.9/ ENSP00000220616.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (PubMed:32025030, PubMed:17532758). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling in the thyroid follicle lumen (PubMed:32025030). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (PubMed:32025030). One dimer produces 7 thyroid hormone molecules (PubMed:32025030). Monomer (PubMed:32025030). Homodimer (via ChEL region); occurs in the endoplasmic reticulum and is required for export to the Golgi apparatus (PubMed:32025030). Homooligomer; disulfide-linked; stored in this form in the thyroid follicle lumen (PubMed:8626858). P01266; Q99523: SORT1; NbExp=3; IntAct=EBI-2800425, EBI-1057058; Secreted te=Secreted into the thyroid follicle lumen (PubMed:19509106). Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers (PubMed:8626858, PubMed:11082042). Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Major; IsoId=P01266-1; Sequence=Displayed; Name=2; Synonyms=Minor; IsoId=P01266-2; Sequence=VSP_012655; Specifically expressed in the thyroid gland. The cholinesterase-like (ChEL) region is required for dimerization and export from the endoplasmic reticulum. Iodinated on tyrosine residues by TPO (PubMed:2760035, PubMed:32025030). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2573 is coupled to donor Tyr-2540, acceptor Tyr-2766 in monomer 1 is coupled to donor Tyr-2766 in monomer 2 and acceptor Tyr- 1310 in monomer 1 is coupled to donor Tyr-108 in monomer 2 (PubMed:32025030). Sulfated tyrosines are desulfated during iodination. Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones. In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL. Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of T4. Following endocytosis, further processing occurs leading to the release of T3 and more T4 hormones. Thyroid dyshormonogenesis 3 (TDH3) [MIM:274700]: A disorder due to thyroid dyshormonogenesis, causing large goiters of elastic and soft consistency in the majority of patients. Although the degree of thyroid dysfunction varies considerably among patients with defective thyroglobulin synthesis, patients usually have a relatively high serum free triiodothyronine (T3) concentration with disproportionately low free tetraiodothyronine (T4) level. The maintenance of relatively high free T3 levels prevents profound tissue hypothyroidism except in brain and pituitary, which are dependent on T4 supply, resulting in neurologic and intellectual defects in some cases. te=The disease is caused by variants affecting the gene represented in this entry. Autoimmune thyroid disease 3 (AITD3) [MIM:608175]: A complex autoimmune disorder comprising two related diseases affecting the thyroid: Graves disease and Hashimoto thyroiditis. In both disorders, thyroid-reactive T-cells are formed and infiltrate the thyroid gland. In Graves disease, the majority of the T-cells undergo a Th2 differentiation and activate B-cells to produce antibodies against the TSH receptor, which stimulate the thyroid and cause clinical hyperthyroidism. In contrast, Hashimoto thyroiditis is characterized by Th1 switching of the thyroid-infiltrating T-cells, which induces apoptosis of thyroid follicular cells and clinical hypothyroidism. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the type-B carboxylesterase/lipase family. The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity. Name=Wikipedia; Note=Thyroglobulin entry; URL="https://en.wikipedia.org/wiki/Thyroglobulin"; hormone activity extracellular region signal transduction iodide transport thyroid gland development regulation of myelination thyroid hormone metabolic process hormone biosynthetic process uc003ytw.1 uc003ytw.2 uc003ytw.3 uc003ytw.4 uc003ytw.5 
ENST00000220659.11 BRF2 ENST00000220659.11 BRF2 RNA polymerase III transcription initiation factor subunit (from RefSeq NM_018310.4) B2RD62 B4DFZ6 BRF2_HUMAN BRFU D3DSW6 ENST00000220659.1 ENST00000220659.10 ENST00000220659.2 ENST00000220659.3 ENST00000220659.4 ENST00000220659.5 ENST00000220659.6 ENST00000220659.7 ENST00000220659.8 ENST00000220659.9 NM_018310 PRO1470 Q9H2Y3 Q9H3B3 Q9HAW0 Q9NUY6 uc003xkk.1 uc003xkk.2 uc003xkk.3 uc003xkk.4 uc003xkk.5 This gene encodes one of the multiple subunits of the RNA polymerase III transcription factor complex required for transcription of genes with promoter elements upstream of the initiation site. The product of this gene, a TFIIB-like factor, is directly recruited to the TATA-box of polymerase III small nuclear RNA gene promoters through its interaction with the TATA-binding protein. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7410570.427703.1, DRR138522.14564.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220659.11/ ENSP00000220659.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites (PubMed:11040218, PubMed:11121026, PubMed:11564744, PubMed:26638071). Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress (PubMed:26638071). Down-regulates expression of target genes in response to oxidative stress (PubMed:26638071). Overexpression protects cells against apoptosis in response to oxidative stress (PubMed:26638071). Component of TFIIIB complexes. The TFIIIB complex has two activities, alpha and beta. The TFIIIB-alpha activity complex is composed of TBP, BDP1, and a complex containing both BRF2 and at least four stably associated proteins; this complex inhibits the transcription by pol III via its phosphorylation by CK2; YY1 facilitates the TFIIIB-alpha complex formation. Interacts with TBP; this interaction promotes recruitment of BRF2 to TATA box-containing promoters (PubMed:26638071). Interacts with TBP and the BURE sequence (GC-rich sequence downstream from the TATA box) to form a strong ternary complex which is joined by BDP1; this ternary complex stimulates pol III transcription. Forms a trimeric complex composed of TBP, BRF2 and mini-SNAPc complex (SNAP43, SNAP50, and the N-terminal third of SNAP190) on the promoter. Assembly of the TBP-BRF2 complex is stimulated by SNAP190. Interacts with MAF1 and SNAPC4. Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9HAW0-1; Sequence=Displayed; Name=2; IsoId=Q9HAW0-2; Sequence=VSP_056834; Down-regulated by epigallocatechin gallate (EGCG) treatment. In response to oxidative stress, Cys-361 is reversibly oxidized to cysteine sulfenic acid. Oxidation of Cys-361 impairs formation of a ternary complex with TBP and DNA and down-regulates expression of target genes in response to oxidative stress. Belongs to the TFIIB family. Sequence=AAG35486.1; Type=Erroneous initiation; Evidence=; transcription factor TFIIIB complex RNA polymerase III type 3 promoter sequence-specific DNA binding RNA polymerase III type 3 promoter DNA binding nucleus nucleoplasm DNA-templated transcription, initiation regulation of transcription, DNA-templated regulation of transcription from RNA polymerase III promoter transcription factor binding cellular response to oxidative stress metal ion binding DNA-templated transcriptional preinitiation complex assembly RNA polymerase III transcriptional preinitiation complex assembly uc003xkk.1 uc003xkk.2 uc003xkk.3 uc003xkk.4 uc003xkk.5 
ENST00000220669.10 ZFAND1 ENST00000220669.10 zinc finger AN1-type containing 1, transcript variant 1 (from RefSeq NM_024699.3) E5RIG0 E5RJ99 ENST00000220669.1 ENST00000220669.2 ENST00000220669.3 ENST00000220669.4 ENST00000220669.5 ENST00000220669.6 ENST00000220669.7 ENST00000220669.8 ENST00000220669.9 NM_024699 Q658R7 Q6IA32 Q6PGQ6 Q8TCF1 Q9H810 ZFAN1_HUMAN ZFAND1 uc003ycj.1 uc003ycj.2 uc003ycj.3 uc003ycj.4 Plays a role in the regulation of cytoplasmic stress granules (SGs) turnover. SGs are dynamic and transient cytoplasmic ribonucleoprotein assemblies important for cellular protein homeostasis when protein production is suspended after acute exogenous stress (PubMed:29804830). Associates with SGs and is involved in the efficient and specific arsenite-induced clearance process of SGs through the recruitment of the ubiquitin-selective ATPase VCP and the 26S proteasome (PubMed:29804830). This process requires both complexes for efficient degradation of damaged ubiquitinated SG proteins during recovery from arsenite stress, and hence avoiding aberrant cytoplasmic SGs degradation via autophagy (PubMed:29804830). Associates with the 26S proteasome; this association occurs upon exposure to arsenite and is reduced in the presence of ATP (PubMed:29804830). Interacts (via AN1-type 1 and 2 zinc fingers) with PSMD1; this interaction is increased upon arsenite treatment and occurs in an ATP-independent manner (PubMed:29804830). Interacts with PSMC4 (PubMed:29804830). Interacts with PSMA1 (PubMed:29804830). Interacts (via its ubiquitin-like region) with VCP; this interaction occurs in an arsenite-dependent manner and is necessary for the recruitment of the ubiquitin-selective ATPase VCP to stress granules (SGs) (PubMed:29804830). Cytoplasm, Stress granule Note=Colocalizes with TIA1, G3BP1, VCP and 26S proteasome in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment in a VCP-independent manner (PubMed:29804830). Not localized in SGs in response to other heat- oxidative- or osmotic-induced stress treatments. Colocalizes with VCP in cytoplasmic speckles (PubMed:29804830). Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q8TCF1-1; Sequence=Displayed; Name=2; IsoId=Q8TCF1-2; Sequence=VSP_014988; Name=3; IsoId=Q8TCF1-3; Sequence=VSP_046404; Name=4; IsoId=Q8TCF1-4; Sequence=VSP_054080, VSP_054081; The ubiquitin-like region is necessary for its localization to stress granules (SGs) in a VCP-independent manner (PubMed:29804830). The AN1-type 1 and 2 zinc finger domains are necessary for the recruitment of the 26S proteasome to SGs (PubMed:29804830). Both the AN1-type 1 and 2 zinc finger domains and the ubiquitin-like region are necessary for efficient SGs clearance upon specific arsenite-induced responses (PubMed:29804830). protein binding cytoplasm zinc ion binding cytoplasmic stress granule stress granule disassembly metal ion binding proteasome binding positive regulation of intracellular protein transport cellular response to arsenite ion cellular response to oxidative stress cellular response to heat cellular response to osmotic stress uc003ycj.1 uc003ycj.2 uc003ycj.3 uc003ycj.4 
ENST00000220676.2 RP1 ENST00000220676.2 RP1 axonemal microtubule associated, transcript variant 1 (from RefSeq NM_006269.2) ENST00000220676.1 NM_006269 ORP1 P56715 RP1_HUMAN uc003xsd.1 uc003xsd.2 This gene encodes a member of the doublecortin family. The protein encoded by this gene contains two doublecortin domains, which bind microtubules and regulate microtubule polymerization. The encoded protein is a photoreceptor microtubule-associated protein and is required for correct stacking of outer segment disc. This protein and the RP1L1 protein, another retinal-specific protein, play essential and synergistic roles in affecting photosensitivity and outer segment morphogenesis of rod photoreceptors. Because of its response to in vivo retinal oxygen levels, this protein was initially named ORP1 (oxygen-regulated protein-1). This protein was subsequently designated RP1 (retinitis pigmentosa 1) when it was found that mutations in this gene cause autosomal dominant retinitis pigmentosa. Mutations in this gene also cause autosomal recessive retinitis pigmentosa. Transcript variants resulted from an alternative promoter and alternative splicings have been found, which overlap the current reference sequence and has several exons upstream and downstream of the current reference sequence. However, the biological validity and full-length nature of some variants cannot be determined at this time.[provided by RefSeq, Sep 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF141021.1, AF146592.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968968, SAMEA2144333 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220676.2/ ENSP00000220676.1 RefSeq Select criteria :: based on computational evidence ##RefSeq-Attributes-END## Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme (By similarity). Interacts (via the doublecortin domains) with microtubules. Interacts with RP1L1 (By similarity). Interacts with MAK (By similarity). Cytoplasm, cytoskeleton, cilium axoneme Cell projection, cilium, photoreceptor outer segment Note=Specifically localized in the connecting cilia of rod and cone photoreceptors. Expressed in retina. Not expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, spleen and pancreas. The doublecortin domains, which mediate interaction with microtubules, are required for regulation of microtubule polymerization and function in photoreceptor differentiation. Retinitis pigmentosa 1 (RP1) [MIM:180100]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. te=The disease is caused by variants affecting the gene represented in this entry. Name=RetNet; Note=Retinal information network; URL="https://sph.uth.tmc.edu/retnet/"; Name=Mutations of the RP1 gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/rp1mut.htm"; photoreceptor outer segment photoreceptor inner segment protein binding cytoplasm cytoskeleton microtubule microtubule associated complex cilium axoneme visual perception phototransduction, visible light microtubule binding cell projection organization photoreceptor connecting cilium axoneme assembly intracellular signal transduction photoreceptor cell outer segment organization photoreceptor cell development cell projection photoreceptor cell maintenance retinal rod cell development retinal cone cell development response to stimulus retina development in camera-type eye retina morphogenesis in camera-type eye cellular response to light stimulus ciliary tip photoreceptor cell cilium positive regulation of non-motile cilium assembly uc003xsd.1 uc003xsd.2 
ENST00000220751.5 RIPK2 ENST00000220751.5 receptor interacting serine/threonine kinase 2, transcript variant 1 (from RefSeq NM_003821.6) B7Z748 CARDIAK ENST00000220751.1 ENST00000220751.2 ENST00000220751.3 ENST00000220751.4 NM_003821 O43353 Q6UWF0 RICK RIP2 RIPK2 RIPK2_HUMAN UNQ277/PRO314/PRO34092 uc003yee.1 uc003yee.2 uc003yee.3 uc003yee.4 uc003yee.5 This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase activation and recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-kappaB and inducer of apoptosis in response to various stimuli. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY358814.1, SRR1660807.150538.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220751.5/ ENSP00000220751.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:9575181, PubMed:9642260, PubMed:14638696, PubMed:21123652, PubMed:17054981, PubMed:28656966). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17562858, PubMed:21123652, PubMed:17054981, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:29452636, PubMed:28545134, PubMed:30279485, PubMed:30478312, PubMed:30026309). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:22607974, PubMed:17562858, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence= In the inactive state, the helix alphaC is packed against the helical, non-phosphorylated activation segment (AS) (PubMed:28545134). Upon activation, helix alphaC is displaced and the phosphorylated AS becomes disordered (PubMed:28545134). Specifically inhibited by GSK583, which blocks NOD2 signaling by interfering with XIAP binding to RIPK2 (PubMed:29452636). Specifically inhibited by CSLP37 and CSLP43, which blocks NOD2 signaling by interfering with XIAP binding to RIPK2 (PubMed:30026309). Interacts (via CARD domain) with NOD2 (via CARD domain) (PubMed:15044951, PubMed:17355968, PubMed:19592251, PubMed:21887730, PubMed:27812135, PubMed:30279485, PubMed:30478312). Interacts (via CARD domain) with NOD1 (via CARD domain) (PubMed:17054981, PubMed:30478312). Homooligomer; following interaction with NOD1 or NOD2, homooligomerizes via its CARD domain and forms long filaments named RIPosomes (PubMed:30279485, PubMed:30478312). Found in a signaling complex consisting of at least ARHGEF2, NOD2 and RIPK2 (PubMed:21887730). Interacts with ARHGEF2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK (PubMed:21887730). Interacts with MAP3K4; this interaction sequesters RIPK2 from the NOD2 signaling pathway (PubMed:18775659). Interacts with IKBKG/NEMO (PubMed:18079694). The polyubiquitinated protein interacts with MAP3K7/TAK1; interaction is indirect and is mediated by TAB2 and TAB3 that bind to polyubiquitin chains attached to RIPK2 (PubMed:18079694). Binds to CFLAR/CLARP and CASP1 via their CARD domains (PubMed:9575181). Binds to BIRC3/c-IAP1 and BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6 (PubMed:21931591). Interacts with NLRP10 (PubMed:22672233). Interacts with CARD9 (By similarity). Interacts with INAVA; the interaction takes place upon PRR stimulation (PubMed:28436939). Interacts (via CARD domain) with NGFR (via death domain) (PubMed:26646181). Interacts with IRGM; promoting RIPK2 degradation (PubMed:36221902). O43353; Q13490: BIRC2; NbExp=3; IntAct=EBI-358522, EBI-514538; O43353; Q13489: BIRC3; NbExp=3; IntAct=EBI-358522, EBI-517709; O43353; Q9BX69: CARD6; NbExp=2; IntAct=EBI-358522, EBI-14405242; O43353; Q7Z434: MAVS; NbExp=3; IntAct=EBI-358522, EBI-995373; O43353; Q9HC29: NOD2; NbExp=3; IntAct=EBI-358522, EBI-7445625; O43353; O43353: RIPK2; NbExp=6; IntAct=EBI-358522, EBI-358522; O43353; Q12933: TRAF2; NbExp=2; IntAct=EBI-358522, EBI-355744; O43353; Q13114: TRAF3; NbExp=6; IntAct=EBI-358522, EBI-357631; O43353; P98170: XIAP; NbExp=21; IntAct=EBI-358522, EBI-517127; O43353; P62258: YWHAE; NbExp=2; IntAct=EBI-358522, EBI-356498; Cytoplasm Cell membrane ; Peripheral membrane protein Endoplasmic reticulum Note=Recruited to the cell membrane by NOD2 following stimulation by bacterial peptidoglycans. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43353-1; Sequence=Displayed; Name=2; IsoId=O43353-2; Sequence=VSP_013266; Detected in heart, brain, placenta, lung, peripheral blood leukocytes, spleen, kidney, testis, prostate, pancreas and lymph node. Contains an N-terminal kinase domain and a C-terminal caspase activation and recruitment domain (CARD) that mediates the recruitment of CARD-containing proteins. Polyubiquitinated via both 'Lys-63'- and 'Met-1'-linked polyubiquitin following recruitment by NOD1 or NOD2, creating docking sites for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitination by XIAP is essential for NOD2 signaling and promotes recruitment of the LUBAC complex (PubMed:22607974, PubMed:29452636, PubMed:30026309). Also polyubiquitinated with 'Lys-63'-linked chains by PELI3, BIRC2/c-IAP1 and BIRC3/c-IAP2 (PubMed:19464198, PubMed:21931591). Ubiquitinated on Lys-209 via 'Lys-63'-linked by ITCH (PubMed:18079694, PubMed:19592251). Undergoes 'Lys-63'-linked deubiquitination by MYSM1 to attenuate NOD2- mediated inflammation and tissue damage (By similarity). Polyubiquitinated with 'Lys-63'-linked chains in response to Shigella infection, promoting its SQSTM1/p62-dependent autophagic degradation (PubMed:36221902). Undergoes 'Met-1'-linked polyubiquitination; the head-to-tail linear polyubiquitination is mediated by the LUBAC complex in response to NOD2 stimulation 'Met-1'-linked polyubiquitination (PubMed:23806334). 'Lys-63'-linked polyubiquitination by XIAP is required for recruimtent of the LUBAC complex and subsequent (PubMed:22607974). Linear polyubiquitination is restricted by FAM105B/otulin, probably to limit NOD2-dependent pro-inflammatory signaling activation of NF-kappa-B (PubMed:23806334). Ubiquitination at Lys-503 by ZNRF4 via 'Lys-48'-linked polyubiquitination promotes RIPK2 degradation by the proteasome; ubiquitination by ZNRF4 takes place during both acute and NOD2 tolerance conditions (PubMed:28656966). Autophosphorylated (PubMed:16824733, PubMed:21123652, PubMed:29452636, PubMed:28545134). Phosphorylated at Ser-176, either via autophosphorylation or by LRRK2, enhancing activity (PubMed:16824733, PubMed:27830463). Autophosphorylation at Tyr-474 is required for effective NOD2 signaling (PubMed:21123652). Autophosphorylation is however not essential for NOD2 signaling (PubMed:29452636). Phosphorylation at Tyr-381 by Src kinase CSK occurs in a ARHGEF2-dependent manner and is required for NOD2-dependent innate immune activation (PubMed:21887730). Degraded via selective autophagy following interaction with IRGM (PubMed:36221902). IRGM promotes NOD1/NOD2-RIPK2 RIPosome recruitment to autophagosome membranes (PubMed:36221902). RIPK2 biquitinated via 'Lys-63'-linked chains is then recognized by SQSTM1/p62, leading to the SQSTM1/p62-dependent autophagic degradation of the NOD1/NOD2-RIPK2 RIPosome (PubMed:36221902). (Microbial infection) Acetylation of Ser-174, Ser-176 and Ser-178 by Yersinia YopJ prevents phosphorylation and activation, thereby promoting cell death. Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. nucleotide binding activation of MAPK activity positive regulation of cytokine-mediated signaling pathway adaptive immune response immune system process positive regulation of T-helper 1 type immune response protein kinase activity protein serine/threonine kinase activity non-membrane spanning protein tyrosine kinase activity receptor binding protein binding ATP binding cytoplasm mitochondrion cytosol cytoskeleton protein phosphorylation apoptotic process inflammatory response signal transduction I-kappaB kinase/NF-kappaB signaling JNK cascade positive regulation of peptidyl-threonine phosphorylation positive regulation of cell death kinase activity phosphorylation transferase activity peptidyl-tyrosine phosphorylation LIM domain binding positive regulation of protein ubiquitination lipopolysaccharide-mediated signaling pathway vesicle positive regulation of protein binding positive regulation of chemokine production positive regulation of interferon-alpha production positive regulation of interferon-beta production positive regulation of interferon-gamma production positive regulation of interleukin-12 production positive regulation of interleukin-2 production positive regulation of interleukin-6 production positive regulation of tumor necrosis factor production positive regulation of stress-activated MAPK cascade macromolecular complex positive regulation of immature T cell proliferation positive regulation of peptidyl-serine phosphorylation toll-like receptor 2 signaling pathway toll-like receptor 4 signaling pathway T cell proliferation identical protein binding protein homodimerization activity regulation of apoptotic process positive regulation of apoptotic process negative regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling response to exogenous dsRNA innate immune response positive regulation of T-helper 1 cell differentiation positive regulation of transcription from RNA polymerase II promoter positive regulation of JNK cascade positive regulation of alpha-beta T cell proliferation CARD domain binding positive regulation of interleukin-1 beta secretion positive regulation of peptidyl-tyrosine phosphorylation defense response to Gram-positive bacterium T cell receptor signaling pathway positive regulation of NF-kappaB transcription factor activity positive regulation of ERK1 and ERK2 cascade nucleotide-binding oligomerization domain containing signaling pathway nucleotide-binding oligomerization domain containing 1 signaling pathway nucleotide-binding oligomerization domain containing 2 signaling pathway interleukin-1-mediated signaling pathway response to interleukin-1 response to interleukin-12 response to interleukin-18 cellular response to lipopolysaccharide cellular response to lipoteichoic acid cellular response to peptidoglycan cellular response to muramyl dipeptide caspase binding activation of cysteine-type endopeptidase activity positive regulation of xenophagy uc003yee.1 uc003yee.2 uc003yee.3 uc003yee.4 uc003yee.5 
ENST00000220763.10 CPQ ENST00000220763.10 carboxypeptidase Q (from RefSeq NM_016134.4) B2RD88 CBPQ_HUMAN ENST00000220763.1 ENST00000220763.2 ENST00000220763.3 ENST00000220763.4 ENST00000220763.5 ENST00000220763.6 ENST00000220763.7 ENST00000220763.8 ENST00000220763.9 LCH1 NM_016134 PGCP Q8NBZ1 Q9UNM8 Q9Y5X6 Q9Y646 uc003yhw.1 uc003yhw.2 uc003yhw.3 uc003yhw.4 uc003yhw.5 uc003yhw.6 This gene encodes a metallopeptidase that belongs to the peptidase M28 family. The encoded protein may catalyze the cleavage of dipeptides with unsubstituted terminals into amino acids. [provided by RefSeq, Jul 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.988663.1, SRR3476690.1004497.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220763.10/ ENSP00000220763.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor. Homodimer. The monomeric form is inactive while the homodimer is active. Endoplasmic reticulum Golgi apparatus Lysosome Secreted Note=Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin. Mainly detected in blood plasma. Abundant in placenta and kidney. Present at low level in muscles, liver and skin fibroblasts. Not detected in brain or white blood cells (at protein level). Up-regulated in the majority of hepatitis C virus-associated hepatocellular carcinoma. N-glycosylated. The secreted form is modified by hybrid or complex type oligosaccharide chains (By similarity). Belongs to the peptidase M28 family. Sequence=AAD31418.1; Type=Frameshift; Evidence=; carboxypeptidase activity extracellular region extracellular space cytoplasm lysosome endoplasmic reticulum Golgi apparatus proteolysis thyroid hormone generation peptidase activity metallopeptidase activity hydrolase activity tissue regeneration protein homodimerization activity peptide catabolic process intracellular membrane-bounded organelle metal ion binding extracellular exosome metallodipeptidase activity uc003yhw.1 uc003yhw.2 uc003yhw.3 uc003yhw.4 uc003yhw.5 uc003yhw.6 
ENST00000220764.7 DECR1 ENST00000220764.7 2,4-dienoyl-CoA reductase 1, transcript variant 1 (from RefSeq NM_001359.2) B7Z6B8 DECR DECR_HUMAN ENST00000220764.1 ENST00000220764.2 ENST00000220764.3 ENST00000220764.4 ENST00000220764.5 ENST00000220764.6 NM_001359 Q16698 Q2M304 Q93085 SDR18C1 uc003yek.1 uc003yek.2 uc003yek.3 This gene encodes an accessory enzyme which participates in the beta-oxidation and metabolism of unsaturated fatty enoyl-CoA esters. [provided by RefSeq, Jul 2008]. Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in mitochondria. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101, ChEBI:CHEBI:85493; EC=1.3.1.124; Evidence=; Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099, ChEBI:CHEBI:85493; EC=1.3.1.124; Evidence=; Reaction=(2E,4E)-hexadienoyl-CoA + H(+) + NADPH = (3E)-hexenoyl-CoA + NADP(+); Xref=Rhea:RHEA:44912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:84788, ChEBI:CHEBI:84790; Evidence=; Kinetic parameters: KM=7.7 uM for NADPH ; KM=14.3 uM for trans-2,trans-4-hexadienoyl-CoA ; Vmax=30.3 umol/min/mg enzyme ; Homotetramer. Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q16698-1; Sequence=Displayed; Name=2; IsoId=Q16698-2; Sequence=VSP_056388; Heart = liver = pancreas > kidney >> skeletal muscle = lung. 2,4-dienoyl-CoA reductase deficiency (DECRD) [MIM:616034]: A rare, autosomal recessive, inborn error of polyunsaturated fatty acids and lysine metabolism, resulting in mitochondrial dysfunction. Affected individuals have a severe encephalopathy with neurologic and metabolic abnormalities beginning in early infancy. Laboratory studies show increased C10:2 carnitine levels and hyperlysinemia. Note=The protein represented in this entry is involved in disease pathogenesis. A selective decrease in mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS. Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily. nucleus nucleoplasm mitochondrion mitochondrial matrix cytosol lipid metabolic process fatty acid metabolic process fatty acid beta-oxidation 2,4-dienoyl-CoA reductase (NADPH) activity oxidoreductase activity protein homotetramerization oxidation-reduction process NADPH binding uc003yek.1 uc003yek.2 uc003yek.3 
ENST00000220772.8 SFRP1 ENST00000220772.8 secreted frizzled related protein 1 (from RefSeq NM_003012.5) ENST00000220772.1 ENST00000220772.2 ENST00000220772.3 ENST00000220772.4 ENST00000220772.5 ENST00000220772.6 ENST00000220772.7 FRP FRP1 NM_003012 O00546 O14779 Q8N474 SARP2 SFRP1_HUMAN uc003xnt.1 uc003xnt.2 uc003xnt.3 uc003xnt.4 uc003xnt.5 This gene encodes a member of the SFRP family that contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. Members of this family act as soluble modulators of Wnt signaling; epigenetic silencing of SFRP genes leads to deregulated activation of the Wnt-pathway which is associated with cancer. This gene may also be involved in determining the polarity of photoreceptor cells in the retina. [provided by RefSeq, Sep 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC036503.1, AF056087.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN03267752, SAMN03267761 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220772.8/ ENSP00000220772.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase (By similarity). In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF- dependent transcription. Interacts with WNT1, WNT2 and FRZD6. Interacts with WNT4, WNT8 and MYOC (By similarity). Q8N474; O60353: FZD6; NbExp=3; IntAct=EBI-3940687, EBI-8754490; Q8N474; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-3940687, EBI-2548832; Secreted. Note=Cell membrane or extracellular matrix-associated. Released by heparin-binding. Widely expressed. Absent from lung, liver and peripheral blood leukocytes. Highest levels in heart and fetal kidney. Also expressed in testis, ovary, fetal brain and lung, leiomyomal cells, myometrial cells and vascular smooth muscle cells. Expressed in foreskin fibroblasts and in keratinocytes. Down-regulated in colorectal and breast tumors. Up-regulated in uterine leiomyomas under high estrogenic conditions. Expression, in leiomyomal cells, also increased both under hypoxic and serum deprivation conditions. The FZ domain is involved in binding with Wnt ligands. May have therapeutic use in cardiac surgery. Belongs to the secreted frizzled-related protein (sFRP) family. osteoblast differentiation ureteric bud development somitogenesis neural tube closure positive regulation of cell-matrix adhesion hematopoietic progenitor cell differentiation cysteine-type endopeptidase activity frizzled binding protein binding extracellular region extracellular space cytosol plasma membrane proteolysis multicellular organism development drug binding heparin binding positive regulation of cell proliferation negative regulation of cell proliferation male gonad development female gonad development cellular response to starvation dorsal/ventral axis specification anterior/posterior pattern specification cell surface regulation of cell cycle process negative regulation of gene expression negative regulation of epithelial to mesenchymal transition regulation of neuron projection development neural crest cell fate commitment response to organic cyclic compound Wnt signaling pathway Wnt-protein binding neural tube development hemopoiesis cell differentiation positive regulation of Wnt signaling pathway negative regulation of Wnt signaling pathway negative regulation of ossification positive regulation of cell growth negative regulation of cell growth negative regulation of cell migration negative regulation of BMP signaling pathway negative regulation of osteoblast proliferation somatic stem cell population maintenance non-canonical Wnt signaling pathway response to drug identical protein binding positive regulation of apoptotic process negative regulation of apoptotic process negative regulation of JUN kinase activity positive regulation of GTPase activity cellular response to fibroblast growth factor stimulus stromal-epithelial cell signaling involved in prostate gland development negative regulation of B cell differentiation positive regulation of fat cell differentiation negative regulation of osteoblast differentiation negative regulation of osteoclast differentiation regulation of angiogenesis positive regulation of smoothened signaling pathway negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated development of primary male sexual characteristics negative regulation of insulin secretion negative regulation of bone remodeling negative regulation of fibroblast proliferation digestive tract morphogenesis positive regulation of epithelial cell proliferation negative regulation of epithelial cell proliferation negative regulation of peptidyl-tyrosine phosphorylation positive regulation of stress fiber assembly positive regulation of focal adhesion assembly canonical Wnt signaling pathway Wnt signaling pathway, planar cell polarity pathway hematopoietic stem cell differentiation bone trabecula formation prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis regulation of branching involved in prostate gland morphogenesis negative regulation of androgen receptor signaling pathway extracellular exosome cellular response to vitamin D cellular response to interleukin-1 cellular response to tumor necrosis factor cellular response to growth factor stimulus cellular response to prostaglandin E stimulus cellular response to estrogen stimulus cellular response to estradiol stimulus cellular response to hypoxia cellular response to X-ray cellular response to heparin dopaminergic neuron differentiation cellular response to transforming growth factor beta stimulus cellular response to BMP stimulus negative regulation of canonical Wnt signaling pathway regulation of establishment of planar polarity planar cell polarity pathway involved in neural tube closure Wnt signaling pathway involved in somitogenesis convergent extension involved in somitogenesis positive regulation of canonical Wnt signaling pathway positive regulation of extrinsic apoptotic signaling pathway via death domain receptors regulation of midbrain dopaminergic neuron differentiation negative regulation of planar cell polarity pathway involved in axis elongation positive regulation of non-canonical Wnt signaling pathway negative regulation of Wnt signaling pathway involved in dorsal/ventral axis specification negative regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation negative regulation of fibroblast apoptotic process positive regulation of fibroblast apoptotic process positive regulation of extrinsic apoptotic signaling pathway uc003xnt.1 uc003xnt.2 uc003xnt.3 uc003xnt.4 uc003xnt.5 
ENST00000220809.9 PLAT ENST00000220809.9 plasminogen activator, tissue type, transcript variant 1 (from RefSeq NM_000930.5) A8K022 B2R8E8 ENST00000220809.1 ENST00000220809.2 ENST00000220809.3 ENST00000220809.4 ENST00000220809.5 ENST00000220809.6 ENST00000220809.7 ENST00000220809.8 NM_000930 P00750 PLAT Q15103 Q503B0 Q6PJA5 Q7Z7N2 Q86YK8 Q9BU99 Q9BZW1 TPA_HUMAN uc003xos.1 uc003xos.2 uc003xos.3 uc003xos.4 This gene encodes tissue-type plasminogen activator, a secreted serine protease that converts the proenzyme plasminogen to plasmin, a fibrinolytic enzyme. The encoded preproprotein is proteolytically processed by plasmin or trypsin to generate heavy and light chains. These chains associate via disulfide linkages to form the heterodimeric enzyme. This enzyme plays a role in cell migration and tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding, while decreased activity leads to hypofibrinolysis, which can result in thrombosis or embolism. Alternative splicing of this gene results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Jan 2016]. Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy (By similarity). Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.68; Inhibited by SERPINA5. Heterodimer of chain A and chain B held by a disulfide bond. Forms a heterodimer with SERPINA5. Binds to fibrin with high affinity. This interaction leads to an increase in the catalytic efficiency of the enzyme between 100-fold and 1000-fold, due to an increase in affinity for plasminogen. Similarly, binding to heparin increases the activation of plasminogen. Binds to annexin A2, cytokeratin-8, fibronectin and laminin. Binds to mannose receptor and the low-density lipoprotein receptor-related protein (LRP1); these proteins are involved in TPA clearance. Yet unidentified interactions on endothelial cells and vascular smooth muscle cells (VSMC) lead to a 100-fold stimulation of plasminogen activation. In addition, binding to VSMC reduces TPA inhibition by PAI-1 by 30-fold. Binds LRP1B; binding is followed by internalization and degradation. In complex with SERPINE1, interacts with SORL1 (PubMed:15053742). Secreted, extracellular space. Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=Long; IsoId=P00750-1; Sequence=Displayed; Name=2; Synonyms=Short; IsoId=P00750-2; Sequence=VSP_005411, VSP_005412; Name=3; IsoId=P00750-3; Sequence=VSP_015957; Name=4; Synonyms=Neonatal; IsoId=P00750-4; Sequence=VSP_028029, VSP_028030; Synthesized in numerous tissues (including tumors) and secreted into most extracellular body fluids, such as plasma, uterine fluid, saliva, gingival crevicular fluid, tears, seminal fluid, and milk. Both FN1 and one of the kringle domains are required for binding to fibrin. Both FN1 and EGF-like domains are important for binding to LRP1. The FN1 domain mediates binding to annexin A2. The second kringle domain is implicated in binding to cytokeratin-8 and to the endothelial cell surface binding site. The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg- 310 catalyzed by plasmin, tissue kallikrein or factor Xa. Differential cell-specific N-linked glycosylation gives rise to two glycoforms, type I (glycosylated at Asn-219) and type II (not glycosylated at Asn-219). The single chain type I glycoform is less readily converted into the two-chain form by plasmin, and the two-chain type I glycoform has a lower activity than the two-chain type II glycoform in the presence of fibrin. N-glycosylation of Asn-152; the bound oligomannosidic glycan is involved in the interaction with the mannose receptor. Characterization of O-linked glycan was studied in Bowes melanoma cell line. Note=Increased activity of TPA results in increased fibrinolysis of fibrin blood clots that is associated with excessive bleeding. Defective release of TPA results in hypofibrinolysis that can lead to thrombosis or embolism. Available under the names Activase (Genentech) and Retavase (Centocor and Roche) [Retavase is a fragment of TPA that contains kringle 2 and the protease domain; it was also known as BM 06.022]. Used in Acute Myocardial Infarction (AMI), in Acute Ischemic Stroke (AIS) and Pulmonary Embolism (PE) to initiate fibrinolysis. [Isoform 2]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the peptidase S1 family. Name=Wikipedia; Note=Tissue plasminogen activator entry; URL="https://en.wikipedia.org/wiki/Tissue_plasminogen_Activator"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/plat/"; Name=Activase; Note=Clinical information on Activase; URL="https://www.activase.com/"; Name=Chiesi; Note=Clinical information on Retavase; URL="https://chiesiusa.com/products/retavase-2/"; response to hypoxia serine-type endopeptidase activity receptor binding protein binding extracellular region extracellular space cytoplasm cellular protein modification process proteolysis blood coagulation peptidase activity serine-type peptidase activity cell surface smooth muscle cell migration hydrolase activity secretory granule plasminogen activation fibrinolysis apical part of cell negative regulation of proteolysis platelet-derived growth factor receptor signaling pathway phosphoprotein binding extracellular exosome glutamatergic synapse uc003xos.1 uc003xos.2 uc003xos.3 uc003xos.4 
ENST00000220812.3 DKK4 ENST00000220812.3 dickkopf WNT signaling pathway inhibitor 4 (from RefSeq NM_014420.3) DKK4_HUMAN ENST00000220812.1 ENST00000220812.2 NM_014420 Q3KNX0 Q9UBT3 Q9Y4C3 uc003xpb.1 uc003xpb.2 uc003xpb.3 uc003xpb.4 uc003xpb.5 This gene encodes a protein that is a member of the dickkopf family. The secreted protein contains two cysteine rich regions and is involved in embryonic development through its interactions with the Wnt signaling pathway. Activity of this protein is modulated by binding to the Wnt co-receptor and the co-factor kremen 2. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: CX167283.1, CX163996.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2144335 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000220812.3/ ENSP00000220812.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). Interacts with LRP5 and LRP6. Q9UBT3; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-18030204, EBI-6166686; Q9UBT3; P11215: ITGAM; NbExp=3; IntAct=EBI-18030204, EBI-2568251; Q9UBT3; Q96CV9: OPTN; NbExp=3; IntAct=EBI-18030204, EBI-748974; Q9UBT3; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-18030204, EBI-12195249; Secreted. Expressed in cerebellum, T-cells, esophagus and lung. The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6. Appears to be not glycosylated. Can be proteolytically processed by a furin-like protease. Belongs to the dickkopf family. molecular_function cellular_component extracellular region extracellular space multicellular organism development Wnt signaling pathway negative regulation of Wnt signaling pathway co-receptor binding receptor antagonist activity negative regulation of hair follicle placode formation negative regulation of canonical Wnt signaling pathway negative regulation of receptor activity uc003xpb.1 uc003xpb.2 uc003xpb.3 uc003xpb.4 uc003xpb.5 
ENST00000220822.12 GDAP1 ENST00000220822.12 ganglioside induced differentiation associated protein 1, transcript variant 1 (from RefSeq NM_018972.4) A8K957 E7FJF3 E7FJF4 ENST00000220822.1 ENST00000220822.10 ENST00000220822.11 ENST00000220822.2 ENST00000220822.3 ENST00000220822.4 ENST00000220822.5 ENST00000220822.6 ENST00000220822.7 ENST00000220822.8 ENST00000220822.9 GDAP1_HUMAN NM_018972 Q8TB36 uc003yah.1 uc003yah.2 uc003yah.3 uc003yah.4 uc003yah.5 This gene encodes a member of the ganglioside-induced differentiation-associated protein family, which may play a role in a signal transduction pathway during neuronal development. Mutations in this gene have been associated with various forms of Charcot-Marie-Tooth Disease and neuropathy. Two transcript variants encoding different isoforms and a noncoding variant have been identified for this gene. [provided by RefSeq, Feb 2012]. Regulates the mitochondrial network by promoting mitochondrial fission. Homodimer. Q8TB36; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-11110431, EBI-10308705; Q8TB36; O95870: ABHD16A; NbExp=3; IntAct=EBI-11110431, EBI-348517; Q8TB36; P05090: APOD; NbExp=3; IntAct=EBI-11110431, EBI-715495; Q8TB36; P54252: ATXN3; NbExp=3; IntAct=EBI-11110431, EBI-946046; Q8TB36; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-11110431, EBI-9092016; Q8TB36; O15392: BIRC5; NbExp=3; IntAct=EBI-11110431, EBI-518823; Q8TB36; Q9UMX3: BOK; NbExp=3; IntAct=EBI-11110431, EBI-7105206; Q8TB36; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-11110431, EBI-747776; Q8TB36; P51798: CLCN7; NbExp=3; IntAct=EBI-11110431, EBI-4402346; Q8TB36; Q16740: CLPP; NbExp=3; IntAct=EBI-11110431, EBI-1056029; Q8TB36; Q9NR90-2: DAZ3; NbExp=3; IntAct=EBI-11110431, EBI-25830216; Q8TB36; Q96PD2-2: DCBLD2; NbExp=5; IntAct=EBI-11110431, EBI-12135455; Q8TB36; Q9UHI6: DDX20; NbExp=3; IntAct=EBI-11110431, EBI-347658; Q8TB36; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-11110431, EBI-6448852; Q8TB36; Q8IWE2: FAM114A1; NbExp=3; IntAct=EBI-11110431, EBI-2686288; Q8TB36; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-11110431, EBI-10253815; Q8TB36; P09017: HOXC4; NbExp=3; IntAct=EBI-11110431, EBI-3923226; Q8TB36; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-11110431, EBI-21911304; Q8TB36; Q8NA54: IQUB; NbExp=3; IntAct=EBI-11110431, EBI-10220600; Q8TB36; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-11110431, EBI-10261141; Q8TB36; Q99683: MAP3K5; NbExp=3; IntAct=EBI-11110431, EBI-476263; Q8TB36; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-11110431, EBI-4397720; Q8TB36; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-11110431, EBI-995714; Q8TB36; O43196-2: MSH5; NbExp=3; IntAct=EBI-11110431, EBI-25844576; Q8TB36; Q96CV9-2: OPTN; NbExp=3; IntAct=EBI-11110431, EBI-9091423; Q8TB36; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-11110431, EBI-9090282; Q8TB36; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-11110431, EBI-8652812; Q8TB36; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-11110431, EBI-25837959; Q8TB36; Q9GZS3: SKIC8; NbExp=3; IntAct=EBI-11110431, EBI-358545; Q8TB36; Q16637-3: SMN2; NbExp=3; IntAct=EBI-11110431, EBI-395447; Q8TB36; O60749: SNX2; NbExp=3; IntAct=EBI-11110431, EBI-1046690; Q8TB36; Q05C28: SPACA3; NbExp=3; IntAct=EBI-11110431, EBI-25845337; Q8TB36; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-11110431, EBI-10696971; Q8TB36; Q96DR4: STARD4; NbExp=3; IntAct=EBI-11110431, EBI-17217258; Q8TB36; P37802: TAGLN2; NbExp=3; IntAct=EBI-11110431, EBI-1056740; Q8TB36; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-11110431, EBI-8638294; Q8TB36; A2RU14: TMEM218; NbExp=3; IntAct=EBI-11110431, EBI-10173151; Q8TB36; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-11110431, EBI-2850578; Q8TB36; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-11110431, EBI-524753; Q8TB36; Q14966-2: ZNF638; NbExp=3; IntAct=EBI-11110431, EBI-25845021; Q8TB36; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-11110431, EBI-25845217; Mitochondrion outer membrane ulti-pass membrane protein Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8TB36-1; Sequence=Displayed; Name=2; IsoId=Q8TB36-2; Sequence=VSP_038393; Highly expressed in whole brain and spinal cord. Predominant expression in central tissues of the nervous system not only in neurons but also in Schwann cells. Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. Charcot-Marie-Tooth disease 4A (CMT4A) [MIM:214400]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie- Tooth disease are designated CMT4. CMT4A is a severe form characterized by early age of onset and rapid progression leading to inability to walk in late childhood or adolescence. te=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, axonal, with vocal cord paresis, autosomal recessive (CMT2RV) [MIM:607706]: A form of Charcot-Marie- Tooth disease characterized by the association of axonal neuropathy with vocal cord paresis. Charcot-Marie-Tooth disease is a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. te=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, axonal, 2K (CMT2K) [MIM:607831]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Charcot-Marie-Tooth disease type 2K onset is in early childhood (younger than 3 years). This phenotype is characterized by foot deformities, kyphoscoliosis, distal limb muscle weakness and atrophy, areflexia, and diminished sensation in the lower limbs. Weakness in the upper limbs is observed in the first decade, with clawing of the fingers. Inheritance can be autosomal dominant or recessive. te=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, recessive intermediate A (CMTRIA) [MIM:608340]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie- Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the GST superfamily. While belonging to the GST superfamily, it lacks glutathione transferase activity. Name=Inherited peripheral neuropathies mutation db; URL="https://uantwerpen.vib.be/CMTMutations"; mitochondrial fission nucleus cytoplasm mitochondrion mitochondrial outer membrane cytosol protein targeting to mitochondrion mitochondrion organization mitochondrial fusion membrane integral component of membrane integral component of mitochondrial outer membrane response to retinoic acid cellular response to vitamin D uc003yah.1 uc003yah.2 uc003yah.3 uc003yah.4 uc003yah.5 
ENST00000220849.10 EIF3E ENST00000220849.10 eukaryotic translation initiation factor 3 subunit E (from RefSeq NM_001568.3) EIF3E EIF3E_HUMAN EIF3S6 ENST00000220849.1 ENST00000220849.2 ENST00000220849.3 ENST00000220849.4 ENST00000220849.5 ENST00000220849.6 ENST00000220849.7 ENST00000220849.8 ENST00000220849.9 INT6 NM_001568 O43902 P60228 Q64058 Q64059 Q64252 Q6FG33 Q8WVK4 uc003ymu.1 uc003ymu.2 uc003ymu.3 uc003ymu.4 uc003ymu.5 Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl- tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway (PubMed:17468741). May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins (PubMed:17310990, PubMed:17324924). Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with COPS3, COPS6, COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and UPF2. Interacts with the HTLV-1 protein Tax-1. Interacts with IFIT1 and IFIT2 (PubMed:16023166, PubMed:16973618). Interacts with BZW2/5MP1 (PubMed:21745818). P60228; Q8IY42: C4orf19; NbExp=4; IntAct=EBI-347740, EBI-10216552; P60228; P04233: CD74; NbExp=2; IntAct=EBI-347740, EBI-2622890; P60228; P02489: CRYAA; NbExp=3; IntAct=EBI-347740, EBI-6875961; P60228; Q8IY21: DDX60; NbExp=2; IntAct=EBI-347740, EBI-2807346; P60228; P55884: EIF3B; NbExp=6; IntAct=EBI-347740, EBI-366696; P60228; Q99613: EIF3C; NbExp=14; IntAct=EBI-347740, EBI-353741; P60228; O15371: EIF3D; NbExp=6; IntAct=EBI-347740, EBI-353818; P60228; Q9UBQ5: EIF3K; NbExp=6; IntAct=EBI-347740, EBI-354344; P60228; Q9Y262: EIF3L; NbExp=7; IntAct=EBI-347740, EBI-373519; P60228; Q99814: EPAS1; NbExp=10; IntAct=EBI-347740, EBI-447470; P60228; O95208-2: EPN2; NbExp=3; IntAct=EBI-347740, EBI-12135243; P60228; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-347740, EBI-8561769; P60228; Q86U28: ISCA2; NbExp=3; IntAct=EBI-347740, EBI-10258659; P60228; Q92993: KAT5; NbExp=3; IntAct=EBI-347740, EBI-399080; P60228; Q5T749: KPRP; NbExp=3; IntAct=EBI-347740, EBI-10981970; P60228; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-347740, EBI-11742507; P60228; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-347740, EBI-2801965; P60228; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-347740, EBI-2857471; P60228; P17252: PRKCA; NbExp=3; IntAct=EBI-347740, EBI-1383528; P60228; Q59EK9: RUNDC3A; NbExp=4; IntAct=EBI-347740, EBI-747225; P60228; Q59EK9-3: RUNDC3A; NbExp=3; IntAct=EBI-347740, EBI-11957366; P60228; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-347740, EBI-9090795; P60228; P14373: TRIM27; NbExp=7; IntAct=EBI-347740, EBI-719493; P60228; P61981: YWHAG; NbExp=3; IntAct=EBI-347740, EBI-359832; P60228; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-347740, EBI-524753; P60228; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-347740, EBI-12006434; P60228; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-347740, EBI-6248094; Cytoplasm. Nucleus, PML body. Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus. Mass=52131.8; Method=Unknown; Evidence=; Mass=52133.4; Mass_error=0.2; Method=MALDI; Evidence=; Belongs to the eIF-3 subunit E family. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay formation of cytoplasmic translation initiation complex cytoplasmic translational initiation RNA binding translation initiation factor activity protein binding nucleus nucleoplasm cytoplasm cytosol eukaryotic translation initiation factor 3 complex translation translational initiation regulation of translational initiation membrane eukaryotic 43S preinitiation complex nuclear body PML body eukaryotic 48S preinitiation complex cadherin binding positive regulation of translation negative regulation of translational initiation protein N-terminus binding extracellular exosome eukaryotic translation initiation factor 3 complex, eIF3e positive regulation of mRNA binding chromatin uc003ymu.1 uc003ymu.2 uc003ymu.3 uc003ymu.4 uc003ymu.5 
ENST00000220853.8 EMC2 ENST00000220853.8 ER membrane protein complex subunit 2, transcript variant 5 (from RefSeq NR_138033.2) EMC2 EMC2_HUMAN ENST00000220853.1 ENST00000220853.2 ENST00000220853.3 ENST00000220853.4 ENST00000220853.5 ENST00000220853.6 ENST00000220853.7 KIAA0103 NR_138033 Q15006 Q8WUE1 TTC35 uc003ymw.1 uc003ymw.2 uc003ymw.3 Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176, PubMed:32439656, PubMed:33964204). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:30415835, PubMed:29809151, PubMed:29242231). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:30415835, PubMed:29809151). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N- terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable). Component of the ER membrane protein complex (EMC) (PubMed:22119785, PubMed:29242231, PubMed:32439656, PubMed:32459176, PubMed:33964204). Interacts with WNK1 (via amphipathic alpha-helix region); promoting the ER membrane protein complex assembly by preventing EMC2 ubiquitination (PubMed:33964204). Q15006; Q53Y03: COX4NB; NbExp=3; IntAct=EBI-359031, EBI-10235116; Q15006; Q9P0I2: EMC3; NbExp=7; IntAct=EBI-359031, EBI-1054670; Q15006; O43402: EMC8; NbExp=13; IntAct=EBI-359031, EBI-741841; Q15006; Q9Y3B6: EMC9; NbExp=10; IntAct=EBI-359031, EBI-748366; Q15006; Q96GW1: HSP90B1; NbExp=3; IntAct=EBI-359031, EBI-12885352; Q15006; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-359031, EBI-747204; Q15006; Q8N4V1: MMGT1; NbExp=9; IntAct=EBI-359031, EBI-6163737; Q15006; Q9Y5F1: PCDHB12; NbExp=3; IntAct=EBI-359031, EBI-12012016; Q15006; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-359031, EBI-747389; Q15006; Q9UHA2: SS18L2; NbExp=3; IntAct=EBI-359031, EBI-10962400; Endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side Note=May also localize to the nuclear envelope. Ubiquitinated when soluble in the cytoplasm, leading to its degradation by the proteasome (PubMed:33964204). Interaction with EMC2 prevents its ubiquitination and degradation (PubMed:33964204). Belongs to the EMC2 family. protein binding nucleus cytoplasm endoplasmic reticulum ER membrane protein complex uc003ymw.1 uc003ymw.2 uc003ymw.3 
ENST00000220876.12 STMN2 ENST00000220876.12 stathmin 2, transcript variant 2 (from RefSeq NM_007029.4) A8K9M2 ENST00000220876.1 ENST00000220876.10 ENST00000220876.11 ENST00000220876.2 ENST00000220876.3 ENST00000220876.4 ENST00000220876.5 ENST00000220876.6 ENST00000220876.7 ENST00000220876.8 ENST00000220876.9 G3V110 NM_007029 O14952 Q6PK68 Q93045 SCG10 SCGN10 STMN2_HUMAN uc003ybj.1 uc003ybj.2 uc003ybj.3 uc003ybj.4 This gene encodes a member of the stathmin family of phosphoproteins. Stathmin proteins function in microtubule dynamics and signal transduction. The encoded protein plays a regulatory role in neuronal growth and is also thought to be involved in osteogenesis. Reductions in the expression of this gene have been associated with Down's syndrome and Alzheimer's disease. Alternatively spliced transcript variants have been observed for this gene. A pseudogene of this gene is located on the long arm of chromosome 6. [provided by RefSeq, Nov 2010]. Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone (By similarity). Interacts with MAPK8 (By similarity). Interacts with ITM2C. Interacts with KIFBP. Interacts (via the N-terminal region) with CIB1 (via C-terminal region); the interaction is direct, occurs in a calcium-dependent manner and attenuates the neurite outgrowth inhibition of STMN2. Q93045; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-714194, EBI-10175300; Q93045; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-714194, EBI-11962928; Q93045; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-714194, EBI-6658203; Q93045; O95983-2: MBD3; NbExp=3; IntAct=EBI-714194, EBI-11978579; Q93045; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-714194, EBI-741158; Q93045; P20618: PSMB1; NbExp=3; IntAct=EBI-714194, EBI-372273; Q93045; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-714194, EBI-6117072; Q93045; Q8IYF3: TEX11; NbExp=5; IntAct=EBI-714194, EBI-742397; Q93045; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-714194, EBI-11523345; Q93045; Q12800: TFCP2; NbExp=3; IntAct=EBI-714194, EBI-717422; Q93045; P40222: TXLNA; NbExp=4; IntAct=EBI-714194, EBI-359793; Cytoplasm Cytoplasm, perinuclear region Cell projection, growth cone. Membrane ; Peripheral membrane protein ; Cytoplasmic side Cell projection, axon. Golgi apparatus. Endosome Cell projection, lamellipodium. Note=Associated with punctate structures in the perinuclear cytoplasm, axons, and growth cones of developing neurons. SCG10 exists in both soluble and membrane- bound forms. Colocalized with CIB1 in neurites of developing hippocampal primary neurons (By similarity). Colocalized with CIB1 in the cell body, neuritis and growth cones of neurons. Colocalized with CIB1 to the leading edge of lamellipodia. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q93045-1; Sequence=Displayed; Name=2; IsoId=Q93045-2; Sequence=VSP_045047; Neuron specific. Sumoylated. Phosphorylated mostly by MAPK8, but also by MAPK9 and MAPK10 in the developing brain cortex. N-terminal palmitoylation promotes specific anchoring to the cytosolic leaflet of Golgi membranes and subsequent vesicular trafficking along dendrites and axons. Neuronal Stathmins are substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15. Belongs to the stathmin family. protein binding cytoplasm endosome Golgi apparatus microtubule depolymerization negative regulation of microtubule depolymerization positive regulation of neuron projection development negative regulation of neuron projection development tubulin binding membrane lamellipodium axon growth cone regulation of microtubule polymerization or depolymerization negative regulation of microtubule polymerization positive regulation of microtubule depolymerization neuron projection development vesicle cell projection neuron projection neuronal cell body calcium-dependent protein binding perinuclear region of cytoplasm regulation of cytoskeleton organization cellular response to nerve growth factor stimulus uc003ybj.1 uc003ybj.2 uc003ybj.3 uc003ybj.4 
ENST00000220913.10 CHRAC1 ENST00000220913.10 chromatin accessibility complex subunit 1, transcript variant 1 (from RefSeq NM_017444.6) CHRAC15 CHRC1_HUMAN ENST00000220913.1 ENST00000220913.2 ENST00000220913.3 ENST00000220913.4 ENST00000220913.5 ENST00000220913.6 ENST00000220913.7 ENST00000220913.8 ENST00000220913.9 NM_017444 Q9NRG0 uc003yvl.1 uc003yvl.2 uc003yvl.3 uc003yvl.4 uc003yvl.5 CHRAC1 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexes for DNA transcription, replication, and packaging.[supplied by OMIM, Apr 2004]. Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. Does not enhance nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling complex (PubMed:14759371). Heterodimer with POLE3; binds to DNA (PubMed:10880450). Component of the CHRAC ISWI chromatin remodeling complex at least composed of SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and POLE3; the complex preferentially binds DNA through the CHRAC1-POLE3 heterodimer and possesses ATP-dependent nucleosome-remodeling activity (PubMed:10880450). Within the complex, the heterodimer with POLE3 interacts with SMARCA5/SNF2H; the interaction is direct and enhances nucleosome sliding activity by the SMARCA5/SNF2H and BAZ1A/ACF1 interaction (PubMed:10880450, PubMed:14759371). Within the complex, the heterodimer with POLE3 interacts with BAZ1A/ACF1; the interactions are direct (PubMed:10880450, PubMed:12434153, PubMed:14759371). Q9NRG0; Q8IZU0: FAM9B; NbExp=7; IntAct=EBI-2795492, EBI-10175124; Q9NRG0; Q9NRF9: POLE3; NbExp=13; IntAct=EBI-2795492, EBI-744901; Nucleus Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. DNA binding transcription factor activity, sequence-specific DNA binding DNA-directed DNA polymerase activity protein binding nucleus chromatin remodeling regulation of transcription, DNA-templated epsilon DNA polymerase complex CHRAC transferase activity nucleotidyltransferase activity protein heterodimerization activity DNA biosynthetic process uc003yvl.1 uc003yvl.2 uc003yvl.3 uc003yvl.4 uc003yvl.5 
ENST00000220931.11 NCALD ENST00000220931.11 neurocalcin delta, transcript variant 8 (from RefSeq NM_032041.3) ENST00000220931.1 ENST00000220931.10 ENST00000220931.2 ENST00000220931.3 ENST00000220931.4 ENST00000220931.5 ENST00000220931.6 ENST00000220931.7 ENST00000220931.8 ENST00000220931.9 NCALD_HUMAN NM_032041 P29554 P61601 Q8IYC3 Q9H0W2 uc003yke.1 uc003yke.2 uc003yke.3 uc003yke.4 uc003yke.5 This gene encodes a member of the neuronal calcium sensor (NCS) family of calcium-binding proteins. The protein contains an N-terminal myristoylation signal and four EF-hand calcium binding loops. The protein is cytosolic at resting calcium levels; however, elevated intracellular calcium levels induce a conformational change that exposes the myristoyl group, resulting in protein association with membranes and partial co-localization with the perinuclear trans-golgi network. The protein is thought to be a regulator of G protein-coupled receptor signal transduction. Several alternatively spliced variants of this gene have been determined, all of which encode the same protein; additional variants may exist but their biological validity has not been determined. [provided by RefSeq, Jul 2008]. May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds three calcium ions. Interacts with GUCY2D. P61601; P23352: ANOS1; NbExp=3; IntAct=EBI-749635, EBI-5272188; P61601; O95236-2: APOL3; NbExp=3; IntAct=EBI-749635, EBI-11976321; P61601; Q9H6X5-2: C19orf44; NbExp=3; IntAct=EBI-749635, EBI-12061599; P61601; Q9BXJ5: C1QTNF2; NbExp=12; IntAct=EBI-749635, EBI-2817707; P61601; Q03060-25: CREM; NbExp=5; IntAct=EBI-749635, EBI-12884642; P61601; Q86UW9: DTX2; NbExp=12; IntAct=EBI-749635, EBI-740376; P61601; P10767: FGF6; NbExp=3; IntAct=EBI-749635, EBI-11479013; P61601; O75084: FZD7; NbExp=3; IntAct=EBI-749635, EBI-746917; P61601; Q7Z5G4: GOLGA7; NbExp=3; IntAct=EBI-749635, EBI-4403685; P61601; Q96SL4: GPX7; NbExp=3; IntAct=EBI-749635, EBI-749411; P61601; P24592: IGFBP6; NbExp=3; IntAct=EBI-749635, EBI-947015; P61601; P02538: KRT6A; NbExp=3; IntAct=EBI-749635, EBI-702198; P61601; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-749635, EBI-10246750; P61601; P15018: LIF; NbExp=3; IntAct=EBI-749635, EBI-1037189; P61601; Q99732: LITAF; NbExp=5; IntAct=EBI-749635, EBI-725647; P61601; O95868: LY6G6D; NbExp=3; IntAct=EBI-749635, EBI-12382527; P61601; P50222: MEOX2; NbExp=3; IntAct=EBI-749635, EBI-748397; P61601; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-749635, EBI-11988931; P61601; P55197-2: MLLT10; NbExp=3; IntAct=EBI-749635, EBI-12853322; P61601; Q969H8: MYDGF; NbExp=5; IntAct=EBI-749635, EBI-718622; P61601; P41271-2: NBL1; NbExp=3; IntAct=EBI-749635, EBI-12135485; P61601; Q9NWW9: PLAAT2; NbExp=3; IntAct=EBI-749635, EBI-12253270; P61601; Q6UWP8-2: SBSN; NbExp=3; IntAct=EBI-749635, EBI-18282351; P61601; Q7Z699: SPRED1; NbExp=9; IntAct=EBI-749635, EBI-5235340; P61601; P10124: SRGN; NbExp=3; IntAct=EBI-749635, EBI-744915; P61601; Q9NRR2: TPSG1; NbExp=3; IntAct=EBI-749635, EBI-17210651; P61601; Q7DB77: tir; Xeno; NbExp=3; IntAct=EBI-749635, EBI-6480811; Retina, cerebrum, cerebellum, brain stem, spinal cord, testis, ovary and small intestine. Belongs to the recoverin family. regulation of systemic arterial blood pressure actin binding calcium ion binding protein binding intracellular cytosol tubulin binding vesicle-mediated transport calcium-mediated signaling clathrin coat of trans-Golgi network vesicle clathrin binding alpha-tubulin binding metal ion binding uc003yke.1 uc003yke.2 uc003yke.3 uc003yke.4 uc003yke.5 
ENST00000220940.2 GML ENST00000220940.2 glycosylphosphatidylinositol anchored molecule like (from RefSeq NM_002066.3) A0AVF6 ENST00000220940.1 GML_HUMAN LY6DL NM_002066 O00686 O00731 Q99445 uc003yxg.1 uc003yxg.2 uc003yxg.3 uc003yxg.4 May play a role in the apoptotic pathway or cell-cycle regulation induced by p53/TP53 after DNA damage. Cell membrane ; Lipid-anchor, GPI- anchor By p53/TP53. plasma membrane apoptotic process DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest negative regulation of cell proliferation membrane extrinsic component of membrane anchored component of membrane uc003yxg.1 uc003yxg.2 uc003yxg.3 uc003yxg.4 
ENST00000221086.8 MTMR9 ENST00000221086.8 myotubularin related protein 9 (from RefSeq NM_015458.4) B7Z291 C8orf9 ENST00000221086.1 ENST00000221086.2 ENST00000221086.3 ENST00000221086.4 ENST00000221086.5 ENST00000221086.6 ENST00000221086.7 MTMR8 MTMR9_HUMAN NM_015458 Q52LU3 Q8WW11 Q96QG6 Q96QG7 Q9NX50 uc003wtm.1 uc003wtm.2 uc003wtm.3 uc003wtm.4 uc003wtm.5 This gene encodes a myotubularin-related protein that is atypical to most other members of the myotubularin-related protein family because it has no dual-specificity phosphatase domain. The encoded protein contains a double-helical motif similar to the SET interaction domain, which is thought to have a role in the control of cell proliferation. In mouse, a protein similar to the encoded protein binds with MTMR7, and together they dephosphorylate phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AJ297823.1, BC034990.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221086.8/ ENSP00000221086.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Acts as an adapter for myotubularin-related phosphatases (PubMed:19038970, PubMed:22647598). Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5- bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols (PubMed:19038970, PubMed:22647598). Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3- phosphate (PubMed:22647598). The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970). Stabilizes MTMR8 protein levels (PubMed:22647598). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580). Negatively regulates autophagy, in part via its association with MTMR8 (PubMed:22647598). Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 (PubMed:19038970, PubMed:22647598). Does not bind mono-, di- and tri- phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (PubMed:19038970). Homodimer (PubMed:19038970). Heterodimer (via C-terminus) with lipid phosphatase MTMR6 (via C-terminus) (PubMed:16787938, PubMed:12890864, PubMed:19038970, PubMed:23188820). Heterodimer (via coiled coil domain) with lipid phosphatase MTMR7 (via C-terminus) (By similarity). Heterodimer with lipid phosphatase MTMR8 (PubMed:22647598, PubMed:16787938). Q96QG7; O75140-2: DEPDC5; NbExp=3; IntAct=EBI-744593, EBI-12366971; Q96QG7; Q9Y6C2: EMILIN1; NbExp=10; IntAct=EBI-744593, EBI-744586; Q96QG7; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-744593, EBI-11748557; Q96QG7; Q9Y6X4: FAM169A; NbExp=3; IntAct=EBI-744593, EBI-1220497; Q96QG7; Q6IC98: GRAMD4; NbExp=3; IntAct=EBI-744593, EBI-10962409; Q96QG7; Q0VD86: INCA1; NbExp=3; IntAct=EBI-744593, EBI-6509505; Q96QG7; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-744593, EBI-3437878; Q96QG7; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-744593, EBI-3044087; Q96QG7; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-744593, EBI-739832; Q96QG7; A8MW99: MEI4; NbExp=3; IntAct=EBI-744593, EBI-19944212; Q96QG7; P00540: MOS; NbExp=6; IntAct=EBI-744593, EBI-1757866; Q96QG7; Q9Y217: MTMR6; NbExp=12; IntAct=EBI-744593, EBI-766064; Q96QG7; Q9Y216: MTMR7; NbExp=14; IntAct=EBI-744593, EBI-10293003; Q96QG7; Q96EF0: MTMR8; NbExp=6; IntAct=EBI-744593, EBI-750578; Q96QG7; Q96EF0-1: MTMR8; NbExp=3; IntAct=EBI-744593, EBI-15985865; Q96QG7; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-744593, EBI-10172876; Q96QG7; Q13287: NMI; NbExp=9; IntAct=EBI-744593, EBI-372942; Q96QG7; P26045: PTPN3; NbExp=3; IntAct=EBI-744593, EBI-1047946; Q96QG7; Q08AM6: VAC14; NbExp=3; IntAct=EBI-744593, EBI-2107455; Q96QG7; Q8N720: ZNF655; NbExp=3; IntAct=EBI-744593, EBI-625509; Cytoplasm ll projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side Cytoplasm, perinuclear region Endoplasmic reticulum Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the perinuclear region (PubMed:19038970). Partially localizes to the endoplasmic reticulum (PubMed:19038970). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96QG7-1; Sequence=Displayed; Name=2; IsoId=Q96QG7-2; Sequence=VSP_056209; Expressed in many tissues. The GRAM domain is required for cell membrane localization. The coiled coil domain mediates interaction with MTMR9. Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily. Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 333 in the dsPTPase catalytic loop, suggesting that it has no phosphatase activity. protein binding cytoplasm endoplasmic reticulum cytosol plasma membrane phosphatidylinositol biosynthetic process endocytosis negative regulation of autophagy positive regulation of phosphatase activity membrane protein phosphatase binding enzyme regulator activity ruffle membrane macromolecular complex cell projection perinuclear region of cytoplasm protein stabilization regulation of phosphatidylinositol dephosphorylation uc003wtm.1 uc003wtm.2 uc003wtm.3 uc003wtm.4 uc003wtm.5 
ENST00000221114.8 DCTN6 ENST00000221114.8 dynactin subunit 6 (from RefSeq NM_006571.4) B2RAC1 DCTN6 DCTN6_HUMAN ENST00000221114.1 ENST00000221114.2 ENST00000221114.3 ENST00000221114.4 ENST00000221114.5 ENST00000221114.6 ENST00000221114.7 NM_006571 O00399 WS3 uc003xhy.1 uc003xhy.2 uc003xhy.3 uc003xhy.4 uc003xhy.5 The protein encoded by this gene contains an RGD (Arg-Gly-Asp) motif in the N-terminal region, which confers adhesive properties to macromolecular proteins like fibronectin. It shares a high degree of sequence similarity with the mouse homolog, which has been suggested to play a role in mitochondrial biogenesis. The exact biological function of this gene is not known. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.517648.1, SRR3476690.1104743.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221114.8/ ENSP00000221114.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. Subunit of dynactin, a multiprotein complex part of a tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or HOOK3. The dynactin complex is built around ACTR1A/ACTB filament and consists of an actin-related filament composed of a shoulder domain, a pointed end and a barbed end (PubMed:23455152). Its length is defined by its flexible shoulder domain. The soulder is composed of 2 DCTN1 subunits, 4 DCTN2 and 2 DCTN3. The 4 DCNT2 (via N-terminus) bind the ACTR1A filament and act as molecular rulers to determine the length. The pointed end is important for binding dynein-dynactin cargo adapters. Consists of 4 subunits: ACTR10, DCNT4, DCTN5 and DCTN6. Within the complex DCTN6 forms a heterodimer with DCTN5 (PubMed:23455152). The barbed end is composed of a CAPZA1:CAPZB heterodimers, which binds ACTR1A/ACTB filament and dynactin and stabilizes dynactin (By similarity). Interacts with PLK1 (PubMed:23455152). Cytoplasm, cytoskeleton Chromosome, centromere, kinetochore Ubiquitous. Phosphorylation at Thr-186 by CDK1 during mitotic prometaphase creates a binding site for PLK1 that facilitates its recruitment to kinetochores. Belongs to the dynactin subunits 5/6 family. Dynactin subunit 6 subfamily. chromosome, centromeric region kinetochore condensed chromosome kinetochore chromosome cytoplasm centrosome cytosol cytoskeleton dynactin complex ER to Golgi vesicle-mediated transport antigen processing and presentation of exogenous peptide antigen via MHC class II uc003xhy.1 uc003xhy.2 uc003xhy.3 uc003xhy.4 uc003xhy.5 
ENST00000221130.11 GSR ENST00000221130.11 glutathione-disulfide reductase, transcript variant 1 (from RefSeq NM_000637.5) ENST00000221130.1 ENST00000221130.10 ENST00000221130.2 ENST00000221130.3 ENST00000221130.4 ENST00000221130.5 ENST00000221130.6 ENST00000221130.7 ENST00000221130.8 ENST00000221130.9 HEL-75 HEL-S-122m NM_000637 V9HW90 V9HW90_HUMAN uc003xih.1 uc003xih.2 uc003xih.3 uc003xih.4 uc003xih.5 This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein. It is a central enzyme of cellular antioxidant defense, and reduces oxidized glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant. Rare mutations in this gene result in hereditary glutathione reductase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been found. [provided by RefSeq, Aug 2010]. Maintains high levels of reduced glutathione in the cytosol. Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7; Evidence=; Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence=; Note=Binds 1 FAD per subunit. ; Cytoplasm Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. nucleotide binding glutathione-disulfide reductase activity cytoplasm glutathione metabolic process electron carrier activity external side of plasma membrane oxidoreductase activity oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor electron transport chain cell redox homeostasis flavin adenine dinucleotide binding NADP binding oxidation-reduction process cellular oxidant detoxification uc003xih.1 uc003xih.2 uc003xih.3 uc003xih.4 uc003xih.5 
ENST00000221132.8 TNFRSF10A ENST00000221132.8 TNF receptor superfamily member 10a (from RefSeq NM_003844.4) A8K5I4 APO2 DR4 ENST00000221132.1 ENST00000221132.2 ENST00000221132.3 ENST00000221132.4 ENST00000221132.5 ENST00000221132.6 ENST00000221132.7 NM_003844 O00220 Q53Y72 Q96E62 TR10A_HUMAN TRAILR1 uc003xda.1 uc003xda.2 uc003xda.3 uc003xda.4 uc003xda.5 The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL), and thus transduces cell death signal and induces cell apoptosis. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DRR138524.404726.1, SRR6380201.98557.17 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221132.8/ ENSP00000221132.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:26457518). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (PubMed:19090789). Promotes the activation of NF- kappa-B (PubMed:9430227). Monomer (PubMed:26457518). Homooligomers and heterooligomers with TNFRSF10B (PubMed:19090789). Three TNFRSF10A molecules interact with the TNFSF10 homotrimer (PubMed:26457518). Can interact with TRADD and RIPK1. Interacts with ARAP1. In the absence of stimulation, interacts with BIRC2, DDX3X and GSK3B. The interaction with BIRC2 and DDX3X is further enhanced upon receptor stimulation and accompanied by DDX3X and BIRC2 cleavage (PubMed:18846110). Interacts with ZDHHC3 (PubMed:22240897). (Microbial infection) Interacts with HCMV protein UL141; this interaction prevents TNFRSF10A cell surface expression. O00220; Q96P48: ARAP1; NbExp=4; IntAct=EBI-518861, EBI-710003; O00220; Q14790: CASP8; NbExp=9; IntAct=EBI-518861, EBI-78060; O00220; Q08380: LGALS3BP; NbExp=2; IntAct=EBI-518861, EBI-354956; O00220; P50591: TNFSF10; NbExp=4; IntAct=EBI-518861, EBI-495373; Cell membrane ; Single-pass type I membrane protein Membrane raft Cytoplasm, cytosol Note=Palmitoylation is required for association with membranes. Widely expressed. High levels are found in spleen, peripheral blood leukocytes, small intestine and thymus, but also in K- 562 erythroleukemia cells, MCF-7 breast carcinoma cells and activated T-cells. Palmitoylated (PubMed:19090789). Palmitoylation of TNFRSF10A is required for its association with lipid rafts, oligomerization and function in TRAIL-induced cell death (PubMed:19090789). Palmitoylated by ZDHHC3 (Probable). protease binding death receptor activity protein binding plasma membrane apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process signal transduction cell surface receptor signaling pathway activation of NF-kappaB-inducing kinase activity transcription factor binding extrinsic apoptotic signaling pathway via death domain receptors cell surface membrane integral component of membrane TRAIL-activated apoptotic signaling pathway signaling receptor activity regulation of apoptotic process positive regulation of apoptotic process TRAIL binding leukocyte migration cellular response to mechanical stimulus extrinsic apoptotic signaling pathway regulation of extrinsic apoptotic signaling pathway via death domain receptors negative regulation of extrinsic apoptotic signaling pathway via death domain receptors uc003xda.1 uc003xda.2 uc003xda.3 uc003xda.4 uc003xda.5 
ENST00000221138.9 PPP2CB ENST00000221138.9 protein phosphatase 2 catalytic subunit beta (from RefSeq NM_001009552.2) D3DSV4 ENST00000221138.1 ENST00000221138.2 ENST00000221138.3 ENST00000221138.4 ENST00000221138.5 ENST00000221138.6 ENST00000221138.7 ENST00000221138.8 NM_001009552 P11082 P62714 PP2AB_HUMAN PPP2CB Q6FHK5 uc003xik.1 uc003xik.2 uc003xik.3 uc003xik.4 uc003xik.5 This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes a beta isoform of the catalytic subunit. [provided by RefSeq, Mar 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.541421.1, SRR1163658.175840.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221138.9/ ENSP00000221138.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events (Probable). PP2A can modulate the activity of phosphorylase B kinase, casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence=; Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Binds 2 manganese ions per subunit. ; Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD (By similarity). PP2A consists of a common heterodimeric core enzyme (composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65) (subunit A)) that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Binds PPME1. May indirectly interact with SGO1, most probably through regulatory B56 subunits. Interacts with CTTNBP2NL. Interacts with PTPA (PubMed:12952889). P62714; Q9Y2T1: AXIN2; NbExp=4; IntAct=EBI-1044367, EBI-4400025; P62714; Q06787-7: FMR1; NbExp=3; IntAct=EBI-1044367, EBI-25856644; P62714; P78318: IGBP1; NbExp=6; IntAct=EBI-1044367, EBI-1055954; P62714; Q5VSL9: STRIP1; NbExp=5; IntAct=EBI-1044367, EBI-1773588; P62714; O75663: TIPRL; NbExp=2; IntAct=EBI-1044367, EBI-1054735; P62714; Q13642-2; NbExp=3; IntAct=EBI-1044367, EBI-8477209; Cytoplasm Nucleus Chromosome, centromere Cytoplasm, cytoskeleton, spindle pole Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization. Phosphorylation of either threonine (by autophosphorylation- activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation. May be monoubiquitinated by NOSIP. Belongs to the PPP phosphatase family. PP-1 subfamily. protein phosphatase type 2A complex chromosome, centromeric region spindle pole phosphoprotein phosphatase activity protein serine/threonine phosphatase activity protein binding nucleus chromosome cytoplasm cytosol cytoskeleton protein dephosphorylation protein C-terminus binding apoptotic mitochondrial changes response to lead ion regulation of gene expression hydrolase activity response to endoplasmic reticulum stress peptidyl-threonine dephosphorylation response to hydrogen peroxide proteasome-mediated ubiquitin-dependent protein catabolic process negative regulation of Ras protein signal transduction response to antibiotic metal ion binding tau protein binding peptidyl-serine dephosphorylation positive regulation of microtubule binding uc003xik.1 uc003xik.2 uc003xik.3 uc003xik.4 uc003xik.5 
ENST00000221166.10 NEFM ENST00000221166.10 neurofilament medium chain, transcript variant 1 (from RefSeq NM_005382.2) B4DGN2 E9PBF7 ENST00000221166.1 ENST00000221166.2 ENST00000221166.3 ENST00000221166.4 ENST00000221166.5 ENST00000221166.6 ENST00000221166.7 ENST00000221166.8 ENST00000221166.9 NEF3 NFM NFM_HUMAN NM_005382 P07197 Q4QRK6 uc003xed.1 uc003xed.2 uc003xed.3 uc003xed.4 uc003xed.5 uc003xed.6 Neurofilaments are type IV intermediate filament heteropolymers composed of light, medium, and heavy chains. Neurofilaments comprise the axoskeleton and functionally maintain neuronal caliber. They may also play a role in intracellular transport to axons and dendrites. This gene encodes the medium neurofilament protein. This protein is commonly used as a biomarker of neuronal damage. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Oct 2008]. Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). Forms heterodimers with NEFL; which can further hetero- oligomerize (in vitro) (By similarity). Forms heterodimers with INA (in vitro) (By similarity). P07197; P05412: JUN; NbExp=2; IntAct=EBI-1105035, EBI-852823; P07197; P07196: NEFL; NbExp=4; IntAct=EBI-1105035, EBI-475646; P07197; P06400: RB1; NbExp=2; IntAct=EBI-1105035, EBI-491274; P07197; Q15796: SMAD2; NbExp=3; IntAct=EBI-1105035, EBI-1040141; P07197; P08670: VIM; NbExp=5; IntAct=EBI-1105035, EBI-353844; Cytoplasm, cytoskeleton Cell projection, axon Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P07197-1; Sequence=Displayed; Name=2; IsoId=P07197-2; Sequence=VSP_046306; There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber. Phosphorylation seems to play a major role in the functioning of the larger neurofilament polypeptides (NF-M and NF-H), the levels of phosphorylation being altered developmentally and coincidentally with a change in the neurofilament function. Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. Belongs to the intermediate filament family. structural molecule activity structural constituent of cytoskeleton protein binding intermediate filament neurofilament microtubule binding axon neurofilament bundle assembly intermediate filament cytoskeleton neurofibrillary tangle uc003xed.1 uc003xed.2 uc003xed.3 uc003xed.4 uc003xed.5 uc003xed.6 
ENST00000221200.9 KCTD9 ENST00000221200.9 potassium channel tetramerization domain containing 9 (from RefSeq NM_017634.4) ENST00000221200.1 ENST00000221200.2 ENST00000221200.3 ENST00000221200.4 ENST00000221200.5 ENST00000221200.6 ENST00000221200.7 ENST00000221200.8 KCTD9_HUMAN NM_017634 Q6NUM8 Q7L273 Q9NXV4 uc003xeo.1 uc003xeo.2 uc003xeo.3 uc003xeo.4 uc003xeo.5 Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. Protein modification; protein ubiquitination. Forms pentamers. Component of a complex composed of 5 subunits of KCTD9 and 5 CUL3. Q7L273; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-4397613, EBI-11976299; Q7L273; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-4397613, EBI-10173507; Q7L273; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-4397613, EBI-11954519; Q7L273; P29972: AQP1; NbExp=3; IntAct=EBI-4397613, EBI-745213; Q7L273; Q03989: ARID5A; NbExp=3; IntAct=EBI-4397613, EBI-948603; Q7L273; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-4397613, EBI-11524452; Q7L273; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-4397613, EBI-2548012; Q7L273; Q9H257: CARD9; NbExp=3; IntAct=EBI-4397613, EBI-751319; Q7L273; Q9HC52: CBX8; NbExp=6; IntAct=EBI-4397613, EBI-712912; Q7L273; Q16543: CDC37; NbExp=3; IntAct=EBI-4397613, EBI-295634; Q7L273; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-4397613, EBI-2802782; Q7L273; P27918: CFP; NbExp=3; IntAct=EBI-4397613, EBI-9038570; Q7L273; P78560: CRADD; NbExp=3; IntAct=EBI-4397613, EBI-520375; Q7L273; Q13618: CUL3; NbExp=10; IntAct=EBI-4397613, EBI-456129; Q7L273; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-4397613, EBI-742054; Q7L273; Q05D60: DEUP1; NbExp=3; IntAct=EBI-4397613, EBI-748597; Q7L273; Q08426: EHHADH; NbExp=4; IntAct=EBI-4397613, EBI-2339219; Q7L273; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-4397613, EBI-6255981; Q7L273; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-4397613, EBI-741626; Q7L273; P55040: GEM; NbExp=6; IntAct=EBI-4397613, EBI-744104; Q7L273; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-4397613, EBI-11163335; Q7L273; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-4397613, EBI-5916454; Q7L273; Q9H8Y8: GORASP2; NbExp=7; IntAct=EBI-4397613, EBI-739467; Q7L273; O95872: GPANK1; NbExp=3; IntAct=EBI-4397613, EBI-751540; Q7L273; P49639: HOXA1; NbExp=5; IntAct=EBI-4397613, EBI-740785; Q7L273; P31273: HOXC8; NbExp=3; IntAct=EBI-4397613, EBI-1752118; Q7L273; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-4397613, EBI-11955401; Q7L273; Q14005-2: IL16; NbExp=3; IntAct=EBI-4397613, EBI-17178971; Q7L273; Q0VD86: INCA1; NbExp=3; IntAct=EBI-4397613, EBI-6509505; Q7L273; Q7L273: KCTD9; NbExp=4; IntAct=EBI-4397613, EBI-4397613; Q7L273; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-4397613, EBI-8472129; Q7L273; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-4397613, EBI-724915; Q7L273; Q15323: KRT31; NbExp=3; IntAct=EBI-4397613, EBI-948001; Q7L273; O76011: KRT34; NbExp=3; IntAct=EBI-4397613, EBI-1047093; Q7L273; Q92764: KRT35; NbExp=3; IntAct=EBI-4397613, EBI-1058674; Q7L273; Q6A162: KRT40; NbExp=3; IntAct=EBI-4397613, EBI-10171697; Q7L273; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-4397613, EBI-11953846; Q7L273; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-4397613, EBI-10241252; Q7L273; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-4397613, EBI-739832; Q7L273; Q17RB8: LONRF1; NbExp=6; IntAct=EBI-4397613, EBI-2341787; Q7L273; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-4397613, EBI-77889; Q7L273; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-4397613, EBI-12516603; Q7L273; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-4397613, EBI-16439278; Q7L273; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-4397613, EBI-2801965; Q7L273; O14561: NDUFAB1; NbExp=3; IntAct=EBI-4397613, EBI-1246261; Q7L273; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-4397613, EBI-740897; Q7L273; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-4397613, EBI-741158; Q7L273; Q8NFH5: NUP35; NbExp=7; IntAct=EBI-4397613, EBI-9050429; Q7L273; Q17RL8: PDZD4; NbExp=3; IntAct=EBI-4397613, EBI-10239064; Q7L273; Q99471: PFDN5; NbExp=3; IntAct=EBI-4397613, EBI-357275; Q7L273; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-4397613, EBI-79165; Q7L273; O60568: PLOD3; NbExp=3; IntAct=EBI-4397613, EBI-741582; Q7L273; Q8N490: PNKD; NbExp=3; IntAct=EBI-4397613, EBI-746368; Q7L273; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-4397613, EBI-11986735; Q7L273; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-4397613, EBI-10293968; Q7L273; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-4397613, EBI-2557469; Q7L273; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-4397613, EBI-11320284; Q7L273; P54646: PRKAA2; NbExp=3; IntAct=EBI-4397613, EBI-1383852; Q7L273; P25786: PSMA1; NbExp=6; IntAct=EBI-4397613, EBI-359352; Q7L273; P49721: PSMB2; NbExp=3; IntAct=EBI-4397613, EBI-359335; Q7L273; Q93062: RBPMS; NbExp=3; IntAct=EBI-4397613, EBI-740322; Q7L273; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-4397613, EBI-746118; Q7L273; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-4397613, EBI-6257312; Q7L273; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-4397613, EBI-12000762; Q7L273; O00560: SDCBP; NbExp=6; IntAct=EBI-4397613, EBI-727004; Q7L273; P63208: SKP1; NbExp=3; IntAct=EBI-4397613, EBI-307486; Q7L273; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-4397613, EBI-10269374; Q7L273; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-4397613, EBI-12275818; Q7L273; Q496A3: SPATS1; NbExp=3; IntAct=EBI-4397613, EBI-3923692; Q7L273; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-4397613, EBI-742688; Q7L273; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-4397613, EBI-10174456; Q7L273; Q8NCR6: SPMIP6; NbExp=3; IntAct=EBI-4397613, EBI-10269322; Q7L273; Q96LM6: SPMIP9; NbExp=3; IntAct=EBI-4397613, EBI-743976; Q7L273; O75558: STX11; NbExp=3; IntAct=EBI-4397613, EBI-714135; Q7L273; Q5T7P8-2: SYT6; NbExp=6; IntAct=EBI-4397613, EBI-10246152; Q7L273; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-4397613, EBI-745958; Q7L273; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-4397613, EBI-10172380; Q7L273; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-4397613, EBI-11139477; Q7L273; Q63HR2: TNS2; NbExp=3; IntAct=EBI-4397613, EBI-949753; Q7L273; P14373: TRIM27; NbExp=6; IntAct=EBI-4397613, EBI-719493; Q7L273; Q13049: TRIM32; NbExp=6; IntAct=EBI-4397613, EBI-742790; Q7L273; Q8IWZ5: TRIM42; NbExp=6; IntAct=EBI-4397613, EBI-5235829; Q7L273; Q15654: TRIP6; NbExp=3; IntAct=EBI-4397613, EBI-742327; Q7L273; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-4397613, EBI-12817837; Q7L273; Q9UK80: USP21; NbExp=3; IntAct=EBI-4397613, EBI-373242; Q7L273; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-4397613, EBI-11975223; Q7L273; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-4397613, EBI-7705033; Q7L273; P24278: ZBTB25; NbExp=3; IntAct=EBI-4397613, EBI-739899; Q7L273; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-4397613, EBI-12287587; Q7L273; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-4397613, EBI-347633; Q7L273; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-4397613, EBI-743265; Q7L273; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-4397613, EBI-4395669; Q7L273; P36508: ZNF76; NbExp=3; IntAct=EBI-4397613, EBI-7254550; Sequence=BAA90904.1; Type=Erroneous initiation; Evidence=; protein binding protein ubiquitination intracellular signal transduction identical protein binding protein self-association protein homooligomerization cullin family protein binding uc003xeo.1 uc003xeo.2 uc003xeo.3 uc003xeo.4 uc003xeo.5 
ENST00000221232.11 CNOT3 ENST00000221232.11 CCR4-NOT transcription complex subunit 3 (from RefSeq NM_014516.4) CNOT3 CNOT3_HUMAN ENST00000221232.1 ENST00000221232.10 ENST00000221232.2 ENST00000221232.3 ENST00000221232.4 ENST00000221232.5 ENST00000221232.6 ENST00000221232.7 ENST00000221232.8 ENST00000221232.9 KIAA0691 LENG2 NM_014516 NOT3 O75175 Q9NZN7 Q9UF76 uc002qdj.1 uc002qdj.2 uc002qdj.3 uc002qdj.4 uc002qdj.5 Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of embryonic stem (ES) cell identity. Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. In the complex interacts directly with CNOT2. Interacts with TIP120B and NANOS2. Interacts with EBF1. O75175; P27797: CALR; NbExp=3; IntAct=EBI-743073, EBI-1049597; O75175; A5YKK6: CNOT1; NbExp=2; IntAct=EBI-743073, EBI-1222758; O75175; Q9NZN8: CNOT2; NbExp=10; IntAct=EBI-743073, EBI-743033; O75175; Q96LI5: CNOT6L; NbExp=2; IntAct=EBI-743073, EBI-1046635; O75175; Q9UFF9: CNOT8; NbExp=3; IntAct=EBI-743073, EBI-742299; O75175; P36957: DLST; NbExp=3; IntAct=EBI-743073, EBI-351007; O75175; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-743073, EBI-1055945; O75175; P16284: PECAM1; NbExp=3; IntAct=EBI-743073, EBI-716404; O75175; Q9HCJ0: TNRC6C; NbExp=10; IntAct=EBI-743073, EBI-6507625; O75175; P50616: TOB1; NbExp=3; IntAct=EBI-743073, EBI-723281; O75175; P55072: VCP; NbExp=3; IntAct=EBI-743073, EBI-355164; O75175; Q6ZQ73: Cand2; Xeno; NbExp=3; IntAct=EBI-743073, EBI-6504831; Cytoplasm Nucleus Cytoplasm, P-body Note=NANOS2 promotes its localization to P-body. Ubiquitous. Highly expressed in brain, heart, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes. Expressed in embryonic stem (ES) cells. Intellectual developmental disorder with speech delay, autism and dysmorphic facies (IDDSADF) [MIM:618672]: An autosomal dominant disorder characterized by mild to severe intellectual disability, developmental delay, delayed or absent speech, hypotonia, short stature, autistic features, and highly variable dysmorphic facial features. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the CNOT2/3/5 family. Sequence=AAF29828.1; Type=Miscellaneous discrepancy; Note=Seems to have an artifactual loop-out at the 3'-end deleting 2 full exons and part of 2 others.; Evidence=; Sequence=BAA31666.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=CAB63766.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence=; nuclear-transcribed mRNA poly(A) tail shortening P-body trophectodermal cell differentiation protein binding nucleus cytoplasm cytosol regulation of transcription, DNA-templated regulation of translation DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest multicellular organism development negative regulation of translation CCR4-NOT complex CCR4-NOT core complex gene silencing by RNA regulation of stem cell population maintenance uc002qdj.1 uc002qdj.2 uc002qdj.3 uc002qdj.4 uc002qdj.5 
ENST00000221233.9 EXOSC5 ENST00000221233.9 exosome component 5 (from RefSeq NM_020158.4) CML28 ENST00000221233.1 ENST00000221233.2 ENST00000221233.3 ENST00000221233.4 ENST00000221233.5 ENST00000221233.6 ENST00000221233.7 ENST00000221233.8 EXOS5_HUMAN NM_020158 Q32Q81 Q8NG16 Q96I89 Q9NQT4 RRP46 uc002oqo.1 uc002oqo.2 uc002oqo.3 uc002oqo.4 uc002oqo.5 Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (PubMed:11782436, PubMed:21269460). In vitro, EXOSC5 does not bind or digest single-stranded RNA and binds to double-stranded DNA without detectable DNase activity (PubMed:20660080). Homodimer (PubMed:20660080). Component of the RNA exosome complex (PubMed:20660080, PubMed:29906447). Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC1. Interacts with GTPBP1. Interacts with ZC3HAV1. Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner. Q9NQT4; Q8WXI4-2: ACOT11; NbExp=3; IntAct=EBI-371876, EBI-17721098; Q9NQT4; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-371876, EBI-10173507; Q9NQT4; Q13490: BIRC2; NbExp=6; IntAct=EBI-371876, EBI-514538; Q9NQT4; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-371876, EBI-10193358; Q9NQT4; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-371876, EBI-739580; Q9NQT4; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-371876, EBI-347573; Q9NQT4; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-371876, EBI-742054; Q9NQT4; Q8NF50-2: DOCK8; NbExp=3; IntAct=EBI-371876, EBI-10174653; Q9NQT4; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-371876, EBI-2349927; Q9NQT4; Q9Y3B2: EXOSC1; NbExp=33; IntAct=EBI-371876, EBI-371892; Q9NQT4; Q01780: EXOSC10; NbExp=4; IntAct=EBI-371876, EBI-358236; Q9NQT4; Q9NQT5: EXOSC3; NbExp=10; IntAct=EBI-371876, EBI-371866; Q9NQT4; Q96B26: EXOSC8; NbExp=22; IntAct=EBI-371876, EBI-371922; Q9NQT4; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-371876, EBI-11977403; Q9NQT4; O14526: FCHO1; NbExp=4; IntAct=EBI-371876, EBI-719823; Q9NQT4; P07954: FH; NbExp=3; IntAct=EBI-371876, EBI-1050358; Q9NQT4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-371876, EBI-618309; Q9NQT4; P09017: HOXC4; NbExp=3; IntAct=EBI-371876, EBI-3923226; Q9NQT4; Q9UKT9: IKZF3; NbExp=7; IntAct=EBI-371876, EBI-747204; Q9NQT4; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-371876, EBI-742916; Q9NQT4; A1A4E9: KRT13; NbExp=3; IntAct=EBI-371876, EBI-10171552; Q9NQT4; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-371876, EBI-3044087; Q9NQT4; Q15323: KRT31; NbExp=3; IntAct=EBI-371876, EBI-948001; Q9NQT4; O76011: KRT34; NbExp=3; IntAct=EBI-371876, EBI-1047093; Q9NQT4; Q92764: KRT35; NbExp=3; IntAct=EBI-371876, EBI-1058674; Q9NQT4; O95447: LCA5L; NbExp=3; IntAct=EBI-371876, EBI-8473670; Q9NQT4; A0A087WWI0: LRMDA; NbExp=3; IntAct=EBI-371876, EBI-18393842; Q9NQT4; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-371876, EBI-741037; Q9NQT4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-371876, EBI-16439278; Q9NQT4; Q13615: MTMR3; NbExp=3; IntAct=EBI-371876, EBI-371938; Q9NQT4; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-371876, EBI-6952711; Q9NQT4; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-371876, EBI-3920396; Q9NQT4; Q86TG7-2: PEG10; NbExp=3; IntAct=EBI-371876, EBI-6259410; Q9NQT4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-371876, EBI-79165; Q9NQT4; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-371876, EBI-10232538; Q9NQT4; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-371876, EBI-11320284; Q9NQT4; Q04864: REL; NbExp=3; IntAct=EBI-371876, EBI-307352; Q9NQT4; Q04864-2: REL; NbExp=3; IntAct=EBI-371876, EBI-10829018; Q9NQT4; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-371876, EBI-12037847; Q9NQT4; Q13573: SNW1; NbExp=3; IntAct=EBI-371876, EBI-632715; Q9NQT4; P02549: SPTA1; NbExp=3; IntAct=EBI-371876, EBI-375617; Q9NQT4; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-371876, EBI-1105213; Q9NQT4; Q08117-2: TLE5; NbExp=3; IntAct=EBI-371876, EBI-11741437; Q9NQT4; Q13829: TNFAIP1; NbExp=6; IntAct=EBI-371876, EBI-2505861; Q9NQT4; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-371876, EBI-492476; Q9NQT4; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-371876, EBI-2130429; Q9NQT4; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-371876, EBI-6929619; Q9NQT4; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-371876, EBI-11419867; Q9NQT4; Q8TAQ5: ZNF420; NbExp=3; IntAct=EBI-371876, EBI-3923307; Q9NQT4; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-371876, EBI-4395669; Q9NQT4; Q8N720: ZNF655; NbExp=5; IntAct=EBI-371876, EBI-625509; Q9NQT4; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-371876, EBI-10240849; Q9NQT4; Q8K3Y6: Zc3hav1; Xeno; NbExp=6; IntAct=EBI-371876, EBI-8860250; Nucleus, nucleolus Cytoplasm Nucleus Highly expressed in a variety of hematopoietic and epithelial tumor cell lines, but not in normal hematopoietic tissues or other normal tissue, with the exception of testis. Cerebellar ataxia, brain abnormalities, and cardiac conduction defects (CABAC) [MIM:619576]: An autosomal recessive disorder characterized by global developmental delay, impaired intellectual development and speech delay that are observed in most patients. Disease manifestations are variable and include infantile-onset hypotonia, poor motor development, poor feeding and overall growth, and ataxic gait due to cerebellar ataxia. Additional variable features are dysarthria, nystagmus, variable ocular anomalies, spasticity, hyperreflexia, and non-specific dysmorphic features. Brain imaging shows cerebellar hypoplasia, often with brainstem hypoplasia, enlarged ventricles, delayed myelination, and thin corpus callosum. A significant number of patients develop cardiac conduction defects in childhood or adolescence. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the RNase PH family. The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active. Sequence=AAM75154.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; 3'-5'-exoribonuclease activity nuclear exosome (RNase complex) cytoplasmic exosome (RNase complex) exosome (RNase complex) RNA binding protein binding nucleus nucleoplasm nucleolus cytoplasm cytosol rRNA processing RNA catabolic process rRNA catabolic process nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' U4 snRNA 3'-end processing transcriptionally active chromatin regulation of mRNA stability exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay DNA deamination defense response to virus nuclear mRNA surveillance polyadenylation-dependent snoRNA 3'-end processing RNA phosphodiester bond hydrolysis, exonucleolytic exoribonuclease activity uc002oqo.1 uc002oqo.2 uc002oqo.3 uc002oqo.4 uc002oqo.5 
ENST00000221265.8 PAF1 ENST00000221265.8 PAF1 homolog, Paf1/RNA polymerase II complex component, transcript variant 1 (from RefSeq NM_019088.4) ENST00000221265.1 ENST00000221265.2 ENST00000221265.3 ENST00000221265.4 ENST00000221265.5 ENST00000221265.6 ENST00000221265.7 M0QX35 NM_019088 O75239 PAF1_HUMAN PD2 Q8N7H5 Q9H166 Q9NUU9 uc002old.1 uc002old.2 uc002old.3 uc002old.4 uc002old.5 uc002old.6 This gene encodes a subunit of the polymerase associated factor (PAF1) complex. The PAF1 complex interacts with RNA polymerase II and plays a role in transcription elongation as well as histone modifications including ubiquitylation and methylation. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Feb 2012]. Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser- 5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro. Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and SKIC8 (PubMed:19952111, PubMed:20178742). The PAF1 complex interacts with PHF5A (By similarity). Interacts with POLR2A, TCEA1, SKIC3, KMT2A/MLL1, SUPT5H, RNF20 and RNF40 (PubMed:15923622, PubMed:16024656, PubMed:19952111, PubMed:20178742, PubMed:20541477, PubMed:16491129, PubMed:19410543). Interacts with UBE2E1 (PubMed:16307923). Interacts with PINT87aa which is encoded by the circular form of the long non-coding RNA LINC-PINT; the interaction enhances the binding of the PAF1 complex to target gene promoters and may anchor the complex on target gene promoters, sequentially pausing RNA polymerase II-induced mRNA elongation (PubMed:30367041). (Microbial infection) Interacts with influenza A strain H3N2 NS1 protein; the interaction interferes with host cell gene transcription, specifically with that of antiviral genes. (Microbial infection) The PAF1 complex interacts with Zika virus French Polynesia 10087PF/2013 non-structural protein 5/NS5 (PubMed:30550790). The interaction with viral NS5 proteins may reduce the antiviral immune response by inhibiting the recruitment of the PAF1 complex to interferon-stimulated genes, thus preventing their transcription (PubMed:30550790). (Microbial infection) The PAF1 complex interacts with Dengue virus DENV2 16681 non-structural protein 5/NS5 (PubMed:30550790). The PAF1 complex interacts with Dengue virus DENV4 Dominica/814669/1981 non-structural protein 5/NS5 (PubMed:30550790). The interaction with viral NS5 proteins may reduce the antiviral immune response by inhibiting the recruitment of the PAF1 complex to interferon-stimulated genes, thus preventing their transcription (PubMed:30550790). Q8N7H5; Q6P1J9: CDC73; NbExp=31; IntAct=EBI-2607770, EBI-930143; Q8N7H5; Q6PD62: CTR9; NbExp=26; IntAct=EBI-2607770, EBI-1019583; Q8N7H5; P51116: FXR2; NbExp=4; IntAct=EBI-2607770, EBI-740459; Q8N7H5; P04792: HSPB1; NbExp=2; IntAct=EBI-2607770, EBI-352682; Q8N7H5; Q03164: KMT2A; NbExp=4; IntAct=EBI-2607770, EBI-591370; Q8N7H5; Q8WVC0: LEO1; NbExp=28; IntAct=EBI-2607770, EBI-932432; Q8N7H5; A0A455ZAR2: LINC-PINT; NbExp=5; IntAct=EBI-2607770, EBI-27121529; Q8N7H5; P24928: POLR2A; NbExp=5; IntAct=EBI-2607770, EBI-295301; Q8N7H5; Q92541: RTF1; NbExp=17; IntAct=EBI-2607770, EBI-1055239; Q8N7H5; Q6PGP7: SKIC3; NbExp=2; IntAct=EBI-2607770, EBI-6083436; Q8N7H5; P23193: TCEA1; NbExp=4; IntAct=EBI-2607770, EBI-2608271; Q8N7H5; P51965: UBE2E1; NbExp=2; IntAct=EBI-2607770, EBI-348546; Q8N7H5; B2BUF1: NS1; Xeno; NbExp=6; IntAct=EBI-2607770, EBI-4291940; Nucleus te=Punctuate distribution throughout the nucleus except in nucleoli and the perinuclear chromatin. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q8N7H5-1; Sequence=Displayed; Name=2; IsoId=Q8N7H5-2; Sequence=VSP_032650, VSP_032651, VSP_032652; Name=3; IsoId=Q8N7H5-3; Sequence=VSP_032650, VSP_055740, VSP_055741; Belongs to the PAF1 family. Sequence=AAC25503.1; Type=Erroneous gene model prediction; Evidence=; Sequence=EAW56880.1; Type=Erroneous gene model prediction; Evidence=; Sequence=EAW56881.1; Type=Erroneous gene model prediction; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44202/PAF1"; negative regulation of transcription from RNA polymerase II promoter RNA polymerase II core binding endodermal cell fate commitment chromatin binding protein binding nucleus nucleoplasm cytoplasm transcription from RNA polymerase II promoter transcription elongation from RNA polymerase II promoter mRNA polyadenylation histone monoubiquitination membrane Wnt signaling pathway protein ubiquitination histone modification nucleosome positioning Cdc73/Paf1 complex stem cell population maintenance cell junction positive regulation of histone methylation positive regulation of mRNA 3'-end processing positive regulation of transcription elongation from RNA polymerase II promoter histone H2B ubiquitination protein localization to nucleus transcriptionally active chromatin negative regulation of myeloid cell differentiation positive regulation of transcription from RNA polymerase II promoter cellular response to lipopolysaccharide positive regulation of cell cycle G1/S phase transition uc002old.1 uc002old.2 uc002old.3 uc002old.4 uc002old.5 uc002old.6 
ENST00000221283.10 STXBP2 ENST00000221283.10 syntaxin binding protein 2, transcript variant 1 (from RefSeq NM_006949.4) B4E175 E7EQD5 ENST00000221283.1 ENST00000221283.2 ENST00000221283.3 ENST00000221283.4 ENST00000221283.5 ENST00000221283.6 ENST00000221283.7 ENST00000221283.8 ENST00000221283.9 NM_006949 Q15833 Q9BU65 STXB2_HUMAN UNC18B uc002mha.1 uc002mha.2 uc002mha.3 uc002mha.4 uc002mha.5 uc002mha.6 uc002mha.7 This gene encodes a member of the STXBP/unc-18/SEC1 family. The encoded protein is involved in intracellular trafficking, control of SNARE (soluble NSF attachment protein receptor) complex assembly, and the release of cytotoxic granules by natural killer cells. Mutations in this gene are associated with familial hemophagocytic lymphohistiocytosis. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene. [provided by RefSeq, Jan 2013]. Involved in intracellular vesicle trafficking and vesicle fusion with membranes. Contributes to the granule exocytosis machinery through interaction with soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins that regulate membrane fusion. Regulates cytotoxic granule exocytosis in natural killer (NK) cells. Interacts with STX1A, STX2 and STX3 (By similarity). Interacts with STX11. Q15833; O75558: STX11; NbExp=4; IntAct=EBI-4401015, EBI-714135; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q15833-1; Sequence=Displayed; Name=2; IsoId=Q15833-2; Sequence=VSP_040121; Name=3; IsoId=Q15833-3; Sequence=VSP_055157; Placenta, lung, liver, kidney and pancreas, as well as in peripheral blood lymphocytes. Hemophagocytic lymphohistiocytosis, familial, 5, with or without microvillus inclusion disease (FHL5) [MIM:613101]: A rare, autosomal recessive disorder characterized by immune dysregulation with hypercytokinemia, defective function of natural killer cell, and massive infiltration of several organs by activated lymphocytes and macrophages. The clinical features of the disease include fever, hepatosplenomegaly, cytopenia, and less frequently neurological abnormalities ranging from irritability and hypotonia to seizures, cranial nerve deficits and ataxia. Some patients may present in early infancy with severe diarrhea, prior to the onset of typical FHL features, whereas others present later in childhood and have a more protracted course without diarrhea. The early-onset diarrhea is due to enteropathy reminiscent of microvillus inclusion disease. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the STXBP/unc-18/SEC1 family. leukocyte mediated cytotoxicity platelet degranulation protein binding extracellular region cytosol plasma membrane exocytosis vesicle docking involved in exocytosis protein transport vesicle-mediated transport apical plasma membrane syntaxin-1 binding syntaxin-3 binding specific granule azurophil granule zymogen granule membrane regulation of mast cell degranulation neutrophil degranulation cytolytic granule phagocytic vesicle extracellular exosome tertiary granule cellular response to interferon-gamma uc002mha.1 uc002mha.2 uc002mha.3 uc002mha.4 uc002mha.5 uc002mha.6 uc002mha.7 
ENST00000221307.13 CYP4F3 ENST00000221307.13 cytochrome P450 family 4 subfamily F member 3, transcript variant 1 (from RefSeq NM_000896.3) B7Z8Z3 CP4F3_HUMAN CYP4F3 ENST00000221307.1 ENST00000221307.10 ENST00000221307.11 ENST00000221307.12 ENST00000221307.2 ENST00000221307.3 ENST00000221307.4 ENST00000221307.5 ENST00000221307.6 ENST00000221307.7 ENST00000221307.8 ENST00000221307.9 LTB4H NM_000896 O60634 Q08477 Q5U740 uc002nbj.1 uc002nbj.2 uc002nbj.3 uc002nbj.4 uc002nbj.5 This gene, CYP4F3, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum. The enzyme starts the process of inactivating and degrading leukotriene B4, a potent mediator of inflammation. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F8, is approximately 18 kb away. Several transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Apr 2019]. A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives (oxylipins) (PubMed:8486631, PubMed:9675028, PubMed:11461919, PubMed:15145985, PubMed:16547005, PubMed:16820285, PubMed:18182499, PubMed:18065749, PubMed:18577768). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:9675028). May play a role in inactivation of pro- inflammatory and anti-inflammatory oxylipins during the resolution of inflammation (PubMed:8486631, PubMed:9675028, PubMed:11461919, PubMed:15145985, PubMed:15364545, PubMed:16547005, PubMed:16820285, PubMed:18182499, PubMed:18065749, PubMed:18577768). [Isoform CYP4F3A]: Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of oxylipins in myeloid cells, displaying higher affinity for arachidonate metabolite leukotriene B4 (LTB4) (PubMed:8486631, PubMed:9675028, PubMed:11461919, PubMed:15364545). Inactivates LTB4 via three successive oxidative transformations to 20-hydroxy-LTB4, then to 20-oxo-LTB4 and to 20- carboxy-LTB4 (PubMed:9675028). Has omega-hydroxylase activity toward long-chain fatty acid epoxides with preference for 8,9-epoxy- (5Z,11Z,14Z)-eicosatrienoate (EET) and 9,10-epoxyoctadecanoate (PubMed:15145985). Omega-hydroxylates monohydroxy polyunsaturated fatty acids (PUFAs), including hydroxyeicosatetraenoates (HETEs) and hydroxyeicosapentaenoates (HEPEs), to dihydroxy compounds (PubMed:15364545, PubMed:9675028). Contributes to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening (PubMed:18182499). Has low hydroxylase activity toward PUFAs (PubMed:18577768, PubMed:11461919). [Isoform CYP4F3B]: Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of polyunsaturated fatty acids (PUFAs) (PubMed:11461919, PubMed:16820285, PubMed:18577768). Participates in the conversion of arachidonic acid to 20- hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:11461919, PubMed:16820285, PubMed:18577768). Has high omega-hydroxylase activity toward other PUFAs, including eicosatrienoic acid (ETA), eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) (PubMed:16820285, PubMed:18577768). Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of PUFAs with lower efficiency (PubMed:18577768). Contributes to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid and hexacosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acids, thereby initiating chain shortening (PubMed:16547005, PubMed:18182499). Omega-hydroxylates long-chain 3-hydroxy fatty acids, likely initiating the oxidative conversion to the corresponding 3-hydroxydicarboxylic fatty acids (PubMed:18065749). Has omega-hydroxylase activity toward long-chain fatty acid epoxides with preference for 8,9-epoxy- (5Z,11Z,14Z)-eicosatrienoate (EET) and 9,10-epoxyoctadecanoate (PubMed:15145985). Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence= PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17151; Evidence= [Isoform CYP4F3A]: Reaction=leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:22176, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57460, ChEBI:CHEBI:57461, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.94; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22177; Evidence= [Isoform CYP4F3A]: Reaction=20-hydroxy-leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-oxo-leukotriene B4 + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:48668, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57460, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90720; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48669; Evidence=; [Isoform CYP4F3A]: Reaction=20-oxo-leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-carboxy-leukotriene B4 + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48672, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90720, ChEBI:CHEBI:90722; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48673; Evidence=; [Isoform CYP4F3A]: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50164, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132026; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50165; Evidence=; [Isoform CYP4F3A]: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76624; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756; Evidence= [Isoform CYP4F3A]: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)- eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39787, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76636; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788; Evidence=; [Isoform CYP4F3A]: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z,17Z)- eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39791, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76639; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792; Evidence=; [Isoform CYP4F3A]: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)- docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50088, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:132025; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50089; Evidence=; [Isoform CYP4F3A]: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)- docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40155, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77015, ChEBI:CHEBI:77016; EC=1.14.14.79; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40156; Evidence=; [Isoform CYP4F3A]: Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)- eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53572, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84025, ChEBI:CHEBI:137474; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573; Evidence=; [Isoform CYP4F3A]: Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-11,12-epoxy-(5Z,8Z,14Z)- eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53576, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76625, ChEBI:CHEBI:137475; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53577; Evidence=; [Isoform CYP4F3A]: Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-14,15-epoxy-(5Z,8Z,11Z)- eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53580, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84024, ChEBI:CHEBI:137476; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53581; Evidence=; [Isoform CYP4F3A]: Reaction=12,13-epoxy-(9Z)-octadecenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-12,13-epoxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53568, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84026, ChEBI:CHEBI:137469; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53569; Evidence=; [Isoform CYP4F3A]: Reaction=9,10-epoxy-(12Z)-octadecenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-9,10-epoxy-(12Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53564, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84023, ChEBI:CHEBI:137467; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53565; Evidence=; [Isoform CYP4F3A]: Reaction=9,10-epoxyoctadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-9,10-epoxy-octadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53560, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:85195, ChEBI:CHEBI:137457; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53561; Evidence=; [Isoform CYP4F3A]: Reaction=(12R)-hydroxy-(9Z)-octadecenoate + O2 + reduced [NADPH-- hemoprotein reductase] = (12R),18-dihydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49384, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:91295, ChEBI:CHEBI:91300; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49385; Evidence=; [Isoform CYP4F3A]: Reaction=12-hydroxyoctadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12,18-dihydroxyoctadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49376, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84201, ChEBI:CHEBI:91294; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49377; Evidence=; [Isoform CYP4F3A]: Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 5,20-dihydroxy-(6E,8Z,11Z,14Z)- eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48656, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:65341, ChEBI:CHEBI:90715; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48657; Evidence=; [Isoform CYP4F3A]: Reaction=8-hydroxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 8,20-dihydroxy-(5Z,9E,11Z,14Z)- eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48660, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90716, ChEBI:CHEBI:90717; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48661; Evidence=; [Isoform CYP4F3A]: Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 12,20-dihydroxy-(5Z,8Z,10E,14Z)- eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48664, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90718, ChEBI:CHEBI:90719; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48665; Evidence=; [Isoform CYP4F3A]: Reaction=5-hydroxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 5,20-dihydroxy-(6E,8Z,11Z,14Z,17Z)- eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49380, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90737, ChEBI:CHEBI:91301; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49381; Evidence=; [Isoform CYP4F3A]: Reaction=lipoxin A4 + O2 + reduced [NADPH--hemoprotein reductase] = 20- hydroxy-lipoxin A4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48648, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:67026, ChEBI:CHEBI:90707; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48649; Evidence=; [Isoform CYP4F3A]: Reaction=lipoxin B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20- hydroxy-lipoxin B4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48652, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:67031, ChEBI:CHEBI:90711; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48653; Evidence=; [Isoform CYP4F3A]: Reaction=22-hydroxydocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-oxodocosanoate + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39055, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76298, ChEBI:CHEBI:76304; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39056; Evidence=; [Isoform CYP4F3A]: Reaction=22-oxodocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = docosanedioate + 2 H(+) + H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39043, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76298, ChEBI:CHEBI:76299; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39044; Evidence=; [Isoform CYP4F3B]: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50164, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132026; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50165; Evidence=; [Isoform CYP4F3B]: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76624; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756; Evidence= [Isoform CYP4F3B]: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)- eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39787, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76636; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788; Evidence=; [Isoform CYP4F3B]: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z,17Z)- eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39791, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76639; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792; Evidence=; [Isoform CYP4F3B]: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)- docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50088, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:132025; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50089; Evidence=; [Isoform CYP4F3B]: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)- docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40155, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77015, ChEBI:CHEBI:77016; EC=1.14.14.79; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40156; Evidence=; [Isoform CYP4F3B]: Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)- eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53572, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84025, ChEBI:CHEBI:137474; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573; Evidence=; [Isoform CYP4F3B]: Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-14,15-epoxy-(5Z,8Z,11Z)- eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53580, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84024, ChEBI:CHEBI:137476; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53581; Evidence=; [Isoform CYP4F3B]: Reaction=12,13-epoxy-(9Z)-octadecenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-12,13-epoxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53568, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84026, ChEBI:CHEBI:137469; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53569; Evidence=; [Isoform CYP4F3B]: Reaction=9,10-epoxy-(12Z)-octadecenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-9,10-epoxy-(12Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53564, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84023, ChEBI:CHEBI:137467; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53565; Evidence=; [Isoform CYP4F3B]: Reaction=9,10-epoxyoctadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-9,10-epoxy-octadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53560, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:85195, ChEBI:CHEBI:137457; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53561; Evidence=; [Isoform CYP4F3B]: Reaction=docosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-hydroxydocosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40079, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23858, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76304; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40080; Evidence=; [Isoform CYP4F3B]: Reaction=22-hydroxydocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-oxodocosanoate + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39055, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76298, ChEBI:CHEBI:76304; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39056; Evidence=; [Isoform CYP4F3B]: Reaction=22-oxodocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = docosanedioate + 2 H(+) + H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39043, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76298, ChEBI:CHEBI:76299; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39044; Evidence=; [Isoform CYP4F3B]: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetracosanoate = 24-hydroxytetracosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39719, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:31014, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76610; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39720; Evidence=; [Isoform CYP4F3B]: Reaction=hexacosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 26-hydroxyhexacosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40083, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:31013, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76305; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40084; Evidence=; [Isoform CYP4F3B]: Reaction=26-hydroxyhexacosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 26-oxohexacosanoate + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39059, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76305, ChEBI:CHEBI:76311; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39060; Evidence=; [Isoform CYP4F3B]: Reaction=26-oxohexacosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 2 H(+) + H2O + hexacosanedioate + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39047, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76311, ChEBI:CHEBI:76312; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39048; Evidence=; [Isoform CYP4F3B]: Reaction=3-hydroxyoctadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 3,18-dihydroxyoctadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39735, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76614, ChEBI:CHEBI:76615; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39736; Evidence=; [Isoform CYP4F3B]: Reaction=3-hydroxyhexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 3,16-dihydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39731, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63904, ChEBI:CHEBI:76613; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39732; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Inhibited by carbon monoxide (CO). [Isoform CYP4F3A]: Kinetic parameters: KM=0.64 uM for leukotriene B4 ; KM=6.5 uM for 20-hydroxy-leukotriene B4 ; KM=0.68 uM for leukotriene B4 ; KM=185.6 uM for arachidonate ; KM=17.9 uM for lipoxin B4 ; KM=25.7 uM for 5-HETE ; KM=40.9 uM for 12-HETE ; KM=49.5 uM for 5-HEPE ; KM=14.2 uM for 12-hydroxyoctadecanoate ; KM=22.8 uM for (12R)-hydroxy-(9Z)-octadecenoate ; KM=6.3 uM for 9(10)-epoxyoctadecanoate ; KM=46.6 uM for 9(10)-epoxy-(12Z)-octadecenoate ; KM=61.8 uM for 12(13)-epoxy-(9Z)-octadecenoate ; KM=0.6 uM for 22-hydroxydocosanoate ; Vmax=34.0 nmol/min/nmol enzyme toward leukotriene B4 ; Vmax=66.7 nmol/min/nmol enzyme toward 20-hydroxy-leukotriene B4 ; Vmax=32.8 pmol/min/pmol enzyme toward leukotriene B4 ; Vmax=11.5 pmol/min/pmol enzyme toward arachidonate ; Vmax=38.5 nmol/min/nmol enzyme toward lipoxin B4 ; Vmax=21.6 nmol/min/nmol enzyme toward 5-HETE ; Vmax=43.2 nmol/min/nmol enzyme toward 12-HETE ; Vmax=95.1 nmol/min/nmol enzyme toward 5-HEPE ; Vmax=54.5 nmol/min/nmol enzyme toward 12-hydroxyoctadecanoate ; Vmax=19.0 nmol/min/nmol enzyme toward (12R)-hydroxy-(9Z)- octadecenoate ; Vmax=10.8 nmol/min/nmol enzyme toward 9(10)-epoxyoctadecanoate ; Vmax=21.2 nmol/min/nmol enzyme toward 9(10)-epoxy-(12Z)-octadecenoate ; Vmax=3 nmol/min/nmol enzyme toward 12(13)-epoxy-(9Z)-octadecenoate ; Vmax=0.2 pmol/min/pmol enzyme toward 22-hydroxydocosanoate ; pH dependence: Optimum pH is 7.5. ; [Isoform CYP4F3B]: Kinetic parameters: KM=20.6 uM for leukotriene B4 ; KM=22.0 uM for arachidonate ; KM=35.7 uM for 9(10)-epoxyoctadecanoate ; KM=108.1 uM for 9(10)-epoxy-(12Z)-octadecenoate ; KM=100.6 uM for 12(13)-epoxy-(9Z)-octadecenoate ; KM=1.6 uM for docosanoate ; KM=3.8 uM for tetracosanoate ; KM=1.3 uM for hexacosanoate ; KM=13.1 uM for 22-hydroxydocosanoate ; KM=5.2 uM for 26-hydroxyhexacosanoate ; Vmax=23.3 pmol/min/pmol enzyme toward leukotriene B4 ; Vmax=13.3 pmol/min/pmol enzyme toward arachidonate ; Vmax=13.2 nmol/min/nmol enzyme toward 9(10)-epoxyoctadecanoate ; Vmax=15.02 nmol/min/nmol enzyme toward 9(10)-epoxy-(12Z)- octadecenoate ; Vmax=3.93 nmol/min/nmol enzyme toward 12(13)-epoxy-(9Z)-octadecenoate ; Vmax=5.0 pmol/min/pmol enzyme toward docosanoate ; Vmax=9.8 pmol/min/pmol enzyme toward tetracosanoate ; Vmax=2.2 pmol/min/pmol enzyme toward hexacosanoate ; Vmax=0.3 pmol/min/pmol enzyme toward 22-hydroxydocosanoate ; Vmax=0.8 pmol/min/pmol enzyme toward 26-hydroxyhexacosanoate ; Note=The omega-hydroxylation of VLCFAs follows dual-enzyme Michaelis- Menten kinetics, suggesting simultaneous binding of two substrate molecules. The high affinity Michaelis-Menten constants are shown. ; [Isoform CYP4F3A]: Lipid metabolism; leukotriene B4 degradation. Lipid metabolism; arachidonate metabolism. Endoplasmic reticulum membrane ; Single-pass membrane protein Microsome membrane ; Single-pass membrane protein Event=Alternative promoter usage, Alternative splicing; Named isoforms=2; Name=CYP4F3A; IsoId=Q08477-1; Sequence=Displayed; Name=CYP4F3B; IsoId=Q08477-2; Sequence=VSP_047193; [Isoform CYP4F3A]: Selectively expressed in blood neutrophils and bone marrow cells. Coexpressed with CYP4F3B in prostate, ileum and trachea. [Isoform CYP4F3B]: Selectively expressed in liver and kidney. It is also the predominant CYP4F isoform in trachea and tissues of the gastrointestinal tract. Belongs to the cytochrome P450 family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cyp4f3/"; monooxygenase activity iron ion binding endoplasmic reticulum endoplasmic reticulum membrane lipid metabolic process fatty acid metabolic process icosanoid metabolic process leukotriene metabolic process membrane integral component of membrane oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen arachidonic acid metabolic process heme binding organelle membrane leukotriene B4 catabolic process intracellular membrane-bounded organelle metal ion binding leukotriene-B4 20-monooxygenase activity oxidation-reduction process aromatase activity uc002nbj.1 uc002nbj.2 uc002nbj.3 uc002nbj.4 uc002nbj.5 
ENST00000221315.10 ZNF432 ENST00000221315.10 zinc finger protein 432, transcript variant 1 (from RefSeq NM_014650.4) ENST00000221315.1 ENST00000221315.2 ENST00000221315.3 ENST00000221315.4 ENST00000221315.5 ENST00000221315.6 ENST00000221315.7 ENST00000221315.8 ENST00000221315.9 KIAA0798 NM_014650 O94892 ZN432_HUMAN uc002pyk.1 uc002pyk.2 uc002pyk.3 uc002pyk.4 uc002pyk.5 May be involved in transcriptional regulation. O94892; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-12121104, EBI-10303987; Nucleus Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=BAA34518.2; Type=Erroneous initiation; Evidence=; nucleic acid binding DNA binding nucleus nucleoplasm regulation of transcription, DNA-templated metal ion binding uc002pyk.1 uc002pyk.2 uc002pyk.3 uc002pyk.4 uc002pyk.5 
ENST00000221399.8 TULP2 ENST00000221399.8 TUB like protein 2 (from RefSeq NM_003323.3) ENST00000221399.1 ENST00000221399.2 ENST00000221399.3 ENST00000221399.4 ENST00000221399.5 ENST00000221399.6 ENST00000221399.7 NM_003323 O00295 Q8TC50 TUBL2 TULP2_HUMAN uc002pkz.1 uc002pkz.2 uc002pkz.3 uc002pkz.4 TULP2 is a member of a family of tubby-like genes (TULPs) that encode proteins of unknown function. Members of this family have been identified in plants, vertebrates, and invertebrates. The TULP proteins share a conserved C-terminal region of approximately 200 amino acid residues. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: BC026070.2, U82469.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968189, SAMEA1968540 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221399.8/ ENSP00000221399.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Cytoplasm Secreted Note=Does not have a cleavable signal peptide and is secreted by a non- conventional pathway. Strongly expressed in testis. Also expressed in retina. Expressed in cancer cell lines. Belongs to the TUB family. extracellular region cytoplasm cilium visual perception macromolecular complex binding protein localization to cilium uc002pkz.1 uc002pkz.2 uc002pkz.3 uc002pkz.4 
ENST00000221403.7 DHDH ENST00000221403.7 dihydrodiol dehydrogenase (from RefSeq NM_014475.4) 2DD DHDH_HUMAN ENST00000221403.1 ENST00000221403.2 ENST00000221403.3 ENST00000221403.4 ENST00000221403.5 ENST00000221403.6 NM_014475 Q9UQ10 uc002ple.1 uc002ple.2 This gene encodes an enzyme that belongs to the family of dihydrodiol dehydrogenases, which exist in multiple forms in mammalian tissues and are involved in the metabolism of xenobiotics and sugars. These enzymes catalyze the NADP1-linked oxidation of transdihydrodiols of aromatic hydrocarbons to corresponding catechols. This enzyme is a dimeric dihydrodiol dehydrogenase, and it differs from monomeric dihydrodiol dehydrogenases in its high substrate specificity for trans-dihydrodiols of aromatic hydrocarbons in the oxidative direction. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC032730.1, SRR5189667.70683.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221403.7/ ENSP00000221403.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Reaction=(1R,2R)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + H(+) + NADPH; Xref=Rhea:RHEA:16729, ChEBI:CHEBI:10702, ChEBI:CHEBI:15378, ChEBI:CHEBI:18135, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.20; Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867, ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.179; Homodimer. Small intestine. Belongs to the Gfo/Idh/MocA family. carbohydrate metabolic process NAD(P)+ transhydrogenase activity electron carrier activity oxidoreductase activity electron transport chain D-xylose catabolic process trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity D-xylose 1-dehydrogenase (NADP+) activity oxidation-reduction process uc002ple.1 uc002ple.2 
ENST00000221418.9 ECH1 ENST00000221418.9 enoyl-CoA hydratase 1 (from RefSeq NM_001398.3) A8K745 ECH1 ECH1_HUMAN ENST00000221418.1 ENST00000221418.2 ENST00000221418.3 ENST00000221418.4 ENST00000221418.5 ENST00000221418.6 ENST00000221418.7 ENST00000221418.8 NM_001398 Q13011 Q8WVX0 Q96EZ9 uc002oji.1 uc002oji.2 uc002oji.3 uc002oji.4 uc002oji.5 This gene encodes a member of the hydratase/isomerase superfamily. The gene product shows high sequence similarity to enoyl-coenzyme A (CoA) hydratases of several species, particularly within a conserved domain characteristic of these proteins. The encoded protein, which contains a C-terminal peroxisomal targeting sequence, localizes to the peroxisome. The rat ortholog, which localizes to the matrix of both the peroxisome and mitochondria, can isomerize 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA, indicating that it is a delta3,5-delta2,4-dienoyl-CoA isomerase. This enzyme functions in the auxiliary step of the fatty acid beta-oxidation pathway. Expression of the rat gene is induced by peroxisome proliferators. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.360432.1, SRR5189655.103444.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2155770 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221418.9/ ENSP00000221418.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4- trans-dienoyl-CoA. Reaction=(3E,5Z)-octadienoyl-CoA = (2E,4E)-octadienoyl-CoA; Xref=Rhea:RHEA:45244, ChEBI:CHEBI:62243, ChEBI:CHEBI:85108; Evidence=; Reaction=(3E,5Z,8Z,11Z,14Z)-eicosapentaenoyl-CoA = (2E,4E,8Z,11Z,14Z)- eicosapentaenoyl-CoA; Xref=Rhea:RHEA:45224, ChEBI:CHEBI:85090, ChEBI:CHEBI:85091; Evidence=; Lipid metabolism; fatty acid beta-oxidation. Homohexamer. Q13011; O75521: ECI2; NbExp=4; IntAct=EBI-711968, EBI-2512024; Q13011; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-711968, EBI-10175124; Q13011; P42858: HTT; NbExp=2; IntAct=EBI-711968, EBI-466029; Q13011; P40763: STAT3; NbExp=2; IntAct=EBI-711968, EBI-518675; Q13011; Q13077: TRAF1; NbExp=4; IntAct=EBI-711968, EBI-359224; Mitochondrion Peroxisome Belongs to the enoyl-CoA hydratase/isomerase family. catalytic activity protein binding mitochondrion peroxisome peroxisomal matrix cytosol protein targeting to peroxisome lipid metabolic process fatty acid metabolic process fatty acid beta-oxidation membrane isomerase activity delta3,5-delta2,4-dienoyl-CoA isomerase activity extracellular exosome uc002oji.1 uc002oji.2 uc002oji.3 uc002oji.4 uc002oji.5 
ENST00000221419.10 HNRNPL ENST00000221419.10 heterogeneous nuclear ribonucleoprotein L, transcript variant 1 (from RefSeq NM_001533.3) A6ND69 A6NIT8 ENST00000221419.1 ENST00000221419.2 ENST00000221419.3 ENST00000221419.4 ENST00000221419.5 ENST00000221419.6 ENST00000221419.7 ENST00000221419.8 ENST00000221419.9 HNRPL HNRPL_HUMAN NM_001533 P/OKcl.14 P14866 Q9H3P3 uc060yfy.1 uc060yfy.2 Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear ribonucleoprotein L is among the proteins that are stably associated with hnRNP complexes and along with other hnRNP proteins is likely to play a major role in the formation, packaging, processing, and function of mRNA. Heterogeneous nuclear ribonucleoprotein L is present in the nucleoplasm as part of the HNRP complex. HNRP proteins have also been identified outside of the nucleoplasm. Exchange of hnRNP for mRNA-binding proteins accompanies transport of mRNA from the nucleus to the cytoplasm. Since HNRP proteins have been shown to shuttle between the nucleus and the cytoplasm, it is possible that they also have cytoplasmic functions. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284). Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). Regulates alternative splicing of a core group of genes involved in neuronal differentiation, likely by mediating H3K36me3-coupled transcription elongation and co-transcriptional RNA processing via interaction with CHD8. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with HNRNPLL (PubMed:18669861). Interacts with APEX1; the interaction is DNA- dependent (PubMed:11809897). Component of a complex with SETD2 (PubMed:19332550, PubMed:36537238). Interacts with ELAVL1 (PubMed:18161049). Part of a transcription inhibitory ribonucleoprotein complex composed at least of the circular RNA circZNF827, ZNF827 and HNRNPK (PubMed:33174841). Interacts with CHD8 in an RNA-dependent manner. P14866; P22626: HNRNPA2B1; NbExp=2; IntAct=EBI-719024, EBI-299649; P14866; P61978: HNRNPK; NbExp=4; IntAct=EBI-719024, EBI-304185; P14866; Q8IUH3: RBM45; NbExp=5; IntAct=EBI-719024, EBI-2512147; P14866; P40337: VHL; NbExp=2; IntAct=EBI-719024, EBI-301246; P14866-1; P22626: HNRNPA2B1; NbExp=4; IntAct=EBI-16071645, EBI-299649; P14866-1; Q12906: ILF3; NbExp=2; IntAct=EBI-16071645, EBI-78756; Nucleus, nucleoplasm toplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P14866-1; Sequence=Displayed; Name=2; IsoId=P14866-2; Sequence=VSP_044301; RRM domain 2 has moderate RNA-binding affinity. RRM domains 3 and 4 may facilitate RNA looping when binding to two appropriately separated binding sites within the same target pre-mRNA (PubMed:23782695). Several isoelectric forms of the L protein are probably the results of post-translational modifications. Phosphorylation at Ser-544 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization. Excess hnRNP L activates NMD of its own mRNA by promoting the inclusion of a 'poison exon' containing a premature stop codon and leading to nonsense-mediated decay. It also cross-regulates inclusion of an analogous 'poison exon' in the hnRNP L-like pre-mRNA (PubMed:19124611). Sequence=CAA34261.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; regulation of alternative mRNA splicing, via spliceosome mRNA splicing, via spliceosome nucleic acid binding RNA binding protein binding nucleus nucleoplasm cytoplasm RNA processing mRNA processing membrane RNA metabolic process ribonucleoprotein granule transcription regulatory region DNA binding extracellular exosome pre-mRNA intronic binding ribonucleoprotein complex uc060yfy.1 uc060yfy.2 
ENST00000221431.11 SARS2 ENST00000221431.11 seryl-tRNA synthetase 2, mitochondrial, transcript variant 2 (from RefSeq NM_017827.4) A6NHW7 B4DE10 ENST00000221431.1 ENST00000221431.10 ENST00000221431.2 ENST00000221431.3 ENST00000221431.4 ENST00000221431.5 ENST00000221431.6 ENST00000221431.7 ENST00000221431.8 ENST00000221431.9 NM_017827 Q9BVP3 Q9NP81 SARSM SYSM_HUMAN uc002oka.1 uc002oka.2 uc002oka.3 uc002oka.4 This gene encodes the mitochondrial seryl-tRNA synthethase precursor, a member of the class II tRNA synthetase family. The mature enzyme catalyzes the ligation of Serine to tRNA(Ser) and participates in the biosynthesis of selenocysteinyl-tRNA(sec) in mitochondria. The enzyme contains an N-terminal tRNA binding domain and a core catalytic domain. It functions in a homodimeric form, which is stabilized by tRNA binding. This gene is regulated by a bidirectional promoter that also controls the expression of mitochondrial ribosomal protein S12. Both genes are within the critical interval for the autosomal dominant deafness locus DFNA4 and might be linked to this disease. Multiple transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Mar 2009]. Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L- seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evidence=; Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L- seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evidence=; Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. Homodimer. The tRNA molecule probably binds across the dimer. Q9NP81; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1049768, EBI-741158; Mitochondrion matrix Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NP81-1; Sequence=Displayed; Name=2; IsoId=Q9NP81-2; Sequence=VSP_043020; Consists of two distinct domains, a catalytic core and a N- terminal extension that is involved in tRNA binding. Hyperuricemia, pulmonary hypertension, renal failure, and alkalosis syndrome (HUPRAS) [MIM:613845]: A multisystem disorder characterized by onset in infancy of progressive renal failure leading to electrolyte imbalances, metabolic alkalosis, pulmonary hypertension, hypotonia, and delayed development. Affected individuals are born prematurely. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily. Sequence=AAH01020.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleotide binding RNA binding aminoacyl-tRNA ligase activity serine-tRNA ligase activity ATP binding mitochondrion mitochondrial matrix translation tRNA aminoacylation for protein translation seryl-tRNA aminoacylation ligase activity selenocysteinyl-tRNA(Sec) biosynthetic process uc002oka.1 uc002oka.2 uc002oka.3 uc002oka.4 
ENST00000221444.2 KCNA7 ENST00000221444.2 potassium voltage-gated channel subfamily A member 7 (from RefSeq NM_031886.3) A1KYX7 ENST00000221444.1 KCNA7_HUMAN NM_031886 Q96RP8 Q9BYS4 uc002pmg.1 uc002pmg.2 uc002pmg.3 uc002pmg.4 Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. The gene is expressed preferentially in skeletal muscle, heart and kidney. It is a candidate gene for inherited cardiac disorders. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AJ310479.1, BC140906.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158188, SAMEA2158800 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient (By similarity). Heterotetramer of potassium channel proteins. Q96RP8; P62258: YWHAE; NbExp=2; IntAct=EBI-42485668, EBI-356498; Membrane ; Multi-pass membrane protein Highly expressed in skeletal muscle, heart and kidney. The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.7/KCNA7 sub-subfamily. ion channel activity voltage-gated ion channel activity voltage-gated potassium channel activity delayed rectifier potassium channel activity potassium channel activity plasma membrane ion transport potassium ion transport voltage-gated potassium channel complex membrane integral component of membrane regulation of ion transmembrane transport protein homooligomerization transmembrane transport potassium ion transmembrane transport uc002pmg.1 uc002pmg.2 uc002pmg.3 uc002pmg.4 
ENST00000221452.13 RELB ENST00000221452.13 RELB proto-oncogene, NF-kB subunit, transcript variant 1 (from RefSeq NM_006509.4) ENST00000221452.1 ENST00000221452.10 ENST00000221452.11 ENST00000221452.12 ENST00000221452.2 ENST00000221452.3 ENST00000221452.4 ENST00000221452.5 ENST00000221452.6 ENST00000221452.7 ENST00000221452.8 ENST00000221452.9 NM_006509 Q01201 Q6GTX7 Q9UEI7 RELB_HUMAN uc060zvi.1 uc060zvi.2 NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post- translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I- kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function (PubMed:26385063). Component of the NF-kappa-B RelB-p50 complex. Component of the NF-kappa-B RelB-p52 complex. Self-associates; the interaction seems to be transient and may prevent degradation allowing for heterodimer formation with p50 or p52. Interacts with NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with NFKBID. Interacts with BMAL1 and the interaction is enhanced in the presence of CLOCK (By similarity). Q01201; Q8N668: COMMD1; NbExp=2; IntAct=EBI-357837, EBI-1550112; Q01201; P49841: GSK3B; NbExp=4; IntAct=EBI-357837, EBI-373586; Q01201; P19838: NFKB1; NbExp=5; IntAct=EBI-357837, EBI-300010; Q01201; Q00653: NFKB2; NbExp=2; IntAct=EBI-357837, EBI-307326; Q01201; Q04206-2: RELA; NbExp=2; IntAct=EBI-357837, EBI-289947; Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with NEK6 in the centrosome. Up-regulated by mitogens and NUPR1. Both N- and C-terminal domains are required for transcriptional activation. Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation. Immunodeficiency 53 (IMD53) [MIM:617585]: An autosomal recessive primary immunodeficiency apparent from early infancy and resulting in recurrent infections, severe autoimmune skin disease rheumatoid arthritis, and failure to thrive. Immunologic workup shows increased CD4+/CD8+ ratio, impaired T-cell proliferative response to multiple antigen, T-cell developmental and functional defects, and impaired ability to produce specific immunoglobulins. Note=The disease is caused by variants affecting the gene represented in this entry. Was originally thought to inhibit the transcriptional activity of nuclear factor NF-kappa-B. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/324/RELB"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding stimulatory C-type lectin receptor signaling pathway DNA binding chromatin binding transcription factor activity, sequence-specific DNA binding transcription corepressor activity protein binding nucleus nucleoplasm cytoplasm microtubule organizing center cytosol cytoskeleton regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter inflammatory response I-kappaB kinase/NF-kappaB signaling positive regulation of gene expression transcriptional repressor complex antigen processing and presentation protein kinase binding lymphocyte differentiation negative regulation of interferon-beta production circadian regulation of gene expression macromolecular complex response to cytokine NIK/NF-kappaB signaling T-helper 1 type immune response identical protein binding myeloid dendritic cell differentiation T-helper 1 cell differentiation negative regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter rhythmic process cellular response to osmotic stress centrosome uc060zvi.1 uc060zvi.2 
ENST00000221455.8 CLASRP ENST00000221455.8 CLK4 associating serine/arginine rich protein, transcript variant 3 (from RefSeq NR_103529.2) A0A0A0MQS2 B4DDT8 CLASR_HUMAN ENST00000221455.1 ENST00000221455.2 ENST00000221455.3 ENST00000221455.4 ENST00000221455.5 ENST00000221455.6 ENST00000221455.7 F8WAG9 NR_103529 O96026 Q6UW71 Q8N2M8 Q96DX2 SFRS16 SWAP2 UNQ2428/PRO4988 uc002pak.1 uc002pak.2 uc002pak.3 uc002pak.4 Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family (By similarity). Probably interacts with CLK4. Q8N2M8; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-751069, EBI-8464238; Q8N2M8; Q9Y6A4: CFAP20; NbExp=4; IntAct=EBI-751069, EBI-1046872; Q8N2M8; P49759-3: CLK1; NbExp=3; IntAct=EBI-751069, EBI-11981867; Q8N2M8; P49760: CLK2; NbExp=3; IntAct=EBI-751069, EBI-750020; Q8N2M8; P49761: CLK3; NbExp=4; IntAct=EBI-751069, EBI-745579; Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q8N2M8-1; Sequence=Displayed; Name=2; IsoId=Q8N2M8-3; Sequence=VSP_013894, VSP_013895; Name=3; IsoId=Q8N2M8-4; Sequence=VSP_055717; Phosphorylated in vitro by CLK4. [Isoform 2]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the splicing factor SR family. It is uncertain whether Met-1 or Met-16 is the initiator. Sequence=AAC82339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAC82340.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH80554.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; protein binding nucleus nucleoplasm mRNA processing RNA splicing uc002pak.1 uc002pak.2 uc002pak.3 uc002pak.4 
ENST00000221459.7 LIN7B ENST00000221459.7 lin-7 homolog B, crumbs cell polarity complex component, transcript variant 1 (from RefSeq NM_022165.3) ENST00000221459.1 ENST00000221459.2 ENST00000221459.3 ENST00000221459.4 ENST00000221459.5 ENST00000221459.6 LIN7B_HUMAN MALS2 NM_022165 Q9HAP6 UNQ3116/PRO10200 VELI2 uc002pmp.1 uc002pmp.2 uc002pmp.3 uc002pmp.4 Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta- catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface (By similarity). Forms a complex with CASK and CASKIN1 (By similarity). Component of the brain-specific heterotrimeric complex (LIN-10-LIN-2- LIN-7 complex) composed of at least APBA1, CASK, and LIN7, which associates with the motor protein KIF17 to transport vesicles along microtubules (By similarity). Forms a heterotrimeric complex composed of MMP5, LIN7B and PATJ; the N-terminal L27 domain of PALS1 interacts with the L27 domain of PATJ and the C-terminal L27 domain of PALS1 interacts with the L27 domain of LIN7B (By similarity). Forms a heterotrimeric complex with DLG1 and CASK via their L27 domains (PubMed:11742811, PubMed:17237226). Interacts with DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ domain (PubMed:11742811). The association of LIN7A with cadherin and beta- catenin is calcium-dependent, occurs at synaptic junctions and requires the actin cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains (PubMed:12967566). Associates with KIF17 via APBA1 (By similarity). Interacts with ASIC3 (PubMed:15317815). Interacts with TOPK. Interacts with RTKN (PubMed:16979770). Interacts with APBA1 (By similarity). Interacts with MPP7 (PubMed:17237226). Interacts with DLG2 (By similarity). Interacts with DLG3 (By similarity). Q9HAP6; O14936-4: CASK; NbExp=3; IntAct=EBI-821335, EBI-12007726; Q9HAP6; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-821335, EBI-744099; Q9HAP6; Q9BXY0: MAK16; NbExp=3; IntAct=EBI-821335, EBI-5280229; Q9HAP6; Q14168-4: MPP2; NbExp=3; IntAct=EBI-821335, EBI-14385193; Q9HAP6; Q13368: MPP3; NbExp=8; IntAct=EBI-821335, EBI-716157; Q9HAP6; Q5T2T1: MPP7; NbExp=3; IntAct=EBI-821335, EBI-2514004; Q9HAP6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-821335, EBI-741158; Q9HAP6; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-821335, EBI-2513978; Q9HAP6; Q9NZW5: PALS2; NbExp=5; IntAct=EBI-821335, EBI-2683764; Q9HAP6; P20618: PSMB1; NbExp=3; IntAct=EBI-821335, EBI-372273; Q9HAP6; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-821335, EBI-11955057; Q9HAP6; Q8WVT3: TRAPPC12; NbExp=3; IntAct=EBI-821335, EBI-2819919; Cell membrane ; Peripheral membrane protein Basolateral cell membrane eripheral membrane protein Cell junction Postsynaptic density membrane ; Peripheral membrane protein Cell junction, tight junction Note=Mainly basolateral in renal epithelial cells. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9HAP6-1; Sequence=Displayed; Name=2; IsoId=Q9HAP6-2; Sequence=VSP_042156; The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane. The PDZ domain regulates endocytosis and recycling of the receptor at the membrane. The L27 domain mediates interaction with CASK and is involved in the formation of multimeric complexes and the association of LIN7 to membranes. Belongs to the lin-7 family. plasma membrane cell-cell junction bicellular tight junction exocytosis neurotransmitter secretion postsynaptic density protein transport membrane basolateral plasma membrane protein domain specific binding cell junction PDZ domain binding neuron projection maintenance of epithelial cell apical/basal polarity synapse postsynaptic membrane L27 domain binding MPP7-DLG1-LIN7 complex presynapse protein localization to basolateral plasma membrane uc002pmp.1 uc002pmp.2 uc002pmp.3 uc002pmp.4 
ENST00000221462.9 PPP1R37 ENST00000221462.9 protein phosphatase 1 regulatory subunit 37 (from RefSeq NM_019121.2) B5MDA4 ENST00000221462.1 ENST00000221462.2 ENST00000221462.3 ENST00000221462.4 ENST00000221462.5 ENST00000221462.6 ENST00000221462.7 ENST00000221462.8 KIAA1986 LRRC68 NM_019121 O75864 PPR37_HUMAN Q8IWK3 Q8TF16 uc021uvs.1 uc021uvs.2 uc021uvs.3 Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. Interacts with PPP1CA. O75864; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-5235692, EBI-10181188; O75864; O75593: FOXH1; NbExp=3; IntAct=EBI-5235692, EBI-1759806; O75864; B2RXH8: HNRNPCL2; NbExp=3; IntAct=EBI-5235692, EBI-9512317; O75864; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-5235692, EBI-11022007; O75864; P62136: PPP1CA; NbExp=5; IntAct=EBI-5235692, EBI-357253; O75864; Q15415: RBMY1J; NbExp=3; IntAct=EBI-5235692, EBI-8642021; O75864; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-5235692, EBI-11987469; O75864; Q96H86: ZNF764; NbExp=3; IntAct=EBI-5235692, EBI-745775; O75864; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-5235692, EBI-11962574; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75864-1; Sequence=Displayed; Name=2; IsoId=O75864-2; Sequence=VSP_031754, VSP_031755; [Isoform 2]: Due to an intron retention. Belongs to the PPP1R37 family. Sequence=AAC62258.1; Type=Erroneous gene model prediction; Evidence=; Sequence=BAB85572.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; protein phosphatase inhibitor activity protein binding negative regulation of phosphatase activity negative regulation of phosphoprotein phosphatase activity uc021uvs.1 uc021uvs.2 uc021uvs.3 
ENST00000221466.10 FCGRT ENST00000221466.10 Fc gamma receptor and transporter, transcript variant 1 (from RefSeq NM_001136019.3) ENST00000221466.1 ENST00000221466.2 ENST00000221466.3 ENST00000221466.4 ENST00000221466.5 ENST00000221466.6 ENST00000221466.7 ENST00000221466.8 ENST00000221466.9 FCGRN_HUMAN FCRN NM_001136019 P55899 Q5HYM5 Q9HBV7 Q9NZ19 uc002poe.1 uc002poe.2 uc002poe.3 uc002poe.4 This gene encodes a receptor that binds the Fc region of monomeric immunoglobulin G. The encoded protein transfers immunoglobulin G antibodies from mother to fetus across the placenta. This protein also binds immunoglobulin G to protect the antibody from degradation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2009]. Cell surface receptor that transfers passive humoral immunity from the mother to the newborn. Binds to the Fc region of monomeric immunoglobulin gamma and mediates its selective uptake from milk (PubMed:7964511, PubMed:10933786). IgG in the milk is bound at the apical surface of the intestinal epithelium. The resultant FcRn-IgG complexes are transcytosed across the intestinal epithelium and IgG is released from FcRn into blood or tissue fluids. Throughout life, contributes to effective humoral immunity by recycling IgG and extending its half-life in the circulation. Mechanistically, monomeric IgG binding to FcRn in acidic endosomes of endothelial and hematopoietic cells recycles IgG to the cell surface where it is released into the circulation (PubMed:10998088). In addition of IgG, regulates homeostasis of the other most abundant circulating protein albumin/ALB (PubMed:24469444, PubMed:28330995). (Microbial infection) Acts as an uncoating receptor for a panel of echoviruses including Echovirus 5, 6, 7, 9, 11, 13, 25 and 29. FcRn complex consists of two subunits: p51, and p14 which is equivalent to beta-2-microglobulin. It forms an MHC class I-like heterodimer (By similarity). Interacts with albumin/ALB; this interaction regulates ALB homeostasis (PubMed:24469444, PubMed:28330995). (Microbial infection) Interacts with Echovirus 6, Echovirus 11 and Echovirus 30 capsid protein VP1. P55899; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-2833934, EBI-12256978; P55899; Q92520: FAM3C; NbExp=3; IntAct=EBI-2833934, EBI-2876774; P55899; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-2833934, EBI-10317425; P55899; Q01453: PMP22; NbExp=3; IntAct=EBI-2833934, EBI-2845982; P55899; O00526: UPK2; NbExp=3; IntAct=EBI-2833934, EBI-10179682; Cell membrane ; Single-pass type I membrane protein Endosome membrane Expressed in full-term placenta, heart, lung, liver, muscle, kidney, pancreas, and both fetal and adult small intestine. Belongs to the immunoglobulin superfamily. positive regulation of T cell mediated cytotoxicity IgG immunoglobulin transcytosis in epithelial cells mediated by FcRn immunoglobulin receptor antigen processing and presentation of endogenous peptide antigen via MHC class Ib antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent extracellular space endosome plasma membrane immune response external side of plasma membrane endosome membrane membrane integral component of membrane IgG binding beta-2-microglobulin binding peptide antigen binding uc002poe.1 uc002poe.2 uc002poe.3 uc002poe.4 
ENST00000221476.4 CKM ENST00000221476.4 creatine kinase, M-type (from RefSeq NM_001824.5) CKMM ENST00000221476.1 ENST00000221476.2 ENST00000221476.3 KCRM_HUMAN NM_001824 P06732 Q96QL9 uc002pbd.1 uc002pbd.2 uc002pbd.3 uc002pbd.4 uc002pbd.5 uc002pbd.6 The protein encoded by this gene is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC007462.1, SRR5189655.101838.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158800, SAMEA2159607 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221476.4/ ENSP00000221476.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence= Dimer of identical or non-identical chains, which can be either B (brain type) or M (muscle type). With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain. P06732; Q96DX5: ASB9; NbExp=10; IntAct=EBI-4287089, EBI-745641; P06732; P12532: CKMT1B; NbExp=3; IntAct=EBI-4287089, EBI-1050662; P06732; P42858: HTT; NbExp=3; IntAct=EBI-4287089, EBI-466029; Cytoplasm. Belongs to the ATP:guanido phosphotransferase family. Name=Wikipedia; Note=Creatine kinase entry; URL="https://en.wikipedia.org/wiki/Creatine_kinase"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ckm/"; nucleotide binding catalytic activity creatine kinase activity protein binding ATP binding extracellular space cytoplasm cytosol creatine metabolic process kinase activity phosphorylation transferase activity transferase activity, transferring phosphorus-containing groups phosphocreatine biosynthetic process uc002pbd.1 uc002pbd.2 uc002pbd.3 uc002pbd.4 uc002pbd.5 uc002pbd.6 
ENST00000221480.6 PEX11G ENST00000221480.6 peroxisomal biogenesis factor 11 gamma, transcript variant 1 (from RefSeq NM_080662.4) ENST00000221480.1 ENST00000221480.2 ENST00000221480.3 ENST00000221480.4 ENST00000221480.5 NM_080662 PEX11C PX11C_HUMAN Q8NDM0 Q96HA9 uc002mgk.1 uc002mgk.2 uc002mgk.3 uc002mgk.4 The protein encoded by this gene is a member of the PEX11 family. This family is reported to regulate the number and size of peroxisomes in evolutionarily distant organisms. The protein encoded by this gene may induce clustering of peroxisomes. Alternative splicing results in multiple transcript variants that encode different protein isoforms. [provided by RefSeq, Jul 2012]. Promotes membrane protrusion and elongation on the peroxisomal surface. Homodimer. Heterodimer with either PEX11A or PEX11B. Interacts with FIS1. Q96HA9; Q13520: AQP6; NbExp=3; IntAct=EBI-17284886, EBI-13059134; Q96HA9; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-17284886, EBI-781551; Q96HA9; P48051: KCNJ6; NbExp=3; IntAct=EBI-17284886, EBI-12017638; Q96HA9; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-17284886, EBI-8638294; Q96HA9; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-17284886, EBI-2548832; Peroxisome membrane ulti-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96HA9-1; Sequence=Displayed; Name=2; IsoId=Q96HA9-2; Sequence=VSP_013539; Belongs to the peroxin-11 family. protein binding peroxisome peroxisomal membrane integral component of peroxisomal membrane membrane integral component of membrane peroxisome fission intrinsic component of peroxisomal membrane macromolecular complex regulation of peroxisome size uc002mgk.1 uc002mgk.2 uc002mgk.3 uc002mgk.4 
ENST00000221485.8 SLC17A7 ENST00000221485.8 solute carrier family 17 member 7 (from RefSeq NM_020309.4) B4DFR9 B4DG46 BNPI ENST00000221485.1 ENST00000221485.2 ENST00000221485.3 ENST00000221485.4 ENST00000221485.5 ENST00000221485.6 ENST00000221485.7 NM_020309 Q6PCD0 Q9P2U7 SLC17A7 VGLU1_HUMAN VGLUT1 uc002pnp.1 uc002pnp.2 uc002pnp.3 uc002pnp.4 uc002pnp.5 The protein encoded by this gene is a vesicle-bound, sodium-dependent phosphate transporter that is specifically expressed in the neuron-rich regions of the brain. It is preferentially associated with the membranes of synaptic vesicles and functions in glutamate transport. The protein shares 82% identity with the differentiation-associated Na-dependent inorganic phosphate cotransporter and they appear to form a distinct class within the Na+/Pi cotransporter family. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from transcript and genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC059379.1, SRR3476690.554678.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145743 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221485.8/ ENSP00000221485.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate (PubMed:10820226). At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells (By similarity). The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane (By similarity). In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification (By similarity). Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake (By similarity). The vesicular K(+)/H(+) antiport activity is electroneutral (By similarity). At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation (PubMed:10820226). The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Is necessary for synaptic signaling of visual-evoked responses from photoreceptors (By similarity). Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence=; Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence=; Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence=; Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823, ChEBI:CHEBI:43474; Evidence=; Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence=; Chloride channel activity is allosterically activated by lumenal H(+) and Cl(-) leading to synaptic vesicles acidification. The L-glutamate transport activity is allosterically activated by lumenal H(+) and Cl(-). The allosteric activation by H(+) efficiently prevents non-vesicular efflux across the plasma membrane, thereby restricting L-glutamate transport activity to acidic membranes such as synaptic vesicles. Interacts with SHANK3. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Cell membrane ; Multi-pass membrane protein Synapse, synaptosome Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9P2U7-1; Sequence=Displayed; Name=2; IsoId=Q9P2U7-2; Sequence=VSP_056110; Name=3; IsoId=Q9P2U7-3; Sequence=VSP_056111; Expressed in several regions of the brain including amygdala, cerebellum, cerebral cortex, hippocampus, frontal lobe, medulla, occipital lobe, putamen and temporal lobe. Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily. Martineau M. et al. show that may function as a L- glutamate/H(+) antiporter (By similarity). However, according to Eriksen J. et al., H(+) is an allosteric activator (By similarity). neural retina development L-glutamate transmembrane transporter activity inorganic phosphate transmembrane transporter activity neurotransmitter transporter activity plasma membrane integral component of plasma membrane ion transport sodium ion transport phosphate ion transport neurotransmitter transport chemical synaptic transmission brain development long-term memory synaptic vesicle extracellular-glutamate-gated chloride channel activity glutamate secretion symporter activity sodium:inorganic phosphate symporter activity sodium-dependent phosphate transmembrane transporter activity L-glutamate transport membrane integral component of membrane cell junction integral component of synaptic vesicle membrane synaptic vesicle membrane cytoplasmic vesicle synaptic transmission, glutamatergic sodium ion transmembrane transport sequestering of neurotransmitter neuron projection intracellular organelle cerebellar mossy fiber sodium-dependent phosphate transport synapse presynaptic active zone regulation of synapse structure or activity L-glutamate import transmembrane transport excitatory synapse excitatory postsynaptic potential clathrin-sculpted glutamate transport vesicle membrane synaptic vesicle lumen acidification neurotransmitter loading into synaptic vesicle postsynapse regulation of synaptic vesicle endocytosis chloride transmembrane transport uc002pnp.1 uc002pnp.2 uc002pnp.3 uc002pnp.4 uc002pnp.5 
ENST00000221486.6 RNASEH2A ENST00000221486.6 ribonuclease H2 subunit A (from RefSeq NM_006397.3) B2RCY1 ENST00000221486.1 ENST00000221486.2 ENST00000221486.3 ENST00000221486.4 ENST00000221486.5 NM_006397 O75792 Q96F11 RNASEHI RNH2A_HUMAN RNHIA uc002mvg.1 uc002mvg.2 uc002mvg.3 uc002mvg.4 The protein encoded by this gene is a component of the heterotrimeric type II ribonuclease H enzyme (RNAseH2). RNAseH2 is the major source of ribonuclease H activity in mammalian cells and endonucleolytically cleaves ribonucleotides. It is predicted to remove Okazaki fragment RNA primers during lagging strand DNA synthesis and to excise single ribonucleotides from DNA-DNA duplexes. Mutations in this gene cause Aicardi-Goutieres Syndrome (AGS), a an autosomal recessive neurological disorder characterized by progressive microcephaly and psychomotor retardation, intracranial calcifications, elevated levels of interferon-alpha and white blood cells in the cerebrospinal fluid.[provided by RefSeq, Aug 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK315327.1, AY363912.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221486.6/ ENSP00000221486.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. ; The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C. Nucleus Aicardi-Goutieres syndrome 4 (AGS4) [MIM:610333]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the RNase HII family. Eukaryotic subfamily. nucleic acid binding RNA binding nuclease activity endonuclease activity RNA-DNA hybrid ribonuclease activity ribonuclease activity nucleus nucleoplasm cytosol DNA replication mismatch repair RNA catabolic process RNA metabolic process hydrolase activity ribonuclease H2 complex DNA replication, removal of RNA primer metal ion binding nucleic acid phosphodiester bond hydrolysis RNA phosphodiester bond hydrolysis RNA phosphodiester bond hydrolysis, endonucleolytic uc002mvg.1 uc002mvg.2 uc002mvg.3 uc002mvg.4 
ENST00000221494.10 SF3A2 ENST00000221494.10 splicing factor 3a subunit 2 (from RefSeq NM_007165.5) B2RBU1 D6W605 ENST00000221494.1 ENST00000221494.2 ENST00000221494.3 ENST00000221494.4 ENST00000221494.5 ENST00000221494.6 ENST00000221494.7 ENST00000221494.8 ENST00000221494.9 NM_007165 O75245 Q15428 SAP62 SF3A2_HUMAN uc002lvg.1 uc002lvg.2 uc002lvg.3 uc002lvg.4 uc002lvg.5 This gene encodes subunit 2 of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer includes subunits 1, 2 and 3 and is necessary for the in vitro conversion of 15S U2 snRNP into an active 17S particle that performs pre-mRNA splicing. Subunit 2 interacts with subunit 1 through its amino-terminus while the single zinc finger domain of subunit 2 plays a role in its binding to the 15S U2 snRNP. Subunit 2 may also function independently of its RNA splicing function as a microtubule-binding protein. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC009903.2, SRR3476690.238362.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221494.10/ ENSP00000221494.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:10882114, PubMed:11533230, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:10882114, PubMed:11533230, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3A2 is part of the SF3A subcomplex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230). Involved in pre-mRNA splicing as a component of pre- catalytic spliceosome 'B' complexes, including the Bact complex (PubMed:29360106, PubMed:29361316, PubMed:30315277). Interacts directly with the duplex formed by U2 snRNA and the intron (PubMed:29360106). Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:32494006, PubMed:21349847, PubMed:34822310, PubMed:36797247). Part of the SF3A subcomplex of the 17S U2 SnRNP complex which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114 (PubMed:10882114, PubMed:11533230, PubMed:21349847). SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the mature 17S U2 small nuclear ribonucleoprotein complex (17S U2 snRNP) (PubMed:10882114, PubMed:11533230). Identified in the spliceosome 'E' complex, a precursor of the spliceosome 'A' complex (PubMed:10882114). Identified in the spliceosome 'A' and 'B' complexes (PubMed:10882114, PubMed:29361316, PubMed:29360106, PubMed:30315277). Identified in the spliceosome 'C' complex (PubMed:11991638). Interacts with HTATSF1 (PubMed:9710584). Q15428; Q12797-6: ASPH; NbExp=3; IntAct=EBI-2462271, EBI-12092171; Q15428; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-2462271, EBI-9092016; Q15428; Q8NDZ0: BEND2; NbExp=3; IntAct=EBI-2462271, EBI-954079; Q15428; Q99459: CDC5L; NbExp=2; IntAct=EBI-2462271, EBI-374880; Q15428; O43143: DHX15; NbExp=2; IntAct=EBI-2462271, EBI-1237044; Q15428; P62993: GRB2; NbExp=3; IntAct=EBI-2462271, EBI-401755; Q15428; P11142: HSPA8; NbExp=2; IntAct=EBI-2462271, EBI-351896; Q15428; Q6MZP7: LIN54; NbExp=3; IntAct=EBI-2462271, EBI-1389411; Q15428; Q8IVT2: MISP; NbExp=3; IntAct=EBI-2462271, EBI-2555085; Q15428; O43639: NCK2; NbExp=3; IntAct=EBI-2462271, EBI-713635; Q15428; Q7RTV0: PHF5A; NbExp=2; IntAct=EBI-2462271, EBI-2555365; Q15428; Q96I25: RBM17; NbExp=2; IntAct=EBI-2462271, EBI-740272; Q15428; Q15637: SF1; NbExp=2; IntAct=EBI-2462271, EBI-744603; Q15428; Q15459: SF3A1; NbExp=4; IntAct=EBI-2462271, EBI-1054743; Q15428; P09661: SNRPA1; NbExp=2; IntAct=EBI-2462271, EBI-876439; Q15428; P62304: SNRPE; NbExp=2; IntAct=EBI-2462271, EBI-348082; Q15428; P62306: SNRPF; NbExp=2; IntAct=EBI-2462271, EBI-356900; Q15428; Q92734: TFG; NbExp=3; IntAct=EBI-2462271, EBI-357061; Q15428; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-2462271, EBI-6550597; Q15428; Q14119: VEZF1; NbExp=3; IntAct=EBI-2462271, EBI-11980193; Q15428; P07947: YES1; NbExp=3; IntAct=EBI-2462271, EBI-515331; Q15428; P25490: YY1; NbExp=5; IntAct=EBI-2462271, EBI-765538; Nucleus Belongs to the SF3A2 family. spliceosomal complex assembly mRNA 3'-splice site recognition mRNA splicing, via spliceosome nucleic acid binding RNA binding protein binding nucleus nucleoplasm spliceosomal complex U2 snRNP mRNA processing zinc ion binding RNA splicing positive regulation of neuron projection development nuclear speck metal ion binding U2-type prespliceosome U2-type precatalytic spliceosome catalytic step 2 spliceosome U2-type prespliceosome assembly uc002lvg.1 uc002lvg.2 uc002lvg.3 uc002lvg.4 uc002lvg.5 
ENST00000221496.5 AMH ENST00000221496.5 anti-Mullerian hormone (from RefSeq NM_000479.5) AMH ENST00000221496.1 ENST00000221496.2 ENST00000221496.3 ENST00000221496.4 MIF MIS_HUMAN NM_000479 O75246 P03971 Q6GTN3 uc002lvh.1 uc002lvh.2 uc002lvh.3 uc002lvh.4 This gene encodes a secreted ligand of the TGF-beta (transforming growth factor-beta) superfamily of proteins. Ligands of this family bind various TGF-beta receptors leading to recruitment and activation of SMAD family transcription factors that regulate gene expression. The encoded preproprotein is proteolytically processed to generate N- and C-terminal cleavage products that homodimerize and associate to form a biologically active noncovalent complex. This complex binds to the anti-Mullerian hormone receptor type 2 and causes the regression of Mullerian ducts in the male embryo that would otherwise differentiate into the uterus and fallopian tubes. This protein also plays a role in Leydig cell differentiation and function and follicular development in adult females. Mutations in this gene result in persistent Mullerian duct syndrome. [provided by RefSeq, Jul 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC049194.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221496.5/ ENSP00000221496.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation (PubMed:3754790, PubMed:34155118, PubMed:8469238). Also plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles (PubMed:14742691). AMH signals by binding to a specific type- II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (PubMed:20861221, PubMed:34155118). Homodimer; disulfide-linked. Secreted In ovaries, AMH is detected in granulosa cells of early growing follicles. Detected in primary follicles and continued to be expressed in follicles in the antral stage. The highest level of AMH expression is present in granulosa cells of secondary, preantral and small antral follicles <4 mm in diameter, whereas expression is lost from follicles at sizes >8 mm. Plasma AMH levels in polycystic ovary syndrome (PCOS) patients are two- to threefold higher than in women with normal ovaries. Preproprotein is proteolytically processed to generate N- and C- terminal cleavage products that homodimerize and associate to form a biologically active non-covalent complex (PubMed:8469238, PubMed:2974034). Binding of the non-covalent complex to AMHR2 induces dissociation of the pro-region from the mature C-terminal dimer (PubMed:20861221). The N-terminal portion of the protein, despite having no intrinsic activity, has the role of amplifying the activity of the C-terminus (PubMed:20861221, PubMed:8469238). Persistent Muellerian duct syndrome 1 (PMDS1) [MIM:261550]: A form of male pseudohermaphroditism characterized by a failure of Muellerian duct regression in otherwise normal males. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TGF-beta family. Name=Wikipedia; Note=Anti-Mullerian hormone entry; URL="https://en.wikipedia.org/wiki/Anti-m%C3%BCllerian_hormone"; preantral ovarian follicle growth urogenital system development Mullerian duct regression receptor binding transforming growth factor beta receptor binding hormone activity extracellular region extracellular space cell-cell signaling gonadal mesoderm development sex determination sex differentiation aging growth factor activity gonad development positive regulation of gene expression response to organic cyclic compound cell differentiation BMP signaling pathway response to drug positive regulation of NF-kappaB transcription factor activity negative regulation of ovarian follicle development uc002lvh.1 uc002lvh.2 uc002lvh.3 uc002lvh.4 
ENST00000221498.7 DKKL1 ENST00000221498.7 dickkopf like acrosomal protein 1, transcript variant 1 (from RefSeq NM_014419.4) DKKL1 DKKL1_HUMAN ENST00000221498.1 ENST00000221498.2 ENST00000221498.3 ENST00000221498.4 ENST00000221498.5 ENST00000221498.6 NM_014419 Q9UK85 SGY1 UNQ735/PRO1429 uc002pnk.1 uc002pnk.2 uc002pnk.3 uc002pnk.4 uc002pnk.5 The dickkopf protein family interacts with the Wnt signaling pathway and its members are characterized by two conserved cysteine-rich domains. This gene encodes a secreted protein that has low sequence similarity to the dickkopf-3 protein. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Oct 2010]. Involved in fertilization by facilitating sperm penetration of the zona pellucida. May promote spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduce testosterone synthesis in Leydig cells. Is not essential either for development or fertility. Interacts with SLXL1; Co-localize in seminiferous tubules. Interacts with SLY. Secreted Cytoplasmic vesicle, secretory vesicle, acrosome Note=Localized specifically to the crescent shaped acrosome at the apex of the sperm head. More highly expressed in adult testis than in fetal testis. Exclusively expressed in the testis (at protein level). Intense expression in stages II, III and IV of spermatogenesis, whereas expression is lower in stage I. Abnormal expression in testes of patients with male infertility. Contains a N-terminal domain similar to that of the N-terminal section of DKK3. N-glycosylated during spermatogenesis. Not N-glycosylated in mature sperm. acrosomal vesicle extracellular region extracellular space penetration of zona pellucida anatomical structure morphogenesis cytoplasmic vesicle co-receptor binding positive regulation of apoptotic process positive regulation of fat cell differentiation receptor antagonist activity negative regulation of canonical Wnt signaling pathway negative regulation of testosterone biosynthetic process negative regulation of receptor activity uc002pnk.1 uc002pnk.2 uc002pnk.3 uc002pnk.4 uc002pnk.5 
ENST00000221515.6 RETN ENST00000221515.6 resistin, transcript variant 1 (from RefSeq NM_020415.4) D6W649 ENST00000221515.1 ENST00000221515.2 ENST00000221515.3 ENST00000221515.4 ENST00000221515.5 FIZZ3 HXCP1 NM_020415 Q540D9 Q76B53 Q9HD89 RETN_HUMAN RSTN UNQ407/PRO1199 uc002mhf.1 uc002mhf.2 uc002mhf.3 This gene belongs to the family defined by the mouse resistin-like genes. The characteristic feature of this family is the C-terminal stretch of 10 cys residues with identical spacing. The mouse homolog of this protein is secreted by adipocytes, and may be the hormone potentially linking obesity to type II diabetes. Alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2010]. Hormone that seems to suppress insulin ability to stimulate glucose uptake into adipose cells (By similarity). Potentially links obesity to diabetes (By similarity). Promotes chemotaxis in myeloid cells (PubMed:15064728). Homodimer; disulfide-linked (By similarity). Interacts with DEFA1 (PubMed:15064728). Q9HD89; O00155: GPR25; NbExp=5; IntAct=EBI-12384280, EBI-10178951; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9HD89-1; Sequence=Displayed; Name=2; Synonyms=delta2ASV; IsoId=Q9HD89-2; Sequence=VSP_055861; Expressed in white adipose tissue (at protein level) (PubMed:11201732). Widely expressed, with particularly strong expression in lung, bone marrow, breast and peripheral blood (PubMed:15248836). Expressed strongly in bone marrow and at lower levels in lung, but not detected in other tissues (PubMed:15064728). Isoform 2 is detected in adipose tissue, bone marrow, brain, lung, peripheral blood, placenta and thymus (PubMed:15248836). Belongs to the resistin/FIZZ family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/retn/"; hormone activity extracellular region extracellular space nucleus signal transduction aging biological_process response to mechanical stimulus response to insulin azurophil granule lumen specific granule lumen neutrophil degranulation fat cell differentiation positive regulation of synaptic transmission extracellular exosome negative regulation of feeding behavior positive regulation of progesterone secretion uc002mhf.1 uc002mhf.2 uc002mhf.3 
ENST00000221538.8 RSPH6A ENST00000221538.8 radial spoke head 6 homolog A (from RefSeq NM_030785.4) ENST00000221538.1 ENST00000221538.2 ENST00000221538.3 ENST00000221538.4 ENST00000221538.5 ENST00000221538.6 ENST00000221538.7 NM_030785 Q53FE2 Q6PEZ9 Q9H0K4 RSH6A_HUMAN RSHL1 RSPH6A uc002pdm.1 uc002pdm.2 uc002pdm.3 uc002pdm.4 uc002pdm.5 The protein encoded by this gene is similar to a sea urchin radial spoke head protein. Radial spoke protein complexes form part of the axoneme of eukaryotic flagella and are located between the axoneme's outer ring of doublet microtubules and central pair of microtubules. In Chlamydomonas, radial spoke proteins are thought to regulate the activity of dynein and the symmetry of flagellar bending patterns. This gene maps to a region of chromosome 19 that is linked to primary ciliary dyskinesia-2 (CILD2). [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AL136761.1, AK098837.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221538.8/ ENSP00000221538.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Functions as part of radial spoke complexes in the axoneme of sperm flagella that play an important part in motility. The triple radial spokes (RS1, RS2 and RS3) are required to modulate beating of the sperm flagellum. Component of the axonemal radial spoke 1 (RS1) and 2 (RS2) complexes, at least composed of spoke head proteins RSPH1, RSPH3, RSPH9 and the cilia-specific component RSPH4A or sperm-specific component RSPH6A, spoke stalk proteins RSPH14, DNAJB13, DYDC1, ROPN1L and NME5, and the RS1 complex-specific anchor protein IQUB. Interacts with RSPH1. Interacts with RSPH3B. Interacts with RSPH4A. Interacts with RSPH9. Interacts with RSPH10B. Q9H0K4; P61968: LMO4; NbExp=3; IntAct=EBI-12169267, EBI-2798728; Q9H0K4; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-12169267, EBI-8463848; Cytoplasm, cytoskeleton, flagellum axoneme Phosphorylated by PKA. Phosphorylation increases in capacitated sperm. Belongs to the flagellar radial spoke RSP4/6 family. radial spoke intracellular cilium assembly cilium movement involved in cell motility uc002pdm.1 uc002pdm.2 uc002pdm.3 uc002pdm.4 uc002pdm.5 
ENST00000221543.10 TBC1D17 ENST00000221543.10 TBC1 domain family member 17, transcript variant 1 (from RefSeq NM_024682.3) B4DT12 B9A6L8 ENST00000221543.1 ENST00000221543.2 ENST00000221543.3 ENST00000221543.4 ENST00000221543.5 ENST00000221543.6 ENST00000221543.7 ENST00000221543.8 ENST00000221543.9 F5H1W7 NM_024682 Q9HA65 TBC17_HUMAN TBC1D17 uc002pqo.1 uc002pqo.2 uc002pqo.3 uc002pqo.4 uc002pqo.5 Probable RAB GTPase-activating protein that inhibits RAB8A/B function. Reduces Rab8 recruitment to tubules emanating from the endocytic recycling compartment (ERC) and inhibits Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TfR) (PubMed:22854040). Involved in regulation of autophagy. Interacts with OPTN; this interaction mediates TBC1D17 transient association with Rab8. Q9HA65; Q96CV9: OPTN; NbExp=7; IntAct=EBI-714625, EBI-748974; Cytoplasmic vesicle, autophagosome Cytoplasm Recycling endosome Note=In the presence of optineurin/OPTN, may be recruited to recycling endosomes. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9HA65-1; Sequence=Displayed; Name=2; IsoId=Q9HA65-2; Sequence=VSP_047344; Name=3; IsoId=Q9HA65-3; Sequence=VSP_053997; The arginine and glutamine fingers are critical for the GTPase- activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. GTPase activator activity protein binding autophagosome cytosol intracellular protein transport autophagy protein transport Rab GTPase binding cytoplasmic vesicle retrograde transport, endosome to Golgi recycling endosome activation of GTPase activity regulation of cilium assembly uc002pqo.1 uc002pqo.2 uc002pqo.3 uc002pqo.4 uc002pqo.5 
ENST00000221554.13 YJU2B ENST00000221554.13 YJU2 splicing factor homolog B, transcript variant 1 (from RefSeq NM_030818.4) CCDC130 ENST00000221554.1 ENST00000221554.10 ENST00000221554.11 ENST00000221554.12 ENST00000221554.2 ENST00000221554.3 ENST00000221554.4 ENST00000221554.5 ENST00000221554.6 ENST00000221554.7 ENST00000221554.8 ENST00000221554.9 NM_030818 P13994 Q9BQ72 SB115 YJU2B YJU2B_HUMAN uc002mxc.1 uc002mxc.2 uc002mxc.3 May be involved in mRNA splicing. P13994; Q92989: CLP1; NbExp=3; IntAct=EBI-716093, EBI-2559831; P13994; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-716093, EBI-743105; P13994; O75031: HSF2BP; NbExp=3; IntAct=EBI-716093, EBI-7116203; P13994; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-716093, EBI-358489; P13994; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-716093, EBI-3918381; P13994; Q96NJ6: ZFP3; NbExp=5; IntAct=EBI-716093, EBI-12302147; P13994; P49910: ZNF165; NbExp=6; IntAct=EBI-716093, EBI-741694; P13994; P17021: ZNF17; NbExp=3; IntAct=EBI-716093, EBI-1105334; P13994; P17028: ZNF24; NbExp=7; IntAct=EBI-716093, EBI-707773; P13994; P15622-3: ZNF250; NbExp=3; IntAct=EBI-716093, EBI-10177272; P13994; P17036: ZNF3; NbExp=5; IntAct=EBI-716093, EBI-1640965; P13994; Q86UD4: ZNF329; NbExp=5; IntAct=EBI-716093, EBI-7233259; P13994; P13682: ZNF35; NbExp=3; IntAct=EBI-716093, EBI-11041653; P13994; Q7Z3I7: ZNF572; NbExp=9; IntAct=EBI-716093, EBI-10172590; P13994; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-716093, EBI-9977294; P13994; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-716093, EBI-10251462; P13994; Q15937: ZNF79; NbExp=3; IntAct=EBI-716093, EBI-10237274; P13994; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-716093, EBI-5667516; P13994; Q3MJ62: ZSCAN23; NbExp=5; IntAct=EBI-716093, EBI-5667532; Nucleus By poly(RI), poly(RC) and Newcastle disease virus. Belongs to the CWC16 family. Sequence=CAA32138.1; Type=Erroneous gene model prediction; Evidence=; Sequence=CAA32138.1; Type=Frameshift; Evidence=; protein binding cellular_component response to virus uc002mxc.1 uc002mxc.2 uc002mxc.3 
ENST00000221566.7 SGTA ENST00000221566.7 small glutamine rich tetratricopeptide repeat co-chaperone alpha (from RefSeq NM_003021.4) D6W610 ENST00000221566.1 ENST00000221566.2 ENST00000221566.3 ENST00000221566.4 ENST00000221566.5 ENST00000221566.6 NM_003021 O43765 Q6FIA9 Q9BTZ9 SGT SGT1 SGTA_HUMAN uc002lwi.1 uc002lwi.2 uc002lwi.3 This gene encodes a protein which is capable of interacting with the major nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate protein; however, its function is not known. Since this transcript is expressed ubiquitously in various tissues, this protein may serve a housekeeping function. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1084371.1, AL050156.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221566.7/ ENSP00000221566.1 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Co-chaperone that binds misfolded and hydrophobic patches- containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails (PubMed:28104892). Functions in tail- anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module (PubMed:28104892). Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins (PubMed:28104892, PubMed:25535373). It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states (PubMed:23129660, PubMed:25179605). Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex (PubMed:27193484). Binds directly to HSC70 and HSP70 and regulates their ATPase activity (PubMed:18759457). (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection via interaction with DNAJB12, DNAJB14 and HSPA8/Hsc70 (PubMed:24675744). Homodimer (PubMed:15708368). Homooligomer (By similarity). Interacts with DNAJC5 and DNAJC5B. Interacts (via TPR repeats) with HSP90AA1 (PubMed:15708368). Interacts (via Gln-rich region) with SLC2A1 (PubMed:15708368). Interacts with HSP90AB1 (PubMed:16580629). Interacts (via TPR repeats) with HSPA8/Hsc70; the interaction is direct (PubMed:24675744). Interacts with BAG6 (via ubiquitin-like domain); interaction prevents interaction between BAG6 and RNF126 (PubMed:23129660, PubMed:25179605, PubMed:27193484). Forms a multiprotein complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is direct (PubMed:24675744). (Microbial infection) Interacts with Vpu and Gag from HIV-1. (Microbial infection) Interacts with SARS-CoV accessory protein 7a. O43765; Q9UKJ8: ADAM21; NbExp=3; IntAct=EBI-347996, EBI-12046857; O43765; A8K660: ADIPOQ; NbExp=3; IntAct=EBI-347996, EBI-10174479; O43765; Q15848: ADIPOQ; NbExp=7; IntAct=EBI-347996, EBI-10827839; O43765; O95994: AGR2; NbExp=3; IntAct=EBI-347996, EBI-712648; O43765; Q8TD06: AGR3; NbExp=6; IntAct=EBI-347996, EBI-3925742; O43765; Q16853: AOC3; NbExp=3; IntAct=EBI-347996, EBI-3921628; O43765; O95816: BAG2; NbExp=2; IntAct=EBI-347996, EBI-355275; O43765; P46379: BAG6; NbExp=6; IntAct=EBI-347996, EBI-347552; O43765; P46379-2: BAG6; NbExp=3; IntAct=EBI-347996, EBI-10988864; O43765; P35070: BTC; NbExp=6; IntAct=EBI-347996, EBI-6590057; O43765; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-347996, EBI-12062109; O43765; Q9BXJ1: C1QTNF1; NbExp=4; IntAct=EBI-347996, EBI-750200; O43765; Q9BXJ0: C1QTNF5; NbExp=3; IntAct=EBI-347996, EBI-19947914; O43765; Q9BXI9: C1QTNF6; NbExp=9; IntAct=EBI-347996, EBI-10301084; O43765; Q6UWT4: C5orf46; NbExp=3; IntAct=EBI-347996, EBI-11986083; O43765; P40259: CD79B; NbExp=6; IntAct=EBI-347996, EBI-2873732; O43765; Q8TCZ2: CD99L2; NbExp=8; IntAct=EBI-347996, EBI-2824782; O43765; P55291: CDH15; NbExp=8; IntAct=EBI-347996, EBI-10215061; O43765; P07510-2: CHRNG; NbExp=3; IntAct=EBI-347996, EBI-11979451; O43765; A0A0S2Z3K0: COL1A2; NbExp=3; IntAct=EBI-347996, EBI-16431143; O43765; P08123: COL1A2; NbExp=11; IntAct=EBI-347996, EBI-983038; O43765; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-347996, EBI-10241815; O43765; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-347996, EBI-852194; O43765; P09603: CSF1; NbExp=6; IntAct=EBI-347996, EBI-2872294; O43765; P01037: CST1; NbExp=3; IntAct=EBI-347996, EBI-1056240; O43765; P78358: CTAG1B; NbExp=3; IntAct=EBI-347996, EBI-1188472; O43765; P07711: CTSL; NbExp=3; IntAct=EBI-347996, EBI-1220160; O43765; Q9UHQ9: CYB5R1; NbExp=3; IntAct=EBI-347996, EBI-953870; O43765; P59861: DEFB131A; NbExp=5; IntAct=EBI-347996, EBI-12304807; O43765; Q9UBP4: DKK3; NbExp=3; IntAct=EBI-347996, EBI-954409; O43765; Q6E0U4: DMKN; NbExp=3; IntAct=EBI-347996, EBI-7943171; O43765; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-347996, EBI-526033; O43765; Q9UNE0-2: EDAR; NbExp=3; IntAct=EBI-347996, EBI-12964110; O43765; A0A0S2Z3V1: EFEMP1; NbExp=3; IntAct=EBI-347996, EBI-16434097; O43765; Q12805: EFEMP1; NbExp=14; IntAct=EBI-347996, EBI-536772; O43765; O95967: EFEMP2; NbExp=7; IntAct=EBI-347996, EBI-743414; O43765; Q96DN0: ERP27; NbExp=7; IntAct=EBI-347996, EBI-953772; O43765; P30040: ERP29; NbExp=3; IntAct=EBI-347996, EBI-946830; O43765; Q9HBU6: ETNK1; NbExp=3; IntAct=EBI-347996, EBI-2834493; O43765; Q9NVM1: EVA1B; NbExp=6; IntAct=EBI-347996, EBI-10314666; O43765; Q9Y624: F11R; NbExp=11; IntAct=EBI-347996, EBI-742600; O43765; Q96RJ6: FERD3L; NbExp=3; IntAct=EBI-347996, EBI-10183007; O43765; Q9NSA1: FGF21; NbExp=3; IntAct=EBI-347996, EBI-3909329; O43765; Q9Y680: FKBP7; NbExp=6; IntAct=EBI-347996, EBI-3918971; O43765; Q12841: FSTL1; NbExp=3; IntAct=EBI-347996, EBI-2349801; O43765; P54710-2: FXYD2; NbExp=5; IntAct=EBI-347996, EBI-13084584; O43765; P58549: FXYD7; NbExp=8; IntAct=EBI-347996, EBI-10216171; O43765; O75084: FZD7; NbExp=3; IntAct=EBI-347996, EBI-746917; O43765; P22466: GAL; NbExp=6; IntAct=EBI-347996, EBI-6624768; O43765; Q9UBC7: GALP; NbExp=3; IntAct=EBI-347996, EBI-12244186; O43765; P09681: GIP; NbExp=6; IntAct=EBI-347996, EBI-8588553; O43765; Q14440: GPErik; NbExp=3; IntAct=EBI-347996, EBI-10232920; O43765; Q96SL4: GPX7; NbExp=7; IntAct=EBI-347996, EBI-749411; O43765; P28799: GRN; NbExp=7; IntAct=EBI-347996, EBI-747754; O43765; Q02747: GUCA2A; NbExp=8; IntAct=EBI-347996, EBI-12244272; O43765; A0A0C4DFT7: GYPA; NbExp=3; IntAct=EBI-347996, EBI-12044847; O43765; B8Q183: GYPA; NbExp=4; IntAct=EBI-347996, EBI-10176190; O43765; P02724: GYPA; NbExp=3; IntAct=EBI-347996, EBI-702665; O43765; P48723: HSPA13; NbExp=8; IntAct=EBI-347996, EBI-750892; O43765; P46695: IER3; NbExp=6; IntAct=EBI-347996, EBI-1748945; O43765; P24592: IGFBP6; NbExp=3; IntAct=EBI-347996, EBI-947015; O43765; Q6PIQ7: IGL@; NbExp=3; IntAct=EBI-347996, EBI-6677651; O43765; Q8N355: IGL@; NbExp=4; IntAct=EBI-347996, EBI-748681; O43765; P40189: IL6ST; NbExp=3; IntAct=EBI-347996, EBI-1030834; O43765; Q14653: IRF3; NbExp=3; IntAct=EBI-347996, EBI-2650369; O43765; Q13568: IRF5; NbExp=3; IntAct=EBI-347996, EBI-3931258; O43765; Q6GPH6: ITPRIPL1; NbExp=3; IntAct=EBI-347996, EBI-953819; O43765; Q6GPH6-2: ITPRIPL1; NbExp=3; IntAct=EBI-347996, EBI-12337095; O43765; Q8N6L0: KASH5; NbExp=8; IntAct=EBI-347996, EBI-749265; O43765; Q09470: KCNA1; NbExp=3; IntAct=EBI-347996, EBI-8286599; O43765; Q16322: KCNA10; NbExp=3; IntAct=EBI-347996, EBI-12265328; O43765; Q9UJ90: KCNE5; NbExp=3; IntAct=EBI-347996, EBI-11981259; O43765; P02538: KRT6A; NbExp=3; IntAct=EBI-347996, EBI-702198; O43765; Q86UP2: KTN1; NbExp=3; IntAct=EBI-347996, EBI-359761; O43765; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-347996, EBI-12007212; O43765; Q6ISS4: LAIR2; NbExp=6; IntAct=EBI-347996, EBI-10250491; O43765; O43561: LAT; NbExp=3; IntAct=EBI-347996, EBI-1222766; O43765; O43561-2: LAT; NbExp=3; IntAct=EBI-347996, EBI-8070286; O43765; P80188: LCN2; NbExp=5; IntAct=EBI-347996, EBI-11911016; O43765; O15165-2: LDLRAD4; NbExp=3; IntAct=EBI-347996, EBI-13302279; O43765; Q8N112: LSMEM2; NbExp=3; IntAct=EBI-347996, EBI-10264855; O43765; Q96G30: MRAP2; NbExp=6; IntAct=EBI-347996, EBI-9537218; O43765; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-347996, EBI-12806656; O43765; P08118: MSMB; NbExp=3; IntAct=EBI-347996, EBI-10195681; O43765; Q969H8: MYDGF; NbExp=8; IntAct=EBI-347996, EBI-718622; O43765; Q99972: MYOC; NbExp=3; IntAct=EBI-347996, EBI-11692272; O43765; Q8IW45: NAXD; NbExp=7; IntAct=EBI-347996, EBI-8650724; O43765; Q13232: NME3; NbExp=12; IntAct=EBI-347996, EBI-713684; O43765; Q9HCQ7: NPVF; NbExp=3; IntAct=EBI-347996, EBI-1753111; O43765; Q9GZP1: NRSN2; NbExp=3; IntAct=EBI-347996, EBI-724857; O43765; Q5JUK9: PAGE3; NbExp=6; IntAct=EBI-347996, EBI-10244544; O43765; C3PTT6: PAUF; NbExp=3; IntAct=EBI-347996, EBI-3505892; O43765; Q96AQ6: PBXIP1; NbExp=4; IntAct=EBI-347996, EBI-740845; O43765; Q9UN74: PCDHA4; NbExp=3; IntAct=EBI-347996, EBI-712273; O43765; Q9Y5G9: PCDHGA4; NbExp=3; IntAct=EBI-347996, EBI-12956949; O43765; Q96PD5-2: PGLYRP2; NbExp=3; IntAct=EBI-347996, EBI-12758027; O43765; Q9UL19: PLAAT4; NbExp=4; IntAct=EBI-347996, EBI-10323452; O43765; Q969W9-2: PMEPA1; NbExp=3; IntAct=EBI-347996, EBI-13318883; O43765; P23284: PPIB; NbExp=6; IntAct=EBI-347996, EBI-359252; O43765; P45877: PPIC; NbExp=6; IntAct=EBI-347996, EBI-953909; O43765; Q96NZ9: PRAP1; NbExp=9; IntAct=EBI-347996, EBI-2116102; O43765; Q8TAS3: PRRG2; NbExp=3; IntAct=EBI-347996, EBI-10272071; O43765; Q9UIG4: PSORS1C2; NbExp=5; IntAct=EBI-347996, EBI-11974061; O43765; Q15293: RCN1; NbExp=3; IntAct=EBI-347996, EBI-948278; O43765; Q5GAN6: RNASE10; NbExp=5; IntAct=EBI-347996, EBI-12423312; O43765; P50876: RNF144A; NbExp=3; IntAct=EBI-347996, EBI-2340657; O43765; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-347996, EBI-12055631; O43765; P04843: RPN1; NbExp=7; IntAct=EBI-347996, EBI-355963; O43765; P31431: SDC4; NbExp=6; IntAct=EBI-347996, EBI-3913237; O43765; Q9HCN8: SDF2L1; NbExp=3; IntAct=EBI-347996, EBI-2339921; O43765; P05121: SERPINE1; NbExp=6; IntAct=EBI-347996, EBI-953978; O43765; O75830: SERPINI2; NbExp=3; IntAct=EBI-347996, EBI-750144; O43765; Q16586: SGCA; NbExp=13; IntAct=EBI-347996, EBI-5663553; O43765; Q16586-2: SGCA; NbExp=4; IntAct=EBI-347996, EBI-16434133; O43765; O43765: SGTA; NbExp=4; IntAct=EBI-347996, EBI-347996; O43765; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-347996, EBI-744081; O43765; Q96DD7: SHISA4; NbExp=3; IntAct=EBI-347996, EBI-18035902; O43765; Q8N114-3: SHISA5; NbExp=3; IntAct=EBI-347996, EBI-13369834; O43765; P03973: SLPI; NbExp=6; IntAct=EBI-347996, EBI-355293; O43765; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-347996, EBI-10226799; O43765; Q96QK8: SMIM14; NbExp=3; IntAct=EBI-347996, EBI-373430; O43765; Q71RC9: SMIM5; NbExp=9; IntAct=EBI-347996, EBI-12334905; O43765; P08294: SOD3; NbExp=3; IntAct=EBI-347996, EBI-10195782; O43765; Q5DT21: SPINK9; NbExp=3; IntAct=EBI-347996, EBI-13119580; O43765; P16150: SPN; NbExp=5; IntAct=EBI-347996, EBI-10049055; O43765; P10451: SPP1; NbExp=8; IntAct=EBI-347996, EBI-723648; O43765; Q8TCT8: SPPL2A; NbExp=7; IntAct=EBI-347996, EBI-750784; O43765; P10124: SRGN; NbExp=10; IntAct=EBI-347996, EBI-744915; O43765; Q86TD4-2: SRL; NbExp=3; IntAct=EBI-347996, EBI-12304565; O43765; E0CX11: STMP1; NbExp=3; IntAct=EBI-347996, EBI-18397783; O43765; P51687: SUOX; NbExp=3; IntAct=EBI-347996, EBI-3921347; O43765; Q9BT88: SYT11; NbExp=7; IntAct=EBI-347996, EBI-751770; O43765; Q9H2B2: SYT4; NbExp=7; IntAct=EBI-347996, EBI-751132; O43765; Q07654: TFF3; NbExp=3; IntAct=EBI-347996, EBI-10224676; O43765; P02786: TFRC; NbExp=6; IntAct=EBI-347996, EBI-355727; O43765; P01135: TGFA; NbExp=3; IntAct=EBI-347996, EBI-1034374; O43765; P01135-2: TGFA; NbExp=6; IntAct=EBI-347996, EBI-12367411; O43765; Q6P9G4: TMEM154; NbExp=3; IntAct=EBI-347996, EBI-13329239; O43765; Q8WUU8: TMEM174; NbExp=6; IntAct=EBI-347996, EBI-10276729; O43765; Q96A57-2: TMEM230; NbExp=3; IntAct=EBI-347996, EBI-17546822; O43765; Q5JXX7: TMEM31; NbExp=3; IntAct=EBI-347996, EBI-10244617; O43765; Q9Y2Y6: TMEM98; NbExp=3; IntAct=EBI-347996, EBI-7333781; O43765; O60235: TMPRSS11D; NbExp=3; IntAct=EBI-347996, EBI-7639969; O43765; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-347996, EBI-2820477; O43765; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-347996, EBI-717441; O43765; O14836: TNFRSF13B; NbExp=3; IntAct=EBI-347996, EBI-519160; O43765; O14836-2: TNFRSF13B; NbExp=8; IntAct=EBI-347996, EBI-12023110; O43765; Q9NS68-2: TNFRSF19; NbExp=3; IntAct=EBI-347996, EBI-12089038; O43765; O75509: TNFRSF21; NbExp=3; IntAct=EBI-347996, EBI-2313231; O43765; O43508: TNFSF12; NbExp=3; IntAct=EBI-347996, EBI-6932080; O43765; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-347996, EBI-12840050; O43765; Q5BVD1: TTMP; NbExp=6; IntAct=EBI-347996, EBI-10243654; O43765; Q9GZX9: TWSG1; NbExp=3; IntAct=EBI-347996, EBI-10304067; O43765; O95881: TXNDC12; NbExp=3; IntAct=EBI-347996, EBI-2564581; O43765; P11441: UBL4A; NbExp=5; IntAct=EBI-347996, EBI-356983; O43765; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-347996, EBI-947187; O43765; O75631: UPK3A; NbExp=3; IntAct=EBI-347996, EBI-10188907; O43765; P01282: VIP; NbExp=3; IntAct=EBI-347996, EBI-751454; O43765; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-347996, EBI-10316321; O43765; Q8WWY7: WFDC12; NbExp=3; IntAct=EBI-347996, EBI-11958577; O43765; Q8IUB5: WFDC13; NbExp=5; IntAct=EBI-347996, EBI-12041955; O43765; Q8TCV5: WFDC5; NbExp=3; IntAct=EBI-347996, EBI-12175871; O43765; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-347996, EBI-17494306; O43765; O60844: ZG16; NbExp=12; IntAct=EBI-347996, EBI-746479; O43765; Q96DA0: ZG16B; NbExp=3; IntAct=EBI-347996, EBI-953824; O43765; A0A1U9X8X8; NbExp=3; IntAct=EBI-347996, EBI-17234977; O43765; P59635: 7a; Xeno; NbExp=3; IntAct=EBI-347996, EBI-25492879; O43765; P0DTD8: 7b; Xeno; NbExp=3; IntAct=EBI-347996, EBI-25475914; O43765; P0DTD3: 9c; Xeno; NbExp=3; IntAct=EBI-347996, EBI-25475917; Cytoplasm Nucleus Note=Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. Ubiquitous. The second tetratricopeptide repeat (TPR 2) mediates the interaction with SARS-CoV accessory protein 7a. Belongs to the SGT family. protein binding nucleus cytoplasm cytosol posttranslational protein targeting to membrane membrane viral process ER-associated ubiquitin-dependent protein catabolic process identical protein binding protein self-association chaperone-mediated protein folding tail-anchored membrane protein insertion into ER membrane TRC complex presynapse extrinsic component of synaptic vesicle membrane negative regulation of ER-associated ubiquitin-dependent protein catabolic process positive regulation of ER-associated ubiquitin-dependent protein catabolic process positive regulation of chaperone-mediated protein folding BAT3 complex binding negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process uc002lwi.1 uc002lwi.2 uc002lwi.3 
ENST00000221573.11 SNAPC2 ENST00000221573.11 small nuclear RNA activating complex polypeptide 2, transcript variant 1 (from RefSeq NM_003083.4) B2RBZ6 D6W663 ENST00000221573.1 ENST00000221573.10 ENST00000221573.2 ENST00000221573.3 ENST00000221573.4 ENST00000221573.5 ENST00000221573.6 ENST00000221573.7 ENST00000221573.8 ENST00000221573.9 NM_003083 Q13486 Q13487 SNAP45 SNPC2_HUMAN uc002miw.1 uc002miw.2 uc002miw.3 uc002miw.4 This gene encodes a subunit of the snRNA-activating protein complex which is associated with the TATA box-binding protein. The encoded protein is necessary for RNA polymerase II and III dependent small-nuclear RNA gene transcription. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2009]. Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box. Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC2 interacts with TBP and SNAPC4. Nucleus. transcription factor activity, sequence-specific DNA binding nucleus nucleoplasm cytosol regulation of transcription, DNA-templated transcription from RNA polymerase II promoter transcription from RNA polymerase III promoter snRNA transcription nuclear body snRNA transcription from RNA polymerase II promoter uc002miw.1 uc002miw.2 uc002miw.3 uc002miw.4 
ENST00000221665.5 FIZ1 ENST00000221665.5 FLT3 interacting zinc finger 1 (from RefSeq NM_032836.3) A2RU72 ENST00000221665.1 ENST00000221665.2 ENST00000221665.3 ENST00000221665.4 FIZ1_HUMAN NM_032836 Q6ZMJ7 Q96SL8 ZNF798 uc002qli.1 uc002qli.2 uc002qli.3 uc002qli.4 uc002qli.5 This gene encodes zinc finger protein, which interacts with a receptor tyrosine kinase involved in the regulation of hematopoietic and lymphoid cells. This gene product also interacts with a transcription factor that regulates the expression of rod-specific genes in retina. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AK027674.1, SRR1163657.14902.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2154405 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221665.5/ ENSP00000221665.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## May be a transcriptional repressor of NRL function in photoreceptors. Does not repress CRX-mediated transactivation (By similarity). Interacts with FLT3 cytoplasmic catalytic domain, following receptor stimulation, in a kinase-independent manner. Does not interact with other structurally related receptor tyrosine kinases, including KIT, CSF1R and PDGFR. Interacts with NRL (By similarity). Cytoplasm Nucleus Widely expressed. Sequence=BAD18728.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; positive regulation of protein phosphorylation nucleic acid binding nucleus cytoplasm receptor tyrosine kinase binding metal ion binding uc002qli.1 uc002qli.2 uc002qli.3 uc002qli.4 uc002qli.5 
ENST00000221671.8 C19orf44 ENST00000221671.8 chromosome 19 open reading frame 44, transcript variant 1 (from RefSeq NM_032207.4) CS044_HUMAN ENST00000221671.1 ENST00000221671.2 ENST00000221671.3 ENST00000221671.4 ENST00000221671.5 ENST00000221671.6 ENST00000221671.7 NM_032207 Q8N6Y7 Q9H6X5 uc002neh.1 uc002neh.2 uc002neh.3 uc002neh.4 Q9H6X5; Q8NA61: CBY2; NbExp=3; IntAct=EBI-7112211, EBI-741724; Q9H6X5-2; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-12061599, EBI-11524851; Q9H6X5-2; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-12061599, EBI-10961624; Q9H6X5-2; P63167: DYNLL1; NbExp=5; IntAct=EBI-12061599, EBI-349105; Q9H6X5-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12061599, EBI-618309; Q9H6X5-2; P37235: HPCAL1; NbExp=4; IntAct=EBI-12061599, EBI-749311; Q9H6X5-2; Q92845: KIFAP3; NbExp=3; IntAct=EBI-12061599, EBI-954040; Q9H6X5-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-12061599, EBI-3044087; Q9H6X5-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-12061599, EBI-11522433; Q9H6X5-2; P61601: NCALD; NbExp=3; IntAct=EBI-12061599, EBI-749635; Q9H6X5-2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-12061599, EBI-726876; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H6X5-1; Sequence=Displayed; Name=2; IsoId=Q9H6X5-2; Sequence=VSP_026311; protein binding uc002neh.1 uc002neh.2 uc002neh.3 uc002neh.4 
ENST00000221700.11 CYP4F2 ENST00000221700.11 cytochrome P450 family 4 subfamily F member 2 (from RefSeq NM_001082.5) A0A024R7K3 A8K425 B4DV75 CP4F2_HUMAN CYP4F2 ENST00000221700.1 ENST00000221700.10 ENST00000221700.2 ENST00000221700.3 ENST00000221700.4 ENST00000221700.5 ENST00000221700.6 ENST00000221700.7 ENST00000221700.8 ENST00000221700.9 NM_001082 P78329 Q16677 Q6NWT4 Q6NWT6 Q9NNZ0 Q9UIU8 uc002nbs.1 uc002nbs.2 uc002nbs.3 This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum. The enzyme starts the process of inactivating and degrading leukotriene B4, a potent mediator of inflammation. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F11, is approximately 16 kb away. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK290790.1, U02388.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2152474, SAMEA2153946 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221700.11/ ENSP00000221700.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids and vitamins (PubMed:18577768, PubMed:10833273, PubMed:10660572, PubMed:11997390, PubMed:17341693, PubMed:18574070). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long- and very long-chain fatty acids. Displays high omega-hydroxylase activity toward polyunsaturated fatty acids (PUFAs) (PubMed:18577768). Participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:10660572, PubMed:17341693, PubMed:18574070). Plays a role in the oxidative inactivation of eicosanoids, including both pro-inflammatory and anti- inflammatory mediators such as leukotriene B4 (LTB4), lipoxin A4 (LXA4), and several HETEs (PubMed:8026587, PubMed:9799565, PubMed:10833273, PubMed:10660572, PubMed:17341693, PubMed:18574070, PubMed:18577768). Catalyzes omega-hydroxylation of 3-hydroxy fatty acids (PubMed:18065749). Converts monoepoxides of linoleic acid leukotoxin and isoleukotoxin to omega-hydroxylated metabolites (PubMed:15145985). Contributes to the degradation of very long-chain fatty acids (VLCFAs) by catalyzing successive omega-oxidations and chain shortening (PubMed:16547005, PubMed:18182499). Plays an important role in vitamin metabolism by chain shortening. Catalyzes omega- hydroxylation of the phytyl chain of tocopherols (forms of vitamin E), with preference for gamma-tocopherols over alpha-tocopherols, thus promoting retention of alpha-tocopherols in tissues (PubMed:11997390). Omega-hydroxylates and inactivates phylloquinone (vitamin K1), and menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in blood coagulation (PubMed:19297519, PubMed:24138531). Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence= Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76624; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756; Evidence=; Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50164, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132026; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50165; Evidence=; Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z,17Z)- eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39791, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76639; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792; Evidence=; Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)- docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40155, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77015, ChEBI:CHEBI:77016; EC=1.14.14.79; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40156; Evidence=; Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH-- hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)- eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53572, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84025, ChEBI:CHEBI:137474; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573; Evidence=; Reaction=(9S,10R)-epoxy-octadecanoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-(9S,10R)-epoxy-octadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53552, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137458, ChEBI:CHEBI:137461; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53553; Evidence=; Reaction=(9R,10S)-epoxy-octadecanoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-(9R,10S)-epoxy-octadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53556, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137459, ChEBI:CHEBI:137460; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53557; Evidence=; Reaction=12,13-epoxy-(9Z)-octadecenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-12,13-epoxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53568, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84026, ChEBI:CHEBI:137469; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53569; Evidence=; Reaction=9,10-epoxy-(12Z)-octadecenoate + O2 + reduced [NADPH-- hemoprotein reductase] = 18-hydroxy-9,10-epoxy-(12Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53564, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84023, ChEBI:CHEBI:137467; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53565; Evidence=; Reaction=8-hydroxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 8,20-dihydroxy-(5Z,9E,11Z,14Z)- eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48660, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90716, ChEBI:CHEBI:90717; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48661; Evidence=; Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 12,20-dihydroxy-(5Z,8Z,10E,14Z)- eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48664, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90718, ChEBI:CHEBI:90719; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48665; Evidence=; Reaction=12-hydroxyoctadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12,18-dihydroxyoctadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49376, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84201, ChEBI:CHEBI:91294; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49377; Evidence=; Reaction=docosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-hydroxydocosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40079, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23858, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76304; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40080; Evidence=; Reaction=22-hydroxydocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-oxodocosanoate + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39055, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76298, ChEBI:CHEBI:76304; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39056; Evidence=; Reaction=22-oxodocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = docosanedioate + 2 H(+) + H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39043, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76298, ChEBI:CHEBI:76299; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39044; Evidence=; Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetracosanoate = 24-hydroxytetracosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39719, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:31014, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76610; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39720; Evidence=; Reaction=hexacosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 26-hydroxyhexacosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40083, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:31013, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76305; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40084; Evidence=; Reaction=26-hydroxyhexacosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 26-oxohexacosanoate + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39059, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76305, ChEBI:CHEBI:76311; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39060; Evidence=; Reaction=26-oxohexacosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 2 H(+) + H2O + hexacosanedioate + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:39047, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76311, ChEBI:CHEBI:76312; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39048; Evidence=; Reaction=3-hydroxyoctadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 3,18-dihydroxyoctadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39735, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76614, ChEBI:CHEBI:76615; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39736; Evidence=; Reaction=3-hydroxyhexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 3,16-dihydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39731, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63904, ChEBI:CHEBI:76613; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39732; Evidence=; Reaction=leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:22176, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57460, ChEBI:CHEBI:57461, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.94; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22177; Evidence=; Reaction=6-trans-leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-6-trans-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48676, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90723, ChEBI:CHEBI:90732; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48677; Evidence=; Reaction=lipoxin A4 + O2 + reduced [NADPH--hemoprotein reductase] = 20- hydroxy-lipoxin A4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48648, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:67026, ChEBI:CHEBI:90707; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48649; Evidence=; Reaction=menaquinone-4 + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + omega-hydroxymenaquinone-4 + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:41520, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78277, ChEBI:CHEBI:78278; EC=1.14.14.78; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41521; Evidence=; Reaction=O2 + phylloquinone + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + omega-hydroxyphylloquinone + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:41516, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18067, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78276; EC=1.14.14.78; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41517; Evidence=; Reaction=(+)-alpha-tocopherol + O2 + reduced [NADPH--hemoprotein reductase] = 13-hydroxy-alpha-tocopherol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:45108, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18145, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84962; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45109; Evidence=; Reaction=gamma-tocopherol + H(+) + NADPH + O2 = 13-hydroxy-gamma- tocopherol + H2O + NADP(+); Xref=Rhea:RHEA:45112, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18185, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:84963; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45113; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Inhibited by dietary sesamin. Kinetic parameters: KM=0.5 uM for docosanoate ; KM=1.1 uM for tetracosanoate ; KM=1.9 uM for hexacosanoate ; KM=75.2 uM for 12-hydroxyoctadecanoate ; KM=19 uM for 8-HETE ; KM=42.3 uM for 12-HETE ; KM=37.6 uM for 22-hydroxydocosanoate ; KM=8.8 uM for 26-hydroxyhexacosanoate ; KM=26.1 uM for 9(10)-epoxyoctadecanoate ; KM=163.1 uM for 9(10)-epoxy-(12Z)-octadecenoate ; KM=135 uM for 12(13)-epoxy-(9Z)-octadecenoate ; KM=60 uM for leukotriene B4 ; KM=55.6 uM for 6-trans-leukotriene B4 ; KM=58.2 uM for lipoxin A4 ; KM=1.7 uM for menaquinone-4 (MK-4) ; KM=21 uM for alpha-tocopherol ; KM=37 uM for gamma-tocopherol ; Vmax=1.6 pmol/min/pmol enzyme toward docosanoate ; Vmax=1.6 pmol/min/pmol enzyme toward tetracosanoate ; Vmax=0.9 pmol/min/pmol enzyme toward hexacosanoate ; Vmax=7 nmol/min/nmol enzyme toward 12-hydroxyoctadecanoate ; Vmax=4 nmol/min/nmol enzyme toward 8-HETE ; Vmax=2.9 nmol/min/nmol enzyme toward 12-HETE ; Vmax=1.6 pmol/min/pmol enzyme toward 22-hydroxydocosanoate ; Vmax=0.7 pmol/min/pmol enzyme toward 26-hydroxyhexacosanoate ; Vmax=7.9 nmol/min/nmol enzyme toward 9(10)-epoxyoctadecanoate ; Vmax=10.6 nmol/min/nmol enzyme toward 9(10)-epoxy-(12Z)-octadecenoate ; Vmax=0.84 nmol/min/nmol enzyme toward 12(13)-epoxy-(9Z)-octadecenoate ; Vmax=2.7 nmol/min/nmol enzyme toward leukotriene B4 ; Vmax=11.9 nmol/min/nmol enzyme toward 6-trans-leukotriene B4 ; Vmax=5.5 nmol/min/nmol enzyme toward lipoxin A4 ; Vmax=0.16 nmol/min/nmol enzyme toward alpha-tocopherol ; Vmax=1.99 nmol/min/nmol enzyme toward gamma-tocopherol ; Note=kcat is 0.067 min(-1) with menaquinone-4 (MK-4) as substrate (PubMed:24138531). The omega-hydroxylation of VLCFAs follows dual- enzyme Michaelis-Menten kinetics, suggesting simultaneous binding of two substrate molecules. The high affinity Michaelis-Menten constants are shown (PubMed:16547005). Lipid metabolism; arachidonate metabolism. Lipid metabolism; leukotriene B4 degradation. Cofactor degradation; phylloquinone degradation. P78329; Q13520: AQP6; NbExp=3; IntAct=EBI-1752413, EBI-13059134; P78329; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-1752413, EBI-18013275; P78329; O43889-2: CREB3; NbExp=3; IntAct=EBI-1752413, EBI-625022; P78329; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1752413, EBI-6942903; P78329; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-1752413, EBI-296550; P78329; Q15125: EBP; NbExp=3; IntAct=EBI-1752413, EBI-3915253; P78329; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-1752413, EBI-18535450; P78329; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1752413, EBI-781551; P78329; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-1752413, EBI-18938272; P78329; P48165: GJA8; NbExp=3; IntAct=EBI-1752413, EBI-17458373; P78329; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-1752413, EBI-18053395; P78329; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-1752413, EBI-10266796; P78329; O95214: LEPROTL1; NbExp=3; IntAct=EBI-1752413, EBI-750776; P78329; Q15546: MMD; NbExp=3; IntAct=EBI-1752413, EBI-17873222; P78329; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-1752413, EBI-3923617; P78329; P15941-11: MUC1; NbExp=3; IntAct=EBI-1752413, EBI-17263240; P78329; P16333: NCK1; NbExp=2; IntAct=EBI-1752413, EBI-389883; P78329; O15173: PGRMC2; NbExp=3; IntAct=EBI-1752413, EBI-1050125; P78329; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-1752413, EBI-949945; P78329; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-1752413, EBI-11337973; P78329; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-1752413, EBI-7545592; P78329; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-1752413, EBI-10192441; P78329; Q03395: ROM1; NbExp=3; IntAct=EBI-1752413, EBI-9395257; P78329; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-1752413, EBI-17247926; P78329; Q9NX18: SDHAF2; NbExp=3; IntAct=EBI-1752413, EBI-713250; P78329; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-1752413, EBI-18159983; P78329; Q8NDX2-2: SLC17A8; NbExp=3; IntAct=EBI-1752413, EBI-17249797; P78329; Q9BZV2: SLC19A3; NbExp=3; IntAct=EBI-1752413, EBI-3923779; P78329; Q96QE2: SLC2A13; NbExp=3; IntAct=EBI-1752413, EBI-18082698; P78329; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-1752413, EBI-10819434; P78329; Q8WY91: THAP4; NbExp=3; IntAct=EBI-1752413, EBI-726691; P78329; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-1752413, EBI-12947623; P78329; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-1752413, EBI-6448756; P78329; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-1752413, EBI-726044; P78329; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1752413, EBI-6447886; P78329; Q12999: TSPAN31; NbExp=3; IntAct=EBI-1752413, EBI-17678331; P78329; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-1752413, EBI-10180829; P78329; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-1752413, EBI-12837904; Microsome membrane eripheral membrane protein Endoplasmic reticulum membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P78329-1; Sequence=Displayed; Name=2; IsoId=P78329-2; Sequence=VSP_055578, VSP_055579, VSP_055580; Liver. Also present in kidney: specifically expressed in the S2 and S3 segments of proximal tubules in cortex and outer medulla (PubMed:10660572). Coumarin resistance (CMRES) [MIM:122700]: A condition characterized by partial or complete resistance to warfarin or other 4- hydroxycoumarin derivatives. These drugs are used as anti-coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. te=Disease susceptibility may be associated with variants affecting the gene represented in this entry. The variant Met-433 is associated with coumarin (the brand name of warfarin) resistance by increasing coumarin maintenance dose in patients on this anti-coagulant therapy. This is probably due to decreased activity of the phylloquinone omega-hydroxylase activity, leading to an increase in hepatic vitamin K levels that warfarin must antagonize (PubMed:24138531). Belongs to the cytochrome P450 family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cyp4f2/"; very long-chain fatty acid metabolic process long-chain fatty acid metabolic process renal water homeostasis pressure natriuresis monooxygenase activity iron ion binding protein binding cytoplasm endoplasmic reticulum endoplasmic reticulum membrane lipid metabolic process fatty acid metabolic process icosanoid metabolic process leukotriene metabolic process blood coagulation regulation of blood pressure arachidonic acid epoxygenase activity membrane apical plasma membrane oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen drug metabolic process alkane 1-monooxygenase activity arachidonic acid metabolic process epoxygenase P450 pathway heme binding organelle membrane negative regulation of icosanoid secretion positive regulation of icosanoid secretion leukotriene B4 catabolic process vitamin E metabolic process menaquinone catabolic process phylloquinone catabolic process vitamin K catabolic process intracellular membrane-bounded organelle metal ion binding leukotriene-B4 20-monooxygenase activity arachidonic acid omega-hydroxylase activity alpha-tocopherol omega-hydroxylase activity tocotrienol omega-hydroxylase activity sodium ion homeostasis oxidation-reduction process aromatase activity omega-hydroxylase P450 pathway uc002nbs.1 uc002nbs.2 uc002nbs.3 
ENST00000221730.8 EPHX3 ENST00000221730.8 epoxide hydrolase 3, transcript variant 1 (from RefSeq NM_024794.3) A3KMR3 ABHD9 ENST00000221730.1 ENST00000221730.2 ENST00000221730.3 ENST00000221730.4 ENST00000221730.5 ENST00000221730.6 ENST00000221730.7 EPHX3_HUMAN NM_024794 Q9H6B9 uc002nap.1 uc002nap.2 uc002nap.3 uc002nap.4 uc002nap.5 Catalyzes the hydrolysis of epoxide-containing fatty acids. Active in vitro against epoxyeicosatrienoic acids (EETs) including 8,9- EET, 9,10-EET, 11,12-EET and 14,15-EET and leukotoxin. Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19038; Evidence=; Reaction=9,10-epoxyoctadecanoate + H2O = 9,10-dihydroxyoctadecanoate; Xref=Rhea:RHEA:45352, ChEBI:CHEBI:15377, ChEBI:CHEBI:85195, ChEBI:CHEBI:85197; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45353; Evidence=; Reaction=9,10-epoxy-(12Z)-octadecenoate + H2O = 9,10-dihydroxy-(12Z)- octadecenoate; Xref=Rhea:RHEA:44032, ChEBI:CHEBI:15377, ChEBI:CHEBI:84023, ChEBI:CHEBI:84027; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44033; Evidence=; Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = 8,9-dihydroxy- (5Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44048, ChEBI:CHEBI:15377, ChEBI:CHEBI:84025, ChEBI:CHEBI:84032; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44049; Evidence=; Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = 11,12- dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44044, ChEBI:CHEBI:15377, ChEBI:CHEBI:76625, ChEBI:CHEBI:84031; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44045; Evidence=; Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = 14,15- dihydroxy-(5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:44040, ChEBI:CHEBI:15377, ChEBI:CHEBI:84024, ChEBI:CHEBI:84029; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44041; Evidence=; Inhibited by 1-(1-acetylpiperidin-4-yl)-3-(4- (trifl uoromethoxy)phenyl)urea (TPAU), 1-cyclohexyl-3-dodecylurea (CDU), 12-(3-adamantan-1-yl-ureido)-dodecanoic acid (AUDA), 1-((3S, 5S, 7S)-adamantan-1-yl)-3-(5-(2-(2-ethoxyethoxy) ethoxy)pentyl)urea (AEPU) and to a lesser extent by 8-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido) octanoic acid (AUOA). Kinetic parameters: KM=30 uM for 8,9-EET ; KM=80 uM for 11,12-EET ; KM=130 uM for 14,15-EET ; KM=25 uM for leukotoxin ; Vmax=12 umol/min/mg enzyme with 8,9-EET as substrate ; Vmax=50 umol/min/mg enzyme with 11,12-EET as substrate ; Vmax=60 umol/min/mg enzyme with 14,15-EET as substrate ; Vmax=22 umol/min/mg enzyme with leukotoxin as substrate ; Microsome membrane ; Single-pass membrane protein Belongs to the AB hydrolase superfamily. Epoxide hydrolase family. catalytic activity epoxide hydrolase activity endoplasmic reticulum lipid metabolic process membrane integral component of membrane hydrolase activity organelle membrane intracellular membrane-bounded organelle epoxide metabolic process uc002nap.1 uc002nap.2 uc002nap.3 uc002nap.4 uc002nap.5 
ENST00000221735.12 ZNF419 ENST00000221735.12 zinc finger protein 419, transcript variant 2 (from RefSeq NM_024691.4) B4DXU7 B4E348 B7ZA41 E9PCP4 E9PED0 E9PET3 E9PFX9 ENST00000221735.1 ENST00000221735.10 ENST00000221735.11 ENST00000221735.2 ENST00000221735.3 ENST00000221735.4 ENST00000221735.5 ENST00000221735.6 ENST00000221735.7 ENST00000221735.8 ENST00000221735.9 NM_024691 Q96HQ0 Q9H5P0 ZN419_HUMAN ZNF419A uc002qov.1 uc002qov.2 uc002qov.3 uc002qov.4 May be involved in transcriptional regulation. Q96HQ0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10288482, EBI-3867333; Q96HQ0; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10288482, EBI-10172290; Q96HQ0; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10288482, EBI-748974; Nucleus Event=Alternative splicing; Named isoforms=6; Name=1; IsoId=Q96HQ0-1; Sequence=Displayed; Name=2; IsoId=Q96HQ0-2; Sequence=VSP_016034, VSP_016033; Name=3; IsoId=Q96HQ0-3; Sequence=VSP_046149; Name=4; IsoId=Q96HQ0-4; Sequence=VSP_047106; Name=5; IsoId=Q96HQ0-5; Sequence=VSP_016034; Name=6; IsoId=Q96HQ0-6; Sequence=VSP_046149, VSP_016033; Belongs to the krueppel C2H2-type zinc-finger protein family. nucleic acid binding DNA binding protein binding nucleus regulation of transcription, DNA-templated metal ion binding uc002qov.1 uc002qov.2 uc002qov.3 uc002qov.4 
ENST00000221797.5 LGALS13 ENST00000221797.5 galectin 13 (from RefSeq NM_013268.3) C5HZ15 ENST00000221797.1 ENST00000221797.2 ENST00000221797.3 ENST00000221797.4 NM_013268 PLAC8 PP13_HUMAN Q9UHV8 uc002omb.1 uc002omb.2 uc002omb.3 uc002omb.4 uc002omb.5 Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene has lysophospholipase activity. It is composed of two identical subunits which are held together by disulfide bonds. This protein has structural similarity to several members of the beta-galactoside-binding S-type lectin family. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC066304.1, CB995660.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2149398, SAMEA2153307 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221797.5/ ENSP00000221797.3 RefSeq Select criteria :: based on expression ##RefSeq-Attributes-END## Binds beta-galactoside and lactose. Strong inducer of T-cell apoptosis (PubMed:10527825, PubMed:19497882). Has hemagglutinating activity towards chicken erythrocytes (PubMed:29343868). Homodimer; disulfide-linked. Q9UHV8; Q02930-3: CREB5; NbExp=3; IntAct=EBI-3957707, EBI-10192698; Q9UHV8; P49639: HOXA1; NbExp=6; IntAct=EBI-3957707, EBI-740785; Q9UHV8; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-3957707, EBI-1210753; Q9UHV8; P32242: OTX1; NbExp=3; IntAct=EBI-3957707, EBI-740446; Q9UHV8; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-3957707, EBI-77926; Q9UHV8; A2BDE7: PHLDA1; NbExp=3; IntAct=EBI-3957707, EBI-14084211; Q9UHV8; Q12837: POU4F2; NbExp=3; IntAct=EBI-3957707, EBI-17236143; Q9UHV8; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-3957707, EBI-3957603; Cytoplasm Nucleus matrix Detected in adult and fetal spleen, fetal kidney, adult urinary bladder and placenta. Placental expression originates predominantly from the syncytiotrophoblast. lysophospholipase activity protein binding nucleus cytoplasm phospholipid metabolic process apoptotic process nuclear matrix carbohydrate binding positive regulation of T cell apoptotic process uc002omb.1 uc002omb.2 uc002omb.3 uc002omb.4 uc002omb.5 
ENST00000221801.8 FBL ENST00000221801.8 fibrillarin (from RefSeq NM_001436.4) B5BUE8 ENST00000221801.1 ENST00000221801.2 ENST00000221801.3 ENST00000221801.4 ENST00000221801.5 ENST00000221801.6 ENST00000221801.7 FBL FBRL_HUMAN FIB1 FLRN NM_001436 O75259 P22087 Q6IAT5 Q9UPI6 uc002omn.1 uc002omn.2 uc002omn.3 uc002omn.4 uc002omn.5 This gene product is a component of a nucleolar small nuclear ribonucleoprotein (snRNP) particle thought to participate in the first step in processing preribosomal RNA. It is associated with the U3, U8, and U13 small nuclear RNAs and is located in the dense fibrillar component (DFC) of the nucleolus. The encoded protein contains an N-terminal repetitive domain that is rich in glycine and arginine residues, like fibrillarins in other species. Its central region resembles an RNA-binding domain and contains an RNP consensus sequence. Antisera from approximately 8% of humans with the autoimmune disease scleroderma recognize fibrillarin. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC019260.1, SRR1163658.428476.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221801.8/ ENSP00000221801.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins (PubMed:24352239, PubMed:30540930, PubMed:32017898). Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (PubMed:30540930). Site specificity is provided by a guide RNA that base pairs with the substrate (By similarity). Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity). Probably catalyzes 2'-O-methylation of U6 snRNAs in box C/D RNP complexes (PubMed:32017898). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017898). Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239, PubMed:30540930). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). Reaction=L-glutaminyl-[histone H2A] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[histone H2A] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50904, Rhea:RHEA-COMP:12837, Rhea:RHEA-COMP:12839, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; Evidence=; Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O- methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48629; Evidence=; Reaction=a ribonucleotide in U6 snRNA + S-adenosyl-L-methionine = a 2'- O-methylribonucleotide in U6 snRNA + H(+) + S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:63088, Rhea:RHEA-COMP:16262, Rhea:RHEA- COMP:16263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63089; Evidence=; Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain SNU13, FBL, NOP5 and NOP56, plus a guide RNA (PubMed:1714385, PubMed:32017898). It is associated with the U3, U8, U13, X and Y small nuclear RNAs (PubMed:1714385). Component of several ribosomal and nucleolar protein complexes. Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Interacts with PRMT5 and UTP20 (PubMed:14583623, PubMed:17498821). Interacts with DDX5 and C1QBP (PubMed:10837141, PubMed:21536856). Interacts with NOL11 (PubMed:22916032). Interacts with PIH1D1 (PubMed:17636026). Interacts with RRP1B (PubMed:20926688). Interacts with NOLC1 (By similarity). Interacts with SDE2 (PubMed:34365507). P22087; P17844: DDX5; NbExp=6; IntAct=EBI-358318, EBI-351962; P22087; Q14684: RRP1B; NbExp=4; IntAct=EBI-358318, EBI-372051; P22087; Q96RS0: TGS1; NbExp=2; IntAct=EBI-358318, EBI-949244; P22087; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-358318, EBI-10240849; Nucleus, nucleolus cleus, nucleoplasm Note=Fibrillar region of the nucleolus. Ubiquitinated. Ubiquitination leads to proteasomal degradation (PubMed:19208757). Deubiquitinated by USP36 (PubMed:19208757). By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA). Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me), without affecting rRNA methylation (PubMed:30540930). Deacetylation by SIRT7 restores methylation of 'Gln- 105' of histone H2A (H2AQ104me) (PubMed:30540930). Belongs to the methyltransferase superfamily. Fibrillarin family. box C/D snoRNA 3'-end processing TFIID-class transcription factor binding osteoblast differentiation fibrillar center dense fibrillar component granular component RNA binding protein binding nucleus nucleoplasm chromosome nucleolus rRNA processing methyltransferase activity rRNA methyltransferase activity Cajal body membrane snoRNA metabolic process transferase activity rRNA methylation box C/D snoRNP complex small-subunit processome methylation snoRNA localization ATPase binding extracellular exosome histone glutamine methylation histone-glutamine methyltransferase activity uc002omn.1 uc002omn.2 uc002omn.3 uc002omn.4 uc002omn.5 
ENST00000221804.5 CLC ENST00000221804.5 Charcot-Leyden crystal galectin (from RefSeq NM_001828.6) C5HZ13 C5HZ14 ENST00000221804.1 ENST00000221804.2 ENST00000221804.3 ENST00000221804.4 LEG10_HUMAN LGALS10 LGALS10A NM_001828 Q05315 Q0VDE3 uc002omh.1 uc002omh.2 uc002omh.3 uc002omh.4 uc002omh.5 Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene is a lysophospholipase expressed in eosinophils and basophils. It hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. This protein may possess carbohydrate or IgE-binding activities. It is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. It may be associated with inflammation and some myeloid leukemias. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AV715152.1, AV714984.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221804.5/ ENSP00000221804.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Regulates immune responses through the recognition of cell- surface glycans. Essential for the anergy and suppressive function of CD25-positive regulatory T-cells (Treg). Interacts with CEL. Q05315; Q05315: CLC; NbExp=4; IntAct=EBI-10485101, EBI-10485101; Cytoplasm, cytosol Cytoplasmic granule Note=Localized in granules from where it may be secreted or transported to other locations in the cell. Expressed abundantly in the bone marrow. Expressed exclusively by eosinophils and basophils. Not detected in monocytes and neutrophils. Expressed in CD25-positive regulatory T-cells (Treg) (at protein level). Found in intestinal tissue from patients with Celiac disease, expression is directly related to the histological grade of mucosal damage and to the number of eosinophils found in the duodenal lesion (at protein level). Found in sputum of patients with eosinophilic inflammatory diseases such as asthma (at protein level). Forms hexagonal bipyramidal crystals, known as Charcot- Leyden crystals, in tissues and secretions from sites of eosinophil- associated inflammation and some myeloid leukemias. Was originally thought to possess lysophospholipase activity but the absence of this activity has been shown by PubMed:11834744. Name=Functional Glycomics Gateway - Glycan Binding; Note=Galectin-10; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_277"; regulation of T cell anergy regulation of T cell cytokine production protein binding cytoplasm cytosol multicellular organism development carbohydrate binding identical protein binding regulation of activated T cell proliferation T cell apoptotic process cysteine-type endopeptidase activity involved in apoptotic process lysophospholipase activity uc002omh.1 uc002omh.2 uc002omh.3 uc002omh.4 uc002omh.5 
ENST00000221847.6 EBI3 ENST00000221847.6 Epstein-Barr virus induced 3 (from RefSeq NM_005755.3) A0N0N2 ENST00000221847.1 ENST00000221847.2 ENST00000221847.3 ENST00000221847.4 ENST00000221847.5 IL27B IL27B_HUMAN NM_005755 O75269 Q14213 uc002lzu.1 uc002lzu.2 uc002lzu.3 uc002lzu.4 uc002lzu.5 This gene was identified by its induced expression in B lymphocytes in response Epstein-Barr virus infection. It encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form interleukin 27 (IL-27). IL-27 regulates T cell and inflammatory responses, in part by activating the Jak/STAT pathway of CD4+ T cells. [provided by RefSeq, Sep 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC015364.1, SRR1163657.205051.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221847.6/ ENSP00000221847.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN- gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines. Heterodimer with IL27/IL27A; not disulfide-linked (PubMed:12121660). This heterodimer is known as interleukin IL-27 (PubMed:12121660). Heterodimer with IL12A; not disulfide-linked (PubMed:9342359). This heterodimer is known as interleukin IL-35 (PubMed:9342359). Interacts with SQSTM1 (PubMed:8551575). Q14213; Q8NEV9: IL27; NbExp=2; IntAct=EBI-742959, EBI-15887997; Secreted By Epstein-Barr virus (EBV). Belongs to the type I cytokine receptor family. Type 3 subfamily. Name=Wikipedia; Note=Interleukin-27 entry; URL="https://en.wikipedia.org/wiki/Interleukin_27"; cytokine receptor activity cytokine activity protein binding extracellular region extracellular space endoplasmic reticulum lumen plasma membrane humoral immune response external side of plasma membrane membrane cytokine binding T-helper 1 type immune response T cell proliferation receptor complex positive regulation of interferon-gamma biosynthetic process interleukin-27 receptor binding positive regulation of alpha-beta T cell proliferation interleukin-27-mediated signaling pathway interleukin-35-mediated signaling pathway uc002lzu.1 uc002lzu.2 uc002lzu.3 uc002lzu.4 uc002lzu.5 
ENST00000221855.8 TBCB ENST00000221855.8 tubulin folding cofactor B, transcript variant 3 (from RefSeq NR_155756.2) CG22 CKAP1 ENST00000221855.1 ENST00000221855.2 ENST00000221855.3 ENST00000221855.4 ENST00000221855.5 ENST00000221855.6 ENST00000221855.7 NR_155756 O00111 O00674 O14728 Q6FGY5 Q99426 TBCB_HUMAN uc002odg.1 uc002odg.2 uc002odg.3 Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer (PubMed:9265649). Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth (By similarity). Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state (PubMed:9265649). Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers (By similarity). Interacts with GAN (PubMed:16303566). Interacts with DCTN1 (PubMed:22777741). Q99426; Q9H2C0: GAN; NbExp=3; IntAct=EBI-764356, EBI-764342; Q99426; Q93009: USP7; NbExp=2; IntAct=EBI-764356, EBI-302474; Cytoplasm toplasm, cytoskeleton Note=Colocalizes with microtubules. In differentiated neurons, located in the cytoplasm. In differentiating neurons, accumulates at the growth cone. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q99426-1; Sequence=Displayed; Name=2; IsoId=Q99426-2; Sequence=VSP_055521; Found in most tissues. Phosphorylation by PAK1 is required for normal function. Ubiquitinated in the presence of GAN which targets it for degradation by the proteasome. (Microbial infection) Glycosylated residues by S.typhimurium protein Ssek1: arginine GlcNAcylation promotes microtubule stability. Belongs to the TBCB family. Sequence=AAB51182.1; Type=Erroneous gene model prediction; Evidence=; protein binding cytoplasm cytosol cytoskeleton microtubule multicellular organism development nervous system development microtubule cytoskeleton cell differentiation uc002odg.1 uc002odg.2 uc002odg.3 
ENST00000221856.11 FSD1 ENST00000221856.11 fibronectin type III and SPRY domain containing 1, transcript variant 1 (from RefSeq NM_024333.3) B2RDT0 ENST00000221856.1 ENST00000221856.10 ENST00000221856.2 ENST00000221856.3 ENST00000221856.4 ENST00000221856.5 ENST00000221856.6 ENST00000221856.7 ENST00000221856.8 ENST00000221856.9 FSD1_HUMAN GLFND MIR1 NM_024333 Q9BTV5 Q9BXN0 Q9HAG4 VLP27 uc002lzy.1 uc002lzy.2 uc002lzy.3 uc002lzy.4 This gene encodes a centrosome associated protein that is characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III domain, and a C-terminal repeats in splA and RyR (SPRY) domain. The encoded protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis. [provided by RefSeq, Apr 2009]. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.965954.1, SRR3476690.765012.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221856.11/ ENSP00000221856.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## May be involved in microtubule organization and stabilization. Oligomerization is required for binding to microtubules. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm. Cleavage furrow. Note=Cell- cycle-dependent association with the centrosome. Colocalizes with a subpopulation of microtubules. Does not associate with microtubules during mitosis but reassociates with microtubules during cytokinesis. Localizes to the central portions of a small subset of microtubules in interphase cells and a subpopulation of microtubules in the cleavage furrow, not present in the mitotic spindle. Highly expressed in brain tissues, including cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe, temporal lobe and putamen. Lower expression in spinal chord. B30.2 box contains a microtubule-binding site. nucleus cytoplasm centrosome microtubule organizing center cytoskeleton microtubule cell cycle microtubule binding cytoplasmic microtubule organization cleavage furrow regulation of cytokinesis protein homodimerization activity protein homooligomerization cell division regulation of cell division regulation of mitotic spindle organization uc002lzy.1 uc002lzy.2 uc002lzy.3 uc002lzy.4 
ENST00000221859.9 POLR2I ENST00000221859.9 RNA polymerase II subunit I (from RefSeq NM_006233.5) B2R5J2 ENST00000221859.1 ENST00000221859.2 ENST00000221859.3 ENST00000221859.4 ENST00000221859.5 ENST00000221859.6 ENST00000221859.7 ENST00000221859.8 NM_006233 P36954 Q6NW05 RPB9_HUMAN uc002ode.1 uc002ode.2 uc002ode.3 uc002ode.4 uc002ode.5 This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit, in combination with two other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA. The product of this gene has two zinc finger motifs with conserved cysteines and the subunit does possess zinc binding activity. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC017112.1, SRR1163655.549868.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2467144 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221859.9/ ENSP00000221859.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity). Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. P36954; P55212: CASP6; NbExp=3; IntAct=EBI-395202, EBI-718729; P36954; P30519: HMOX2; NbExp=3; IntAct=EBI-395202, EBI-712096; P36954; P13473-2: LAMP2; NbExp=3; IntAct=EBI-395202, EBI-21591415; P36954; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-395202, EBI-5280197; P36954; P62826: RAN; NbExp=3; IntAct=EBI-395202, EBI-286642; Nucleus, nucleolus Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family. mRNA splicing, via spliceosome maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter nucleic acid binding DNA-directed 5'-3' RNA polymerase activity nucleus nucleoplasm DNA-directed RNA polymerase II, core complex nucleolus transcription-coupled nucleotide-excision repair transcription, DNA-templated transcription from RNA polymerase II promoter transcription initiation from RNA polymerase II promoter transcription elongation from RNA polymerase II promoter 7-methylguanosine mRNA capping mRNA cleavage zinc ion binding fibroblast growth factor receptor signaling pathway RNA metabolic process somatic stem cell population maintenance snRNA transcription from RNA polymerase II promoter metal ion binding positive regulation of viral transcription regulation of gene silencing by miRNA uc002ode.1 uc002ode.2 uc002ode.3 uc002ode.4 uc002ode.5 
ENST00000221891.9 APLP1 ENST00000221891.9 amyloid beta precursor like protein 1, transcript variant 1 (from RefSeq NM_001024807.3) APLP1_HUMAN ENST00000221891.1 ENST00000221891.2 ENST00000221891.3 ENST00000221891.4 ENST00000221891.5 ENST00000221891.6 ENST00000221891.7 ENST00000221891.8 NM_001024807 O00113 P51693 Q96A92 uc002ocf.1 uc002ocf.2 uc002ocf.3 uc002ocf.4 uc002ocf.5 This gene encodes a member of the highly conserved amyloid precursor protein gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]. May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis. Monomer and homodimer. Heparin binding promotes homodimerization. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB and APBA family members, MAPK8IP1 and DAB1 (By similarity). Binding to Dab1 inhibits its serine phosphorylation (By similarity). Interacts with CPEB1. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Interacts (via NPXY motif) with DAB1 (By similarity). P51693; P51693: APLP1; NbExp=4; IntAct=EBI-74648, EBI-74648; P51693; Q06481: APLP2; NbExp=2; IntAct=EBI-74648, EBI-79306; P51693; P05067-4: APP; NbExp=2; IntAct=EBI-74648, EBI-302641; P51693; Q93074: MED12; NbExp=2; IntAct=EBI-74648, EBI-394357; P51693; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-74648, EBI-11141397; P51693; P17028: ZNF24; NbExp=2; IntAct=EBI-74648, EBI-707773; Cell membrane; Single-pass type I membrane protein. [C30]: Cytoplasm. Note=C-terminally processed in the Golgi complex. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P51693-1; Sequence=Displayed; Name=2; IsoId=P51693-2; Sequence=VSP_039100; Expressed in the cerebral cortex where it is localized to the postsynaptic density (PSD). The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The NPXY site is also involved in clathrin-mediated endocytosis. Proteolytically cleaved by caspases during neuronal apoptosis. Cleaved, in vitro, at Asp-620 by caspase-3 (By similarity). N- and O-glycosylated. O-glycosylation with core 1 or possibly core 8 glycans. Glycosylation on Ser-227 is the preferred site to Thr- 228. Binds zinc and copper in the extracellular domain. Zinc- binding increases heparin binding. No Cu(2+) reducing activity with copper-binding. Belongs to the APP family. protein binding basement membrane cytoplasm plasma membrane endocytosis apoptotic process cell adhesion nervous system development heparin binding animal organ morphogenesis membrane integral component of membrane alpha-2A adrenergic receptor binding alpha-2B adrenergic receptor binding alpha-2C adrenergic receptor binding identical protein binding metal ion binding transition metal ion binding perinuclear region of cytoplasm cellular response to norepinephrine stimulus uc002ocf.1 uc002ocf.2 uc002ocf.3 uc002ocf.4 uc002ocf.5 
ENST00000221922.11 CCDC9 ENST00000221922.11 coiled-coil domain containing 9 (from RefSeq NM_015603.3) CCDC9 CCDC9_HUMAN ENST00000221922.1 ENST00000221922.10 ENST00000221922.2 ENST00000221922.3 ENST00000221922.4 ENST00000221922.5 ENST00000221922.6 ENST00000221922.7 ENST00000221922.8 ENST00000221922.9 NM_015603 Q9Y3X0 uc010xym.1 uc010xym.2 uc010xym.3 uc010xym.4 Probable component of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon- exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Probable component of the exon junction complex (EJC); the association is RNA-dependent. Q9Y3X0; P13569: CFTR; NbExp=4; IntAct=EBI-2557532, EBI-349854; Q9Y3X0; P42858: HTT; NbExp=3; IntAct=EBI-2557532, EBI-466029; Q9Y3X0; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2557532, EBI-10975473; Q9Y3X0; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-2557532, EBI-717399; Q9Y3X0; O76024: WFS1; NbExp=3; IntAct=EBI-2557532, EBI-720609; RNA binding protein binding uc010xym.1 uc010xym.2 uc010xym.3 uc010xym.4 
ENST00000221930.6 TGFB1 ENST00000221930.6 transforming growth factor beta 1 (from RefSeq NM_000660.7) A8K792 ENST00000221930.1 ENST00000221930.2 ENST00000221930.3 ENST00000221930.4 ENST00000221930.5 NM_000660 P01137 Q9UCG4 TGFB TGFB1 TGFB1_HUMAN uc002oqh.1 uc002oqh.2 uc002oqh.3 uc002oqh.4 uc002oqh.5 This gene encodes a secreted ligand of the TGF-beta (transforming growth factor-beta) superfamily of proteins. Ligands of this family bind various TGF-beta receptors leading to recruitment and activation of SMAD family transcription factors that regulate gene expression. The encoded preproprotein is proteolytically processed to generate a latency-associated peptide (LAP) and a mature peptide, and is found in either a latent form composed of a mature peptide homodimer, a LAP homodimer, and a latent TGF-beta binding protein, or in an active form consisting solely of the mature peptide homodimer. The mature peptide may also form heterodimers with other TGFB family members. This encoded protein regulates cell proliferation, differentiation and growth, and can modulate expression and activation of other growth factors including interferon gamma and tumor necrosis factor alpha. This gene is frequently upregulated in tumor cells, and mutations in this gene result in Camurati-Engelmann disease. [provided by RefSeq, Aug 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X02812.1, SRR3476690.819241.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA2142670 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221930.6/ ENSP00000221930.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix (PubMed:28117447). Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1 (PubMed:2022183, PubMed:8617200, PubMed:8939931, PubMed:19750484, PubMed:22278742, PubMed:19651619). Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia (Probable). Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:22278742, PubMed:19651619). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). [Transforming growth factor beta-1]: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency- associated peptide (LAP) and Transforming growth factor beta-1 (TGF- beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix (PubMed:29109152). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF- beta-1 and maintain it in a latent state during storage in extracellular milieus (PubMed:2022183, PubMed:8617200, PubMed:8939931, PubMed:19750484, PubMed:22278742, PubMed:19651619). TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin- binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). Once activated following release of LAP, TGF-beta-1 acts by binding to TGF- beta receptors (TGFBR1 and TGFBR2), which transduce signal (PubMed:20207738). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency-associated peptide chain (LAP) and 'milieu molecules' (By similarity). Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (By similarity). At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL- 17 expression, favoring Treg cell development (By similarity). At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP) (PubMed:25310401). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus (PubMed:25893292, PubMed:29483653, PubMed:30696809). Positively regulates odontoblastic differentiation in dental papilla cells, via promotion of IPO7-mediated translocation of phosphorylated SMAD2 to the nucleus and subsequent transcription of target genes (By similarity). Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (PubMed:25893292, PubMed:30696809). Homodimer; disulfide-linked (PubMed:20207738, PubMed:25209176, PubMed:28117447, PubMed:29109152). Interacts with the serine proteases, HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated signaling and the HTRA protease activity is required for this inhibition (By similarity). May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling (By similarity). Interacts with CD109, DPT and ASPN (PubMed:9895299, PubMed:16754747, PubMed:17827158). Interacts with EFEMP2 (PubMed:27339457). Interacts with TSKU; the interaction contributes to regulation of the hair cycle (By similarity). [Latency-associated peptide]: Homodimer; disulfide-linked (PubMed:28117447, PubMed:29109152). Interacts with transforming growth factor beta-1 (TGF-beta-1) chain; interaction is non-covalent and maintains TGF-beta-1 in a latent state; each latency-associated peptide (LAP) monomer interacts with TGF-beta-1 in the other monomer (PubMed:29109152). Interacts with LTBP1; leading to regulation of TGF- beta-1 activation (PubMed:2022183, PubMed:8617200, PubMed:8939931). Interacts with LRRC32/GARP; leading to regulation of TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:22278742, PubMed:19651619). Interacts with LRRC33/NRROS; leading to regulation of TGF-beta-1 in macrophages and microglia (Probable). Interacts (via cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). Interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction (By similarity). Interacts with HSP90AB1; inhibits latent TGFB1 activation (PubMed:20599762). Interact with PSG9; leading to TGFB1 activation (PubMed:27389696). [Transforming growth factor beta-1]: Homodimer; disulfide- linked (PubMed:20207738, PubMed:25209176, PubMed:28117447, PubMed:29109152). Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (PubMed:20207738). P01137; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-779636, EBI-10173507; P01137; P05067: APP; NbExp=3; IntAct=EBI-779636, EBI-77613; P01137; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-779636, EBI-744545; P01137; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-779636, EBI-3867333; P01137; Q14689: DIP2A; NbExp=2; IntAct=EBI-779636, EBI-2564275; P01137; P17813: ENG; NbExp=2; IntAct=EBI-779636, EBI-2834630; P01137; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-779636, EBI-11977403; P01137; Q12841: FSTL1; NbExp=2; IntAct=EBI-779636, EBI-2349801; P01137; P49639: HOXA1; NbExp=3; IntAct=EBI-779636, EBI-740785; P01137; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-779636, EBI-11959885; P01137; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-779636, EBI-11749135; P01137; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-779636, EBI-10171774; P01137; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-779636, EBI-10302392; P01137; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-779636, EBI-11962058; P01137; Q5T751: LCE1C; NbExp=3; IntAct=EBI-779636, EBI-12224199; P01137; Q5T752: LCE1D; NbExp=3; IntAct=EBI-779636, EBI-11741311; P01137; O14633: LCE2B; NbExp=3; IntAct=EBI-779636, EBI-11478468; P01137; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-779636, EBI-11973993; P01137; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-779636, EBI-9394625; P01137; Q5TA77: LCE3B; NbExp=3; IntAct=EBI-779636, EBI-11974495; P01137; Q9BYE3: LCE3D; NbExp=3; IntAct=EBI-779636, EBI-6658837; P01137; O60711: LPXN; NbExp=3; IntAct=EBI-779636, EBI-744222; P01137; Q14392: LRRC32; NbExp=2; IntAct=EBI-779636, EBI-15796956; P01137; Q14766-1: LTBP1; NbExp=4; IntAct=EBI-779636, EBI-11173861; P01137; P50222: MEOX2; NbExp=3; IntAct=EBI-779636, EBI-748397; P01137; P07237: P4HB; NbExp=3; IntAct=EBI-779636, EBI-395883; P01137; Q12837: POU4F2; NbExp=3; IntAct=EBI-779636, EBI-17236143; P01137; P11464: PSG1; NbExp=3; IntAct=EBI-779636, EBI-716740; P01137; P01137: TGFB1; NbExp=2; IntAct=EBI-779636, EBI-779636; P01137; P36897: TGFBR1; NbExp=2; IntAct=EBI-779636, EBI-1027557; P01137; P37173: TGFBR2; NbExp=11; IntAct=EBI-779636, EBI-296151; P01137; Q03167: TGFBR3; NbExp=2; IntAct=EBI-779636, EBI-2852679; P01137; P07996: THBS1; NbExp=2; IntAct=EBI-779636, EBI-2530274; P01137; P22105: TNXB; NbExp=3; IntAct=EBI-779636, EBI-2821024; P01137; Q90998: TGFBR3; Xeno; NbExp=2; IntAct=EBI-779636, EBI-6620843; PRO_0000033762; P11464: PSG1; NbExp=2; IntAct=EBI-15487336, EBI-716740; [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix [Transforming growth factor beta-1]: Secreted Highly expressed in bone (PubMed:11746498, PubMed:17827158). Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA) (PubMed:11746498, PubMed:17827158). Colocalizes with ASPN in chondrocytes within OA lesions of articular cartilage (PubMed:17827158). [Latency-associated peptide]: The 'straitjacket' and 'arm' domains encircle the Transforming growth factor beta-1 (TGF-beta-1) monomers and are fastened together by strong bonding between Lys-56 and Tyr-103/Tyr-104. [Latency-associated peptide]: The cell attachment site motif mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8) (PubMed:28117447). The motif locates to a long loop in the arm domain called the bowtie tail (PubMed:28117447). Integrin-binding stabilizes an alternative conformation of the bowtie tail (PubMed:28117447). Activation by integrin requires force application by the actin cytoskeleton, which is resisted by the 'milieu molecules' (such as LTBP1, LRRC32/GARP and/or LRRC33/NRROS), resulting in distortion of the prodomain and release of the active TGF-beta-1 (PubMed:28117447). Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. [Latency-associated peptide]: N-glycosylated (PubMed:3162913, PubMed:2493139, PubMed:28117447). Deglycosylation leads to activation of Transforming growth factor beta-1 (TGF-beta-1); mechanisms triggering deglycosylation-driven activation of TGF-beta-1 are however unclear (PubMed:2493139). In post-menopausal Japanese women, the frequency of Leu- 10 is higher in subjects with osteoporosis than in controls. Camurati-Engelmann disease (CAEND) [MIM:131300]: An autosomal dominant disorder characterized by hyperostosis and sclerosis of the diaphyses of long bones. The disease typically presents in early childhood with pain, muscular weakness and waddling gait, and in some cases other features such as exophthalmos, facial paralysis, hearing difficulties and loss of vision. te=The disease is caused by variants affecting the gene represented in this entry. Inflammatory bowel disease, immunodeficiency, and encephalopathy (IBDIMDE) [MIM:618213]: An autosomal recessive disorder characterized by severe infantile inflammatory bowel disease manifesting as bloody diarrhea and failure to thrive, global developmental delay, epilepsy, brain atrophy and encephalopathy. Affected individuals suffer from recurrent infections associated with impaired T-cell response to stimulation and decreased T-cell subsets, including regulatory and helper T cells. Note=The disease is caused by variants affecting the gene represented in this entry. TGF-beta-1 is inactivated by fresolimumab (also named GC1008), a monoclonal-neutralizing antibody. Belongs to the TGF-beta family. Name=Wikipedia; Note=TGF beta-1 entry; URL="https://en.wikipedia.org/wiki/TGF_beta_1"; negative regulation of transcription from RNA polymerase II promoter MAPK cascade vasculogenesis ureteric bud development response to hypoxia morphogenesis of a branching structure cell activation epithelial to mesenchymal transition neural tube closure negative regulation of protein phosphorylation positive regulation of protein phosphorylation regulation of sodium ion transport chondrocyte differentiation hematopoietic progenitor cell differentiation connective tissue replacement involved in inflammatory response wound healing adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains tolerance induction to self antigen platelet degranulation heart valve morphogenesis aortic valve morphogenesis antigen binding type II transforming growth factor beta receptor binding cytokine activity transforming growth factor beta receptor binding protein binding extracellular region extracellular space nucleus cytoplasm Golgi lumen plasma membrane protein phosphorylation protein export from nucleus ATP biosynthetic process phosphate-containing compound metabolic process cellular calcium ion homeostasis inflammatory response cell cycle arrest mitotic cell cycle checkpoint epidermal growth factor receptor signaling pathway transforming growth factor beta receptor signaling pathway common-partner SMAD protein phosphorylation SMAD protein complex assembly Notch signaling pathway negative regulation of neuroblast proliferation salivary gland morphogenesis endoderm development heart development female pregnancy aging growth factor activity cell proliferation positive regulation of cell proliferation negative regulation of cell proliferation germ cell migration response to radiation response to wounding response to glucose defense response to fungus, incompatible interaction cell surface response to organic substance regulation of gene expression positive regulation of vascular endothelial growth factor production positive regulation of gene expression negative regulation of gene expression negative regulation of extracellular matrix disassembly positive regulation of epithelial to mesenchymal transition macrophage derived foam cell differentiation positive regulation of fibroblast migration positive regulation of peptidyl-threonine phosphorylation positive regulation of pathway-restricted SMAD protein phosphorylation negative regulation of macrophage cytokine production oligodendrocyte development positive regulation of microglia differentiation response to organic cyclic compound regulation of striated muscle tissue development cell migration regulation of transforming growth factor beta receptor signaling pathway evasion or tolerance of host defenses by virus cytokine-mediated signaling pathway enzyme binding neural tube development negative regulation of cell-cell adhesion secretory granule hyaluronan catabolic process T cell differentiation negative regulation of ossification negative regulation of cell growth osteoclast differentiation regulation of cell migration positive regulation of cell migration axon positive regulation of bone mineralization BMP signaling pathway negative regulation of transforming growth factor beta receptor signaling pathway mammary gland development extracellular matrix positive regulation of histone deacetylation platelet alpha granule lumen animal organ regeneration membrane protein intracellular domain proteolysis positive regulation of protein complex assembly positive regulation of exit from mitosis lipopolysaccharide-mediated signaling pathway positive regulation of cellular protein metabolic process response to estradiol response to progesterone regulation of interleukin-23 production negative regulation of interleukin-17 production positive regulation of interleukin-17 production receptor catabolic process positive regulation of superoxide anion generation mononuclear cell proliferation positive regulation of collagen biosynthetic process positive regulation of peptidyl-serine phosphorylation response to vitamin D response to laminar fluid shear stress type I transforming growth factor beta receptor binding type III transforming growth factor beta receptor binding positive regulation of histone acetylation positive regulation of protein dephosphorylation response to immobilization stress wound healing T cell activation regulation of cell proliferation negative regulation of T cell proliferation regulation of protein import into nucleus positive regulation of protein import into nucleus positive regulation of odontogenesis response to drug myelination identical protein binding protein homodimerization activity regulation of apoptotic process myeloid dendritic cell differentiation neuronal cell body T cell homeostasis positive regulation of apoptotic process positive regulation of vascular permeability positive regulation of MAP kinase activity regulation of MAPK cascade protein kinase B signaling positive regulation of blood vessel endothelial cell migration negative regulation of blood vessel endothelial cell migration protein serine/threonine kinase activator activity positive regulation of phosphatidylinositol 3-kinase activity ossification involved in bone remodeling regulatory T cell differentiation cell-cell junction organization regulation of regulatory T cell differentiation positive regulation of regulatory T cell differentiation negative regulation of cell differentiation negative regulation of fat cell differentiation negative regulation of myoblast differentiation negative regulation of cell cycle negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated negative regulation of cytolysis negative regulation of mitotic cell cycle positive regulation of transcription from RNA polymerase II promoter muscle cell cellular homeostasis protein heterodimerization activity protein N-terminus binding positive regulation of fibroblast proliferation positive regulation of isotype switching to IgA isotypes cell development lymph node development digestive tract development negative regulation of skeletal muscle tissue development inner ear development positive regulation of epithelial cell proliferation negative regulation of epithelial cell proliferation positive regulation of protein secretion positive regulation of peptidyl-tyrosine phosphorylation negative regulation of phagocytosis negative regulation of immune response negative regulation of T cell activation leukocyte migration positive regulation of chemotaxis positive regulation of NF-kappaB transcription factor activity regulation of binding regulation of DNA binding positive regulation of smooth muscle cell differentiation negative regulation of release of sequestered calcium ion into cytosol positive regulation of cell division positive regulation of protein kinase B signaling ventricular cardiac muscle tissue morphogenesis regulation of blood vessel remodeling face morphogenesis frontal suture morphogenesis pathway-restricted SMAD protein phosphorylation regulation of SMAD protein import into nucleus positive regulation of SMAD protein import into nucleus SMAD protein signal transduction mammary gland branching involved in thelarche branch elongation involved in mammary gland duct branching regulation of branching involved in mammary gland duct morphogenesis negative regulation of gene silencing by miRNA regulation of cartilage development connective tissue development negative regulation of biomineral tissue development lens fiber cell differentiation positive regulation of ERK1 and ERK2 cascade response to cholesterol positive regulation of cell cycle arrest cellular response to mechanical stimulus cellular response to growth factor stimulus cellular response to organic cyclic compound cellular response to ionizing radiation cellular response to dexamethasone stimulus cellular response to transforming growth factor beta stimulus positive regulation of mononuclear cell migration blood microparticle extracellular matrix assembly positive regulation of branching involved in ureteric bud morphogenesis extrinsic apoptotic signaling pathway liver regeneration negative regulation of hyaluronan biosynthetic process positive regulation of protein localization to nucleus positive regulation of extracellular matrix assembly positive regulation of NAD+ ADP-ribosyltransferase activity response to salt positive regulation of pri-miRNA transcription from RNA polymerase II promoter negative regulation of protein localization to plasma membrane negative regulation of production of miRNAs involved in gene silencing by miRNA positive regulation of production of miRNAs involved in gene silencing by miRNA positive regulation of receptor clustering transforming growth factor beta receptor signaling pathway involved in heart development cellular response to insulin-like growth factor stimulus embryonic liver development regulation of actin cytoskeleton reorganization positive regulation of transcription regulatory region DNA binding positive regulation of cardiac muscle cell differentiation microvillus apoptotic process regulation of pri-miRNA transcription from RNA polymerase II promoter regulation of epithelial to mesenchymal transition involved in endocardial cushion formation uc002oqh.1 uc002oqh.2 uc002oqh.3 uc002oqh.4 uc002oqh.5 
ENST00000221943.14 DMAC2 ENST00000221943.14 distal membrane arm assembly component 2, transcript variant 15 (from RefSeq NR_135478.2) ATP5SL B4DDC0 B4DMZ4 B4DP55 B4DXE8 DMAC2 DMAC2_HUMAN ENST00000221943.1 ENST00000221943.10 ENST00000221943.11 ENST00000221943.12 ENST00000221943.13 ENST00000221943.2 ENST00000221943.3 ENST00000221943.4 ENST00000221943.5 ENST00000221943.6 ENST00000221943.7 ENST00000221943.8 ENST00000221943.9 F5H4W7 K7EMF6 NR_135478 Q96D43 Q9NW81 uc002oqw.1 uc002oqw.2 uc002oqw.3 uc002oqw.4 Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I. Interacts with incompletely assembled mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Q9NW81-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-22730614, EBI-3867333; Mitochondrion Event=Alternative splicing; Named isoforms=6; Name=1; IsoId=Q9NW81-1; Sequence=Displayed; Name=2; IsoId=Q9NW81-2; Sequence=VSP_031270, VSP_031271; Name=3; IsoId=Q9NW81-3; Sequence=VSP_043807, VSP_031271; Name=4; IsoId=Q9NW81-4; Sequence=VSP_043807; Name=5; IsoId=Q9NW81-5; Sequence=VSP_031270; Name=6; IsoId=Q9NW81-6; Sequence=VSP_031271; Belongs to the ATP synthase subunit s family. mitochondrion ubiquitin-dependent protein catabolic process protein ubiquitination SCF ubiquitin ligase complex SCF-dependent proteasomal ubiquitin-dependent protein catabolic process mitochondrial respiratory chain complex I assembly mitochondrial respiratory chain complex I ubiquitin-protein transferase activity uc002oqw.1 uc002oqw.2 uc002oqw.3 uc002oqw.4 
ENST00000221954.7 CEACAM4 ENST00000221954.7 CEA cell adhesion molecule 4, transcript variant 1 (from RefSeq NM_001817.4) CEAM4_HUMAN CGM7 ENST00000221954.1 ENST00000221954.2 ENST00000221954.3 ENST00000221954.4 ENST00000221954.5 ENST00000221954.6 NM_001817 O75871 Q03715 Q7LDZ7 uc002orh.1 uc002orh.2 Granulocyte orphan receptor that acts as an trigger efficient phagocytosis of attached particles. Interacts through its phosphorylated ITAM domain with the SH2 domain-containing cytoplasmic proteins involved in signaling processes during phagocytosis. Membrane; Single-pass type I membrane protein. Granulocytes. N-glycosylated. The cytoplasmic ITAM-like sequence becomes tyrosine phosphorylated by SRC family PTKs upon ligand-mediated receptor clustering and allows to initiate phagocytosis of bound ligand. To study the function of the orphan receptor CEACAM4 chimeric proteins containing the extracellular bacteria-binding domain of CEACAM3 and the transmembrane and cytoplasmic part of CEACAM4 has been used. Belongs to the immunoglobulin superfamily. CEA family. integral component of plasma membrane phagocytosis membrane integral component of membrane uc002orh.1 uc002orh.2 
ENST00000221957.9 PLIN3 ENST00000221957.9 perilipin 3, transcript variant 1 (from RefSeq NM_005817.5) A8K4Y9 ENST00000221957.1 ENST00000221957.2 ENST00000221957.3 ENST00000221957.4 ENST00000221957.5 ENST00000221957.6 ENST00000221957.7 ENST00000221957.8 K7EQF4 M6PRBP1 NM_005817 O60664 PLIN3_HUMAN Q53G77 Q9BS03 Q9UBD7 Q9UP92 TIP47 uc002mbj.1 uc002mbj.2 uc002mbj.3 uc002mbj.4 Mannose 6-phophate receptors (MPRs) deliver lysosomal hydrolase from the Golgi to endosomes and then return to the Golgi complex. The protein encoded by this gene interacts with the cytoplasmic domains of both cation-independent and cation-dependent MPRs, and is required for endosome-to-Golgi transport. This protein also binds directly to the GTPase RAB9 (RAB9A), a member of the RAS oncogene family. The interaction with RAB9 has been shown to increase the affinity of this protein for its cargo. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Aug 2009]. Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets (PubMed:34077757). Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network (PubMed:9590177). Homooligomer (PubMed:9590177). Interacts with M6PR (via the cytoplasmic domain) (PubMed:9590177). Interacts with IGF2R (via the cytoplasmic domain) (PubMed:9590177). [Isoform 2]: May exist as a homodimer. O60664; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-725795, EBI-7131019; O60664; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-725795, EBI-2813554; O60664; P55212: CASP6; NbExp=3; IntAct=EBI-725795, EBI-718729; O60664; P24863: CCNC; NbExp=3; IntAct=EBI-725795, EBI-395261; O60664; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-725795, EBI-749627; O60664; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-725795, EBI-2548702; O60664; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-725795, EBI-11522780; O60664; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-725795, EBI-2680384; O60664; Q05329: GAD2; NbExp=3; IntAct=EBI-725795, EBI-9304251; O60664; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-725795, EBI-18053395; O60664; P13473-2: LAMP2; NbExp=3; IntAct=EBI-725795, EBI-21591415; O60664; Q9C0E8-2: LNPK; NbExp=3; IntAct=EBI-725795, EBI-11024283; O60664; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-725795, EBI-740987; O60664; Q9HB07: MYG1; NbExp=3; IntAct=EBI-725795, EBI-709754; O60664; Q96AL5: PBX3; NbExp=3; IntAct=EBI-725795, EBI-741171; O60664; Q9Y6X2: PIAS3; NbExp=3; IntAct=EBI-725795, EBI-2803703; O60664; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-725795, EBI-5280197; O60664; P43378: PTPN9; NbExp=3; IntAct=EBI-725795, EBI-742898; O60664; O95562: SFT2D2; NbExp=3; IntAct=EBI-725795, EBI-4402330; O60664; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-725795, EBI-2623095; O60664; Q13596: SNX1; NbExp=4; IntAct=EBI-725795, EBI-2822329; O60664; O60749: SNX2; NbExp=3; IntAct=EBI-725795, EBI-1046690; O60664; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-725795, EBI-12187159; O60664; O43761: SYNGR3; NbExp=3; IntAct=EBI-725795, EBI-11321949; O60664; P08247: SYP; NbExp=3; IntAct=EBI-725795, EBI-9071725; O60664; Q9BW92: TARS2; NbExp=3; IntAct=EBI-725795, EBI-1045099; O60664; Q9NVG8: TBC1D13; NbExp=3; IntAct=EBI-725795, EBI-12264956; O60664; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-725795, EBI-2339195; O60664; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=5; IntAct=EBI-725795, EBI-6863748; Lipid droplet dosome membrane ; Peripheral membrane protein ; Cytoplasmic side Cytoplasm te=Membrane associated on endosomes (PubMed:15545278). Detected in the envelope and the core of lipid bodies and in lipid sails (PubMed:15545278). Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=PP17b ; IsoId=O60664-1; Sequence=Displayed; Name=2; Synonyms=PP17a ; IsoId=O60664-2; Sequence=VSP_004664; Name=3; IsoId=O60664-3; Sequence=VSP_040325; Name=4; IsoId=O60664-4; Sequence=VSP_047038; Phosphorylation at Tyr-251 by isoform 1 of CHKA (CHKalpha2) promotes dissociation from lipid droplets: dissociation is followed by recruitment of autophagosome machinery to lipid droplets and subsequent lipid droplet lipolysis. Belongs to the perilipin family. protein binding cytoplasm endosome Golgi apparatus lipid particle cytosol endosome membrane membrane vesicle-mediated transport transport vesicle cadherin binding uc002mbj.1 uc002mbj.2 uc002mbj.3 uc002mbj.4 
ENST00000221972.8 CD79A ENST00000221972.8 CD79a molecule, transcript variant 1 (from RefSeq NM_001783.4) A0N775 CD79A_HUMAN ENST00000221972.1 ENST00000221972.2 ENST00000221972.3 ENST00000221972.4 ENST00000221972.5 ENST00000221972.6 ENST00000221972.7 IGA MB1 NM_001783 P11912 Q53FB8 uc002orv.1 uc002orv.2 uc002orv.3 uc002orv.4 The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-alpha protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]. Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B- cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B- cells. Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains (PubMed:35981043). Interacts through its phosphorylated ITAM domain with the SH2 domains of SYK which stimulates SYK autophosphorylation and activation. Also interacts, when phosphorylated on Tyr-210, with the SH2 domain of BLNK/SLP65, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK which is necessary for trafficking of the BCR to late endosomes. Interacts with Src-family tyrosine kinases including FYN and LYN, increasing their activity (By similarity). P11912; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-7797864, EBI-10827839; P11912; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-7797864, EBI-11522760; P11912; Q5BKT4: ALG10; NbExp=3; IntAct=EBI-7797864, EBI-13064220; P11912; Q5I7T1: ALG10B; NbExp=3; IntAct=EBI-7797864, EBI-18075734; P11912; Q92685: ALG3; NbExp=3; IntAct=EBI-7797864, EBI-2848814; P11912; P05090: APOD; NbExp=3; IntAct=EBI-7797864, EBI-715495; P11912; P29972: AQP1; NbExp=3; IntAct=EBI-7797864, EBI-745213; P11912; Q92482: AQP3; NbExp=3; IntAct=EBI-7797864, EBI-2808854; P11912; P27449: ATP6V0C; NbExp=3; IntAct=EBI-7797864, EBI-721179; P11912; Q92843: BCL2L2; NbExp=3; IntAct=EBI-7797864, EBI-707714; P11912; O15155: BET1; NbExp=3; IntAct=EBI-7797864, EBI-749204; P11912; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-7797864, EBI-12244618; P11912; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-7797864, EBI-8648738; P11912; O14523: C2CD2L; NbExp=3; IntAct=EBI-7797864, EBI-12822627; P11912; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-7797864, EBI-12003442; P11912; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-7797864, EBI-9083477; P11912; O14735: CDIPT; NbExp=3; IntAct=EBI-7797864, EBI-358858; P11912; O95832: CLDN1; NbExp=3; IntAct=EBI-7797864, EBI-723889; P11912; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-7797864, EBI-6165897; P11912; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-7797864, EBI-11522780; P11912; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-7797864, EBI-2807956; P11912; O95406: CNIH1; NbExp=3; IntAct=EBI-7797864, EBI-12172273; P11912; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-7797864, EBI-12208021; P11912; P29400-2: COL4A5; NbExp=3; IntAct=EBI-7797864, EBI-12211159; P11912; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-7797864, EBI-12019274; P11912; P49447: CYB561; NbExp=3; IntAct=EBI-7797864, EBI-8646596; P11912; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-7797864, EBI-10269179; P11912; O14569: CYB561D2; NbExp=3; IntAct=EBI-7797864, EBI-717654; P11912; O43169: CYB5B; NbExp=3; IntAct=EBI-7797864, EBI-1058710; P11912; Q9H1M4: DEFB127; NbExp=3; IntAct=EBI-7797864, EBI-10305240; P11912; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-7797864, EBI-8645574; P11912; P56851: EDDM3B; NbExp=3; IntAct=EBI-7797864, EBI-10215665; P11912; Q9BV81: EMC6; NbExp=3; IntAct=EBI-7797864, EBI-2820492; P11912; P54849: EMP1; NbExp=3; IntAct=EBI-7797864, EBI-4319440; P11912; P54852: EMP3; NbExp=3; IntAct=EBI-7797864, EBI-3907816; P11912; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-7797864, EBI-11337888; P11912; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-7797864, EBI-12118888; P11912; Q969F0: FATE1; NbExp=6; IntAct=EBI-7797864, EBI-743099; P11912; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-7797864, EBI-12142299; P11912; P37268: FDFT1; NbExp=3; IntAct=EBI-7797864, EBI-714550; P11912; O14843: FFAR3; NbExp=3; IntAct=EBI-7797864, EBI-17762181; P11912; Q14318: FKBP8; NbExp=3; IntAct=EBI-7797864, EBI-724839; P11912; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-7797864, EBI-714482; P11912; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-7797864, EBI-12175685; P11912; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-7797864, EBI-3925203; P11912; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-7797864, EBI-11991950; P11912; P08034: GJB1; NbExp=3; IntAct=EBI-7797864, EBI-17565645; P11912; O15529: GPR42; NbExp=3; IntAct=EBI-7797864, EBI-18076404; P11912; Q5VWC8: HACD4; NbExp=3; IntAct=EBI-7797864, EBI-18076069; P11912; P09601: HMOX1; NbExp=3; IntAct=EBI-7797864, EBI-2806151; P11912; P30519: HMOX2; NbExp=3; IntAct=EBI-7797864, EBI-712096; P11912; P46695: IER3; NbExp=3; IntAct=EBI-7797864, EBI-1748945; P11912; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-7797864, EBI-8503746; P11912; P11215: ITGAM; NbExp=3; IntAct=EBI-7797864, EBI-2568251; P11912; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-7797864, EBI-10266796; P11912; P07942: LAMB1; NbExp=3; IntAct=EBI-7797864, EBI-949174; P11912; O95214: LEPROTL1; NbExp=3; IntAct=EBI-7797864, EBI-750776; P11912; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-7797864, EBI-2820517; P11912; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-7797864, EBI-12033434; P11912; Q16873: LTC4S; NbExp=3; IntAct=EBI-7797864, EBI-12241118; P11912; Q13021: MALL; NbExp=3; IntAct=EBI-7797864, EBI-750078; P11912; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-7797864, EBI-10317612; P11912; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-7797864, EBI-11956541; P11912; Q6NUT3-2: MFSD12; NbExp=3; IntAct=EBI-7797864, EBI-17295698; P11912; Q6N075: MFSD5; NbExp=3; IntAct=EBI-7797864, EBI-3920969; P11912; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-7797864, EBI-2858252; P11912; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-7797864, EBI-12866138; P11912; Q8IY49-2: MMD2; NbExp=3; IntAct=EBI-7797864, EBI-13349813; P11912; O75425: MOSPD3; NbExp=3; IntAct=EBI-7797864, EBI-12179105; P11912; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-7797864, EBI-12070086; P11912; Q96S97: MYADM; NbExp=3; IntAct=EBI-7797864, EBI-13301517; P11912; A6NDP7: MYADML2; NbExp=3; IntAct=EBI-7797864, EBI-17641390; P11912; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-7797864, EBI-2863634; P11912; Q99519: NEU1; NbExp=3; IntAct=EBI-7797864, EBI-721517; P11912; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-7797864, EBI-10317425; P11912; Q6P499: NIPAL3; NbExp=3; IntAct=EBI-7797864, EBI-10252783; P11912; Q16617: NKG7; NbExp=3; IntAct=EBI-7797864, EBI-3919611; P11912; Q8N912: NRAC; NbExp=3; IntAct=EBI-7797864, EBI-12051377; P11912; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-7797864, EBI-11075081; P11912; Q7RTS6: OTOP2; NbExp=3; IntAct=EBI-7797864, EBI-7642372; P11912; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-7797864, EBI-12092917; P11912; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-7797864, EBI-12257782; P11912; Q04941: PLP2; NbExp=3; IntAct=EBI-7797864, EBI-608347; P11912; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-7797864, EBI-11721828; P11912; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-7797864, EBI-12955265; P11912; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-7797864, EBI-8652812; P11912; Q59EV6: PPGB; NbExp=3; IntAct=EBI-7797864, EBI-14210385; P11912; O60831: PRAF2; NbExp=3; IntAct=EBI-7797864, EBI-2506064; P11912; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-7797864, EBI-14199621; P11912; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-7797864, EBI-14065960; P11912; P08100: RHO; NbExp=3; IntAct=EBI-7797864, EBI-1394177; P11912; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-7797864, EBI-10244780; P11912; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-7797864, EBI-3917235; P11912; O75396: SEC22B; NbExp=3; IntAct=EBI-7797864, EBI-1058865; P11912; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-7797864, EBI-10329948; P11912; P11686: SFTPC; NbExp=3; IntAct=EBI-7797864, EBI-10197617; P11912; Q9UKG4: SLC13A4; NbExp=6; IntAct=EBI-7797864, EBI-12808018; P11912; Q86YT5: SLC13A5; NbExp=3; IntAct=EBI-7797864, EBI-12002412; P11912; Q6ZSM3: SLC16A12; NbExp=3; IntAct=EBI-7797864, EBI-17460560; P11912; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-7797864, EBI-12243266; P11912; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-7797864, EBI-8644112; P11912; P78383: SLC35B1; NbExp=3; IntAct=EBI-7797864, EBI-12147661; P11912; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-7797864, EBI-10281213; P11912; Q9H2H9: SLC38A1; NbExp=6; IntAct=EBI-7797864, EBI-9978441; P11912; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-7797864, EBI-12898013; P11912; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-7797864, EBI-2823239; P11912; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-7797864, EBI-12266234; P11912; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-7797864, EBI-10290130; P11912; Q7Z3Q1-2: SLC46A3; NbExp=3; IntAct=EBI-7797864, EBI-18074862; P11912; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-7797864, EBI-3907610; P11912; P48065: SLC6A12; NbExp=3; IntAct=EBI-7797864, EBI-3843589; P11912; P30825: SLC7A1; NbExp=3; IntAct=EBI-7797864, EBI-4289564; P11912; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-7797864, EBI-8640191; P11912; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-7797864, EBI-741850; P11912; P0DN84: STRIT1; NbExp=3; IntAct=EBI-7797864, EBI-12200293; P11912; Q86Y82: STX12; NbExp=3; IntAct=EBI-7797864, EBI-2691717; P11912; Q13277: STX3; NbExp=3; IntAct=EBI-7797864, EBI-1394295; P11912; Q9UNK0: STX8; NbExp=3; IntAct=EBI-7797864, EBI-727240; P11912; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-7797864, EBI-1049004; P11912; Q9NZ01: TECR; NbExp=3; IntAct=EBI-7797864, EBI-2877718; P11912; P07204: THBD; NbExp=3; IntAct=EBI-7797864, EBI-941422; P11912; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-7797864, EBI-6448756; P11912; P48230: TM4SF4; NbExp=3; IntAct=EBI-7797864, EBI-8650934; P11912; P55061: TMBIM6; NbExp=3; IntAct=EBI-7797864, EBI-1045825; P11912; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-7797864, EBI-12845616; P11912; P17152: TMEM11; NbExp=3; IntAct=EBI-7797864, EBI-723946; P11912; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-7797864, EBI-10694905; P11912; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-7797864, EBI-2844246; P11912; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-7797864, EBI-348587; P11912; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-7797864, EBI-8638294; P11912; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-7797864, EBI-2800645; P11912; Q14656: TMEM187; NbExp=3; IntAct=EBI-7797864, EBI-13046724; P11912; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-7797864, EBI-741829; P11912; A2RU14: TMEM218; NbExp=3; IntAct=EBI-7797864, EBI-10173151; P11912; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-7797864, EBI-347385; P11912; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-7797864, EBI-12195227; P11912; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-7797864, EBI-11528917; P11912; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-7797864, EBI-12887458; P11912; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-7797864, EBI-11956809; P11912; E9PQX1: TMEM262; NbExp=3; IntAct=EBI-7797864, EBI-17180389; P11912; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-7797864, EBI-12038591; P11912; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-7797864, EBI-12015604; P11912; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-7797864, EBI-2548832; P11912; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-7797864, EBI-11724433; P11912; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-7797864, EBI-717441; P11912; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-7797864, EBI-11996766; P11912; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-7797864, EBI-12003468; P11912; O60636: TSPAN2; NbExp=3; IntAct=EBI-7797864, EBI-3914288; P11912; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-7797864, EBI-12195249; P11912; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-7797864, EBI-11988865; P11912; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-7797864, EBI-988826; P11912; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-7797864, EBI-2819725; P11912; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-7797864, EBI-4401271; P11912; Q15836: VAMP3; NbExp=3; IntAct=EBI-7797864, EBI-722343; P11912; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-7797864, EBI-1059156; P11912; O95292: VAPB; NbExp=3; IntAct=EBI-7797864, EBI-1188298; P11912; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-7797864, EBI-723716; P11912; Q14508: WFDC2; NbExp=3; IntAct=EBI-7797864, EBI-723529; P11912; O76024: WFS1; NbExp=3; IntAct=EBI-7797864, EBI-720609; P11912; O95070: YIF1A; NbExp=3; IntAct=EBI-7797864, EBI-2799703; P11912; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-7797864, EBI-751253; P11912; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-7797864, EBI-751210; P11912; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-7797864, EBI-12837904; P11912; Q8N966: ZDHHC22; NbExp=3; IntAct=EBI-7797864, EBI-10268111; Cell membrane; Single-pass type I membrane protein. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Long; IsoId=P11912-1; Sequence=Displayed; Name=2; Synonyms=Short; IsoId=P11912-2; Sequence=VSP_002476; B-cells. The transmembrane helices of CD79A and CD79B chains and two IgM heavy chains assembly in a four-helix bundle structure that appears to be conserved among different BCR isotypes. Phosphorylated on tyrosine, serine and threonine residues upon B- cell activation. Phosphorylation of tyrosine residues by Src-family kinases is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases, leading to their activation which in turn leads to phosphorylation of downstream targets. Phosphorylated by LYN. Phosphorylation of serine and threonine residues may prevent subsequent tyrosine phosphorylation. Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation (By similarity). Agammaglobulinemia 3, autosomal recessive (AGM3) [MIM:613501]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. te=The disease is caused by variants affecting the gene represented in this entry. Two different mutations, one at the splice donor site of intron 2 and the other at the splice acceptor site for exon 3, have been identified. Both mutations give rise to a truncated protein. Name=CD79Abase; Note=CD79A mutation db; URL="http://structure.bmc.lu.se/idbase/CD79Abase/"; adaptive immune response immune system process transmembrane signaling receptor activity protein binding multivesicular body plasma membrane cell surface receptor signaling pathway external side of plasma membrane membrane integral component of membrane B cell receptor complex B cell differentiation B cell proliferation B cell activation protein homodimerization activity membrane raft B cell receptor signaling pathway protein homotetramerization uc002orv.1 uc002orv.2 uc002orv.3 uc002orv.4 
ENST00000221978.10 NKG7 ENST00000221978.10 natural killer cell granule protein 7, transcript variant 1 (from RefSeq NM_005601.4) ENST00000221978.1 ENST00000221978.2 ENST00000221978.3 ENST00000221978.4 ENST00000221978.5 ENST00000221978.6 ENST00000221978.7 ENST00000221978.8 ENST00000221978.9 GIG1 NKG7_HUMAN NM_005601 Q16617 uc002pwj.1 uc002pwj.2 uc002pwj.3 uc002pwj.4 uc002pwj.5 Regulates cytotoxic granule exocytosis in effector lymphocytes, thus acting as a critical mediator of inflammation in a broad range of infectious and non-infectious diseases (By similarity). Essential for cytotoxic degranulation of natural killer (NK) cells and CD8(+) T-cells and for the activation of CD4(+) T-cells following infection (By similarity). Plays a critical role in CD8(+) T-cell and NK cell-mediated cytolysis of target cells and contributes to the cytolytic activity via the perforin/granzyme pathway by enhancing exocytosis of LAMP1-carrying lytic granules (By similarity). Contributes to NK cell-mediated control of cancer metastasis (By similarity). Q16617; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-3919611, EBI-741181; Q16617; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-3919611, EBI-11522760; Q16617; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-3919611, EBI-19125216; Q16617; Q13520: AQP6; NbExp=3; IntAct=EBI-3919611, EBI-13059134; Q16617; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-3919611, EBI-11343438; Q16617; O75787: ATP6AP2; NbExp=3; IntAct=EBI-3919611, EBI-2512037; Q16617; Q13145: BAMBI; NbExp=3; IntAct=EBI-3919611, EBI-742991; Q16617; P19397: CD53; NbExp=3; IntAct=EBI-3919611, EBI-6657396; Q16617; P11912: CD79A; NbExp=3; IntAct=EBI-3919611, EBI-7797864; Q16617; O95471: CLDN7; NbExp=3; IntAct=EBI-3919611, EBI-740744; Q16617; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-3919611, EBI-11749983; Q16617; Q9ULY5: CLEC4E; NbExp=4; IntAct=EBI-3919611, EBI-12807010; Q16617; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-3919611, EBI-11291074; Q16617; Q15125: EBP; NbExp=3; IntAct=EBI-3919611, EBI-3915253; Q16617; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-3919611, EBI-526033; Q16617; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3919611, EBI-781551; Q16617; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-3919611, EBI-18938272; Q16617; O15552: FFAR2; NbExp=3; IntAct=EBI-3919611, EBI-2833872; Q16617; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-3919611, EBI-12142257; Q16617; P36382: GJA5; NbExp=3; IntAct=EBI-3919611, EBI-750433; Q16617; Q8TED1: GPX8; NbExp=3; IntAct=EBI-3919611, EBI-11721746; Q16617; Q6UXK2: ISLR2; NbExp=3; IntAct=EBI-3919611, EBI-1266923; Q16617; P26715: KLRC1; NbExp=3; IntAct=EBI-3919611, EBI-9018187; Q16617; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-3919611, EBI-2820517; Q16617; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-3919611, EBI-2858252; Q16617; O14880: MGST3; NbExp=3; IntAct=EBI-3919611, EBI-724754; Q16617; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-3919611, EBI-12806656; Q16617; P21757: MSR1; NbExp=7; IntAct=EBI-3919611, EBI-1776976; Q16617; P15941-11: MUC1; NbExp=3; IntAct=EBI-3919611, EBI-17263240; Q16617; P41145: OPRK1; NbExp=3; IntAct=EBI-3919611, EBI-925028; Q16617; O00623: PEX12; NbExp=3; IntAct=EBI-3919611, EBI-594836; Q16617; O60894: RAMP1; NbExp=3; IntAct=EBI-3919611, EBI-962893; Q16617; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-3919611, EBI-13044680; Q16617; Q05940: SLC18A2; NbExp=3; IntAct=EBI-3919611, EBI-18036244; Q16617; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-3919611, EBI-10262251; Q16617; P27105: STOM; NbExp=5; IntAct=EBI-3919611, EBI-1211440; Q16617; Q16623: STX1A; NbExp=4; IntAct=EBI-3919611, EBI-712466; Q16617; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-3919611, EBI-12947623; Q16617; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-3919611, EBI-2821497; Q16617; Q8N3G9: TMEM130; NbExp=3; IntAct=EBI-3919611, EBI-19763514; Q16617; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-3919611, EBI-7238458; Q16617; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-3919611, EBI-11742770; Q16617; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-3919611, EBI-17198826; Cell membrane ; Multi-pass membrane protein Cytolytic granule membrane ; Multi-pass membrane protein Expressed in activated T-cells, in kidney, liver, lung and pancreas. Not expressed in brain, heart, or skeletal muscle. Expressed at high levels in TCR gamma delta-expressing CTL clones, and in some TCR alpha beta-expressing CTL clones (both CD4+ and CD8+), but is not expressed in other TCR alpha beta-expressing CTL clones and in cell lines representing B-cells, monocytes, and myeloid cells. By CSF3/G-CSF (PubMed:7510105). Up-regulated in CD4(+) T- cells from peripheral blood mononuclear cells of patients with visceral leishmaniasis (PubMed:32839608). Belongs to the PMP-22/EMP/MP20 family. protein binding plasma membrane integral component of plasma membrane membrane integral component of membrane uc002pwj.1 uc002pwj.2 uc002pwj.3 uc002pwj.4 uc002pwj.5 
ENST00000221980.5 ICAM5 ENST00000221980.5 intercellular adhesion molecule 5 (from RefSeq NM_003259.4) ENST00000221980.1 ENST00000221980.2 ENST00000221980.3 ENST00000221980.4 ICAM5_HUMAN NM_003259 Q9UMF0 Q9Y6F3 TLCN TLN uc002mnu.1 uc002mnu.2 uc002mnu.3 uc002mnu.4 uc002mnu.5 uc002mnu.6 The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2-9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein. This protein is expressed on the surface of telencephalic neurons and displays two types of adhesion activity, homophilic binding between neurons and heterophilic binding between neurons and leukocytes. It may be a critical component in neuron-microglial cell interactions in the course of normal development or as part of neurodegenerative diseases. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC026338.1, U72671.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2154665, SAMN02400288 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221980.5/ ENSP00000221980.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). Q9UMF0; Q99996-3: AKAP9; NbExp=3; IntAct=EBI-6398041, EBI-11022349; Q9UMF0; P13196: ALAS1; NbExp=3; IntAct=EBI-6398041, EBI-3905054; Q9UMF0; Q9NP70: AMBN; NbExp=3; IntAct=EBI-6398041, EBI-11893530; Q9UMF0; P05067: APP; NbExp=3; IntAct=EBI-6398041, EBI-77613; Q9UMF0; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-6398041, EBI-25843552; Q9UMF0; Q9HCU0: CD248; NbExp=3; IntAct=EBI-6398041, EBI-9680942; Q9UMF0; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-6398041, EBI-25836090; Q9UMF0; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-6398041, EBI-2872414; Q9UMF0; Q9H410: DSN1; NbExp=3; IntAct=EBI-6398041, EBI-1001144; Q9UMF0; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-6398041, EBI-3893327; Q9UMF0; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-6398041, EBI-25835236; Q9UMF0; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-6398041, EBI-2857315; Q9UMF0; P51674: GPM6A; NbExp=3; IntAct=EBI-6398041, EBI-7187133; Q9UMF0; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-6398041, EBI-2868501; Q9UMF0; Q13887: KLF5; NbExp=3; IntAct=EBI-6398041, EBI-2696013; Q9UMF0; Q96NJ5: KLHL32; NbExp=3; IntAct=EBI-6398041, EBI-6426390; Q9UMF0; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-6398041, EBI-8473062; Q9UMF0; Q9BV99: LRRC61; NbExp=3; IntAct=EBI-6398041, EBI-2350424; Q9UMF0; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-6398041, EBI-741037; Q9UMF0; P02795: MT2A; NbExp=3; IntAct=EBI-6398041, EBI-996616; Q9UMF0; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-6398041, EBI-6952711; Q9UMF0; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-6398041, EBI-1058491; Q9UMF0; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-6398041, EBI-11984839; Q9UMF0; Q96EN9: REX1BD; NbExp=3; IntAct=EBI-6398041, EBI-745810; Q9UMF0; Q96EP0: RNF31; NbExp=3; IntAct=EBI-6398041, EBI-948111; Q9UMF0; O75528: TADA3; NbExp=3; IntAct=EBI-6398041, EBI-473249; Q9UMF0; P45880: VDAC2; NbExp=3; IntAct=EBI-6398041, EBI-354022; Q9UMF0; P05094: ACTN1; Xeno; NbExp=3; IntAct=EBI-6398041, EBI-5847257; Membrane; Single-pass type I membrane protein. Expressed on neurons in the most rostral segment of the mammalian brain, the telencephalon. Glycosylation at Asn-54 is critical for functional folding. Belongs to the immunoglobulin superfamily. ICAM family. integrin binding protein binding plasma membrane integral component of plasma membrane phagocytosis cell adhesion membrane integral component of membrane extracellular matrix organization regulation of immune response cell-cell adhesion uc002mnu.1 uc002mnu.2 uc002mnu.3 uc002mnu.4 uc002mnu.5 uc002mnu.6 
ENST00000221992.11 CEACAM5 ENST00000221992.11 CEA cell adhesion molecule 5, transcript variant 1 (from RefSeq NM_004363.6) CEA CEAM5_HUMAN ENST00000221992.1 ENST00000221992.10 ENST00000221992.2 ENST00000221992.3 ENST00000221992.4 ENST00000221992.5 ENST00000221992.6 ENST00000221992.7 ENST00000221992.8 ENST00000221992.9 H9KVA7 NM_004363 P06731 uc002orl.1 uc002orl.2 uc002orl.3 uc002orl.4 uc002orl.5 This gene encodes a cell surface glycoprotein that represents the founding member of the carcinoembryonic antigen (CEA) family of proteins. The encoded protein is used as a clinical biomarker for gastrointestinal cancers and may promote tumor development through its role as a cell adhesion molecule. Additionally, the encoded protein may regulate differentiation, apoptosis, and cell polarity. This gene is present in a CEA family gene cluster on chromosome 19. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2015]. Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression (PubMed:2803308, PubMed:10910050, PubMed:10864933). Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:2803308). Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells (PubMed:10910050). (Microbial infection) Receptor for E.coli Dr adhesins. Binding of E.coli Dr adhesins leads to dissociation of the homodimer. Homodimer. P06731; P06731: CEACAM5; NbExp=7; IntAct=EBI-3914938, EBI-3914938; P06731; K0BRG7: S; Xeno; NbExp=4; IntAct=EBI-3914938, EBI-16040613; Cell membrane ipid-anchor, GPI-anchor ical cell membrane Cell surface Note=Localized to the apical glycocalyx surface. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P06731-1; Sequence=Displayed; Name=2; IsoId=P06731-2; Sequence=VSP_053414; Expressed in columnar epithelial and goblet cells of the colon (at protein level) (PubMed:10436421). Found in adenocarcinomas of endodermally derived digestive system epithelium and fetal colon. Complex immunoreactive glycoprotein with a MW of 180 kDa comprising 60% carbohydrate. Belongs to the immunoglobulin superfamily. CEA family. Sequence=AAA62835.1; Type=Frameshift; Evidence=; extracellular region plasma membrane integral component of plasma membrane apoptotic process cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules cell surface negative regulation of myotube differentiation membrane basolateral plasma membrane apical plasma membrane anchored component of membrane homotypic cell-cell adhesion GPI anchor binding identical protein binding protein homodimerization activity negative regulation of apoptotic process leukocyte migration extracellular exosome integral component of external side of plasma membrane negative regulation of anoikis uc002orl.1 uc002orl.2 uc002orl.3 uc002orl.4 uc002orl.5 
ENST00000221996.12 CRX ENST00000221996.12 cone-rod homeobox (from RefSeq NM_000554.6) CORD2 CRX_HUMAN ENST00000221996.1 ENST00000221996.10 ENST00000221996.11 ENST00000221996.2 ENST00000221996.3 ENST00000221996.4 ENST00000221996.5 ENST00000221996.6 ENST00000221996.7 ENST00000221996.8 ENST00000221996.9 NM_000554 O43186 Q0QD45 uc002phq.1 uc002phq.2 uc002phq.3 uc002phq.4 uc002phq.5 uc002phq.6 The protein encoded by this gene is a photoreceptor-specific transcription factor which plays a role in the differentiation of photoreceptor cells. This homeodomain protein is necessary for the maintenance of normal cone and rod function. Mutations in this gene are associated with photoreceptor degeneration, Leber congenital amaurosis type III and the autosomal dominant cone-rod dystrophy 2. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some variants has not been determined. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BQ423938.1, BU187765.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000221996.12/ ENSP00000221996.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors. Interacts (via the homeobox) with NRL (via the leucine-zipper domain). Interacts with PDC, RAX2, RORB and SCA7. O43186; Q9NRN7: AASDHPPT; NbExp=3; IntAct=EBI-748171, EBI-740884; O43186; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-748171, EBI-743598; O43186; K7EM05: ACBD4; NbExp=3; IntAct=EBI-748171, EBI-16431307; O43186; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-748171, EBI-8643161; O43186; O95376: ARIH2; NbExp=3; IntAct=EBI-748171, EBI-711158; O43186; O94817: ATG12; NbExp=3; IntAct=EBI-748171, EBI-746742; O43186; Q8N8Y2: ATP6V0D2; NbExp=3; IntAct=EBI-748171, EBI-3923949; O43186; P54253: ATXN1; NbExp=3; IntAct=EBI-748171, EBI-930964; O43186; Q9H503-2: BANF2; NbExp=3; IntAct=EBI-748171, EBI-11977289; O43186; A0A0S2Z5G4: BANP; NbExp=3; IntAct=EBI-748171, EBI-16429704; O43186; B4DE54: BANP; NbExp=3; IntAct=EBI-748171, EBI-16429313; O43186; Q8N9N5-2: BANP; NbExp=6; IntAct=EBI-748171, EBI-11524452; O43186; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-748171, EBI-16429296; O43186; Q8IYS8: BOD1L2; NbExp=3; IntAct=EBI-748171, EBI-12118438; O43186; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-748171, EBI-741214; O43186; Q9BV19: C1orf50; NbExp=3; IntAct=EBI-748171, EBI-2874661; O43186; Q96LT7: C9orf72; NbExp=3; IntAct=EBI-748171, EBI-2961725; O43186; P35219: CA8; NbExp=7; IntAct=EBI-748171, EBI-718700; O43186; P24863: CCNC; NbExp=4; IntAct=EBI-748171, EBI-395261; O43186; P42773: CDKN2C; NbExp=3; IntAct=EBI-748171, EBI-711290; O43186; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-748171, EBI-749051; O43186; O43247-2: CIMIP4; NbExp=3; IntAct=EBI-748171, EBI-12093053; O43186; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-748171, EBI-11962928; O43186; Q14154: DELE1; NbExp=3; IntAct=EBI-748171, EBI-2805660; O43186; P63241: EIF5A; NbExp=3; IntAct=EBI-748171, EBI-373150; O43186; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-748171, EBI-12013806; O43186; O75593: FOXH1; NbExp=3; IntAct=EBI-748171, EBI-1759806; O43186; O75603: GCM2; NbExp=11; IntAct=EBI-748171, EBI-10188645; O43186; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-748171, EBI-7251368; O43186; Q96NT3: GUCD1; NbExp=3; IntAct=EBI-748171, EBI-8293751; O43186; P13807: GYS1; NbExp=3; IntAct=EBI-748171, EBI-740553; O43186; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-748171, EBI-14103818; O43186; O14964: HGS; NbExp=6; IntAct=EBI-748171, EBI-740220; O43186; P35680: HNF1B; NbExp=3; IntAct=EBI-748171, EBI-2798841; O43186; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-748171, EBI-11955401; O43186; P78412: IRX6; NbExp=3; IntAct=EBI-748171, EBI-12100506; O43186; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-748171, EBI-2556193; O43186; Q5THT1: KLHL32; NbExp=3; IntAct=EBI-748171, EBI-10247181; O43186; Q71RC2-6: LARP4; NbExp=3; IntAct=EBI-748171, EBI-10255841; O43186; P17931: LGALS3; NbExp=3; IntAct=EBI-748171, EBI-1170392; O43186; P0CW20: LIMS4; NbExp=3; IntAct=EBI-748171, EBI-10196832; O43186; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-748171, EBI-739832; O43186; Q17RB8: LONRF1; NbExp=5; IntAct=EBI-748171, EBI-2341787; O43186; Q8TC57: M1AP; NbExp=4; IntAct=EBI-748171, EBI-748182; O43186; Q9BUN1: MENT; NbExp=3; IntAct=EBI-748171, EBI-12022316; O43186; Q6P2C6: MLLT6; NbExp=3; IntAct=EBI-748171, EBI-5773143; O43186; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-748171, EBI-744402; O43186; Q969S2: NEIL2; NbExp=3; IntAct=EBI-748171, EBI-10281234; O43186; Q13952-2: NFYC; NbExp=3; IntAct=EBI-748171, EBI-11956831; O43186; Q9Y221: NIP7; NbExp=3; IntAct=EBI-748171, EBI-749003; O43186; P34130: NTF4; NbExp=3; IntAct=EBI-748171, EBI-3907456; O43186; O95007: OR6B1; NbExp=3; IntAct=EBI-748171, EBI-12176191; O43186; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-748171, EBI-9057006; O43186; Q7Z2X4: PID1; NbExp=3; IntAct=EBI-748171, EBI-10256685; O43186; P0CW24: PNMA6A; NbExp=3; IntAct=EBI-748171, EBI-721270; O43186; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-748171, EBI-1389308; O43186; Q96T49: PPP1R16B; NbExp=4; IntAct=EBI-748171, EBI-10293968; O43186; O43741: PRKAB2; NbExp=9; IntAct=EBI-748171, EBI-1053424; O43186; P0CG20: PRR35; NbExp=3; IntAct=EBI-748171, EBI-11986293; O43186; P25786: PSMA1; NbExp=3; IntAct=EBI-748171, EBI-359352; O43186; P40306: PSMB10; NbExp=3; IntAct=EBI-748171, EBI-603329; O43186; Q2TAL8: QRICH1; NbExp=6; IntAct=EBI-748171, EBI-2798044; O43186; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-748171, EBI-372094; O43186; A1L4F5: ROR2; NbExp=3; IntAct=EBI-748171, EBI-10172778; O43186; Q01974: ROR2; NbExp=4; IntAct=EBI-748171, EBI-6422642; O43186; Q9UBE0: SAE1; NbExp=3; IntAct=EBI-748171, EBI-743154; O43186; O00560: SDCBP; NbExp=3; IntAct=EBI-748171, EBI-727004; O43186; Q9UDX3: SEC14L4; NbExp=3; IntAct=EBI-748171, EBI-10320311; O43186; P84022: SMAD3; NbExp=3; IntAct=EBI-748171, EBI-347161; O43186; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-748171, EBI-12061577; O43186; Q8WU79: SMAP2; NbExp=3; IntAct=EBI-748171, EBI-2822515; O43186; Q53HV7: SMUG1; NbExp=3; IntAct=EBI-748171, EBI-749970; O43186; P56693: SOX10; NbExp=3; IntAct=EBI-748171, EBI-1167533; O43186; O95416: SOX14; NbExp=3; IntAct=EBI-748171, EBI-9087806; O43186; P41225: SOX3; NbExp=3; IntAct=EBI-748171, EBI-9078386; O43186; P35711: SOX5; NbExp=4; IntAct=EBI-748171, EBI-3505701; O43186; P35711-4: SOX5; NbExp=3; IntAct=EBI-748171, EBI-11954419; O43186; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-748171, EBI-742688; O43186; O75716: STK16; NbExp=3; IntAct=EBI-748171, EBI-749295; O43186; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-748171, EBI-740595; O43186; P51687: SUOX; NbExp=3; IntAct=EBI-748171, EBI-3921347; O43186; Q5T011-5: SZT2; NbExp=3; IntAct=EBI-748171, EBI-10245139; O43186; O95947: TBX6; NbExp=3; IntAct=EBI-748171, EBI-2824328; O43186; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-748171, EBI-11746252; O43186; Q92734: TFG; NbExp=3; IntAct=EBI-748171, EBI-357061; O43186; Q08117: TLE5; NbExp=3; IntAct=EBI-748171, EBI-717810; O43186; Q08117-2: TLE5; NbExp=3; IntAct=EBI-748171, EBI-11741437; O43186; O43711: TLX3; NbExp=3; IntAct=EBI-748171, EBI-3939165; O43186; Q63HR2: TNS2; NbExp=3; IntAct=EBI-748171, EBI-949753; O43186; Q14CS0: UBXN2B; NbExp=3; IntAct=EBI-748171, EBI-1993619; O43186; O94888: UBXN7; NbExp=3; IntAct=EBI-748171, EBI-1993627; O43186; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-748171, EBI-2559305; O43186; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-748171, EBI-742550; O43186; Q15915: ZIC1; NbExp=3; IntAct=EBI-748171, EBI-11963196; O43186; Q6P088: ZNF483; NbExp=3; IntAct=EBI-748171, EBI-10196963; O43186; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-748171, EBI-16429989; O43186; P03410: tax; Xeno; NbExp=3; IntAct=EBI-748171, EBI-9676218; Nucleus Retina. Leber congenital amaurosis 7 (LCA7) [MIM:613829]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. te=The disease is caused by variants affecting the gene represented in this entry. Cone-rod dystrophy 2 (CORD2) [MIM:120970]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa, due to cone photoreceptors degenerating at a higher rate than rod photoreceptors. te=The disease is caused by variants affecting the gene represented in this entry. Retinitis pigmentosa (RP) [MIM:268000]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Retinitis pigmentosa can be inherited as an autosomal dominant, autosomal recessive or X-linked condition. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the paired homeobox family. Name=Mutations of the CRX gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/crxmut.htm"; nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated multicellular organism development nervous system development visual perception circadian rhythm animal organ morphogenesis cell differentiation nuclear hormone receptor binding leucine zipper domain binding sequence-specific DNA binding positive regulation of transcription from RNA polymerase II promoter positive regulation of photoreceptor cell differentiation response to stimulus uc002phq.1 uc002phq.2 uc002phq.3 uc002phq.4 uc002phq.5 uc002phq.6 
ENST00000222002.4 SULT2A1 ENST00000222002.4 sulfotransferase family 2A member 1 (from RefSeq NM_003167.4) ENST00000222002.1 ENST00000222002.2 ENST00000222002.3 HST NM_003167 Q06520 ST2A1_HUMAN STD uc002phr.1 uc002phr.2 uc002phr.3 This gene encodes a member of the sulfotransferase family. Sulfotransferases aid in the metabolism of drugs and endogenous compounds by converting these substances into more hydrophilic water-soluble sulfate conjugates that can be easily excreted. This protein catalyzes the sulfation of steroids and bile acids in the liver and adrenal glands, and may have a role in the inherited adrenal androgen excess in women with polycystic ovary syndrome. [provided by RefSeq, Mar 2010]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC020755.1, SRR5189664.117161.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2155590, SAMN03267753 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222002.4/ ENSP00000222002.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups (PubMed:7678732, PubMed:2268288, PubMed:14573603, PubMed:18042734, PubMed:19589875, PubMed:21187059, PubMed:29671343, PubMed:7854148). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis (PubMed:21187059, PubMed:19589875, PubMed:14573603). Plays a key role in bile acid metabolism (PubMed:2268288). In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity). Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'- bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22553; Evidence=; Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)- hydroxycholesterol 24-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52344, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52345; Evidence=; Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)- hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349; Evidence=; Reaction=(24S)-hydroxycholesterol 24-sulfate + 3'-phosphoadenylyl sulfate = (24S)-hydroxycholesterol 3,24-disulfate + adenosine 3',5'- bisphosphate + H(+); Xref=Rhea:RHEA:52352, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566, ChEBI:CHEBI:136568; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52353; Evidence=; Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate + H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217; Evidence=; Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'- bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356, ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133000; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357; Evidence=; Reaction=3'-phosphoadenylyl sulfate + androsterone = adenosine 3',5'- bisphosphate + androsterone 3alpha-sulfate + H(+); Xref=Rhea:RHEA:60644, ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133003; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60645; Evidence=; Reaction=3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + H(+) + taurolithocholate 3-sulfate; Xref=Rhea:RHEA:14013, ChEBI:CHEBI:15378, ChEBI:CHEBI:17179, ChEBI:CHEBI:58301, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=2.8.2.14; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14014; Evidence=; Reaction=3'-phosphoadenylyl sulfate + lithocholate = adenosine 3',5'- bisphosphate + H(+) + lithocholate sulfate; Xref=Rhea:RHEA:51064, ChEBI:CHEBI:15378, ChEBI:CHEBI:29744, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133940; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51065; Evidence=; Subject to substrate inhibition. Alternate orientations for binding of steroid substrates to SULT2A1 may play a role in substrate inhibition. Kinetic parameters: KM=0.8 uM for DHEA ; KM=3.1 uM for DHEA ; KM=1.6 uM for DHEA ; KM=0.1 uM for (24S)-hydroxycholesterol 24-sulfate ; KM=3.7 uM for (24S)-hydroxycholesterol ; KM=1.5 uM for lithocholic acid ; KM=4.2 uM for taurolithocholate ; KM=2.1 uM for 3alpha-hydroxy-5alpha-androstan-17-one, ; KM=1.4 uM for androsterone ; KM=24.88 uM for PAPS ; Vmax=227 nmol/min/mg enzyme with DHEA ; Vmax=22.55 nmol/min/mg enzyme with DHEA ; Vmax=54.3 umol/min/mg enzyme with lithocholic acid ; Vmax=203 nmol/min/mg enzyme with androsterone as substrate ; Vmax=245 nmol/min/mg enzyme with DHEA ; Homodimer. Q06520; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-3921363, EBI-740897; Q06520; P40763: STAT3; NbExp=2; IntAct=EBI-3921363, EBI-518675; Q06520; O43704: SULT1B1; NbExp=6; IntAct=EBI-3921363, EBI-10179062; Cytoplasm Liver, adrenal and at lower level in the kidney. Is present in human fetus in higher level in the adrenal than the liver and the kidney. The N-terminus is blocked. Belongs to the sulfotransferase 1 family. protein binding cytoplasm cytosol ethanol catabolic process lipid metabolic process sulfotransferase activity steroid metabolic process lipid catabolic process transferase activity regulation of lipid metabolic process bile acid catabolic process bile-salt sulfotransferase activity steroid sulfotransferase activity 3'-phosphoadenosine 5'-phosphosulfate metabolic process sulfation uc002phr.1 uc002phr.2 uc002phr.3 
ENST00000222005.7 CDC37 ENST00000222005.7 cell division cycle 37, HSP90 cochaperone (from RefSeq NM_007065.4) CDC37A CDC37_HUMAN ENST00000222005.1 ENST00000222005.2 ENST00000222005.3 ENST00000222005.4 ENST00000222005.5 ENST00000222005.6 NM_007065 Q16543 Q53YA2 uc002mof.1 uc002mof.2 uc002mof.3 The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1159146.1, SRR3476690.452014.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222005.7/ ENSP00000222005.1 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1 ATPase activity (PubMed:23569206). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Forms a complex with Hsp90/HSP90AB1 and CDK6 (PubMed:9482106). Interacts with HSP90AA1 (PubMed:23569206, PubMed:27353360). Interacts with AR, CDK4, CDK6 and EIF2AK1 (PubMed:11036079, PubMed:11085988, PubMed:9150368, PubMed:9482106). Interacts with RB1 (By similarity). Interacts with KSR1 (PubMed:10409742). Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360). Q16543; P60709: ACTB; NbExp=3; IntAct=EBI-295634, EBI-353944; Q16543; P63261: ACTG1; NbExp=3; IntAct=EBI-295634, EBI-351292; Q16543; P31749: AKT1; NbExp=5; IntAct=EBI-295634, EBI-296087; Q16543; Q9Y243: AKT3; NbExp=2; IntAct=EBI-295634, EBI-296115; Q16543; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-295634, EBI-746752; Q16543; P02649: APOE; NbExp=3; IntAct=EBI-295634, EBI-1222467; Q16543; Q96GD4: AURKB; NbExp=5; IntAct=EBI-295634, EBI-624291; Q16543; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-295634, EBI-10181188; Q16543; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-295634, EBI-2548012; Q16543; Q9Y2F9: BTBD3; NbExp=3; IntAct=EBI-295634, EBI-311155; Q16543; Q9UQM7: CAMK2A; NbExp=5; IntAct=EBI-295634, EBI-1383687; Q16543; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-295634, EBI-11523526; Q16543; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-295634, EBI-12020154; Q16543; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-295634, EBI-3866279; Q16543; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-295634, EBI-11530605; Q16543; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-295634, EBI-2559016; Q16543; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-295634, EBI-11524851; Q16543; Q96M89-2: CCDC138; NbExp=3; IntAct=EBI-295634, EBI-10972887; Q16543; Q4G0S7: CCDC152; NbExp=3; IntAct=EBI-295634, EBI-18398007; Q16543; Q7Z6B0-2: CCDC91; NbExp=3; IntAct=EBI-295634, EBI-12012082; Q16543; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-295634, EBI-10175300; Q16543; Q14004: CDK13; NbExp=2; IntAct=EBI-295634, EBI-968626; Q16543; Q96Q40: CDK15; NbExp=2; IntAct=EBI-295634, EBI-1051975; Q16543; P11802: CDK4; NbExp=14; IntAct=EBI-295634, EBI-295644; Q16543; Q00534: CDK6; NbExp=3; IntAct=EBI-295634, EBI-295663; Q16543; P50750: CDK9; NbExp=5; IntAct=EBI-295634, EBI-1383449; Q16543; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-295634, EBI-747776; Q16543; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-295634, EBI-739624; Q16543; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-295634, EBI-723153; Q16543; O15111: CHUK; NbExp=5; IntAct=EBI-295634, EBI-81249; Q16543; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-295634, EBI-12051833; Q16543; P78358: CTAG1B; NbExp=3; IntAct=EBI-295634, EBI-1188472; Q16543; Q13620: CUL4B; NbExp=2; IntAct=EBI-295634, EBI-456067; Q16543; Q9NTM9: CUTC; NbExp=3; IntAct=EBI-295634, EBI-714918; Q16543; Q16832: DDR2; NbExp=3; IntAct=EBI-295634, EBI-1381484; Q16543; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-295634, EBI-11988027; Q16543; P00533: EGFR; NbExp=13; IntAct=EBI-295634, EBI-297353; Q16543; P04626: ERBB2; NbExp=5; IntAct=EBI-295634, EBI-641062; Q16543; Q9NWS6: FAM118A; NbExp=3; IntAct=EBI-295634, EBI-8638992; Q16543; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-295634, EBI-10175124; Q16543; Q969F0: FATE1; NbExp=3; IntAct=EBI-295634, EBI-743099; Q16543; Q9UKT8: FBXW2; NbExp=2; IntAct=EBI-295634, EBI-914727; Q16543; P16591: FER; NbExp=3; IntAct=EBI-295634, EBI-1380661; Q16543; P22607: FGFR3; NbExp=3; IntAct=EBI-295634, EBI-348399; Q16543; Q02790: FKBP4; NbExp=3; IntAct=EBI-295634, EBI-1047444; Q16543; P06241: FYN; NbExp=4; IntAct=EBI-295634, EBI-515315; Q16543; O60861-1: GAS7; NbExp=3; IntAct=EBI-295634, EBI-11745923; Q16543; O95995: GAS8; NbExp=3; IntAct=EBI-295634, EBI-1052570; Q16543; P14136: GFAP; NbExp=3; IntAct=EBI-295634, EBI-744302; Q16543; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-295634, EBI-2548508; Q16543; Q08379: GOLGA2; NbExp=3; IntAct=EBI-295634, EBI-618309; Q16543; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-295634, EBI-5916454; Q16543; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-295634, EBI-11519926; Q16543; Q96HH9: GRAMD2B; NbExp=3; IntAct=EBI-295634, EBI-2832937; Q16543; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-295634, EBI-717919; Q16543; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-295634, EBI-748420; Q16543; O75031: HSF2BP; NbExp=3; IntAct=EBI-295634, EBI-7116203; Q16543; P07900: HSP90AA1; NbExp=14; IntAct=EBI-295634, EBI-296047; Q16543; P08238: HSP90AB1; NbExp=11; IntAct=EBI-295634, EBI-352572; Q16543; O14879: IFIT3; NbExp=4; IntAct=EBI-295634, EBI-745127; Q16543; O14920: IKBKB; NbExp=4; IntAct=EBI-295634, EBI-81266; Q16543; Q14164: IKBKE; NbExp=3; IntAct=EBI-295634, EBI-307369; Q16543; Q9Y6K9: IKBKG; NbExp=6; IntAct=EBI-295634, EBI-81279; Q16543; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-295634, EBI-747204; Q16543; O75564-2: JRK; NbExp=3; IntAct=EBI-295634, EBI-17181882; Q16543; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-295634, EBI-715394; Q16543; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-295634, EBI-742916; Q16543; Q7L273: KCTD9; NbExp=3; IntAct=EBI-295634, EBI-4397613; Q16543; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-295634, EBI-14069005; Q16543; O95198: KLHL2; NbExp=3; IntAct=EBI-295634, EBI-746999; Q16543; O95678: KRT75; NbExp=3; IntAct=EBI-295634, EBI-2949715; Q16543; Q01546: KRT76; NbExp=3; IntAct=EBI-295634, EBI-2952745; Q16543; Q6VAB6: KSR2; NbExp=7; IntAct=EBI-295634, EBI-6424389; Q16543; P53671: LIMK2; NbExp=2; IntAct=EBI-295634, EBI-1384350; Q16543; Q03252: LMNB2; NbExp=3; IntAct=EBI-295634, EBI-2830427; Q16543; Q5S007: LRRK2; NbExp=7; IntAct=EBI-295634, EBI-5323863; Q16543; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-295634, EBI-1216080; Q16543; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-295634, EBI-742610; Q16543; Q99558: MAP3K14; NbExp=6; IntAct=EBI-295634, EBI-358011; Q16543; O43318: MAP3K7; NbExp=2; IntAct=EBI-295634, EBI-358684; Q16543; O43318-2: MAP3K7; NbExp=5; IntAct=EBI-295634, EBI-358700; Q16543; Q99750: MDFI; NbExp=3; IntAct=EBI-295634, EBI-724076; Q16543; O15344: MID1; NbExp=3; IntAct=EBI-295634, EBI-2340316; Q16543; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-295634, EBI-2548751; Q16543; P00540: MOS; NbExp=2; IntAct=EBI-295634, EBI-1757866; Q16543; Q9BYD2: MRPL9; NbExp=3; IntAct=EBI-295634, EBI-726059; Q16543; O15146: MUSK; NbExp=3; IntAct=EBI-295634, EBI-6423196; Q16543; Q8N987: NECAB1; NbExp=3; IntAct=EBI-295634, EBI-11956853; Q16543; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-295634, EBI-10172876; Q16543; P29474: NOS3; NbExp=4; IntAct=EBI-295634, EBI-1391623; Q16543; Q9NQ35: NRIP3; NbExp=3; IntAct=EBI-295634, EBI-10311735; Q16543; Q9BXI3: NT5C1A; NbExp=3; IntAct=EBI-295634, EBI-10441581; Q16543; P22234: PAICS; NbExp=3; IntAct=EBI-295634, EBI-712261; Q16543; O76083-2: PDE9A; NbExp=3; IntAct=EBI-295634, EBI-11524542; Q16543; Q8N165: PDIK1L; NbExp=3; IntAct=EBI-295634, EBI-6423298; Q16543; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-295634, EBI-14066006; Q16543; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-295634, EBI-302355; Q16543; P78424: POU6F2; NbExp=3; IntAct=EBI-295634, EBI-12029004; Q16543; P53041: PPP5C; NbExp=5; IntAct=EBI-295634, EBI-716663; Q16543; P31321: PRKAR1B; NbExp=3; IntAct=EBI-295634, EBI-2805516; Q16543; Q99873-3: PRMT1; NbExp=3; IntAct=EBI-295634, EBI-17165527; Q16543; O14744: PRMT5; NbExp=3; IntAct=EBI-295634, EBI-351098; Q16543; P41219: PRPH; NbExp=3; IntAct=EBI-295634, EBI-752074; Q16543; P86480: PRR20D; NbExp=3; IntAct=EBI-295634, EBI-12754095; Q16543; P49768: PSEN1; NbExp=3; IntAct=EBI-295634, EBI-297277; Q16543; Q96QS6: PSKH2; NbExp=3; IntAct=EBI-295634, EBI-6424813; Q16543; P62333: PSMC6; NbExp=3; IntAct=EBI-295634, EBI-357669; Q16543; Q13882: PTK6; NbExp=4; IntAct=EBI-295634, EBI-1383632; Q16543; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-295634, EBI-14093916; Q16543; P04049: RAF1; NbExp=19; IntAct=EBI-295634, EBI-365996; Q16543; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-295634, EBI-14065960; Q16543; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-295634, EBI-1378139; Q16543; Q9UH03: SEPTIN3; NbExp=3; IntAct=EBI-295634, EBI-727037; Q16543; Q13501: SQSTM1; NbExp=8; IntAct=EBI-295634, EBI-307104; Q16543; P12931: SRC; NbExp=5; IntAct=EBI-295634, EBI-621482; Q16543; A7MD48: SRRM4; NbExp=3; IntAct=EBI-295634, EBI-3867173; Q16543; O43805: SSNA1; NbExp=3; IntAct=EBI-295634, EBI-2515299; Q16543; Q15831: STK11; NbExp=5; IntAct=EBI-295634, EBI-306838; Q16543; Q8WU08-2: STK32A; NbExp=3; IntAct=EBI-295634, EBI-13046508; Q16543; Q9Y2H1: STK38L; NbExp=6; IntAct=EBI-295634, EBI-991501; Q16543; Q16623: STX1A; NbExp=3; IntAct=EBI-295634, EBI-712466; Q16543; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-295634, EBI-11958386; Q16543; Q8IZU3: SYCP3; NbExp=3; IntAct=EBI-295634, EBI-7574149; Q16543; P15884-3: TCF4; NbExp=3; IntAct=EBI-295634, EBI-13636688; Q16543; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-295634, EBI-741515; Q16543; Q9BT49: THAP7; NbExp=3; IntAct=EBI-295634, EBI-741350; Q16543; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-295634, EBI-2505861; Q16543; Q15025: TNIP1; NbExp=3; IntAct=EBI-295634, EBI-357849; Q16543; Q12933: TRAF2; NbExp=3; IntAct=EBI-295634, EBI-355744; Q16543; Q13114: TRAF3; NbExp=3; IntAct=EBI-295634, EBI-357631; Q16543; O00463: TRAF5; NbExp=3; IntAct=EBI-295634, EBI-523498; Q16543; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-295634, EBI-2130429; Q16543; Q9BXA6: TSSK6; NbExp=2; IntAct=EBI-295634, EBI-851883; Q16543; Q6PHR2: ULK3; NbExp=2; IntAct=EBI-295634, EBI-1383475; Q16543; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-295634, EBI-739895; Q16543; P07947: YES1; NbExp=4; IntAct=EBI-295634, EBI-515331; Q16543; O96006: ZBED1; NbExp=3; IntAct=EBI-295634, EBI-740037; Q16543; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-295634, EBI-3918996; Q16543; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-295634, EBI-742740; Q16543; Q8N554: ZNF276; NbExp=3; IntAct=EBI-295634, EBI-750821; Q16543; Q8N720: ZNF655; NbExp=3; IntAct=EBI-295634, EBI-625509; Q16543; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-295634, EBI-11962574; Q16543; Q8N446: ZNF843; NbExp=2; IntAct=EBI-295634, EBI-6428016; Q16543; P33279: EIF2AK1; Xeno; NbExp=3; IntAct=EBI-295634, EBI-640100; Q16543; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-295634, EBI-25475856; Q16543; P11500; Xeno; NbExp=3; IntAct=EBI-295634, EBI-640126; Cytoplasm Constitutively sumoylated by UBE2I. Belongs to the CDC37 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc37/"; regulation of cyclin-dependent protein serine/threonine kinase activity protein binding cytoplasm cytosol protein folding protein targeting posttranscriptional regulation of gene expression protein kinase regulator activity kinase binding protein kinase binding heat shock protein binding ERBB2 signaling pathway regulation of protein kinase activity protein stabilization unfolded protein binding chaperone binding Hsp90 protein binding regulation of interferon-gamma-mediated signaling pathway regulation of type I interferon-mediated signaling pathway extracellular exosome scaffold protein binding mitophagy in response to mitochondrial depolarization HSP90-CDC37 chaperone complex uc002mof.1 uc002mof.2 uc002mof.3 
ENST00000222008.11 RABAC1 ENST00000222008.11 Rab acceptor 1 (from RefSeq NM_006423.3) ENST00000222008.1 ENST00000222008.10 ENST00000222008.2 ENST00000222008.3 ENST00000222008.4 ENST00000222008.5 ENST00000222008.6 ENST00000222008.7 ENST00000222008.8 ENST00000222008.9 NM_006423 PRA1 PRAF1 PRAF1_HUMAN Q7Z4Y2 Q9UI14 Q9Y3R1 uc002osf.1 uc002osf.2 uc002osf.3 uc002osf.4 uc002osf.5 General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI. Homodimer. Interacts with VAMP2 (synaptobrevin-2), GDI1, and PCLO (By similarity). Interacts specifically with prenylated Rab proteins; strongly with RAB4B, RAB5A and RAB5C, and weakly with RAB4A, RAB6, RAB7A, RAB17 and RAB22. Interacts with NDRG1. Q9UI14; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-712367, EBI-7131019; Q9UI14; O95873: C6orf47; NbExp=3; IntAct=EBI-712367, EBI-719613; Q9UI14; Q8NI60: COQ8A; NbExp=12; IntAct=EBI-712367, EBI-745535; Q9UI14; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-712367, EBI-17233035; Q9UI14; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-712367, EBI-8637742; Q9UI14; Q9UNI6: DUSP12; NbExp=7; IntAct=EBI-712367, EBI-715161; Q9UI14; O14681: EI24; NbExp=3; IntAct=EBI-712367, EBI-2339413; Q9UI14; P54849: EMP1; NbExp=3; IntAct=EBI-712367, EBI-4319440; Q9UI14; Q9Y624: F11R; NbExp=3; IntAct=EBI-712367, EBI-742600; Q9UI14; P51114: FXR1; NbExp=2; IntAct=EBI-712367, EBI-713291; Q9UI14; P51116: FXR2; NbExp=3; IntAct=EBI-712367, EBI-740459; Q9UI14; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-712367, EBI-13345167; Q9UI14; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-712367, EBI-18053395; Q9UI14; Q9Y2U8: LEMD3; NbExp=3; IntAct=EBI-712367, EBI-2561428; Q9UI14; P36941: LTBR; NbExp=3; IntAct=EBI-712367, EBI-3509981; Q9UI14; Q96C03: MIEF2; NbExp=3; IntAct=EBI-712367, EBI-750153; Q9UI14; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-712367, EBI-11988931; Q9UI14; Q9UN36-1: NDRG2; NbExp=7; IntAct=EBI-712367, EBI-8084503; Q9UI14; Q9ULP0: NDRG4; NbExp=3; IntAct=EBI-712367, EBI-10323810; Q9UI14; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-712367, EBI-11978907; Q9UI14; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-712367, EBI-740897; Q9UI14; Q96HA8: NTAQ1; NbExp=9; IntAct=EBI-712367, EBI-741158; Q9UI14; Q6ZVK8: NUDT18; NbExp=3; IntAct=EBI-712367, EBI-740486; Q9UI14; Q96AL5: PBX3; NbExp=5; IntAct=EBI-712367, EBI-741171; Q9UI14; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-712367, EBI-742388; Q9UI14; Q14088: RAB33A; NbExp=3; IntAct=EBI-712367, EBI-744685; Q9UI14; Q9UI14: RABAC1; NbExp=6; IntAct=EBI-712367, EBI-712367; Q9UI14; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-712367, EBI-11337973; Q9UI14; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-712367, EBI-10192441; Q9UI14; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-712367, EBI-9091816; Q9UI14; Q99942: RNF5; NbExp=3; IntAct=EBI-712367, EBI-348482; Q9UI14; A8MRB1: S100B; NbExp=3; IntAct=EBI-712367, EBI-16432654; Q9UI14; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-712367, EBI-6503765; Q9UI14; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-712367, EBI-2623095; Q9UI14; Q96DU3: SLAMF6; NbExp=3; IntAct=EBI-712367, EBI-14058448; Q9UI14; P37840: SNCA; NbExp=4; IntAct=EBI-712367, EBI-985879; Q9UI14; Q13596: SNX1; NbExp=3; IntAct=EBI-712367, EBI-2822329; Q9UI14; Q8N5Z3: SNX10; NbExp=3; IntAct=EBI-712367, EBI-10266928; Q9UI14; Q9Y5X0: SNX10; NbExp=3; IntAct=EBI-712367, EBI-10329478; Q9UI14; Q9Y5W9: SNX11; NbExp=6; IntAct=EBI-712367, EBI-10329449; Q9UI14; Q9NRS6: SNX15; NbExp=4; IntAct=EBI-712367, EBI-725924; Q9UI14; Q15036: SNX17; NbExp=3; IntAct=EBI-712367, EBI-1752620; Q9UI14; Q9Y5X2: SNX8; NbExp=3; IntAct=EBI-712367, EBI-1752557; Q9UI14; Q9NZD8: SPG21; NbExp=7; IntAct=EBI-712367, EBI-742688; Q9UI14; Q9UNL2: SSR3; NbExp=3; IntAct=EBI-712367, EBI-1043938; Q9UI14; Q13586: STIM1; NbExp=3; IntAct=EBI-712367, EBI-448878; Q9UI14; Q9UJZ1: STOML2; NbExp=3; IntAct=EBI-712367, EBI-1044428; Q9UI14; Q17RD7: SYT16; NbExp=8; IntAct=EBI-712367, EBI-10238936; Q9UI14; Q12893: TMEM115; NbExp=3; IntAct=EBI-712367, EBI-8633987; Q9UI14; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-712367, EBI-8638294; Q9UI14; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-712367, EBI-12038591; Q9UI14; Q9Y320: TMX2; NbExp=3; IntAct=EBI-712367, EBI-6447886; Q9UI14; Q13049: TRIM32; NbExp=10; IntAct=EBI-712367, EBI-742790; Q9UI14; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-712367, EBI-10180829; Q9UI14; Q9Y4P8: WIPI2; NbExp=3; IntAct=EBI-712367, EBI-719396; Q9UI14; Q9Y4P8-4: WIPI2; NbExp=3; IntAct=EBI-712367, EBI-12205107; Q9UI14; Q9BQ24: ZFYVE21; NbExp=6; IntAct=EBI-712367, EBI-2849569; Q9UI14; P03230: LMP1; Xeno; NbExp=9; IntAct=EBI-712367, EBI-6973030; Cell membrane ; Multi-pass membrane protein Cytoplasm Golgi apparatus Cytoplasmic vesicle, secretory vesicle, synaptic vesicle Note=According to some authors, it is an integral membrane protein, while others showed that it is cytoplasmic and membrane-associated to Golgi and synaptic vesicles. Ubiquitous. Strongest expression found in placenta, pituitary gland, kidney, lung and stomach. In fetal tissues, it is more abundant in kidney and lung. Belongs to the PRA1 family. In contrast to the mouse ortholog, it does not interact with Ras. protein binding cytoplasm Golgi apparatus plasma membrane synaptic vesicle protein C-terminus binding membrane integral component of membrane cell junction cytoplasmic vesicle identical protein binding synapse proline-rich region binding uc002osf.1 uc002osf.2 uc002osf.3 uc002osf.4 uc002osf.5 
ENST00000222032.10 CNFN ENST00000222032.10 cornifelin (from RefSeq NM_032488.4) B2R569 CNFN_HUMAN ENST00000222032.1 ENST00000222032.2 ENST00000222032.3 ENST00000222032.4 ENST00000222032.5 ENST00000222032.6 ENST00000222032.7 ENST00000222032.8 ENST00000222032.9 NM_032488 Q9BYD5 uc002otp.1 uc002otp.2 uc002otp.3 uc002otp.4 uc002otp.5 uc002otp.6 Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. Directly or indirectly cross-linked to CE proteins loricin and involucrin (IVL). Q9BYD5; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-12819063, EBI-744556; Q9BYD5; Q02930-3: CREB5; NbExp=3; IntAct=EBI-12819063, EBI-10192698; Q9BYD5; Q03828: EVX2; NbExp=3; IntAct=EBI-12819063, EBI-17280301; Q9BYD5; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-12819063, EBI-2807642; Q9BYD5; P49639: HOXA1; NbExp=3; IntAct=EBI-12819063, EBI-740785; Q9BYD5; P09067: HOXB5; NbExp=3; IntAct=EBI-12819063, EBI-3893317; Q9BYD5; O43593: HR; NbExp=3; IntAct=EBI-12819063, EBI-2880706; Q9BYD5; Q5T749: KPRP; NbExp=3; IntAct=EBI-12819063, EBI-10981970; Q9BYD5; Q9UP95: SLC12A4; NbExp=3; IntAct=EBI-12819063, EBI-7244836; Q9BYD5; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-12819063, EBI-11746252; Q9BYD5; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-12819063, EBI-11952651; Q9BYD5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-12819063, EBI-11741437; Q9BYD5; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-12819063, EBI-11957216; Q9BYD5; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-12819063, EBI-12032042; Q9BYD5; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-12819063, EBI-744257; Q9BYD5; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-12819063, EBI-745520; Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope. Abundant in the cervix. Moderately abundant in the uterus and fetal skin. Expression is markedly increased in psoriatic skin (18.5 fold increase in comparison with normal skin) and its overexpression alters the protein composition of cornified cell envelope (CE), but does not affect keratinocyte differentiation. Expressed in the granular cell layer of epidermis in uninvolved psoriatic skin and in the psoriatic lesions it is found in the upper- spinous layer. Increased expression also seen in atopic dermatitis (14.3 fold increase in comparison with normal skin) and mycosis fungoides (4.6 fold increase in comparison with normal skin) and in both conditions expressed in the granular cell layer of epidermis. Belongs to the cornifelin family. cornified envelope cytoplasm keratinization uc002otp.1 uc002otp.2 uc002otp.3 uc002otp.4 uc002otp.5 uc002otp.6 
ENST00000222033.6 ZNRF4 ENST00000222033.6 zinc and ring finger 4 (from RefSeq NM_181710.4) A8K886 ENST00000222033.1 ENST00000222033.2 ENST00000222033.3 ENST00000222033.4 ENST00000222033.5 NM_181710 O75866 Q8WWF5 RNF204 ZNRF4 ZNRF4_HUMAN uc002mca.1 uc002mca.2 uc002mca.3 uc002mca.4 uc002mca.5 uc002mca.6 E3 ubiquitin-protein ligase that acts as a negative regulator of NOD2 signaling by mediating ubiquitination and degradation of RIPK2 (PubMed:28656966). Also catalyzes ubiquitination and proteasomal degradation of CANX within the endoplasmic reticulum (PubMed:21205830). Could have a role in spermatogenesis (By similarity). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence= Protein modification; protein ubiquitination. Interacts with CANX. Q8WWF5; P21589: NT5E; NbExp=3; IntAct=EBI-2129267, EBI-6393623; Q8WWF5; Q8N7U7-2: TPRX1; NbExp=3; IntAct=EBI-2129267, EBI-14115717; Q8WWF5; O00526: UPK2; NbExp=3; IntAct=EBI-2129267, EBI-10179682; Endoplasmic reticulum membrane ingle-pass type I membrane protein The RING-type zinc finger is involved in CANX ubiquitination and degradation, but is not required for interaction with CANX. Sequence=AAC62428.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; protein binding lysosomal membrane endoplasmic reticulum endoplasmic reticulum membrane ubiquitin-dependent protein catabolic process membrane integral component of membrane protein ubiquitination transferase activity metal ion binding ubiquitin protein ligase activity uc002mca.1 uc002mca.2 uc002mca.3 uc002mca.4 uc002mca.5 uc002mca.6 
ENST00000222120.8 RAB3D ENST00000222120.8 RAB3D, member RAS oncogene family (from RefSeq NM_004283.4) ENST00000222120.1 ENST00000222120.2 ENST00000222120.3 ENST00000222120.4 ENST00000222120.5 ENST00000222120.6 ENST00000222120.7 GOV NM_004283 O95716 RAB16 RAB3D_HUMAN uc002mqx.1 uc002mqx.2 uc002mqx.3 uc002mqx.4 Protein transport. Probably involved in regulated exocytosis (By similarity). Interacts with RIMS1, RIMS2, RPH3A, RPH3AL and RAB3IP (By similarity). Interacts with CHM and CHML; phosphorylation at Thr-86 disrupts these interactions (PubMed:29125462). Interacts with MADD (via uDENN domain); the GTP-bound form is preferred for interaction (By similarity). O95716; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-3386067, EBI-11984839; O95716; P47224: RABIF; NbExp=3; IntAct=EBI-3386067, EBI-713992; O95716; Q96C24: SYTL4; NbExp=3; IntAct=EBI-3386067, EBI-747142; O95716; Q9H8Y1: VRTN; NbExp=3; IntAct=EBI-3386067, EBI-12894399; Cell membrane ; Lipid-anchor ; Cytoplasmic side Highly expressed in granulocytes of peripheral blood. Constitutively expressed at low levels in all hematopoietic cell lines investigated. Activated in myeloid differentiation. Phosphorylation of Thr-86 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM and CHML. Belongs to the small GTPase superfamily. Rab family. nucleotide binding GTPase activity GTP binding endosome cytoplasmic microtubule plasma membrane intracellular protein transport exocytosis vesicle docking involved in exocytosis synaptic vesicle protein secretion protein transport membrane regulation of exocytosis peptidyl-cysteine methylation transport vesicle GTP-dependent protein binding myosin V binding vesicle Rab protein signal transduction azurophil granule membrane zymogen granule neutrophil degranulation bone resorption extracellular exosome protein localization to plasma membrane secretory vesicle positive regulation of regulated secretory pathway uc002mqx.1 uc002mqx.2 uc002mqx.3 uc002mqx.4 
ENST00000222122.10 DBP ENST00000222122.10 D-box binding PAR bZIP transcription factor (from RefSeq NM_001352.5) A2I2P4 DBP_HUMAN ENST00000222122.1 ENST00000222122.2 ENST00000222122.3 ENST00000222122.4 ENST00000222122.5 ENST00000222122.6 ENST00000222122.7 ENST00000222122.8 ENST00000222122.9 NM_001352 Q10586 uc002pjx.1 uc002pjx.2 uc002pjx.3 uc002pjx.4 uc002pjx.5 uc002pjx.6 The protein encoded by this gene is a member of the PAR bZIP transcription factor family and binds to specific sequences in the promoters of several genes, such as albumin, CYP2A4, and CYP2A5. The encoded protein can bind DNA as a homo- or heterodimer and is involved in the regulation of some circadian rhythm genes. [provided by RefSeq, Jul 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7346977.333055.1, SRR7346977.851635.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968189 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222122.10/ ENSP00000222122.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## This transcriptional activator recognizes and binds to the sequence 5'-RTTAYGTAAY-3' found in the promoter of genes such as albumin, CYP2A4 and CYP2A5. It is not essential for circadian rhythm generation, but modulates important clock output genes. May be a direct target for regulation by the circadian pacemaker component clock. May affect circadian period and sleep regulation. Binds DNA as a homodimer or a heterodimer. Can form a heterodimer with TEF. Q10586; Q16520: BATF; NbExp=2; IntAct=EBI-3908088, EBI-749503; Q10586; Q9NR55: BATF3; NbExp=2; IntAct=EBI-3908088, EBI-10312707; Q10586; P35638: DDIT3; NbExp=4; IntAct=EBI-3908088, EBI-742651; Q10586; Q16534: HLF; NbExp=3; IntAct=EBI-3908088, EBI-2798854; Nucleus. Ubiquitously expressed. Expressed in the suprachiasmatic nuclei (SCN) and in most peripheral tissues, with a strong circadian rhythmicity. Belongs to the bZIP family. PAR subfamily. nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding liver development DNA binding transcription factor activity, sequence-specific DNA binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter circadian rhythm positive regulation of transcription from RNA polymerase II promoter rhythmic process uc002pjx.1 uc002pjx.2 uc002pjx.3 uc002pjx.4 uc002pjx.5 uc002pjx.6 
ENST00000222139.11 EPOR ENST00000222139.11 erythropoietin receptor, transcript variant 1 (from RefSeq NM_000121.4) B2RCG4 ENST00000222139.1 ENST00000222139.10 ENST00000222139.2 ENST00000222139.3 ENST00000222139.4 ENST00000222139.5 ENST00000222139.6 ENST00000222139.7 ENST00000222139.8 ENST00000222139.9 EPOR_HUMAN NM_000121 P19235 Q15443 Q2M205 uc002mrj.1 uc002mrj.2 uc002mrj.3 uc002mrj.4 This gene encodes the erythropoietin receptor which is a member of the cytokine receptor family. Upon erythropoietin binding, this receptor activates Jak2 tyrosine kinase which activates different intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. The stimulated erythropoietin receptor appears to have a role in erythroid cell survival. Defects in the erythropoietin receptor may produce erythroleukemia and familial erythrocytosis. Dysregulation of this gene may affect the growth of certain tumors. Alternate splicing results in multiple transcript variants.[provided by RefSeq, May 2010]. Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase. Isoform EPOR-T acts as a dominant-negative receptor of EPOR- mediated signaling. Forms homodimers on EPO stimulation. The tyrosine- phosphorylated form interacts with several SH2 domain-containing proteins including LYN (By similarity), the adapter protein SH2B2, PTPN6 (By similarity), PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3, CRKL (By similarity). Interacts with INPP5D/SHIP1 (By similarity). The N- terminal SH2 domain of PTPN6 binds Tyr-454 and inhibits signaling through dephosphorylation of JAK2 (By similarity). SH2B2 binding also inhibits the JAK-STAT signaling. Binding to PTPN11, preferentially through the N-terminal SH2 domain, promotes mitogenesis and phosphorylation of PTPN11 (By similarity). Binding of JAK2 (through its N-terminal) promotes cell-surface expression (By similarity). Interacts with RHEX; this interaction occurs in a erythropoietin (EPO)-dependent manner (PubMed:25092874). Interaction with the ubiquitin ligase NOSIP mediates EPO-induced cell proliferation. Interacts with ATXN2L. P19235; Q8WWM7: ATXN2L; NbExp=2; IntAct=EBI-617321, EBI-948363; P19235; P01588: EPO; NbExp=3; IntAct=EBI-617321, EBI-1027362; P19235; PRO_0000008401 [P01588]: EPO; NbExp=2; IntAct=EBI-617321, EBI-11508463; P19235; P19235: EPOR; NbExp=3; IntAct=EBI-617321, EBI-617321; P19235; P16885: PLCG2; NbExp=3; IntAct=EBI-617321, EBI-617403; P19235; P18031: PTPN1; NbExp=3; IntAct=EBI-617321, EBI-968788; P19235; P29350: PTPN6; NbExp=11; IntAct=EBI-617321, EBI-78260; P19235; O14508: SOCS2; NbExp=3; IntAct=EBI-617321, EBI-617737; P19235; Q62225: Cish; Xeno; NbExp=4; IntAct=EBI-617321, EBI-617489; Cell membrane; Single-pass type I membrane protein. [Isoform EPOR-S]: Secreted Note=Secreted and located to the cell surface. Event=Alternative splicing; Named isoforms=3; Name=EPOR-F; Synonyms=Full-length form; IsoId=P19235-1; Sequence=Displayed; Name=EPOR-S; Synonyms=Soluble form; IsoId=P19235-2; Sequence=VSP_009508, VSP_009509; Name=EPOR-T; Synonyms=Truncated form; IsoId=P19235-3; Sequence=VSP_009510, VSP_009511; Erythroid cells and erythroid progenitor cells. Isoform EPOR-F is the most abundant form in EPO-dependent erythroleukemia cells and in late-stage erythroid progenitors. Isoform EPOR-S and isoform EPOR-T are the predominant forms in bone marrow. Isoform EPOR-T is the most abundant from in early-stage erythroid progenitor cells. The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box 1 motif is required for JAK interaction and/or activation. Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2. The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation. Phosphorylation on Tyr-454 is required for PTPN6 interaction, Tyr-426 for PTPN11. Tyr-426 is also required for SOCS3 binding, but Tyr-454/Tyr-456 motif is the preferred binding site. Ubiquitination at Lys-281 mediates receptor internalization, whereas ubiquitination at Lys-453 promotes trafficking of activated receptors to the lysosomes for degradation (By similarity). Ubiquitinated by NOSIP; appears to be either multi-monoubiquitinated or polyubiquitinated. Ubiquitination mediates proliferation and survival of EPO-dependent cells. Erythrocytosis, familial, 1 (ECYT1) [MIM:133100]: An autosomal dominant disorder characterized by elevated hemoglobin and hematocrit, hypersensitivity of erythroid progenitors to erythropoietin, erythropoietin low serum levels, and no increase in platelets nor leukocytes. It has a relatively benign course and does not progress to leukemia. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the type I cytokine receptor family. Type 1 subfamily. transmembrane signaling receptor activity cytokine receptor activity erythropoietin receptor activity protein binding extracellular region plasma membrane integral component of plasma membrane signal transduction brain development heart development positive regulation of phosphatidylinositol 3-kinase signaling membrane integral component of membrane cytokine-mediated signaling pathway erythropoietin-mediated signaling pathway identical protein binding positive regulation of Ras protein signal transduction decidualization uc002mrj.1 uc002mrj.2 uc002mrj.3 uc002mrj.4 
ENST00000222145.9 RASIP1 ENST00000222145.9 Ras interacting protein 1 (from RefSeq NM_017805.3) ENST00000222145.1 ENST00000222145.2 ENST00000222145.3 ENST00000222145.4 ENST00000222145.5 ENST00000222145.6 ENST00000222145.7 ENST00000222145.8 NM_017805 Q5U651 Q6U676 RAIN_HUMAN uc002pki.1 uc002pki.2 uc002pki.3 uc002pki.4 uc002pki.5 Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Regulates the activity of Rho GTPases in part by recruiting ARHGAP29 and suppressing RhoA signaling and dampening ROCK and MYH9 activities in endothelial cells (By similarity). May act as effector for Golgi-bound HRAS and other Ras- like proteins. May promote HRAS-mediated transformation. Negative regulator of amino acid starvation-induced autophagy. Interacts with Ras family members that have been activated by GTP binding. Interacts with HRAS, RAP1A, RAP2, RRAS, RAF1 and RRAS2. Interacts with MYH9 and ARHGAP29 (By similarity). Cytoplasm, perinuclear region Golgi apparatus, Golgi stack Note=Associated with perinuclear vesicles. Is recruited to Golgi stacks by activated HRAS. Highly expressed in heart. Detected at lower levels in placenta and pancreas. angiogenesis vasculogenesis protein binding cytoplasm Golgi apparatus Golgi stack cell-cell junction signal transduction negative regulation of autophagy macromolecular complex positive regulation of integrin activation negative regulation of Rho protein signal transduction protein homodimerization activity regulation of GTPase activity perinuclear region of cytoplasm branching morphogenesis of an epithelial tube GTPase binding negative regulation of membrane permeability negative regulation of Rho-dependent protein serine/threonine kinase activity uc002pki.1 uc002pki.2 uc002pki.3 uc002pki.4 uc002pki.5 
ENST00000222214.10 GCDH ENST00000222214.10 glutaryl-CoA dehydrogenase, transcript variant 4 (from RefSeq NR_102317.1) A8K2Z2 ENST00000222214.1 ENST00000222214.2 ENST00000222214.3 ENST00000222214.4 ENST00000222214.5 ENST00000222214.6 ENST00000222214.7 ENST00000222214.8 ENST00000222214.9 GCDH_HUMAN NR_102317 O14719 Q92947 uc002mvq.1 uc002mvq.2 uc002mvq.3 uc002mvq.4 uc002mvq.5 uc002mvq.6 The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family. It catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. The enzyme exists in the mitochondrial matrix as a homotetramer of 45-kD subunits. Mutations in this gene result in the metabolic disorder glutaric aciduria type 1, which is also known as glutaric acidemia type I. Alternative splicing of this gene results in multiple transcript variants. A related pseudogene has been identified on chromosome 12. [provided by RefSeq, Mar 2013]. Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive. Reaction=glutaryl-CoA + 2 H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:13389, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57332, ChEBI:CHEBI:57378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.6; Evidence=; Name=FAD; Xref=ChEBI:CHEBI:57692; Strongly inhibited by MCPA-CoA, a metabolite of hypoglycin which is present in unripened fruit of the ackee tree. Kinetic parameters: KM=4.7 uM for glutaryl-CoA (at pH 6.5) KM=5.5 uM for glutaryl-CoA (at pH 7.5) KM=8.1 uM for glutaryl-CoA (at pH 7.6) KM=34.0 uM for glutaryl-CoA (at pH 8.5) Note=Release of crotonyl-CoA product from the enzyme is the rate- determining step in its steady-state turnover.; Amino-acid metabolism; lysine degradation. Amino-acid metabolism; tryptophan metabolism. Homotetramer. Mitochondrion matrix. Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=Q92947-1; Sequence=Displayed; Name=Short; IsoId=Q92947-2; Sequence=VSP_000145; Isoform Long and isoform Short are expressed in fibroblasts and liver. Glutaric aciduria 1 (GA1) [MIM:231670]: An autosomal recessive metabolic disorder characterized by progressive dystonia and athetosis due to gliosis and neuronal loss in the basal ganglia. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the acyl-CoA dehydrogenase family. fatty-acyl-CoA binding acyl-CoA dehydrogenase activity glutaryl-CoA dehydrogenase activity mitochondrion mitochondrial matrix lysine catabolic process tryptophan metabolic process acyl-CoA metabolic process oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors fatty acid oxidation fatty acid beta-oxidation using acyl-CoA dehydrogenase glutaryl-CoA hydrolase activity fatty-acyl-CoA biosynthetic process flavin adenine dinucleotide binding oxidation-reduction process uc002mvq.1 uc002mvq.2 uc002mvq.3 uc002mvq.4 uc002mvq.5 uc002mvq.6 
ENST00000222219.8 DNASE2 ENST00000222219.8 deoxyribonuclease 2, lysosomal (from RefSeq NM_001375.3) B2RD06 B7Z4K6 DNASE2A DNL2 DNS2A_HUMAN ENST00000222219.1 ENST00000222219.2 ENST00000222219.3 ENST00000222219.4 ENST00000222219.5 ENST00000222219.6 ENST00000222219.7 NM_001375 O00115 O43910 uc002mvn.1 uc002mvn.2 uc002mvn.3 This gene encodes a member of the DNase family. The protein, located in the lysosome, hydrolyzes DNA under acidic conditions and mediates the breakdown of DNA during erythropoiesis and apoptosis. Two codominant alleles have been characterized, DNASE2*L (low activity) and DNASE2*H (high activity), that differ at one nucleotide in the promoter region. The DNASE2*H allele is represented in this record. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803615.28874.1, SRR3476690.755593.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2151358 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222219.8/ ENSP00000222219.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation (PubMed:29259162, PubMed:31775019). Necessary for proper fetal development and for definitive erythropoiesis in fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells (PubMed:29259162). Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'- phosphooligonucleotide end-products.; EC=3.1.22.1; Evidence=; Lysosome. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O00115-1; Sequence=Displayed; Name=2; IsoId=O00115-2; Sequence=VSP_056921; Expressed in monocytes/macrophages (at protein level). Glycosylated. Genetic variations that affect N-glycosylation sites reduce activity, but enzymatic deglycosylation has no effect. Autoinflammatory-pancytopenia syndrome (AIPCS) [MIM:619858]: An autosomal recessive disorder characterized by severe anemia and thrombocytopenia apparent from early infancy, hepatosplenomegaly, and recurrent fevers associated with a hyperinflammatory state. Additional systemic features may include chronic diarrhea, proteinuria with renal disease, liver fibrosis with elevated liver enzymes, deforming arthropathy, and vasculitic skin lesions. Some patients may have motor delay or learning difficulties associated with subcortical white matter lesions on brain imaging. te=The disease is caused by variants affecting the gene represented in this entry. The genetic variation producing the missense variant p.G116A, associated with AIPCS, has been shown to predominantly affect splicing, leading to in-frame deletion of exon 4, encoding amino acids 116 to 171. The protein resulting from this aberrant splicing may be unstable. Belongs to the DNase II family. DNA catabolic process, endonucleolytic DNA binding nuclease activity endonuclease activity endodeoxyribonuclease activity deoxyribonuclease II activity lysosome DNA metabolic process DNA catabolic process apoptotic DNA fragmentation apoptotic process multicellular organism development hydrolase activity erythrocyte differentiation regulation of immune response extracellular exosome uc002mvn.1 uc002mvn.2 uc002mvn.3 
ENST00000222224.4 LENG1 ENST00000222224.4 leukocyte receptor cluster member 1 (from RefSeq NM_024316.3) ENST00000222224.1 ENST00000222224.2 ENST00000222224.3 LENG1_HUMAN NM_024316 Q96BZ8 Q9HCU7 uc002qdm.1 uc002qdm.2 uc002qdm.3 uc002qdm.4 uc002qdm.5 Q96BZ8; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-726510, EBI-11096309; Q96BZ8; Q8WXK4-2: ASB12; NbExp=3; IntAct=EBI-726510, EBI-18394052; Q96BZ8; Q8N9N5: BANP; NbExp=4; IntAct=EBI-726510, EBI-744695; Q96BZ8; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-726510, EBI-742722; Q96BZ8; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-726510, EBI-725606; Q96BZ8; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-726510, EBI-739580; Q96BZ8; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-726510, EBI-3866279; Q96BZ8; Q9H257: CARD9; NbExp=3; IntAct=EBI-726510, EBI-751319; Q96BZ8; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-726510, EBI-11530605; Q96BZ8; Q8NA61: CBY2; NbExp=3; IntAct=EBI-726510, EBI-741724; Q96BZ8; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-726510, EBI-10171570; Q96BZ8; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-726510, EBI-10171416; Q96BZ8; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-726510, EBI-2808286; Q96BZ8; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-726510, EBI-10961624; Q96BZ8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-726510, EBI-10175300; Q96BZ8; Q01850: CDR2; NbExp=6; IntAct=EBI-726510, EBI-1181367; Q96BZ8; Q86X02: CDR2L; NbExp=3; IntAct=EBI-726510, EBI-11063830; Q96BZ8; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-726510, EBI-10181988; Q96BZ8; Q8NHQ1: CEP70; NbExp=7; IntAct=EBI-726510, EBI-739624; Q96BZ8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-726510, EBI-742054; Q96BZ8; P17661: DES; NbExp=3; IntAct=EBI-726510, EBI-1055572; Q96BZ8; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-726510, EBI-11988027; Q96BZ8; O60447: EVI5; NbExp=3; IntAct=EBI-726510, EBI-852291; Q96BZ8; A1L4K1: FSD2; NbExp=6; IntAct=EBI-726510, EBI-5661036; Q96BZ8; P14136: GFAP; NbExp=3; IntAct=EBI-726510, EBI-744302; Q96BZ8; Q08379: GOLGA2; NbExp=8; IntAct=EBI-726510, EBI-618309; Q96BZ8; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-726510, EBI-5916454; Q96BZ8; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-726510, EBI-10961706; Q96BZ8; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-726510, EBI-747204; Q96BZ8; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-726510, EBI-18398632; Q96BZ8; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-726510, EBI-2556193; Q96BZ8; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-726510, EBI-749265; Q96BZ8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-726510, EBI-2125614; Q96BZ8; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-726510, EBI-14069005; Q96BZ8; P08727: KRT19; NbExp=3; IntAct=EBI-726510, EBI-742756; Q96BZ8; Q15323: KRT31; NbExp=6; IntAct=EBI-726510, EBI-948001; Q96BZ8; Q92764: KRT35; NbExp=3; IntAct=EBI-726510, EBI-1058674; Q96BZ8; Q6A162: KRT40; NbExp=6; IntAct=EBI-726510, EBI-10171697; Q96BZ8; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-726510, EBI-10171774; Q96BZ8; O95751: LDOC1; NbExp=8; IntAct=EBI-726510, EBI-740738; Q96BZ8; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-726510, EBI-18273118; Q96BZ8; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-726510, EBI-1216080; Q96BZ8; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-726510, EBI-10268010; Q96BZ8; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-726510, EBI-742610; Q96BZ8; Q99687-3: MEIS3; NbExp=3; IntAct=EBI-726510, EBI-18582591; Q96BZ8; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-726510, EBI-10172526; Q96BZ8; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-726510, EBI-2548751; Q96BZ8; Q13084: MRPL28; NbExp=3; IntAct=EBI-726510, EBI-723426; Q96BZ8; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-726510, EBI-742948; Q96BZ8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-726510, EBI-11522433; Q96BZ8; Q15742: NAB2; NbExp=6; IntAct=EBI-726510, EBI-8641936; Q96BZ8; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-726510, EBI-10172876; Q96BZ8; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-726510, EBI-741158; Q96BZ8; P61970: NUTF2; NbExp=3; IntAct=EBI-726510, EBI-591778; Q96BZ8; O43482: OIP5; NbExp=3; IntAct=EBI-726510, EBI-536879; Q96BZ8; Q9P286: PAK5; NbExp=3; IntAct=EBI-726510, EBI-741896; Q96BZ8; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-726510, EBI-1105124; Q96BZ8; P31321: PRKAR1B; NbExp=3; IntAct=EBI-726510, EBI-2805516; Q96BZ8; P41219: PRPH; NbExp=3; IntAct=EBI-726510, EBI-752074; Q96BZ8; P20618: PSMB1; NbExp=3; IntAct=EBI-726510, EBI-372273; Q96BZ8; Q15276: RABEP1; NbExp=3; IntAct=EBI-726510, EBI-447043; Q96BZ8; Q04864-2: REL; NbExp=4; IntAct=EBI-726510, EBI-10829018; Q96BZ8; Q9HAT0: ROPN1; NbExp=8; IntAct=EBI-726510, EBI-1378139; Q96BZ8; Q96KG9-4: SCYL1; NbExp=3; IntAct=EBI-726510, EBI-12023020; Q96BZ8; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-726510, EBI-744066; Q96BZ8; O75558: STX11; NbExp=3; IntAct=EBI-726510, EBI-714135; Q96BZ8; P15884: TCF4; NbExp=3; IntAct=EBI-726510, EBI-533224; Q96BZ8; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-726510, EBI-11139477; Q96BZ8; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-726510, EBI-12090309; Q96BZ8; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-726510, EBI-1105213; Q96BZ8; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-726510, EBI-9675724; Q96BZ8; Q12933: TRAF2; NbExp=3; IntAct=EBI-726510, EBI-355744; Q96BZ8; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-726510, EBI-492476; Q96BZ8; P36406: TRIM23; NbExp=3; IntAct=EBI-726510, EBI-740098; Q96BZ8; P14373: TRIM27; NbExp=3; IntAct=EBI-726510, EBI-719493; Q96BZ8; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-726510, EBI-2130429; Q96BZ8; Q86WV8: TSC1; NbExp=3; IntAct=EBI-726510, EBI-12806590; Q96BZ8; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-726510, EBI-607755; Q96BZ8; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-726510, EBI-11524408; Q96BZ8; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-726510, EBI-739895; Q96BZ8; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-726510, EBI-12030590; Q96BZ8; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-726510, EBI-527853; Belongs to the leukocyte receptor cluster (LRC) present on 19q13.4. Sequence=AAG01393.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; molecular_function protein binding cellular_component biological_process uc002qdm.1 uc002qdm.2 uc002qdm.3 uc002qdm.4 uc002qdm.5 
ENST00000222247.10 RPL18A ENST00000222247.10 ribosomal protein L18a (from RefSeq NM_000980.4) ENST00000222247.1 ENST00000222247.2 ENST00000222247.3 ENST00000222247.4 ENST00000222247.5 ENST00000222247.6 ENST00000222247.7 ENST00000222247.8 ENST00000222247.9 NM_000980 Q02543 RL18A_HUMAN uc002nhp.1 uc002nhp.2 uc002nhp.3 uc002nhp.4 uc002nhp.5 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a member of the L18AE family of ribosomal proteins that is a component of the 60S subunit. The encoded protein may play a role in viral replication by interacting with the hepatitis C virus internal ribosome entry site (IRES). This gene is co-transcribed with the U68 snoRNA, located within the third intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed throughout the genome. [provided by RefSeq, Jul 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: CD174123.1, CD173034.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222247.10/ ENSP00000222247.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547). Binds IPO9 with high affinity (PubMed:11823430). Q02543; P36578: RPL4; NbExp=2; IntAct=EBI-350523, EBI-348313; Cytoplasm Belongs to the eukaryotic ribosomal protein eL20 family. Sequence=CAA56788.1; Type=Frameshift; Evidence=; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay cytoplasmic translation RNA binding structural constituent of ribosome protein binding cytosol ribosome translation translational initiation SRP-dependent cotranslational protein targeting to membrane membrane viral transcription cytosolic large ribosomal subunit polysomal ribosome uc002nhp.1 uc002nhp.2 uc002nhp.3 uc002nhp.4 uc002nhp.5 
ENST00000222248.4 SLC5A5 ENST00000222248.4 solute carrier family 5 member 5 (from RefSeq NM_000453.3) ENST00000222248.1 ENST00000222248.2 ENST00000222248.3 NIS NM_000453 O43702 Q2M335 Q92911 Q9NYB6 SC5A5_HUMAN uc002nhr.1 uc002nhr.2 uc002nhr.3 uc002nhr.4 uc002nhr.5 This gene encodes a member of the sodium glucose cotransporter family. The encoded protein is responsible for the uptake of iodine in tissues such as the thyroid and lactating breast tissue. The iodine taken up by the thyroid is incorporated into the metabolic regulators triiodothyronine (T3) and tetraiodothyronine (T4). Mutations in this gene are associated with thyroid dyshormonogenesis 1.[provided by RefSeq, Sep 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U66088.1, D87920.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968832, SAMEA2142586 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222248.4/ ENSP00000222248.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Sodium:iodide symporter that mediates the transport of iodide into the thyroid gland (PubMed:8806637, PubMed:9329364, PubMed:20797386, PubMed:12488351, PubMed:18372236, PubMed:18708479, PubMed:31310151, PubMed:32084174). Can also mediate the transport of chlorate, thiocynate, nitrate and selenocynate (PubMed:12488351). Reaction=iodide(out) + 2 Na(+)(out) = iodide(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71207, ChEBI:CHEBI:16382, ChEBI:CHEBI:29101; Evidence= Reaction=chlorate(out) + 2 Na(+)(out) = chlorate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71211, ChEBI:CHEBI:29101, ChEBI:CHEBI:49709; Evidence=; Reaction=2 Na(+)(out) + thiocyanate(out) = 2 Na(+)(in) + thiocyanate(in); Xref=Rhea:RHEA:71215, ChEBI:CHEBI:18022, ChEBI:CHEBI:29101; Evidence=; Reaction=2 Na(+)(out) + nitrate(out) = 2 Na(+)(in) + nitrate(in); Xref=Rhea:RHEA:71219, ChEBI:CHEBI:17632, ChEBI:CHEBI:29101; Evidence=; Reaction=2 Na(+)(out) + selenocyanate(out) = 2 Na(+)(in) + selenocyanate(in); Xref=Rhea:RHEA:71227, ChEBI:CHEBI:29101, ChEBI:CHEBI:29445; Evidence=; Dysidenin and perchlorate inhibit iodide transport activity. Kinetic parameters: KM=9 uM for iodide ; KM=12 uM for iodide ; KM=81.6 mM for sodium ; Homodimer; disulfide-linked (PubMed:20797386, PubMed:18372236, PubMed:31310151). Monomer (PubMed:20797386, PubMed:18372236, PubMed:31310151). Homooligomer (PubMed:20797386, PubMed:18372236, PubMed:31310151). Q92911; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12313867, EBI-3867333; Q92911; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12313867, EBI-22310682; Cell membrane ulti-pass membrane protein Cytoplasm Expression is primarily in thyroid tissue, but also to a lower extent in mammary gland and ovary. Expression is reduced in tumors. Up-regulated by forskolin and thyrotropin (at protein level). Glycosylated. Thyroid dyshormonogenesis 1 (TDH1) [MIM:274400]: A disorder characterized by the inability of the thyroid to maintain a concentration difference of readily exchangeable iodine between the plasma and the thyroid gland, leading to congenital hypothyroidism. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44476/SLC5A5"; nucleus plasma membrane thyroid hormone generation ion transport sodium ion transport sodium:iodide symporter activity iodide transmembrane transporter activity symporter activity iodide transport membrane integral component of membrane transmembrane transporter activity transmembrane transport extracellular exosome cellular response to cAMP cellular response to gonadotropin stimulus extracellular vesicle uc002nhr.1 uc002nhr.2 uc002nhr.3 uc002nhr.4 uc002nhr.5 
ENST00000222250.5 ARRDC2 ENST00000222250.5 arrestin domain containing 2, transcript variant 1 (from RefSeq NM_015683.2) ARRD2_HUMAN B2RBG9 ENST00000222250.1 ENST00000222250.2 ENST00000222250.3 ENST00000222250.4 NM_015683 O95895 PP2703 Q6ZRV9 Q8TBH0 Q8WYG6 uc002nhv.1 uc002nhv.2 uc002nhv.3 uc002nhv.4 Interacts with WWP1 (via WW domains). Q8TBH0; O95208-2: EPN2; NbExp=3; IntAct=EBI-12191751, EBI-12135243; Q8TBH0; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-12191751, EBI-527853; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8TBH0-1; Sequence=Displayed; Name=2; IsoId=Q8TBH0-2; Sequence=VSP_019544; Belongs to the arrestin family. plasma membrane cytoplasmic vesicle uc002nhv.1 uc002nhv.2 uc002nhv.3 uc002nhv.4 
ENST00000222254.13 PIK3R2 ENST00000222254.13 phosphoinositide-3-kinase regulatory subunit 2, transcript variant 2 (from RefSeq NR_073517.2) ENST00000222254.1 ENST00000222254.10 ENST00000222254.11 ENST00000222254.12 ENST00000222254.2 ENST00000222254.3 ENST00000222254.4 ENST00000222254.5 ENST00000222254.6 ENST00000222254.7 ENST00000222254.8 ENST00000222254.9 NR_073517 O00459 P85B_HUMAN Q5EAT5 Q9UPH9 uc002nia.1 uc002nia.2 uc002nia.3 uc002nia.4 Phosphatidylinositol 3-kinase (PI3K) is a lipid kinase that phosphorylates phosphatidylinositol and similar compounds, creating second messengers important in growth signaling pathways. PI3K functions as a heterodimer of a regulatory and a catalytic subunit. The protein encoded by this gene is a regulatory component of PI3K. Three transcript variants, one protein coding and the other two non-protein coding, have been found for this gene. [provided by RefSeq, Apr 2019]. Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5- bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein- tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (PubMed:23604317). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin- dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity). Heterodimer of a regulatory subunit PIK3R2 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD) (PubMed:23604317). Interacts with AXL (PubMed:9178760). Interacts with FLT1 (tyrosine- phosphorylated) and FLT4 (tyrosine-phosphorylated) (PubMed:9600074, PubMed:15102829). Interacts with NYAP1, NYAP2 and MYO16 (By similarity). Interacts with FBXL2; PIK3R2 is a substrate of the SCF(FBXL2) complex (PubMed:23604317). Interacts with PTPN13; dephosphorylates PIK3R2 (PubMed:23604317). Interacts with XBP1 isoform 2; the interaction is direct and induces translocation of XBP1 isoform 2 into the nucleus in a ER stress- and/or insulin-dependent but PI3K- independent manner (By similarity). Interacts with PIK3R1; the interaction is dissociated in an insulin-dependent manner (By similarity). Interacts with SRC (PubMed:28903391). O00459; P10275: AR; NbExp=14; IntAct=EBI-346930, EBI-608057; O00459; P22681: CBL; NbExp=4; IntAct=EBI-346930, EBI-518228; O00459; G5E9A7: DMWD; NbExp=3; IntAct=EBI-346930, EBI-10976677; O00459; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-346930, EBI-740680; O00459; P00533: EGFR; NbExp=5; IntAct=EBI-346930, EBI-297353; O00459; P04626: ERBB2; NbExp=7; IntAct=EBI-346930, EBI-641062; O00459; P21860: ERBB3; NbExp=16; IntAct=EBI-346930, EBI-720706; O00459; Q13480: GAB1; NbExp=23; IntAct=EBI-346930, EBI-517684; O00459; Q08379: GOLGA2; NbExp=3; IntAct=EBI-346930, EBI-618309; O00459; P62993: GRB2; NbExp=4; IntAct=EBI-346930, EBI-401755; O00459; P42858: HTT; NbExp=6; IntAct=EBI-346930, EBI-466029; O00459; P08069: IGF1R; NbExp=3; IntAct=EBI-346930, EBI-475981; O00459; Q9UKT9: IKZF3; NbExp=4; IntAct=EBI-346930, EBI-747204; O00459; P10721: KIT; NbExp=19; IntAct=EBI-346930, EBI-1379503; O00459; P19012: KRT15; NbExp=3; IntAct=EBI-346930, EBI-739566; O00459; P35900: KRT20; NbExp=3; IntAct=EBI-346930, EBI-742094; O00459; O76015: KRT38; NbExp=5; IntAct=EBI-346930, EBI-1047263; O00459; P08581: MET; NbExp=11; IntAct=EBI-346930, EBI-1039152; O00459; Q96HT8: MRFAP1L1; NbExp=4; IntAct=EBI-346930, EBI-748896; O00459; P42336: PIK3CA; NbExp=48; IntAct=EBI-346930, EBI-2116585; O00459; P42338: PIK3CB; NbExp=5; IntAct=EBI-346930, EBI-2609540; O00459; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-346930, EBI-726876; O00459; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-346930, EBI-5235340; O00459; P36406: TRIM23; NbExp=3; IntAct=EBI-346930, EBI-740098; O00459; P03496: NS; Xeno; NbExp=13; IntAct=EBI-346930, EBI-2547442; O00459; Q82506: NS; Xeno; NbExp=2; IntAct=EBI-346930, EBI-6149498; The SH2 2 domain is required for interaction with FBXL2 and PTPN13. Phosphorylated in response to signaling from activated receptor- type protein kinases (PubMed:19690332, PubMed:20068231). Dephosphorylated by PTPRJ (PubMed:18348712). Dephosphorylated at Tyr- 655 by PTPN13. Phosphorylation of Tyr-655 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)- mediated polyubiquitination (PubMed:23604317). Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex probably promotes proteasomal degradation of PIK3R2. Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 1 (MPPH1) [MIM:603387]: A syndrome characterized by megalencephaly, hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly-capillary malformation syndrome. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the PI3K p85 subunit family. cellular glucose homeostasis phosphotyrosine binding protein binding nucleus cytosol phosphatidylinositol 3-kinase complex phosphatidylinositol biosynthetic process signal transduction insulin receptor signaling pathway regulation of autophagy phosphatidylinositol 3-kinase signaling protein transport protein phosphatase binding receptor tyrosine kinase binding cellular response to insulin stimulus response to endoplasmic reticulum stress Fc-epsilon receptor signaling pathway Fc-gamma receptor signaling pathway involved in phagocytosis positive regulation of protein import into nucleus negative regulation of MAPK cascade regulation of phosphatidylinositol 3-kinase activity positive regulation of transcription from RNA polymerase II promoter phosphatidylinositol phosphorylation 1-phosphatidylinositol-3-kinase regulator activity protein heterodimerization activity vascular endothelial growth factor receptor signaling pathway phosphatidylinositol-mediated signaling T cell receptor signaling pathway leukocyte migration regulation of small GTPase mediated signal transduction positive regulation of protein kinase B signaling uc002nia.1 uc002nia.2 uc002nia.3 uc002nia.4 
ENST00000222256.9 RAB3A ENST00000222256.9 RAB3A, member RAS oncogene family (from RefSeq NM_002866.5) A8K0J4 ENST00000222256.1 ENST00000222256.2 ENST00000222256.3 ENST00000222256.4 ENST00000222256.5 ENST00000222256.6 ENST00000222256.7 ENST00000222256.8 NM_002866 P20336 Q9NYE1 RAB3A_HUMAN uc002nie.1 uc002nie.2 uc002nie.3 uc002nie.4 Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (By similarity). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 or RPH3AL effectors in pancreatic beta cells (By similarity). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (PubMed:27325790). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (PubMed:22248876, PubMed:30599141). Also plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity). Interacts with MADD (via uDENN domain); the GTP-bound form is preferred for interaction (By similarity). Interacts with RIMS1 and RIMS2 (By similarity). Interacts with Rabphilin-3A/RPH3A and Rab effector Noc2/RPH3AL (By similarity). Interacts with SYTL4 (By similarity). Interacts with RAB3IP (By similarity). Interacts with SGSM1 and SGSM3 (By similarity). Interacts with SYT1 (By similarity). Interacts with MYH9; this interaction is essential for lysosome exocytosis and plasma membrane repair (PubMed:27325790). Interacts with STXBP1; this interaction promotes RAB3A dissociation from the vesicle membrane (By similarity). Interacts with SNCA (PubMed:15207266). Interacts with GDI1, GDI2, CHM and CHML; phosphorylation at Thr-86 disrupts these interactions (PubMed:29125462). P20336; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1045943, EBI-10171774; P20336; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-1045943, EBI-743796; P20336; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-1045943, EBI-747844; P20336; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-1045943, EBI-11984839; P20336; P47224: RABIF; NbExp=9; IntAct=EBI-1045943, EBI-713992; P20336; Q9H8Y1: VRTN; NbExp=5; IntAct=EBI-1045943, EBI-12894399; Cytoplasm, cytosol Lysosome Cytoplasmic vesicle, secretory vesicle Cell projection, axon Cell membrane ; Lipid-anchor ; Cytoplasmic side Presynapse Postsynapse Note=Cycles between a vesicle- associated GTP-bound form and a cytosolic GDP-bound form. Specifically expressed in brain. Phosphorylation of Thr-86 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2. Belongs to the small GTPase superfamily. Rab family. nucleotide binding acrosomal vesicle ATPase activator activity plasma membrane repair respiratory system process GTPase activity protein binding GTP binding cytoplasm lysosome endosome cytosol plasma membrane intracellular protein transport exocytosis vesicle docking involved in exocytosis mitochondrion organization neurotransmitter secretion neuromuscular synaptic transmission axonogenesis synaptic vesicle protein C-terminus binding protein secretion post-embryonic development regulation of synaptic vesicle priming glutamate secretion protein transport membrane synaptic vesicle exocytosis synaptic vesicle maturation calcium ion regulated exocytosis regulation of exocytosis transport vesicle secretory granule lung development axon secretory granule membrane GTP-dependent protein binding cytoplasmic vesicle myosin V binding regulation of synaptic vesicle fusion to presynaptic membrane vesicle lysosome localization Rab protein signal transduction positive regulation of ATPase activity macromolecular complex synaptic vesicle recycling terminal bouton intracellular organelle neutrophil degranulation post-translational protein modification constitutive secretory pathway regulated exocytosis positive regulation of exocytosis regulation of short-term neuronal synaptic plasticity perinuclear region of cytoplasm synaptic vesicle transport presynaptic active zone maintenance of presynaptic active zone structure sensory perception of touch GDP-dissociation inhibitor binding ATPase binding response to electrical stimulus clathrin-sculpted acetylcholine transport vesicle membrane clathrin-sculpted glutamate transport vesicle membrane acrosomal vesicle exocytosis clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane evoked neurotransmitter secretion clathrin-sculpted monoamine transport vesicle membrane protein localization to plasma membrane synaptic vesicle clustering anchored component of synaptic vesicle membrane positive regulation of regulated secretory pathway extracellular vesicle regulation of plasma membrane repair regulation of synaptic vesicle exocytosis uc002nie.1 uc002nie.2 uc002nie.3 uc002nie.4 
ENST00000222271.7 COMP ENST00000222271.7 cartilage oligomeric matrix protein (from RefSeq NM_000095.3) B4DKJ3 COMP COMP_HUMAN ENST00000222271.1 ENST00000222271.2 ENST00000222271.3 ENST00000222271.4 ENST00000222271.5 ENST00000222271.6 NM_000095 O14592 P49747 Q16388 Q16389 Q2NL86 Q8N4T2 uc002nke.1 uc002nke.2 uc002nke.3 uc002nke.4 uc002nke.5 The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein. It consists of five identical glycoprotein subunits, each with EGF-like and calcium-binding (thrombospondin-like) domains. Oligomerization results from formation of a five-stranded coiled coil and disulfides. Binding to other ECM proteins such as collagen appears to depend on divalent cations. Contraction or expansion of a 5 aa aspartate repeat and other mutations can cause pseudochondroplasia (PSACH) and multiple epiphyseal dysplasia (MED). [provided by RefSeq, Jul 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK223216.1, SRR1660809.75424.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2467144 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222271.7/ ENSP00000222271.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors (PubMed:16542502, PubMed:16051604). Could play a role in the pathogenesis of osteoarthritis (PubMed:16542502). Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (PubMed:17993464). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity). Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence= Note=Binds 11-14 calcium ions per subunit. ; Pentamer; disulfide-linked (PubMed:32686688). Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium (PubMed:19276170). Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca(2+), Mg(2+) or Mn(2+)). The greatest amount of binding is seen in the presence of Mn(2+) (PubMed:16051604, PubMed:12225811). Interacts with MATN1, MATN3, MATN4 and ACAN (PubMed:15075323, PubMed:17588949). Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate (PubMed:17588949). Interacts with collagen I, II and IX, and interaction with these collagens is dependent on the presence of zinc ions (PubMed:11084047). Interacts with ADAMTS12 (PubMed:16611630). Interacts with ITGA7 (By similarity). P49747; P58397: ADAMTS12; NbExp=3; IntAct=EBI-2531022, EBI-9028051; P49747; P29972: AQP1; NbExp=3; IntAct=EBI-2531022, EBI-745213; P49747; O00244: ATOX1; NbExp=3; IntAct=EBI-2531022, EBI-10179267; P49747; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2531022, EBI-3867333; P49747; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2531022, EBI-16439278; P49747; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-2531022, EBI-1210753; P49747; P32242: OTX1; NbExp=7; IntAct=EBI-2531022, EBI-740446; P49747; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2531022, EBI-744081; P49747; P13608: ACAN; Xeno; NbExp=2; IntAct=EBI-2531022, EBI-6259246; Secreted, extracellular space, extracellular matrix Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49747-1; Sequence=Displayed; Name=2; IsoId=P49747-2; Sequence=VSP_055758; Abundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. Increased amounts are produced during late stages of osteoarthritis in the area adjacent to the main defect. Present during the earliest stages of limb maturation and is later found in regions where the joints develop. The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response. The TSP C-terminal domain mediates interaction with FN1 and ACAN. Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions. Multiple epiphyseal dysplasia 1 (EDM1) [MIM:132400]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. te=The disease is caused by variants affecting the gene represented in this entry. Pseudoachondroplasia (PSACH) [MIM:177170]: A skeletal dysplasia usually manifesting in the second year of life and characterized by moderate to severe disproportionate short stature, deformity of the lower limbs, brachydactyly, ligamentous laxity, and degenerative joint disease. te=The disease is caused by variants affecting the gene represented in this entry. Carpal tunnel syndrome 2 (CTS2) [MIM:619161]: An autosomal dominant form of carpal tunnel syndrome, a condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the thrombospondin family. Sequence=AAB86501.1; Type=Erroneous gene model prediction; Evidence=; skeletal system development ossification protease binding chondrocyte development endochondral bone growth growth plate cartilage development integrin binding extracellular matrix structural constituent calcium ion binding protein binding collagen binding extracellular region extracellular space apoptotic process response to unfolded protein cell adhesion blood coagulation heparin binding protein secretion animal organ morphogenesis multicellular organism aging animal organ senescence regulation of gene expression vascular smooth muscle contraction protein processing extracellular matrix organization collagen fibril organization bone mineralization regulation of bone mineralization BMP signaling pathway extracellular matrix macromolecular complex multicellular organism growth chondrocyte proliferation tendon development BMP binding negative regulation of apoptotic process proteoglycan binding heparan sulfate proteoglycan binding skin development muscle fiber development artery morphogenesis musculoskeletal movement neuromuscular process cartilage development limb development bone morphogenesis extracellular exosome platelet aggregation vascular smooth muscle cell development bone growth negative regulation of hemostasis positive regulation of chondrocyte proliferation uc002nke.1 uc002nke.2 uc002nke.3 uc002nke.4 uc002nke.5 
ENST00000222275.3 UPK1A ENST00000222275.3 uroplakin 1A, transcript variant 1 (from RefSeq NM_007000.4) ENST00000222275.1 ENST00000222275.2 NM_007000 O00322 Q3KNU5 Q3KNU6 TSPAN21 UPK1A_HUMAN uc060xgs.1 uc060xgs.2 The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is found in the asymmetrical unit membrane (AUM) where it can complex with other transmembrane 4 superfamily proteins. It may play a role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions. The protein may also play a role in tumor suppression. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jul 2013]. Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). Homodimer; disulfide-linked. Interacts with uroplakin-2 (UPK2) (By similarity). O00322; P35247: SFTPD; NbExp=3; IntAct=EBI-14031976, EBI-11316157; O00322; P08191: fimH; Xeno; NbExp=2; IntAct=EBI-14031976, EBI-1028015; Membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O00322-1; Sequence=Displayed; Name=2; IsoId=O00322-2; Sequence=VSP_030005; High expression restricted to ureteric urothelium (most superficial cells); low expression in prostate. Expression in normal urothelial cells is lost in culture. Some expression in tumor cell lines derived from urothelial malignancies. Belongs to the tetraspanin (TM4SF) family. protein binding endoplasmic reticulum plasma membrane integral component of plasma membrane cell surface membrane integral component of membrane apical plasma membrane epithelial cell differentiation protein homodimerization activity protein oligomerization extracellular exosome uc060xgs.1 uc060xgs.2 
ENST00000222284.10 TMEM147 ENST00000222284.10 transmembrane protein 147, transcript variant 1 (from RefSeq NM_032635.4) A8MWW0 ENST00000222284.1 ENST00000222284.2 ENST00000222284.3 ENST00000222284.4 ENST00000222284.5 ENST00000222284.6 ENST00000222284.7 ENST00000222284.8 ENST00000222284.9 NM_032635 O75790 Q9BVK8 TM147_HUMAN TMEM147 uc002oaj.1 uc002oaj.2 uc002oaj.3 uc002oaj.4 Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (PubMed:32820719, PubMed:36261522). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (PubMed:36261522). Also acts as a negative regulator of CHRM3 function, most likely by interfering with its trafficking to the cell membrane (PubMed:21056967). Negatively regulates CHRM3-mediated calcium mobilization and activation of RPS6KA1/p90RSK activity (PubMed:21056967). Regulates LBR localization to the nucleus inner membrane (PubMed:32694168). Component of the back of Sec61 (BOS) complex, composed of NCLN/Nicalin, NOMO (NOMO1, NOMO2 or NOMO3) and TMEM147 (PubMed:20538592, PubMed:36261522). The BOS complex is part of the multi-pass translocon (MPT) complex, composed of three subcomplexes, the GEL complex (composed of RAB5IF/OPTI and TMCO1), the BOS complex (composed of NCLN/Nicalin, NOMO and TMEM147) and the PAT complex (composed of WDR83OS/Asterix and CCDC47) (PubMed:32820719, PubMed:36261522). The MPT complex associates with the SEC61 complex (PubMed:32820719, PubMed:36261522). Interacts with CHRM3, CHRM1 and AVPR2 (PubMed:21056967). Interacts with LBR; promoting LBR localization to the nucleus inner membrane (PubMed:32694168). Interacts with DHCR7 (PubMed:32694168). Q9BVK8; O95870: ABHD16A; NbExp=4; IntAct=EBI-348587, EBI-348517; Q9BVK8; P25942: CD40; NbExp=3; IntAct=EBI-348587, EBI-525714; Q9BVK8; P11912: CD79A; NbExp=3; IntAct=EBI-348587, EBI-7797864; Q9BVK8; O95471: CLDN7; NbExp=3; IntAct=EBI-348587, EBI-740744; Q9BVK8; P58418: CLRN1; NbExp=3; IntAct=EBI-348587, EBI-17274839; Q9BVK8; Q96BA8: CREB3L1; NbExp=9; IntAct=EBI-348587, EBI-6942903; Q9BVK8; P25025: CXCR2; NbExp=3; IntAct=EBI-348587, EBI-2835281; Q9BVK8; Q9P2X0-2: DPM3; NbExp=3; IntAct=EBI-348587, EBI-10962476; Q9BVK8; Q15125: EBP; NbExp=3; IntAct=EBI-348587, EBI-3915253; Q9BVK8; P52798: EFNA4; NbExp=3; IntAct=EBI-348587, EBI-5241592; Q9BVK8; Q9Y6X5: ENPP4; NbExp=3; IntAct=EBI-348587, EBI-17442870; Q9BVK8; Q9Y624: F11R; NbExp=3; IntAct=EBI-348587, EBI-742600; Q9BVK8; O15552: FFAR2; NbExp=3; IntAct=EBI-348587, EBI-2833872; Q9BVK8; P48165: GJA8; NbExp=3; IntAct=EBI-348587, EBI-17458373; Q9BVK8; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-348587, EBI-712073; Q9BVK8; Q96P66: GPR101; NbExp=3; IntAct=EBI-348587, EBI-17935713; Q9BVK8; O60883: GPR37L1; NbExp=3; IntAct=EBI-348587, EBI-2927498; Q9BVK8; O15529: GPR42; NbExp=3; IntAct=EBI-348587, EBI-18076404; Q9BVK8; Q9BZJ8: GPR61; NbExp=3; IntAct=EBI-348587, EBI-12808020; Q9BVK8; P28335: HTR2C; NbExp=4; IntAct=EBI-348587, EBI-994141; Q9BVK8; P26951: IL3RA; NbExp=3; IntAct=EBI-348587, EBI-1757512; Q9BVK8; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-348587, EBI-749265; Q9BVK8; Q5T700: LDLRAD1; NbExp=7; IntAct=EBI-348587, EBI-10173166; Q9BVK8; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-348587, EBI-17490413; Q9BVK8; Q6ZUX7: LHFPL2; NbExp=3; IntAct=EBI-348587, EBI-17566767; Q9BVK8; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-348587, EBI-3923617; Q9BVK8; P15941-11: MUC1; NbExp=3; IntAct=EBI-348587, EBI-17263240; Q9BVK8; Q9H813: PACC1; NbExp=4; IntAct=EBI-348587, EBI-4319734; Q9BVK8; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-348587, EBI-16427978; Q9BVK8; P15151: PVR; NbExp=3; IntAct=EBI-348587, EBI-3919694; Q9BVK8; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-348587, EBI-1056589; Q9BVK8; Q96GF1: RNF185; NbExp=3; IntAct=EBI-348587, EBI-2340249; Q9BVK8; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-348587, EBI-4403649; Q9BVK8; A0PJX4: SHISA3; NbExp=3; IntAct=EBI-348587, EBI-10171518; Q9BVK8; Q14973: SLC10A1; NbExp=3; IntAct=EBI-348587, EBI-3923031; Q9BVK8; Q9Y666-2: SLC12A7; NbExp=3; IntAct=EBI-348587, EBI-12854384; Q9BVK8; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-348587, EBI-12808018; Q9BVK8; Q96L08: SUSD3; NbExp=3; IntAct=EBI-348587, EBI-18194029; Q9BVK8; Q8N205: SYNE4; NbExp=3; IntAct=EBI-348587, EBI-7131783; Q9BVK8; P25103: TACR1; NbExp=3; IntAct=EBI-348587, EBI-6655287; Q9BVK8; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-348587, EBI-19027521; Q9BVK8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-348587, EBI-8638294; Q9BVK8; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-348587, EBI-10982110; Q9BVK8; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-348587, EBI-10314986; Q9BVK8; Q8N6L7: TMEM252; NbExp=3; IntAct=EBI-348587, EBI-8787626; Q9BVK8; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-348587, EBI-12038591; Q9BVK8; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-348587, EBI-18178701; Q9BVK8; O95859: TSPAN12; NbExp=3; IntAct=EBI-348587, EBI-2466403; Endoplasmic reticulum membrane ulti-pass membrane protein Nucleus membrane ; Multi- pass membrane protein Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BVK8-1; Sequence=Displayed; Name=2; IsoId=Q9BVK8-2; Sequence=VSP_047210; Neurodevelopmental disorder with facial dysmorphism, absent language, and pseudo-Pelger-Huet anomaly (NEDFLPH) [MIM:620075]: An autosomal recessive disorder with onset in infancy and characterized by global developmental delay, intellectual disability, dysmorphic facial features, coarse facies, and behavioral problems. Affected individuals may have variable findings on brain imaging, such as cortical atrophy, thin corpus callosum and enlarged ventricles. Laboratory studies show nuclear lobulation defects in a subset of neutrophils, indicating a pseudo-Pelger-Huet anomaly. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TMEM147 family. Sequence=BG697070; Type=Frameshift; Evidence=; protein binding endoplasmic reticulum endoplasmic reticulum membrane membrane integral component of membrane macromolecular complex uc002oaj.1 uc002oaj.2 uc002oaj.3 uc002oaj.4 
ENST00000222286.9 GAPDHS ENST00000222286.9 glyceraldehyde-3-phosphate dehydrogenase, spermatogenic (from RefSeq NM_014364.5) B2RC82 ENST00000222286.1 ENST00000222286.2 ENST00000222286.3 ENST00000222286.4 ENST00000222286.5 ENST00000222286.6 ENST00000222286.7 ENST00000222286.8 G3PT_HUMAN GAPD2 GAPDH2 GAPDS HSD-35 HSD35 NM_014364 O14556 O60823 Q6JTT9 Q9HCU6 uc002oaf.1 uc002oaf.2 uc002oaf.3 This gene encodes a protein belonging to the glyceraldehyde-3-phosphate dehydrogenase family of enzymes that play an important role in carbohydrate metabolism. Like its somatic cell counterpart, this sperm-specific enzyme functions in a nicotinamide adenine dinucleotide-dependent manner to remove hydrogen and add phosphate to glyceraldehyde 3-phosphate to form 1,3-diphosphoglycerate. During spermiogenesis, this enzyme may play an important role in regulating the switch between different energy-producing pathways, and it is required for sperm motility and male fertility. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189667.262758.1, SRR5189667.118236.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222286.9/ ENSP00000222286.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity). Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3- phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence=; Carbohydrate degradation; glycolysis; pyruvate from D- glyceraldehyde 3-phosphate: step 1/5. Homotetramer. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. O14556; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1057431, EBI-746595; Cytoplasm Testis specific. The testis-specific N-terminal extension mediates tight association with the cytoskeletal fibrous sheath of the spermatozoa flagellum, possibly via interchain disulfide-bonding of Cys-21 with sheath components. Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity protein binding nucleus cytoplasm cytosol glucose metabolic process gluconeogenesis glycolytic process oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor flagellated sperm motility positive regulation of glycolytic process NADP binding NAD binding oxidation-reduction process canonical glycolysis uc002oaf.1 uc002oaf.2 uc002oaf.3 
ENST00000222304.5 HAMP ENST00000222304.5 hepcidin antimicrobial peptide (from RefSeq NM_021175.4) ENST00000222304.1 ENST00000222304.2 ENST00000222304.3 ENST00000222304.4 HAMP HEPC HEPC_HUMAN LEAP1 NM_021175 P81172 Q1HE14 Q9BY68 UNQ487/PRO1003 uc060xaz.1 uc060xaz.2 uc060xaz.3 The product encoded by this gene is involved in the maintenance of iron homeostasis, and it is necessary for the regulation of iron storage in macrophages, and for intestinal iron absorption. The preproprotein is post-translationally cleaved into mature peptides of 20, 22 and 25 amino acids, and these active peptides are rich in cysteines, which form intramolecular bonds that stabilize their beta-sheet structures. These peptides exhibit antimicrobial activity against bacteria and fungi. Mutations in this gene cause hemochromatosis type 2B, also known as juvenile hemochromatosis, a disease caused by severe iron overload that results in cardiomyopathy, cirrhosis, and endocrine failure. [provided by RefSeq, Oct 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC020612.1, BP346863.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222304.5/ ENSP00000222304.2 Protein has antimicrobial activity :: PMID: 11034317 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin/SLC40A1, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma (PubMed:22682227, PubMed:29237594, PubMed:32814342). Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes (PubMed:22306005). Has strong antimicrobial activity against E.coli ML35P N.cinerea and weaker against S.epidermidis, S.aureus and group b streptococcus bacteria. Active against the fungus C.albicans. No activity against P.aeruginosa (PubMed:11113131, PubMed:11034317). Interacts with SLC40A1; this interaction promotes SLC40A1 rapid ubiquitination. Secreted Highest expression in liver and to a lesser extent in heart and brain. Low levels in lung, tonsils, salivary gland, trachea, prostate gland, adrenal gland and thyroid gland. Secreted into the urine and blood (PubMed:11034317). Expressed by hepatocytes (PubMed:15124018). Expression in hepatocytes is induced by LPS stimulus and the induction is mediated by IL6 (PubMed:15124018). Expression is inhibited in presence of TNF (PubMed:15124018). [Hepcidin-25]: Mass=2789.8; Method=MALDI; Evidence=; Hemochromatosis 2B (HFE2B) [MIM:613313]: A juvenile form of hemochromatosis, a disorder of iron metabolism with excess deposition of iron in a variety of organs leading to their failure, bronze skin pigmentation, hepatic cirrhosis, arthropathy and diabetes. The most common symptoms of juvenile hemochromatosis at presentation are hypogonadism and cardiomyopathy. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the hepcidin family. Name=Wikipedia; Note=Hepcidin entry; URL="https://en.wikipedia.org/wiki/Hepcidin"; negative regulation of transcription from RNA polymerase II promoter positive regulation of receptor internalization receptor binding hormone activity extracellular region extracellular space cell cytoplasm cellular iron ion homeostasis acute-phase response immune response signal transduction aging response to iron ion response to zinc ion intercalated disc killing of cells of other organism negative regulation of ion transmembrane transporter activity response to vitamin A negative regulation of iron ion transmembrane transport response to erythropoietin defense response to bacterium apical cortex response to ethanol defense response to Gram-negative bacterium defense response to Gram-positive bacterium defense response to fungus multicellular organismal iron ion homeostasis positive regulation of cell growth involved in cardiac muscle cell development cellular response to lipopolysaccharide cellular response to interleukin-6 cellular response to tumor necrosis factor cellular response to X-ray liver regeneration iron channel inhibitor activity positive regulation of protein polyubiquitination cellular response to bile acid negative regulation of ferrous iron export negative regulation of iron channel activity negative regulation of intestinal absorption response to iron ion starvation positive regulation of receptor catabolic process uc060xaz.1 uc060xaz.2 uc060xaz.3 
ENST00000222305.8 USF2 ENST00000222305.8 upstream transcription factor 2, c-fos interacting, transcript variant 1 (from RefSeq NM_003367.4) BHLHB12 ENST00000222305.1 ENST00000222305.2 ENST00000222305.3 ENST00000222305.4 ENST00000222305.5 ENST00000222305.6 ENST00000222305.7 NM_003367 O00671 O00709 Q05750 Q07952 Q15851 Q15852 Q15853 Q6FI33 Q6YI47 USF2_HUMAN uc002nyq.1 uc002nyq.2 uc002nyq.3 This gene encodes a member of the basic helix-loop-helix leucine zipper family of transcription factors. The encoded protein can activate transcription through pyrimidine-rich initiator (Inr) elements and E-box motifs and is involved in regulating multiple cellular processes. [provided by RefSeq, Mar 2016]. Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. Interacts with MAF (By similarity). Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer (USF1/USF2). In vivo, the USF1/USF2A heterodimer represents over 66% of the usf binding activity whereas the USF1 and USF2A homodimers represent less than 10%. The USF1/USF2B heterodimer accounted for almost 15% in some cell. Q15853; Q6FG41: FOS; NbExp=3; IntAct=EBI-1055994, EBI-10198738; Q15853; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1055994, EBI-741037; Q15853; Q15562: TEAD2; NbExp=3; IntAct=EBI-1055994, EBI-6427252; Nucleus. Event=Alternative splicing; Named isoforms=4; Comment=Additional isoforms seem to exist.; Name=USF2A; IsoId=Q15853-1; Sequence=Displayed; Name=USF2A-delta-H; IsoId=Q15853-2; Sequence=VSP_002165; Name=USF2B; IsoId=Q15853-3; Sequence=VSP_002164; Name=USF2c; IsoId=Q15853-4; Sequence=VSP_047804; Ubiquitous. [Isoform USF2c]: Can bind as a homodimer to the E-box of the cathepsin B (CTSB) promoter. regulation of transcription from RNA polymerase II promoter by glucose positive regulation of transcription from RNA polymerase II promoter by glucose nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm regulation of transcription from RNA polymerase II promoter transcription from RNA polymerase II promoter lactation late viral transcription protein homodimerization activity intracellular membrane-bounded organelle bHLH transcription factor binding sequence-specific DNA binding positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity protein dimerization activity lipid homeostasis uc002nyq.1 uc002nyq.2 uc002nyq.3 
ENST00000222307.9 KXD1 ENST00000222307.9 KxDL motif containing 1, transcript variant 2 (from RefSeq NM_024069.4) C19orf50 ENST00000222307.1 ENST00000222307.2 ENST00000222307.3 ENST00000222307.4 ENST00000222307.5 ENST00000222307.6 ENST00000222307.7 ENST00000222307.8 KXDL1_HUMAN NM_024069 O76098 Q9BQD3 uc002njo.1 uc002njo.2 uc002njo.3 uc002njo.4 uc002njo.5 As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167). May be involved in the biogenesis of lysosome- related organelles such as melanosomes (By similarity). Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (PubMed:25898167). Associates with the BLOC-1 complex. Interacts with BLOC1S1. Interacts with DTNBP1/BLOC1S7 (via coiled-coil domain) (By similarity). Q9BQD3; Q99819: ARHGDIG; NbExp=3; IntAct=EBI-739657, EBI-10295284; Q9BQD3; Q96GS4: BORCS6; NbExp=4; IntAct=EBI-739657, EBI-10193358; Q9BQD3; Q504U0: C4orf46; NbExp=6; IntAct=EBI-739657, EBI-6657981; Q9BQD3; Q96LK0: CEP19; NbExp=7; IntAct=EBI-739657, EBI-741885; Q9BQD3; Q92630: DYRK2; NbExp=3; IntAct=EBI-739657, EBI-749432; Q9BQD3; Q14241: ELOA; NbExp=3; IntAct=EBI-739657, EBI-742350; Q9BQD3; O00471: EXOC5; NbExp=3; IntAct=EBI-739657, EBI-949824; Q9BQD3; Q9UPT5-1: EXOC7; NbExp=3; IntAct=EBI-739657, EBI-6251402; Q9BQD3; Q9H0R8: GABARAPL1; NbExp=4; IntAct=EBI-739657, EBI-746969; Q9BQD3; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-739657, EBI-2514791; Q9BQD3; Q8IY31: IFT20; NbExp=5; IntAct=EBI-739657, EBI-744203; Q9BQD3; Q8WYH8: ING5; NbExp=4; IntAct=EBI-739657, EBI-488533; Q9BQD3; Q14533: KRT81; NbExp=2; IntAct=EBI-739657, EBI-739648; Q9BQD3; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-739657, EBI-739832; Q9BQD3; Q96CN5: LRRC45; NbExp=4; IntAct=EBI-739657, EBI-2805176; Q9BQD3; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-739657, EBI-10268010; Q9BQD3; Q9H492: MAP1LC3A; NbExp=6; IntAct=EBI-739657, EBI-720768; Q9BQD3; Q9GZQ8: MAP1LC3B; NbExp=4; IntAct=EBI-739657, EBI-373144; Q9BQD3; Q96EZ8: MCRS1; NbExp=4; IntAct=EBI-739657, EBI-348259; Q9BQD3; Q9H8S9: MOB1A; NbExp=4; IntAct=EBI-739657, EBI-748229; Q9BQD3; P12883: MYH7; NbExp=3; IntAct=EBI-739657, EBI-519141; Q9BQD3; Q9UJ41: RABGEF1; NbExp=2; IntAct=EBI-739657, EBI-913954; Q9BQD3; P32969: RPL9P9; NbExp=3; IntAct=EBI-739657, EBI-358122; Q9BQD3; Q15560: TCEA2; NbExp=3; IntAct=EBI-739657, EBI-710310; Q9BQD3; P09493: TPM1; NbExp=4; IntAct=EBI-739657, EBI-351158; Q9BQD3; P09493-5: TPM1; NbExp=3; IntAct=EBI-739657, EBI-10196387; Q9BQD3; P09493-10: TPM1; NbExp=7; IntAct=EBI-739657, EBI-12123928; Q9BQD3; P06753: TPM3; NbExp=11; IntAct=EBI-739657, EBI-355607; Q9BQD3; Q5VU62: TPM3; NbExp=3; IntAct=EBI-739657, EBI-10184033; Q9BQD3; Q8TAU3: ZNF417; NbExp=6; IntAct=EBI-739657, EBI-740727; Lysosome membrane Belongs to the KXD1 family. Sequence=AAC25583.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; protein binding lysosome lysosomal membrane membrane vesicle-mediated transport BLOC-1 complex lysosome localization BORC complex uc002njo.1 uc002njo.2 uc002njo.3 uc002njo.4 uc002njo.5 
ENST00000222329.9 ERF ENST00000222329.9 ETS2 repressor factor, transcript variant 1 (from RefSeq NM_006494.4) B2RAP1 B7Z4R0 ENST00000222329.1 ENST00000222329.2 ENST00000222329.3 ENST00000222329.4 ENST00000222329.5 ENST00000222329.6 ENST00000222329.7 ENST00000222329.8 ERF_HUMAN NM_006494 P50548 Q59G38 Q9UPI7 uc002ote.1 uc002ote.2 uc002ote.3 uc002ote.4 uc002ote.5 uc002ote.6 ETS2 is a transcription factor and protooncogene involved in development, apoptosis, and the regulation of telomerase. The protein encoded by this gene binds to the ETS2 promoter and is a strong repressor of ETS2 transcription. Several transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Aug 2015]. Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity). May be important for regulating trophoblast stem cell differentiation (By similarity). P50548; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-8465203, EBI-348259; P50548; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-8465203, EBI-16439278; P50548; Q08117-2: TLE5; NbExp=3; IntAct=EBI-8465203, EBI-11741437; P50548; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-8465203, EBI-527853; Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P50548-1; Sequence=Displayed; Name=2; IsoId=P50548-2; Sequence=VSP_055487; Highest levels in testis, ovary, pancreas, and heart. Phosphorylated by multiple kinases including MAPK1/ERK2 at THR- 526. Phosphorylation regulates the activity of ERF. Craniosynostosis 4 (CRS4) [MIM:600775]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability. Note=The disease is caused by variants affecting the gene represented in this entry. Chitayat syndrome (CHYTS) [MIM:617180]: An autosomal dominant syndrome characterized by hyperphalangism, partial syndactyly, bilateral accessory phalanx resulting in shortened index fingers, hallux valgus, brachydactyly, facial anomalies, diffuse bronchomalacia, and respiratory distress at birth and in infancy. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the ETS family. Sequence=BAD92508.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence=; negative regulation of transcription from RNA polymerase II promoter mitotic cell cycle nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding transcription corepressor activity nucleus nucleoplasm cytosol regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter cell differentiation sequence-specific DNA binding uc002ote.1 uc002ote.2 uc002ote.3 uc002ote.4 uc002ote.5 uc002ote.6 
ENST00000222330.8 GSK3A ENST00000222330.8 glycogen synthase kinase 3 alpha (from RefSeq NM_019884.3) ENST00000222330.1 ENST00000222330.2 ENST00000222330.3 ENST00000222330.4 ENST00000222330.5 ENST00000222330.6 ENST00000222330.7 GSK3A_HUMAN NM_019884 O14959 P49840 uc002otb.1 uc002otb.2 uc002otb.3 This gene encodes a multifunctional Ser/Thr protein kinase that is implicated in the control of several regulatory proteins including glycogen synthase, and transcription factors, such as JUN. It also plays a role in the WNT and PI3K signaling pathways, as well as regulates the production of beta-amyloid peptides associated with Alzheimer's disease. [provided by RefSeq, Oct 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC027984.1, BC051865.2 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222330.8/ ENSP00000222330.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1 (PubMed:11749387, PubMed:17478001, PubMed:19366350). Requires primed phosphorylation of the majority of its substrates (PubMed:11749387, PubMed:17478001, PubMed:19366350). Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:11749387, PubMed:17478001, PubMed:19366350). Regulates glycogen metabolism in liver, but not in muscle (By similarity). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:10868943, PubMed:17478001). In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin (PubMed:17229088). Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease (PubMed:12761548). May be involved in the regulation of replication in pancreatic beta-cells (By similarity). Is necessary for the establishment of neuronal polarity and axon outgrowth (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions which activates KAT5/TIP60 acetyltransferase activity and promotes acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti- apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (By similarity). Phosphorylates mTORC2 complex component RICTOR at 'Thr- 1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl- [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA- COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L- threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.26; Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Activated by phosphorylation at Tyr-279. In response to insulin, inhibited by phosphorylation at Ser-21 by PKB/AKT1; phosphorylation at this site causes a conformational change, preventing access of substrates to the active site. Inhibited by lithium. Monomer. Interacts with ARRB2 (By similarity). Interacts with AXIN1 and CTNNB1/beta-catenin (PubMed:17229088). Interacts with CTNND2 (PubMed:19706605). Interacts with LMBR1L (PubMed:31073040). Interacts with DDX3X (PubMed:18846110). Interacts with TNFRSF10B (PubMed:18846110). Interacts with RICTOR; the interaction results in phosphorylation of RICTOR at 'Thr-1695' by GSK3A which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). (Microbial infection) Interacts with M.tuberculosis PtpA. P49840; PRO_0000000093 [P05067]: APP; NbExp=3; IntAct=EBI-1044067, EBI-2431589; P49840; O15169: AXIN1; NbExp=3; IntAct=EBI-1044067, EBI-710484; P49840; O75398: DEAF1; NbExp=3; IntAct=EBI-1044067, EBI-718185; P49840; Q92837: FRAT1; NbExp=3; IntAct=EBI-1044067, EBI-3934879; P49840; P08238: HSP90AB1; NbExp=3; IntAct=EBI-1044067, EBI-352572; P49840; P42858: HTT; NbExp=6; IntAct=EBI-1044067, EBI-466029; P49840; O75581: LRP6; NbExp=3; IntAct=EBI-1044067, EBI-910915; P49840; P10636-8: MAPT; NbExp=2; IntAct=EBI-1044067, EBI-366233; P49840; Q14596: NBR1; NbExp=5; IntAct=EBI-1044067, EBI-742698; P49840; P62258: YWHAE; NbExp=3; IntAct=EBI-1044067, EBI-356498; P49840; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-1044067, EBI-524753; Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and deactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279. (Microbial infection) Dephosphorylated at Tyr-279 by M.tuberculosis PtpA, which leads to prevention of apoptosis during early stages of microbial infection. Higher expression and activity of GSK3A are found in the skeletal muscle (vastus lateralis) of patients with type 2 diabetes (PubMed:10868943). Several potent GSK3 (GSK3A and GSK3B) inhibitors have been identified and characterized in preclinical models for treatments of type 2 diabetes (PubMed:19366350). Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily. nucleotide binding regulation of systemic arterial blood pressure cardiac left ventricle morphogenesis protein kinase activity protein serine/threonine kinase activity receptor binding protein binding ATP binding nucleus mitochondrion cytosol carbohydrate metabolic process glycogen metabolic process protein phosphorylation signal transduction dopamine receptor signaling pathway nervous system development insulin receptor signaling pathway negative regulation of signal transduction positive regulation of autophagy positive regulation of gene expression negative regulation of UDP-glucose catabolic process Wnt signaling pathway kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation peptidyl-threonine phosphorylation protein kinase binding axon beta-catenin destruction complex positive regulation of protein ubiquitination negative regulation of TOR signaling positive regulation of proteasomal ubiquitin-dependent protein catabolic process cellular response to insulin stimulus protein kinase A catalytic subunit binding cellular response to interleukin-3 IRE1-mediated unfolded protein response neuronal cell body proteasome-mediated ubiquitin-dependent protein catabolic process negative regulation of glycogen biosynthetic process positive regulation of protein catabolic process positive regulation of heart contraction negative regulation of glucose import negative regulation of insulin receptor signaling pathway tau protein binding tau-protein kinase activity excitatory postsynaptic potential negative regulation of cell growth involved in cardiac muscle cell development regulation of microtubule cytoskeleton organization positive regulation of adrenergic receptor signaling pathway negative regulation of canonical Wnt signaling pathway extrinsic apoptotic signaling pathway extrinsic apoptotic signaling pathway in absence of ligand apical dendrite postsynapse positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway positive regulation of beta-amyloid formation regulation of mitophagy positive regulation of protein targeting to mitochondrion negative regulation of glycogen synthase activity, transferring glucose-1-phosphate proximal dendrite negative regulation of type B pancreatic cell development negative regulation of dendrite development negative regulation of glycogen (starch) synthase activity positive regulation of glycogen (starch) synthase activity uc002otb.1 uc002otb.2 uc002otb.3 
ENST00000222345.11 SIPA1L3 ENST00000222345.11 signal induced proliferation associated 1 like 3 (from RefSeq NM_015073.3) ENST00000222345.1 ENST00000222345.10 ENST00000222345.2 ENST00000222345.3 ENST00000222345.4 ENST00000222345.5 ENST00000222345.6 ENST00000222345.7 ENST00000222345.8 ENST00000222345.9 KIAA0545 NM_015073 O60292 Q2TV87 SI1L3_HUMAN SPAL3 uc002ohk.1 uc002ohk.2 uc002ohk.3 uc002ohk.4 uc002ohk.5 This gene belongs to the signal induced proliferation associated 1 family of genes, which encode GTPase-activating proteins specific for the GTP-binding protein Rap1. Rap1 has been implicated in regulation of cell adhesion, cell polarity, and organization of the cytoskeleton. Like other members of the family, the protein encoded by this gene contains RapGAP and PDZ domains. In addition, this protein contains a C-terminal leucine zipper domain. This gene is proposed to function in epithelial cell morphogenesis and establishment or maintenance of polarity. Consistently, expression of the protein in cell culture showed localization to cell-cell borders in apical regions, and downregulation of the gene in 3D Caco2 cell culture resulted in abnormal cell polarity and morphogenesis. Allelic variants of this gene have been associated with congenital cataracts in humans. [provided by RefSeq, Feb 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: BC150620.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222345.11/ ENSP00000222345.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217). O60292; P31947: SFN; NbExp=4; IntAct=EBI-2559690, EBI-476295; O60292; P63104: YWHAZ; NbExp=3; IntAct=EBI-2559690, EBI-347088; Apical cell membrane Note=Detected in tricellular junctions. Colocalizes with apical F-actin. Note=A chromosomal translocation involving SIPA1L3 is found in a patient with bilateral severe ocular abnormalities including congenital cataracts, corneal clouding, iridocorneal and lenticular adhesions and microphthalmia. Chromosomal translocation t(2;19)(q37.3;q13.1). In addition to translocation, missense variant has been found in patient with bilateral congenital cataracts (PubMed:26231217). Cataract 45 (CTRCT45) [MIM:616851]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Note=The disease is caused by variants affecting the gene represented in this entry. eye development stress fiber hematopoietic progenitor cell differentiation epithelial cell morphogenesis GTPase activator activity protein binding extracellular space plasma membrane cytoskeleton organization membrane apical plasma membrane positive regulation of GTPase activity apical part of cell regulation of small GTPase mediated signal transduction tricellular tight junction establishment of epithelial cell polarity uc002ohk.1 uc002ohk.2 uc002ohk.3 uc002ohk.4 uc002ohk.5 
ENST00000222374.3 CADM4 ENST00000222374.3 cell adhesion molecule 4 (from RefSeq NM_145296.2) B2R7L5 CADM4_HUMAN ENST00000222374.1 ENST00000222374.2 IGSF4C NECL4 NM_145296 Q8NFZ8 Q9Y4A4 TSLL2 uc002oxc.1 uc002oxc.2 uc002oxc.3 Involved in the cell-cell adhesion. Has calcium- and magnesium-independent cell-cell adhesion activity. May have tumor- suppressor activity. Monomer and homodimer. Membrane ; Single-pass type I membrane protein Expressed in brain, prostate, brain, kidney and some other organs. N-glycosylated. Belongs to the nectin family. Sequence=AAC32740.1; Type=Erroneous gene model prediction; Evidence=; regulation of protein phosphorylation negative regulation of protein phosphorylation cell adhesion negative regulation of peptidyl-threonine phosphorylation membrane integral component of membrane protein phosphatase binding negative regulation of vascular endothelial growth factor receptor signaling pathway receptor tyrosine kinase binding cell leading edge regulation of Rac protein signal transduction regulation of cell proliferation vascular endothelial growth factor receptor 1 binding vascular endothelial growth factor receptor 2 binding cell-cell contact zone negative regulation of peptidyl-tyrosine phosphorylation regulation of wound healing negative regulation of vascular endothelial growth factor signaling pathway regulation of cell motility uc002oxc.1 uc002oxc.2 uc002oxc.3 
ENST00000222381.8 PON1 ENST00000222381.8 paraoxonase 1 (from RefSeq NM_000446.7) B2RA40 ENST00000222381.1 ENST00000222381.2 ENST00000222381.3 ENST00000222381.4 ENST00000222381.5 ENST00000222381.6 ENST00000222381.7 NM_000446 P27169 PON PON1_HUMAN Q16052 Q6B0J6 Q9UCB1 uc003uns.1 uc003uns.2 uc003uns.3 uc003uns.4 uc003uns.5 This gene encodes a member of the paraoxonase family of enzymes and exhibits lactonase and ester hydrolase activity. Following synthesis in the kidney and liver, the enzyme is secreted into the circulation, where it binds to high density lipoprotein (HDL) particles and hydrolyzes thiolactones and xenobiotics, including paraoxon, a metabolite of the insecticide parathion. Polymorphisms in this gene may be associated with coronary artery disease and diabetic retinopathy. The gene is found in a cluster of three related paraoxonase genes on chromosome 7. [provided by RefSeq, Aug 2017]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: D84371.1, U53784.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968540, SAMEA1968832 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222381.8/ ENSP00000222381.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation. Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence= Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; Evidence= Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81; Evidence=; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; Homodimer. Heterooligomer with phosphate-binding protein (HPBP). Interacts with CLU. Secreted, extracellular space. Plasma, associated with HDL (at protein level). Expressed in liver, but not in heart, brain, placenta, lung, skeletal muscle, kidney or pancreas. Glycosylated. The signal sequence is not cleaved. Present in two forms, form B contains a disulfide bond, form A does not. The allelic form of the enzyme with Gln-192 (allozyme A) hydrolyzes paraoxon with a low turnover number and the one with Arg-192 (allozyme B) with a high turnover number. Microvascular complications of diabetes 5 (MVCD5) [MIM:612633]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Homozygosity for the Leu-55 allele is strongly associated with the development of retinal disease in diabetic patients. The preferential association of PON1 with HDL is mediated in part by its signal peptide, by binding phospholipids directly, rather than binding apo AI. The retained signal peptide may allow transfer of the protein between phospholipid surfaces. Belongs to the paraoxonase family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/pon1/"; aryldialkylphosphatase activity arylesterase activity calcium ion binding phospholipid binding extracellular region extracellular space lipid metabolic process cholesterol metabolic process response to toxic substance positive regulation of cholesterol efflux dephosphorylation hydrolase activity lipoxygenase pathway aromatic compound catabolic process response to nutrient levels positive regulation of transporter activity high-density lipoprotein particle spherical high-density lipoprotein particle protein homodimerization activity intracellular membrane-bounded organelle carboxylic acid catabolic process organophosphate catabolic process phosphatidylcholine metabolic process metal ion binding positive regulation of binding extracellular exosome response to fatty acid blood microparticle acyl-L-homoserine-lactone lactonohydrolase activity response to fluoride negative regulation of plasma lipoprotein particle oxidation uc003uns.1 uc003uns.2 uc003uns.3 uc003uns.4 uc003uns.5 
ENST00000222388.6 ABCF2-H2BK1 ENST00000222388.6 ABCF2-H2BK1 readthrough, transcript variant 2 (from RefSeq NR_160983.1) A0A090N7Y2 A0A090N7Y2_HUMAN ABCF2 ENST00000222388.1 ENST00000222388.2 ENST00000222388.3 ENST00000222388.4 ENST00000222388.5 NR_160983 tcag7.790 uc003wjo.1 uc003wjo.2 uc003wjo.3 This gene represents readthrough transcription between ABCF2 and a downstream histone H2B-like gene. [provided by RefSeq, Mar 2019]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. ##RefSeq-Attributes-START## readthrough transcript :: includes exons from GeneID 10061, 114483833 ##RefSeq-Attributes-END## Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily. The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. nucleotide binding ATP binding ATPase activity uc003wjo.1 uc003wjo.2 uc003wjo.3 
ENST00000222390.11 HGF ENST00000222390.11 hepatocyte growth factor, transcript variant 1 (from RefSeq NM_000601.6) A1L3U6 ENST00000222390.1 ENST00000222390.10 ENST00000222390.2 ENST00000222390.3 ENST00000222390.4 ENST00000222390.5 ENST00000222390.6 ENST00000222390.7 ENST00000222390.8 ENST00000222390.9 HGF_HUMAN HPTA NM_000601 P14210 Q02935 Q13494 Q14519 Q3KRB2 Q8TCE2 Q9BYL9 Q9BYM0 Q9UDU6 uc285zri.1 uc285zri.2 This gene encodes a protein that binds to the hepatocyte growth factor receptor to regulate cell growth, cell motility and morphogenesis in numerous cell and tissue types. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate alpha and beta chains, which form the mature heterodimer. This protein is secreted by mesenchymal cells and acts as a multi-functional cytokine on cells of mainly epithelial origin. This protein also plays a role in angiogenesis, tumorogenesis, and tissue regeneration. Although the encoded protein is a member of the peptidase S1 family of serine proteases, it lacks peptidase activity. Mutations in this gene are associated with nonsyndromic hearing loss. [provided by RefSeq, Nov 2015]. Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types (PubMed:20624990). Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization (PubMed:20977675, PubMed:15167892). Activates MAPK signaling following TMPRSS13 cleavage and activation (PubMed:20977675). Dimer of an alpha chain and a beta chain linked by a disulfide bond. Interacts with SRPX2; the interaction increases HGF mitogenic activity. P14210; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1039104, EBI-10173507; P14210; P14210: HGF; NbExp=2; IntAct=EBI-1039104, EBI-1039104; P14210; P50222: MEOX2; NbExp=3; IntAct=EBI-1039104, EBI-748397; P14210; P08581: MET; NbExp=7; IntAct=EBI-1039104, EBI-1039152; P14210; P16056: Met; Xeno; NbExp=2; IntAct=EBI-1039104, EBI-1798780; P14210-6; P14210-6: HGF; NbExp=3; IntAct=EBI-6280319, EBI-6280319; P14210-6; P08581: MET; NbExp=3; IntAct=EBI-6280319, EBI-1039152; Event=Alternative splicing; Named isoforms=6; Name=1; IsoId=P14210-1; Sequence=Displayed; Name=2; IsoId=P14210-2; Sequence=VSP_009622, VSP_009623; Name=3; IsoId=P14210-3; Sequence=VSP_009617; Name=4; Synonyms=HGF/NK2; IsoId=P14210-4; Sequence=VSP_009620, VSP_009621; Name=5; IsoId=P14210-5; Sequence=VSP_009617, VSP_009622, VSP_009623; Name=6; Synonyms=HGF/NK1; IsoId=P14210-6; Sequence=VSP_009618, VSP_009619; The single-chain precursor undergoes proteolytic processing by TMPRSS13 resulting in an active two-chain form. Deafness, autosomal recessive, 39 (DFNB39) [MIM:608265]: A form of profound prelingual sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 4]: Acts as a competitive antagonist in MET- signaling. Belongs to the peptidase S1 family. Plasminogen subfamily. Has lost two of the three essential catalytic residues and so probably has no enzymatic activity. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/hgf/"; Name=Wikipedia; Note=Hepatocyte growth factor entry; URL="https://en.wikipedia.org/wiki/Hepatocyte_growth_factor"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/385/HGF"; MAPK cascade activation of MAPK activity mitotic cell cycle cell morphogenesis epithelial to mesenchymal transition liver development positive regulation of protein phosphorylation platelet degranulation serine-type endopeptidase activity protein binding extracellular region extracellular space proteolysis growth factor activity negative regulation of autophagy positive regulation of phosphatidylinositol 3-kinase signaling membrane cytokine-mediated signaling pathway hyaluronan metabolic process positive regulation of cell migration platelet alpha granule lumen animal organ regeneration positive regulation of myelination negative regulation of interleukin-6 production positive regulation of interleukin-10 production negative regulation of peptidyl-serine phosphorylation cellular response to hepatocyte growth factor stimulus chemoattractant activity identical protein binding negative regulation of apoptotic process negative regulation of cysteine-type endopeptidase activity involved in apoptotic process positive regulation of osteoblast differentiation positive regulation of angiogenesis positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity hepatocyte growth factor receptor signaling pathway epithelial cell proliferation negative regulation of inflammatory response positive regulation of peptidyl-tyrosine phosphorylation positive chemotaxis myoblast proliferation positive regulation of protein kinase B signaling cell chemotaxis regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling positive regulation of neuron projection regeneration negative regulation of release of cytochrome c from mitochondria regulation of p38MAPK cascade negative regulation of hydrogen peroxide-mediated programmed cell death negative regulation of extrinsic apoptotic signaling pathway via death domain receptors regulation of tau-protein kinase activity positive regulation of DNA biosynthetic process uc285zri.1 uc285zri.2 
ENST00000222399.11 LAMB1 ENST00000222399.11 laminin subunit beta 1 (from RefSeq NM_002291.3) ENST00000222399.1 ENST00000222399.10 ENST00000222399.2 ENST00000222399.3 ENST00000222399.4 ENST00000222399.5 ENST00000222399.6 ENST00000222399.7 ENST00000222399.8 ENST00000222399.9 LAMB1_HUMAN NM_002291 P07942 Q14D91 uc003vew.1 uc003vew.2 uc003vew.3 uc003vew.4 Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis. [provided by RefSeq, Aug 2011]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by published experimental evidence. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660803.8226.1, SRR1803611.79860.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222399.11/ ENSP00000222399.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface. Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin- 211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213). Interacts with ITGB1 (By similarity). P07942; P11912: CD79A; NbExp=3; IntAct=EBI-949174, EBI-7797864; P07942; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-949174, EBI-13345167; P07942; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-949174, EBI-741480; P07942; C5MBE7: CTRG_03389; Xeno; NbExp=2; IntAct=EBI-949174, EBI-16225951; Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. Domains VI and IV are globular. Lissencephaly 5 (LIS5) [MIM:615191]: An autosomal recessive brain malformation characterized by cobblestone changes in the cortex, more severe in the posterior region, and subcortical band heterotopia. Affected individuals have hydrocephalus, seizures, and severely delayed psychomotor development. Note=The disease is caused by variants affecting the gene represented in this entry. integrin binding structural molecule activity extracellular matrix structural constituent protein binding extracellular region basement membrane laminin-1 complex laminin-2 complex extracellular space endoplasmic reticulum lumen cell adhesion animal organ morphogenesis tissue development cell migration neuronal-glial interaction involved in cerebral cortex radial glia guided migration extracellular matrix organization positive regulation of cell migration neuron projection development substrate adhesion-dependent cell spreading endodermal cell differentiation odontogenesis laminin complex laminin-8 complex laminin-10 complex post-translational protein modification cellular protein metabolic process perinuclear region of cytoplasm positive regulation of epithelial cell proliferation extracellular exosome basement membrane assembly uc003vew.1 uc003vew.2 uc003vew.3 uc003vew.4 
ENST00000222402.8 UBE2D4 ENST00000222402.8 ubiquitin conjugating enzyme E2 D4 (putative) (from RefSeq NM_015983.4) A4D1V0 ENST00000222402.1 ENST00000222402.2 ENST00000222402.3 ENST00000222402.4 ENST00000222402.5 ENST00000222402.6 ENST00000222402.7 NM_015983 Q9Y2X8 UB2D4_HUMAN UBCH5D uc003tja.1 uc003tja.2 uc003tja.3 uc003tja.4 Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11' and 'Lys-48'-linked polyubiquitination. Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin- activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin- conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence= Protein modification; protein ubiquitination. Q9Y2X8; Q15038: DAZAP2; NbExp=3; IntAct=EBI-745527, EBI-724310; Q9Y2X8; Q86UW9: DTX2; NbExp=13; IntAct=EBI-745527, EBI-740376; Q9Y2X8; Q8N9I9: DTX3; NbExp=4; IntAct=EBI-745527, EBI-2340258; Q9Y2X8; P62879: GNB2; NbExp=3; IntAct=EBI-745527, EBI-356942; Q9Y2X8; P42858: HTT; NbExp=3; IntAct=EBI-745527, EBI-466029; Q9Y2X8; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-745527, EBI-81279; Q9Y2X8; Q0VD86: INCA1; NbExp=3; IntAct=EBI-745527, EBI-6509505; Q9Y2X8; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-745527, EBI-739832; Q9Y2X8; O15344: MID1; NbExp=4; IntAct=EBI-745527, EBI-2340316; Q9Y2X8; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-745527, EBI-10172526; Q9Y2X8; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-745527, EBI-373524; Q9Y2X8; Q9H000: MKRN2; NbExp=6; IntAct=EBI-745527, EBI-2341005; Q9Y2X8; Q96FW1: OTUB1; NbExp=9; IntAct=EBI-745527, EBI-1058491; Q9Y2X8; Q9BWX1: PHF7; NbExp=3; IntAct=EBI-745527, EBI-4307517; Q9Y2X8; P19388: POLR2E; NbExp=3; IntAct=EBI-745527, EBI-395189; Q9Y2X8; Q04864-2: REL; NbExp=3; IntAct=EBI-745527, EBI-10829018; Q9Y2X8; Q06587: RING1; NbExp=4; IntAct=EBI-745527, EBI-752313; Q9Y2X8; Q9Y3C5: RNF11; NbExp=10; IntAct=EBI-745527, EBI-396669; Q9Y2X8; Q9Y4L5: RNF115; NbExp=12; IntAct=EBI-745527, EBI-2129242; Q9Y2X8; Q9BV68: RNF126; NbExp=3; IntAct=EBI-745527, EBI-357322; Q9Y2X8; Q9UBS8: RNF14; NbExp=5; IntAct=EBI-745527, EBI-2130308; Q9Y2X8; Q96A37: RNF166; NbExp=4; IntAct=EBI-745527, EBI-2130320; Q9Y2X8; Q9P0P0: RNF181; NbExp=4; IntAct=EBI-745527, EBI-2129136; Q9Y2X8; Q96GF1: RNF185; NbExp=4; IntAct=EBI-745527, EBI-2340249; Q9Y2X8; Q99496: RNF2; NbExp=4; IntAct=EBI-745527, EBI-722416; Q9Y2X8; Q96BH1: RNF25; NbExp=3; IntAct=EBI-745527, EBI-2129220; Q9Y2X8; Q99942: RNF5; NbExp=7; IntAct=EBI-745527, EBI-348482; Q9Y2X8; Q9HCM9: TRIM39; NbExp=5; IntAct=EBI-745527, EBI-739510; Q9Y2X8; Q9HCM9-2: TRIM39; NbExp=7; IntAct=EBI-745527, EBI-11523450; Q9Y2X8; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-745527, EBI-9867283; Q9Y2X8; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-745527, EBI-2130429; Q9Y2X8; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-745527, EBI-6929619; Q9Y2X8; Q9BZR9: TRIM8; NbExp=4; IntAct=EBI-745527, EBI-2340370; Q9Y2X8; Q9HAC8: UBTD1; NbExp=9; IntAct=EBI-745527, EBI-745871; Q9Y2X8; Q8WUN7: UBTD2; NbExp=3; IntAct=EBI-745527, EBI-12867288; Q9Y2X8; Q8ND25: ZNRF1; NbExp=6; IntAct=EBI-745527, EBI-2129250; Belongs to the ubiquitin-conjugating enzyme family. ubiquitin ligase complex nucleotide binding ubiquitin-protein transferase activity protein binding ATP binding ubiquitin-dependent protein catabolic process protein ubiquitination transferase activity ubiquitin protein ligase binding protein K29-linked ubiquitination protein K27-linked ubiquitination ubiquitin conjugating enzyme activity protein K63-linked ubiquitination protein K48-linked ubiquitination protein K11-linked ubiquitination protein K6-linked ubiquitination uc003tja.1 uc003tja.2 uc003tja.3 uc003tja.4 
ENST00000222462.3 WNT16 ENST00000222462.3 Wnt family member 16, transcript variant 1 (from RefSeq NM_057168.2) ENST00000222462.1 ENST00000222462.2 NM_057168 Q2M3G1 Q9UBV4 Q9Y5C0 WNT16_HUMAN uc003vjw.1 uc003vjw.2 uc003vjw.3 uc003vjw.4 uc003vjw.5 The WNT gene family consists of structurally related genes which encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It contains two transcript variants diverging at the 5' termini. These two variants are proposed to be the products of separate promoters and not to be splice variants from a single promoter. They are differentially expressed in normal tissues, one of which (variant 2) is expressed at significant levels only in the pancreas, whereas another one (variant 1) is expressed more ubiquitously with highest levels in adult kidney, placenta, brain, heart, and spleen. [provided by RefSeq, Jul 2008]. Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). Secreted, extracellular space, extracellular matrix. Event=Alternative splicing; Named isoforms=2; Name=Wnt-16b; IsoId=Q9UBV4-1; Sequence=Displayed; Name=Wnt-16a; IsoId=Q9UBV4-2; Sequence=VSP_006797; Isoform Wnt-16b is expressed in peripheral lymphoid organs such as spleen, appendix, and lymph nodes, in kidney but not in bone marrow. Isoform Wnt-16a is expressed at significant levels only in the pancreas. Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. Belongs to the Wnt family. optic cup formation involved in camera-type eye development receptor binding frizzled binding extracellular region extracellular space cytoplasm multicellular organism development positive regulation of gene expression positive regulation of phosphatidylinositol 3-kinase signaling Wnt signaling pathway neuron differentiation keratinocyte differentiation keratinocyte proliferation cell fate commitment positive regulation of JNK cascade bone remodeling cardiac epithelial to mesenchymal transition negative regulation of cell death replicative senescence oxidative stress-induced premature senescence uc003vjw.1 uc003vjw.2 uc003vjw.3 uc003vjw.4 uc003vjw.5 
ENST00000222481.9 CPA2 ENST00000222481.9 carboxypeptidase A2 (from RefSeq NM_001869.3) A4D1M4 C9JIK1 CBPA2_HUMAN ENST00000222481.1 ENST00000222481.2 ENST00000222481.3 ENST00000222481.4 ENST00000222481.5 ENST00000222481.6 ENST00000222481.7 ENST00000222481.8 NM_001869 P48052 Q53XS1 Q96A12 Q96QN3 Q9UCF1 uc003vpq.1 uc003vpq.2 uc003vpq.3 uc003vpq.4 uc003vpq.5 Three different forms of human pancreatic procarboxypeptidase A have been isolated. The encoded protein represents the A2 form, which is a monomeric protein with different biochemical properties from the A1 and A3 forms. The A2 form of pancreatic procarboxypeptidase acts on aromatic C-terminal residues and is a secreted protein. [provided by RefSeq, Dec 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC007009.1, BC014571.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968832, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222481.9/ ENSP00000222481.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Reaction=Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.; EC=3.4.17.15; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. Secreted. Belongs to the peptidase M14 family. Sequence=AAA74425.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH07009.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH14571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH15140.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=EAL24092.1; Type=Erroneous gene model prediction; Evidence=; carboxypeptidase activity metallocarboxypeptidase activity extracellular region extracellular space vacuole proteolysis protein catabolic process in the vacuole peptidase activity metallopeptidase activity zinc ion binding hydrolase activity metal ion binding uc003vpq.1 uc003vpq.2 uc003vpq.3 uc003vpq.4 uc003vpq.5 
ENST00000222482.10 CPA4 ENST00000222482.10 carboxypeptidase A4, transcript variant 1 (from RefSeq NM_016352.4) B7Z576 CBPA4_HUMAN CPA3 ENST00000222482.1 ENST00000222482.2 ENST00000222482.3 ENST00000222482.4 ENST00000222482.5 ENST00000222482.6 ENST00000222482.7 ENST00000222482.8 ENST00000222482.9 NM_016352 Q86UY9 Q9UI42 UNQ694/PRO1339 uc285zyb.1 uc285zyb.2 This gene is a member of the carboxypeptidase A/B subfamily, and it is located in a cluster with three other family members on chromosome 7. Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. This gene could be involved in the histone hyperacetylation pathway. It is imprinted and may be a strong candidate gene for prostate cancer aggressiveness. [provided by RefSeq, Jul 2008]. Metalloprotease that could be involved in the histone hyperacetylation pathway (PubMed:10383164). Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val (PubMed:20385563). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Inhibited by interaction with the metallocarboxypeptidase inhibitor (MCPI) from N.versicolor that binds to the catalytic zinc ion. Kinetic parameters: KM=55.6 uM for 3-(2-furyl)acryloyl-Phe-Phe ; KM=19.4 uM for 3-(2-furyl)acryloyl-Phe-Leu ; KM=23.3 uM for 3-(2-furyl)acryloyl-Phe-Ile ; KM=40.4 uM for 3-(2-furyl)acryloyl-Phe-Met ; KM=57.3 uM for 3-(2-furyl)acryloyl-Phe-Val ; KM=0.329 uM for neurotensin ; KM=9.23 uM for Met-enkephalin-Arg-Phe ; pH dependence: Optimum pH is 8.5-9. ; Monomer. Interacts with LXN. Q9UI42-1; P84875; Xeno; NbExp=3; IntAct=EBI-16060275, EBI-16060264; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UI42-1; Sequence=Displayed; Name=2; IsoId=Q9UI42-2; Sequence=VSP_042894; Fetal expression in the adrenal gland, brain, heart, intestine, kidney, liver and lung. Except for fetal brain that shows no imprinting, expression was found preferentially from the maternal allele. Up-regulated by inhibitors of histone dacetylation. Belongs to the peptidase M14 family. carboxypeptidase activity metallocarboxypeptidase activity protein binding cellular_component extracellular region extracellular space proteolysis peptidase activity metallopeptidase activity zinc ion binding histone acetylation hydrolase activity metal ion binding uc285zyb.1 uc285zyb.2 
ENST00000222511.11 GTPBP10 ENST00000222511.11 GTP binding protein 10, transcript variant 2 (from RefSeq NM_033107.4) A4D1E9 B4DFY6 ENST00000222511.1 ENST00000222511.10 ENST00000222511.2 ENST00000222511.3 ENST00000222511.4 ENST00000222511.5 ENST00000222511.6 ENST00000222511.7 ENST00000222511.8 ENST00000222511.9 GTPBA_HUMAN NM_033107 OBGH2 Q3B7A6 Q5H9V2 Q8IXG8 Q8N982 Q8WU16 Q9BSP1 Q9Y6T6 UG0751c10 uc003ukm.1 uc003ukm.2 uc003ukm.3 uc003ukm.4 Small G proteins, such as GTPBP10, act as molecular switches that play crucial roles in the regulation of fundamental cellular processes such as protein synthesis, nuclear transport, membrane trafficking, and signal transduction (Hirano et al., 2006 [PubMed 17054726]).[supplied by OMIM, Mar 2008]. May be involved in the ribosome maturation process. Complements an ObgE(CgtA) function in E.coli ribosome maturation. Plays a role of GTPase in vitro. When missing, disorganization of the nucleolar architecture is observed. A4D1E9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-5453796, EBI-618309; A4D1E9; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-5453796, EBI-742948; A4D1E9; Q8ND90: PNMA1; NbExp=4; IntAct=EBI-5453796, EBI-302345; Nucleus, nucleolus Chromosome Note=Found in the dense fibrillar compartment region of the nucleolus. At the onset of mitosis moves to the chromosome surface and remains there until anaphase. Gradually re-assembles into the nucleolus at late anaphase to telophase. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=A4D1E9-1; Sequence=Displayed; Name=2; IsoId=A4D1E9-2; Sequence=VSP_029880; Name=3; IsoId=A4D1E9-3; Sequence=VSP_029881, VSP_029882; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. nucleotide binding RNA binding protein binding GTP binding nucleus chromosome nucleolus ribosome biogenesis uc003ukm.1 uc003ukm.2 uc003ukm.3 uc003ukm.4 
ENST00000222543.11 TFPI2 ENST00000222543.11 tissue factor pathway inhibitor 2, transcript variant 1 (from RefSeq NM_006528.4) ENST00000222543.1 ENST00000222543.10 ENST00000222543.2 ENST00000222543.3 ENST00000222543.4 ENST00000222543.5 ENST00000222543.6 ENST00000222543.7 ENST00000222543.8 ENST00000222543.9 NM_006528 P48307 Q66ME8 Q8NAK6 Q9UC86 TFPI2_HUMAN uc003umy.1 uc003umy.2 uc003umy.3 uc003umy.4 This gene encodes a member of the Kunitz-type serine proteinase inhibitor family. The protein can inhibit a variety of serine proteases including factor VIIa/tissue factor, factor Xa, plasmin, trypsin, chymotryspin and plasma kallikrein. This gene has been identified as a tumor suppressor gene in several types of cancer. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2012]. May play a role in the regulation of plasmin-mediated matrix remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and weakly factor Xa. Has no effect on thrombin. Finds in a complex with ABCB1, TFPI2 and PPP2R3C; leading to the dephosphorylation of ABCB1. Secreted. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P48307-1; Sequence=Displayed; Name=2; IsoId=P48307-2; Sequence=VSP_056031; Umbilical vein endothelial cells, liver, placenta, heart, pancreas, and maternal serum at advanced pregnancy. This inhibitor contains three inhibitory domains. serine-type endopeptidase inhibitor activity extracellular matrix structural constituent extracellular region extracellular space blood coagulation hemostasis negative regulation of peptidase activity negative regulation of endopeptidase activity peptidase inhibitor activity extracellular matrix cellular response to fluid shear stress uc003umy.1 uc003umy.2 uc003umy.3 uc003umy.4 
ENST00000222547.8 BET1 ENST00000222547.8 Bet1 golgi vesicular membrane trafficking protein, transcript variant 1 (from RefSeq NM_005868.6) BET1 ENST00000222547.1 ENST00000222547.2 ENST00000222547.3 ENST00000222547.4 ENST00000222547.5 ENST00000222547.6 ENST00000222547.7 NM_005868 Q53XK0 Q53XK0_HUMAN hCG_19198 tcag7.252 uc003unf.1 uc003unf.2 uc003unf.3 This gene encodes a golgi-associated membrane protein that participates in vesicular transport from the endoplasmic reticulum (ER) to the Golgi complex. The encoded protein functions as a soluble N-ethylaleimide-sensitive factor attachment protein receptor and may be involved in the docking of ER-derived vesicles with the cis-Golgi membrane. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2015]. Endoplasmic reticulum membrane ; Single-pass type IV membrane protein Membrane ; Single-pass type IV membrane protein Belongs to the BET1 family. protein binding protein transport membrane integral component of membrane integral component of Golgi membrane uc003unf.1 uc003unf.2 uc003unf.3 
ENST00000222553.8 NAMPT ENST00000222553.8 nicotinamide phosphoribosyltransferase (from RefSeq NM_005746.3) A4D0Q9 A4D0R0 ENST00000222553.1 ENST00000222553.2 ENST00000222553.3 ENST00000222553.4 ENST00000222553.5 ENST00000222553.6 ENST00000222553.7 NAMPT_HUMAN NM_005746 P43490 PBEF PBEF1 Q3KQV0 Q8WW95 uc003vdq.1 uc003vdq.2 uc003vdq.3 uc003vdq.4 uc003vdq.5 This gene encodes a protein that catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, one step in the biosynthesis of nicotinamide adenine dinucleotide. The protein belongs to the nicotinic acid phosphoribosyltransferase (NAPRTase) family and is thought to be involved in many important biological processes, including metabolism, stress response and aging. This gene has a pseudogene on chromosome 10. [provided by RefSeq, Feb 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.25741.1, SRR1803617.277343.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222553.8/ ENSP00000222553.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-BMAL1 heterodimer from NAD-dependent SIRT1- mediated suppression (By similarity). Reaction=beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho- alpha-D-ribose 1-diphosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:16149, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.12; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16151; Evidence=; Inhibited by FK866. FK866 competes for the same binding site as nicotinamide, but due to its very low dissociation rate, it is essentially an irreversible inhibitor. Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D- ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide: step 1/1. Homodimer. P43490; P02792: FTL; NbExp=3; IntAct=EBI-2829310, EBI-713279; P43490; Q01628: IFITM3; NbExp=3; IntAct=EBI-2829310, EBI-7932862; P43490; P03886: MT-ND1; NbExp=3; IntAct=EBI-2829310, EBI-1246156; P43490; P43490: NAMPT; NbExp=5; IntAct=EBI-2829310, EBI-2829310; P43490; Q70CQ1-2: USP49; NbExp=3; IntAct=EBI-2829310, EBI-12133829; Nucleus Cytoplasm Secreted Note=Under non-inflammatory conditions, visfatin predominantly exhibits a granular pattern within the nucleus. Secreted by endothelial cells upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100- fold higher concentrations compared to maternal serum. Expressed in large amounts in bone marrow, liver tissue, and muscle. Also present in heart, placenta, lung, and kidney tissues. Belongs to the NAPRTase family. Sequence=AAQ96862.1; Type=Erroneous gene model prediction; Evidence=; Sequence=EAL24400.1; Type=Erroneous gene model prediction; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/43890/NAMPT"; microglial cell activation catalytic activity nicotinate-nucleotide diphosphorylase (carboxylating) activity cytokine activity protein binding extracellular region extracellular space nucleus cytoplasm cytosol plasma membrane signal transduction cell-cell signaling female pregnancy aging circadian rhythm drug binding positive regulation of cell proliferation NAD biosynthetic process negative regulation of autophagy response to organic cyclic compound regulation of lung blood pressure nuclear speck transferase activity transferase activity, transferring glycosyl groups pyridine nucleotide biosynthetic process cell junction circadian regulation of gene expression NAD biosynthesis via nicotinamide riboside salvage pathway identical protein binding protein homodimerization activity positive regulation of transcription from RNA polymerase II promoter nicotinamide phosphoribosyltransferase activity rhythmic process positive regulation of smooth muscle cell proliferation positive regulation of nitric-oxide synthase biosynthetic process extracellular exosome neuron death cellular response to ionizing radiation cellular response to oxygen-glucose deprivation cellular response to beta-amyloid response to D-galactose negative regulation of cellular senescence insulin receptor signaling pathway adipose tissue development uc003vdq.1 uc003vdq.2 uc003vdq.3 uc003vdq.4 uc003vdq.5 
ENST00000222567.6 POLR1F ENST00000222567.6 RNA polymerase I subunit F (from RefSeq NM_001002926.2) A0PJ45 B7Z724 ENST00000222567.1 ENST00000222567.2 ENST00000222567.3 ENST00000222567.4 ENST00000222567.5 NM_001002926 POLR1F Q3B726 RPA43_HUMAN TWISTNB uc003sup.1 uc003sup.2 uc003sup.3 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Through its association with RRN3/TIF-IA may be involved in recruitment of Pol I to rDNA promoters. Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits (By similarity). Interacts with RRN3/TIF-IA. Nucleus, nucleolus Widely expressed. Expressed in all fetal and adult tissues tested, with highest expression in fetal lung, liver, and kidney, and low expression in all adult tissues. Belongs to the eukaryotic RPA43 RNA polymerase subunit family. Sequence=AAH14574.1; Type=Frameshift; Evidence=; DNA-directed 5'-3' RNA polymerase activity nucleus nucleoplasm nucleolus DNA-directed RNA polymerase I complex transcription, DNA-templated transcription initiation from RNA polymerase I promoter transcription elongation from RNA polymerase I promoter termination of RNA polymerase I transcription positive regulation of gene expression, epigenetic cellular response to leukemia inhibitory factor RNA polymerase I activity uc003sup.1 uc003sup.2 uc003sup.3 
ENST00000222572.8 PON2 ENST00000222572.8 paraoxonase 2, transcript variant 1 (from RefSeq NM_000305.3) A4D1H7 B2RCP9 B4DJD5 ENST00000222572.1 ENST00000222572.2 ENST00000222572.3 ENST00000222572.4 ENST00000222572.5 ENST00000222572.6 ENST00000222572.7 NM_000305 O15114 O15115 O75856 PON2_HUMAN Q15165 Q5FBX7 Q86YL0 uc003unv.1 uc003unv.2 uc003unv.3 uc003unv.4 uc003unv.5 This gene encodes a member of the paraoxonase gene family, which includes three known members located adjacent to each other on the long arm of chromosome 7. The encoded protein is ubiquitously expressed in human tissues, membrane-bound, and may act as a cellular antioxidant, protecting cells from oxidative stress. Hydrolytic activity against acylhomoserine lactones, important bacterial quorum-sensing mediators, suggests the encoded protein may also play a role in defense responses to pathogenic bacteria. Mutations in this gene may be associated with vascular disease and a number of quantitative phenotypes related to diabetes. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]. Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis. Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence=; Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81; Evidence=; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Note=Binds 2 calcium ions per subunit. ; Homotrimer. Membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=3; Name=2; IsoId=Q15165-2; Sequence=Displayed; Name=1; IsoId=Q15165-1; Sequence=VSP_004533; Name=3; IsoId=Q15165-3; Sequence=VSP_040715; Widely expressed with highest expression in liver, lung, placenta, testis and heart. The signal sequence is not cleaved. Ser-311 is associated with an increased risk of cornary heart disease. Belongs to the paraoxonase family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/pon2/"; arylesterase activity extracellular region nucleus mitochondrion lysosome plasma membrane response to oxidative stress response to toxic substance membrane hydrolase activity lipoxygenase pathway aromatic compound catabolic process identical protein binding intracellular membrane-bounded organelle metal ion binding acyl-L-homoserine-lactone lactonohydrolase activity uc003unv.1 uc003unv.2 uc003unv.3 uc003unv.4 uc003unv.5 
ENST00000222573.5 ITGB8 ENST00000222573.5 integrin subunit beta 8 (from RefSeq NM_002214.3) A4D133 B4DHD4 ENST00000222573.1 ENST00000222573.2 ENST00000222573.3 ENST00000222573.4 ITB8_HUMAN ITGB8 NM_002214 P26012 uc003suu.1 uc003suu.2 uc003suu.3 uc003suu.4 uc003suu.5 This gene is a member of the integrin beta chain family and encodes a single-pass type I membrane protein with a VWFA domain and four cysteine-rich repeats. This protein noncovalently binds to an alpha subunit to form a heterodimeric integrin complex. In general, integrin complexes mediate cell-cell and cell-extracellular matrix interactions and this complex plays a role in human airway epithelial proliferation. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.12804.1, M73780.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222573.5/ ENSP00000222573.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin (PubMed:1918072). It recognizes the sequence R-G-D in its ligands (PubMed:1918072). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (Probable). Required during vasculogenesis (By similarity). Heterodimer of an alpha and a beta subunit (PubMed:1918072). Beta-8 (ITGB8) associates with alpha-V (ITGAV) to form ITGAV:ITGB8 (PubMed:1918072, PubMed:22278742). ITGAV:ITGB8 interacts with TGFB1 (PubMed:22278742). Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P26012-1; Sequence=Displayed; Name=2; IsoId=P26012-2; Sequence=VSP_056531; Placenta, kidney, brain, ovary, uterus and in several transformed cells. Transiently expressed in 293 human embryonic kidney cells. The VWFA domain (or beta I domain) contains two cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS) and the metal ion-dependent adhesion site (MIDAS) (PubMed:31792290). Unlike in the other beta integrins, the cation-binding site adjacent MIDAS site (ADMIDAS) in ITGB8 is not functional due to the presence of two Asn residues instead of 2 Asp residues (PubMed:31792290). This domain is also part of the ligand-binding site (PubMed:31792290). Belongs to the integrin beta chain family. vasculogenesis ganglioside metabolic process receptor binding integrin binding plasma membrane cell adhesion integrin-mediated signaling pathway integrin complex cell surface positive regulation of gene expression negative regulation of gene expression membrane integral component of membrane cell migration extracellular matrix organization cell adhesion mediated by integrin integrin alphav-beta8 complex signaling receptor activity positive regulation of angiogenesis cartilage development placenta blood vessel development extracellular exosome regulation of transforming growth factor beta activation extracellular matrix protein binding cell-matrix adhesion uc003suu.1 uc003suu.2 uc003suu.3 uc003suu.4 uc003suu.5 
ENST00000222574.9 HBP1 ENST00000222574.9 HMG-box transcription factor 1, transcript variant 2 (from RefSeq NM_012257.4) B3KVB7 ENST00000222574.1 ENST00000222574.2 ENST00000222574.3 ENST00000222574.4 ENST00000222574.5 ENST00000222574.6 ENST00000222574.7 ENST00000222574.8 HBP1_HUMAN NM_012257 O60381 Q8TBM1 Q8TE93 Q96AJ2 uc003vdy.1 uc003vdy.2 uc003vdy.3 uc003vdy.4 Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'- TTCATTCATTCA-3'. Binding to the histone H1.0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4. Binds the second PAH repeat of SIN3A (Probable). Binds TCF4 (PubMed:11500377). Binds RB1 (PubMed:10958660). O60381; P06400: RB1; NbExp=2; IntAct=EBI-954175, EBI-491274; Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O60381-1; Sequence=Displayed; Name=2; IsoId=O60381-2; Sequence=VSP_014655; Name=3; IsoId=O60381-3; Sequence=VSP_014656; Ubiquitinated by the CTLH E3 ubiquitin-protein ligase complex, leading to subsequent proteasomal degradation. Sequence=BAB85059.1; Type=Erroneous initiation; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40791/HBP1"; nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding RNA binding protein binding nucleus nucleoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter cell cycle arrest Wnt signaling pathway nuclear speck uc003vdy.1 uc003vdy.2 uc003vdy.3 uc003vdy.4 
ENST00000222584.8 SP4 ENST00000222584.8 Sp4 transcription factor, transcript variant 1 (from RefSeq NM_003112.5) ENST00000222584.1 ENST00000222584.2 ENST00000222584.3 ENST00000222584.4 ENST00000222584.5 ENST00000222584.6 ENST00000222584.7 NM_003112 O60402 Q02446 Q32M52 SP4_HUMAN uc003sva.1 uc003sva.2 uc003sva.3 uc003sva.4 uc003sva.5 The protein encoded by this gene is a transcription factor that can bind to the GC promoter region of a variety of genes, including those of the photoreceptor signal transduction system. The encoded protein binds to the same sites in promoter CpG islands as does the transcription factor SP1, although its expression is much more restricted compared to that of SP1. This gene may be involved in bipolar disorder and schizophrenia. [provided by RefSeq, May 2016]. Binds to GT and GC boxes promoters elements. Probable transcriptional activator. Q02446; Q13444: ADAM15; NbExp=3; IntAct=EBI-10198587, EBI-77818; Q02446; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-10198587, EBI-541426; Q02446; Q9BTQ8: ATXN7L1; NbExp=3; IntAct=EBI-10198587, EBI-10298510; Q02446; A0A0S2Z5G4: BANP; NbExp=3; IntAct=EBI-10198587, EBI-16429704; Q02446; B4DE54: BANP; NbExp=3; IntAct=EBI-10198587, EBI-16429313; Q02446; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-10198587, EBI-11524452; Q02446; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-10198587, EBI-16429296; Q02446; Q96Q77: CIB3; NbExp=6; IntAct=EBI-10198587, EBI-10292696; Q02446; P27658: COL8A1; NbExp=3; IntAct=EBI-10198587, EBI-747133; Q02446; P41970: ELK3; NbExp=3; IntAct=EBI-10198587, EBI-1758534; Q02446; Q75MZ5: FOXP2; NbExp=4; IntAct=EBI-10198587, EBI-10255915; Q02446; P52655: GTF2A1; NbExp=3; IntAct=EBI-10198587, EBI-389518; Q02446; A0A024R5S0: hCG_2003792; NbExp=6; IntAct=EBI-10198587, EBI-10188461; Q02446; Q8TAP4: LMO3; NbExp=3; IntAct=EBI-10198587, EBI-742259; Q02446; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10198587, EBI-739832; Q02446; Q4G0S1: LOC730441; NbExp=3; IntAct=EBI-10198587, EBI-10241801; Q02446; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-10198587, EBI-348259; Q02446; Q13952-2: NFYC; NbExp=3; IntAct=EBI-10198587, EBI-11956831; Q02446; Q16656: NRF1; NbExp=3; IntAct=EBI-10198587, EBI-2547810; Q02446; Q16656-4: NRF1; NbExp=3; IntAct=EBI-10198587, EBI-11742836; Q02446; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-10198587, EBI-448407; Q02446; Q96T60: PNKP; NbExp=3; IntAct=EBI-10198587, EBI-1045072; Q02446; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-10198587, EBI-1389308; Q02446; P14859: POU2F1; NbExp=5; IntAct=EBI-10198587, EBI-624770; Q02446; P14859-6: POU2F1; NbExp=3; IntAct=EBI-10198587, EBI-11526590; Q02446; P86479: PRR20C; NbExp=5; IntAct=EBI-10198587, EBI-10172814; Q02446; P86480: PRR20D; NbExp=3; IntAct=EBI-10198587, EBI-12754095; Q02446; Q02446: SP4; NbExp=3; IntAct=EBI-10198587, EBI-10198587; Q02446; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-10198587, EBI-12023934; Q02446; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-10198587, EBI-12037215; Q02446; Q14119: VEZF1; NbExp=3; IntAct=EBI-10198587, EBI-11980193; Nucleus. Abundant in brain. The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. In SP4, the motif is inactive. Belongs to the Sp1 C2H2-type zinc-finger protein family. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding transcription coactivator activity protein binding nucleus nucleoplasm cytosol regulation of transcription from RNA polymerase II promoter sequence-specific DNA binding metal ion binding positive regulation of nucleic acid-templated transcription uc003sva.1 uc003sva.2 uc003sva.3 uc003sva.4 uc003sva.5 
ENST00000222644.10 PALS2 ENST00000222644.10 protein associated with LIN7 2, MAGUK p55 family member, transcript variant 2 (from RefSeq NM_001303037.2) A4D157 ENST00000222644.1 ENST00000222644.2 ENST00000222644.3 ENST00000222644.4 ENST00000222644.5 ENST00000222644.6 ENST00000222644.7 ENST00000222644.8 ENST00000222644.9 MPP6 NM_001303037 PALS2 PALS2_HUMAN Q9H0E1 Q9NZW5 VAM1 uc003swy.1 uc003swy.2 uc003swy.3 uc003swy.4 uc003swy.5 Members of the peripheral membrane-associated guanylate kinase (MAGUK) family function in tumor suppression and receptor clustering by forming multiprotein complexes containing distinct sets of transmembrane, cytoskeletal, and cytoplasmic signaling proteins. All MAGUKs contain a PDZ-SH3-GUK core and are divided into 4 subfamilies, DLG-like (see DLG1; MIM 601014), ZO1-like (see TJP1; MIM 601009), p55-like (see MPP1; MIM 305360), and LIN2-like (see CASK; MIM 300172), based on their size and the presence of additional domains. MPP6 is a member of the p55-like MAGUK subfamily (Tseng et al., 2001 [PubMed 11311936]).[supplied by OMIM, Mar 2008]. Interacts with CADM1 (By similarity). Interacts with the LIN7 proteins. Q9NZW5; O14910: LIN7A; NbExp=4; IntAct=EBI-2683764, EBI-2513988; Q9NZW5; Q9HAP6: LIN7B; NbExp=5; IntAct=EBI-2683764, EBI-821335; Q9NZW5; Q9NUP9: LIN7C; NbExp=6; IntAct=EBI-2683764, EBI-1171517; Membrane ; Peripheral membrane protein Abundant in testis, brain, and kidney with lower levels detectable in other tissues. Belongs to the MAGUK family. protein binding plasma membrane membrane macromolecular complex assembly extracellular exosome uc003swy.1 uc003swy.2 uc003swy.3 uc003swy.4 uc003swy.5 
ENST00000222673.6 OGDH ENST00000222673.6 oxoglutarate dehydrogenase, transcript variant 1 (from RefSeq NM_002541.4) B4E2U9 D3DVL0 E9PBM1 ENST00000222673.1 ENST00000222673.2 ENST00000222673.3 ENST00000222673.4 ENST00000222673.5 NM_002541 ODO1_HUMAN OGDH Q02218 Q96DD3 Q9UDX0 uc003tln.1 uc003tln.2 uc003tln.3 uc003tln.4 uc003tln.5 This gene encodes one subunit of the 2-oxoglutarate dehydrogenase complex. This complex catalyzes the overall conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA and CO(2) during the Krebs cycle. The protein is located in the mitochondrial matrix and uses thiamine pyrophosphate as a cofactor. A congenital deficiency in 2-oxoglutarate dehydrogenase activity is believed to lead to hypotonia, metabolic acidosis, and hyperlactatemia. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Sep 2009]. 2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC) (PubMed:24495017, PubMed:25210035, PubMed:28435050). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC (PubMed:24495017, PubMed:25210035, PubMed:28435050). Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine- residue succinyltransferase or DLST) (PubMed:24495017, PubMed:25210035, PubMed:28435050). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids (PubMed:25210035). Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate (PubMed:28435050). Mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl- [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)- S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189; Evidence= Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence=; Calcium ions and ADP stimulate, whereas ATP and NADH reduce catalytic activity. The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2), DLD (dihydrolipoamide dehydrogenase; E3), and the assembly factor KGD4 (By similarity). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A (PubMed:29211711). Interacts with ABHD11; this interaction maintains the functional lipoylation of the 2-oxoglutarate dehydrogenase complex (PubMed:32792488). Q02218; P54253: ATXN1; NbExp=3; IntAct=EBI-747213, EBI-930964; Q02218; P42858: HTT; NbExp=3; IntAct=EBI-747213, EBI-466029; Mitochondrion Nucleus Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2- oxoglutarate dehydrogenase complex is required for histone succinylation. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q02218-1; Sequence=Displayed; Name=2; IsoId=Q02218-2; Sequence=VSP_042313; Name=3; IsoId=Q02218-3; Sequence=VSP_043628, VSP_043629; [Isoform 2]: Probably insensitive to calcium. The mitochondrial 2-oxoglutarate and 2-oxoadipate dehydrogenase complexes (OGDHC and OADHC, respectively) share their E2 (DLST) and E3 (dihydrolipoyl dehydrogenase or DLD) components, but the E1 component is specific to each complex (E1o and E1a (DHTK1), respectively). Belongs to the alpha-ketoglutarate dehydrogenase family. Sequence=BAA01393.1; Type=Frameshift; Evidence=; Sequence=BAA06836.1; Type=Frameshift; Evidence=; Name=Wikipedia; Note=Alpha-ketoglutarate dehydrogenase entry; URL="https://en.wikipedia.org/wiki/Alpha-ketoglutarate_dehydrogenase"; oxoglutarate dehydrogenase (succinyl-transferring) activity nucleus mitochondrion mitochondrial matrix generation of precursor metabolites and energy glycolytic process tricarboxylic acid cycle 2-oxoglutarate metabolic process succinyl-CoA metabolic process lysine catabolic process oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor thiamine pyrophosphate binding mitochondrial membrane oxoglutarate dehydrogenase complex metal ion binding oxidation-reduction process uc003tln.1 uc003tln.2 uc003tln.3 uc003tln.4 uc003tln.5 
ENST00000222674.2 NPVF ENST00000222674.2 neuropeptide VF precursor (from RefSeq NM_022150.3) A4D164 C7orf9 ENST00000222674.1 NM_022150 NPVF_HUMAN Q7LE27 Q96PI9 Q9HCQ7 RFRP uc003sxo.1 uc003sxo.2 uc003sxo.3 uc003sxo.4 Neuropeptide RFRP-1 acts as a potent negative regulator of gonadotropin synthesis and secretion. Neuropeptides NPSF and NPVF efficiently inhibit forskolin-induced production of cAMP, but RFRP-2 shows no inhibitory activity. Neuropeptide RFRP-1 induces secretion of prolactin in rats. Neuropeptide NPVF blocks morphine-induced analgesia. Q9HCQ7; O43765: SGTA; NbExp=3; IntAct=EBI-1753111, EBI-347996; Q9HCQ7; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1753111, EBI-947187; Secreted. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9HCQ7-1; Sequence=Displayed; Name=2; IsoId=Q9HCQ7-2; Sequence=VSP_039962; Isoform 1 is specifically expressed in the retina. Neuropeptides RFRP-1 and NPVF are detected in the hypothalamus. [Neuropeptide RFRP-1]: Mass=1428.85; Method=MALDI; Evidence=; [Neuropeptide NPVF]: Mass=969.56; Method=MALDI; Evidence=; Belongs to the FARP (FMRFamide related peptide) family. extracellular region neuropeptide signaling pathway negative regulation of gonadotropin secretion uc003sxo.1 uc003sxo.2 uc003sxo.3 uc003sxo.4 
ENST00000222693.5 CAV2 ENST00000222693.5 caveolin 2, transcript variant 1 (from RefSeq NM_001233.5) CAV2 ENST00000222693.1 ENST00000222693.2 ENST00000222693.3 ENST00000222693.4 NM_001233 Q53X57 Q53X57_HUMAN hCG_39087 tcag7.25 uc003vid.1 uc003vid.2 uc003vid.3 uc003vid.4 uc003vid.5 The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. This gene and related family member (CAV1) are located next to each other on chromosome 7, and express colocalizing proteins that form a stable hetero-oligomeric complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. Additional isoforms resulting from the use of alternate in-frame translation initiation codons have also been described, and shown to have preferential localization in the cell (PMID:11238462). [provided by RefSeq, May 2011]. May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression. Cell membrane eripheral membrane protein Golgi apparatus membrane ; Peripheral membrane protein Membrane, caveola ; Peripheral membrane protein Membrane ; Peripheral membrane protein Belongs to the caveolin family. Golgi membrane negative regulation of endothelial cell proliferation positive regulation of endothelial cell proliferation acrosomal membrane caveolar macromolecular signaling complex Golgi apparatus plasma membrane caveola focal adhesion mitochondrion organization endoplasmic reticulum organization negative regulation of cell proliferation membrane integral component of membrane protein kinase binding negative regulation of transforming growth factor beta receptor signaling pathway protein binding, bridging macromolecular complex protein heterodimerization activity skeletal muscle fiber development binding, bridging caveola assembly basement membrane organization scaffold protein binding uc003vid.1 uc003vid.2 uc003vid.3 uc003vid.4 uc003vid.5 
ENST00000222718.7 HOXA2 ENST00000222718.7 homeobox A2 (from RefSeq NM_006735.4) A1L4K3 B2RMW3 ENST00000222718.1 ENST00000222718.2 ENST00000222718.3 ENST00000222718.4 ENST00000222718.5 ENST00000222718.6 HOX1K HXA2_HUMAN NM_006735 O43364 uc003syh.1 uc003syh.2 uc003syh.3 uc003syh.4 uc003syh.5 In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. The encoded protein may be involved in the placement of hindbrain segments in the proper location along the anterior-posterior axis during development. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC130571.1, CN431833.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142670 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222718.7/ ENSP00000222718.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Nucleus. Microtia, hearing impairment, and cleft palate (MHICP) [MIM:612290]: A disease characterized by microtia, mixed symmetric severe to profound hearing impairment, and partial cleft palate. Microtia is a congenital deformity of the outer ear that is small and abnormally shaped. In classic microtia, the pinna is essentially absent, except for a vertical sausage-shaped skin remnant. The superior aspect of this sausage-shaped skin remnant consists of underlying unorganized cartilage, and the inferior aspect of this remnant consists of a relatively well-formed lobule. Syndromic forms of microtia occur in conjunction with other abnormalities including cleft palate, a congenital fissure of the soft and/or hard palate due to faulty fusion. Note=The disease is caused by variants affecting the gene represented in this entry. Microtia with or without hearing impairment (MCRT) [MIM:612290]: Microtia is a congenital deformity of the outer ear that is small and abnormally shaped. In classic microtia, the pinna is essentially absent, except for a vertical sausage-shaped skin remnant. The superior aspect of this sausage-shaped skin remnant consists of underlying unorganized cartilage, and the inferior aspect of this remnant consists of a relatively well-formed lobule. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the Antp homeobox family. Proboscipedia subfamily. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding cell fate determination osteoblast development DNA binding transcription factor activity, sequence-specific DNA binding nucleus regulation of transcription, DNA-templated multicellular organism development segment specification pattern specification process motor neuron axon guidance anterior/posterior pattern specification dorsal/ventral pattern formation rhombomere 2 development rhombomere 3 development rhombomere 3 morphogenesis brain segmentation middle ear morphogenesis intracellular membrane-bounded organelle sequence-specific DNA binding cell fate commitment negative regulation of neuron differentiation negative regulation of osteoblast differentiation positive regulation of transcription from RNA polymerase II promoter embryonic viscerocranium morphogenesis embryonic skeletal system morphogenesis cellular response to retinoic acid uc003syh.1 uc003syh.2 uc003syh.3 uc003syh.4 uc003syh.5 
ENST00000222725.10 LFNG ENST00000222725.10 LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase, transcript variant 1 (from RefSeq NM_001040167.2) B3KTY6 B5MCR5 ENST00000222725.1 ENST00000222725.2 ENST00000222725.3 ENST00000222725.4 ENST00000222725.5 ENST00000222725.6 ENST00000222725.7 ENST00000222725.8 ENST00000222725.9 LFNG LFNG_HUMAN NM_001040167 O00589 Q8NES3 Q96C39 Q9UJW5 uc003smf.1 uc003smf.2 uc003smf.3 uc003smf.4 uc003smf.5 This gene is a member of the glycosyltransferase 31 gene family. Members of this gene family, which also includes the MFNG (GeneID: 4242) and RFNG (GeneID: 5986) genes, encode evolutionarily conserved glycosyltransferases that act in the Notch signaling pathway to define boundaries during embryonic development. While their genomic structure is distinct from other glycosyltransferases, these proteins have a fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity that leads to elongation of O-linked fucose residues on Notch, which alters Notch signaling. The protein encoded by this gene is predicted to be a single-pass type II Golgi membrane protein but it may also be secreted and proteolytically processed like the related proteins in mouse and Drosophila (PMID: 9187150). Mutations in this gene have been associated with autosomal recessive spondylocostal dysostosis 3. [provided by RefSeq, May 2018]. Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O- fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (PubMed:11346656). Essential mediator of somite segmentation and patterning (By similarity). Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl- (1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA- COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222; Evidence=; Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP- N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl- (1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA- COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence=; Note=Manganese is the most effective. Can also use cobalt with lower efficiency. Has some activity with magnesium and calcium, but not zinc. ; Golgi apparatus Golgi apparatus membrane ; Single-pass type II membrane protein Event=Alternative splicing; Named isoforms=4; Comment=Experimental confirmation may be lacking for some isoforms.; Name=1; IsoId=Q8NES3-1; Sequence=Displayed; Name=2; IsoId=Q8NES3-2; Sequence=VSP_001792, VSP_001793; Name=3; IsoId=Q8NES3-3; Sequence=VSP_001794, VSP_001795; Name=4; IsoId=Q8NES3-4; Sequence=VSP_044850, VSP_044851; A soluble form may be derived from the membrane form by proteolytic processing. Spondylocostal dysostosis 3, autosomal recessive (SCDO3) [MIM:609813]: A condition of variable severity associated with vertebral and rib segmentation defects. The main skeletal malformations include fusion of vertebrae, hemivertebrae, fusion of certain ribs, and other rib malformations. Deformity of the chest and spine (severe scoliosis, kyphoscoliosis and lordosis) is a natural consequence of the malformation and leads to a dwarf-like appearance. As the thorax is small, infants frequently have respiratory insufficiency and repeated respiratory infections resulting in life-threatening complications in the first year of life. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyltransferase 31 family. Name=Functional Glycomics Gateway - GTase; Note=Beta-1,3- N-acetylglucosaminyltransferase lunatic fringe; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_551"; Golgi membrane ovarian follicle development somitogenesis marginal zone B cell differentiation molecular_function extracellular region Golgi apparatus multicellular organism development compartment pattern specification pattern specification process regulation of Notch signaling pathway animal organ morphogenesis regulation of somitogenesis membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups integral component of Golgi membrane T cell differentiation positive regulation of protein binding O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity protein O-linked fucosylation positive regulation of Notch signaling pathway metal ion binding positive regulation of meiotic cell cycle negative regulation of Notch signaling pathway involved in somitogenesis extracellular vesicle uc003smf.1 uc003smf.2 uc003smf.3 uc003smf.4 uc003smf.5 
ENST00000222726.4 HOXA5 ENST00000222726.4 homeobox A5 (from RefSeq NM_019102.4) A4D179 ENST00000222726.1 ENST00000222726.2 ENST00000222726.3 HOX1C HXA5_HUMAN NM_019102 O43367 P20719 Q96CY6 uc003syn.1 uc003syn.2 uc003syn.3 In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. Methylation of this gene may result in the loss of its expression and, since the encoded protein upregulates the tumor suppressor p53, this protein may play an important role in tumorigenesis. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC013682.1, ERR279833.10864.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN03267755, SAMN03267761 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222726.4/ ENSP00000222726.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Also binds to its own promoter. Binds specifically to the motif 5'-CYYNATTA[TG]Y-3'. Forms a DNA-binding heterodimer with transcription factor PBX1. P20719; Q92870-2: APBB2; NbExp=3; IntAct=EBI-8470697, EBI-21535880; P20719; P56545-3: CTBP2; NbExp=5; IntAct=EBI-8470697, EBI-10171902; P20719; Q92997: DVL3; NbExp=3; IntAct=EBI-8470697, EBI-739789; P20719; P42858: HTT; NbExp=9; IntAct=EBI-8470697, EBI-466029; P20719; P40425: PBX2; NbExp=5; IntAct=EBI-8470697, EBI-348489; P20719; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-8470697, EBI-79165; Nucleus. Expressed during embryogenesis and in adult kidney. Belongs to the Antp homeobox family. nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding skeletal system development morphogenesis of an epithelium respiratory system process DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated multicellular organism development pattern specification process respiratory gaseous exchange anterior/posterior pattern specification positive regulation of receptor biosynthetic process cell migration negative regulation of angiogenesis lung development thyroid gland development regulation of mammary gland epithelial cell proliferation multicellular organism growth positive regulation of apoptotic process sequence-specific DNA binding positive regulation of myeloid cell differentiation negative regulation of erythrocyte differentiation positive regulation of transcription from RNA polymerase II promoter lung alveolus development embryonic skeletal system morphogenesis embryonic skeletal system development bronchiole development trachea morphogenesis epithelial tube branching involved in lung morphogenesis lung goblet cell differentiation lobar bronchus epithelium development lung-associated mesenchyme development trachea cartilage morphogenesis cartilage morphogenesis intestinal epithelial cell maturation mesenchymal-epithelial cell signaling mammary gland epithelial cell differentiation mammary gland alveolus development cell-cell signaling involved in mammary gland development uc003syn.1 uc003syn.2 uc003syn.3 
ENST00000222728.3 HOXA6 ENST00000222728.3 homeobox A6 (from RefSeq NM_024014.4) A4D192 ENST00000222728.1 ENST00000222728.2 HOX1B HXA6_HUMAN NM_024014 P31267 Q2M3G3 Q9UPM0 uc003syo.1 uc003syo.2 uc003syo.3 In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC104915.1, EL736261.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222728.3/ ENSP00000222728.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Nucleus. Belongs to the Antp homeobox family. nuclear chromatin RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development anterior/posterior pattern specification sequence-specific DNA binding embryonic skeletal system morphogenesis embryonic skeletal system development uc003syo.1 uc003syo.2 uc003syo.3 
ENST00000222747.8 TSPAN12 ENST00000222747.8 tetraspanin 12 (from RefSeq NM_012338.4) A4D0V8 B4DRG6 ENST00000222747.1 ENST00000222747.2 ENST00000222747.3 ENST00000222747.4 ENST00000222747.5 ENST00000222747.6 ENST00000222747.7 NET2 NM_012338 O95859 Q549U9 Q8N5Y0 TM4SF12 TSN12_HUMAN UNQ774/PRO1568 uc003vjk.1 uc003vjk.2 uc003vjk.3 uc003vjk.4 uc003vjk.5 The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY358703.1, SRR3476690.754286.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222747.8/ ENSP00000222747.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt- dependent activation of FZD4, suggesting the existence of a Wnt- independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP- dependent cleavage activity. Component of a complex, at least composed of TSPAN12, FZD4 and norrin (NDP) (By similarity). Interacts (when palmitoylated) with ADAM10. Interacts with MMP14/MT1-MMP. O95859; O14672: ADAM10; NbExp=2; IntAct=EBI-2466403, EBI-1536151; O95859; PRO_0000029067 [O14672]: ADAM10; NbExp=2; IntAct=EBI-2466403, EBI-21222747; O95859; O95674: CDS2; NbExp=3; IntAct=EBI-2466403, EBI-3913685; O95859; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-2466403, EBI-12019274; O95859; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-2466403, EBI-2680384; O95859; P54852: EMP3; NbExp=3; IntAct=EBI-2466403, EBI-3907816; O95859; O00155: GPR25; NbExp=3; IntAct=EBI-2466403, EBI-10178951; O95859; O60883: GPR37L1; NbExp=3; IntAct=EBI-2466403, EBI-2927498; O95859; P24593: IGFBP5; NbExp=3; IntAct=EBI-2466403, EBI-720480; O95859; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-2466403, EBI-10317612; O95859; O14880: MGST3; NbExp=3; IntAct=EBI-2466403, EBI-724754; O95859; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-2466403, EBI-10317425; O95859; Q01453: PMP22; NbExp=3; IntAct=EBI-2466403, EBI-2845982; O95859; Q96AA3: RFT1; NbExp=3; IntAct=EBI-2466403, EBI-6269616; O95859; Q8N8N0: RNF152; NbExp=3; IntAct=EBI-2466403, EBI-2129725; O95859; Q9UNK0: STX8; NbExp=3; IntAct=EBI-2466403, EBI-727240; O95859; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-2466403, EBI-10329860; O95859; Q12800: TFCP2; NbExp=3; IntAct=EBI-2466403, EBI-717422; O95859; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-2466403, EBI-2844246; O95859; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-2466403, EBI-348587; O95859; Q6ZP80: TMEM182; NbExp=3; IntAct=EBI-2466403, EBI-10255122; O95859; A2RU14: TMEM218; NbExp=3; IntAct=EBI-2466403, EBI-10173151; Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95859-1; Sequence=Displayed; Name=2; IsoId=O95859-2; Sequence=VSP_038525; Palmitoylated; required for interaction with ADAM10. The precise position of palmitoylated residues is unclear and occurs either on Cys- 9, Cys-12 and/or Cys-83. Vitreoretinopathy, exudative 5 (EVR5) [MIM:613310]: A disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. te=The disease is caused by variants affecting the gene represented in this entry. TSPAN12 dominant and recessive mutations have been identified in patients with exudative vitreoretinopathy. Patients with mutations in both alleles of TSPAN12 have severe exudative vitreoretinopathy or retinal dysplasia. These mutations appear to result in a milder phenotype in heterozygous mutation carriers (PubMed:22427576). Belongs to the tetraspanin (TM4SF) family. angiogenesis protein binding plasma membrane integral component of plasma membrane cell surface receptor signaling pathway retina layer formation membrane integral component of membrane Wnt signaling pathway regulation of angiogenesis Wnt-activated receptor activity uc003vjk.1 uc003vjk.2 uc003vjk.3 uc003vjk.4 uc003vjk.5 
ENST00000222792.11 CHN2 ENST00000222792.11 chimerin 2, transcript variant 2 (from RefSeq NM_004067.4) A4D1A2 ARHGAP3 B3VCF1 B3VCF2 B3VCF3 B3VCF7 B3VCG1 BCH C9J7B0 CHIO_HUMAN E9PGE0 ENST00000222792.1 ENST00000222792.10 ENST00000222792.2 ENST00000222792.3 ENST00000222792.4 ENST00000222792.5 ENST00000222792.6 ENST00000222792.7 ENST00000222792.8 ENST00000222792.9 F8QPL9 NM_004067 P52757 Q2M203 Q75MM2 uc003szz.1 uc003szz.2 uc003szz.3 uc003szz.4 uc003szz.5 This gene encodes a guanosine triphosphate (GTP)-metabolizing protein that contains a phorbol-ester/diacylglycerol (DAG)-type zinc finger, a Rho-GAP domain, and an SH2 domain. The encoded protein translocates from the cytosol to the Golgi apparatus membrane upon binding by diacylglycerol (DAG). Activity of this protein is important in cell proliferation and migration, and expression changes in this gene have been detected in cancers. A mutation in this gene has also been associated with schizophrenia in men. Alternative transcript splicing and the use of alternative promoters results in multiple transcript variants. [provided by RefSeq, May 2014]. GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low- grade to high-grade tumors. In the inactive state, the N terminus protrudes into the active site of the Rho-GAP domain, sterically blocking Rac binding. Phospholipid binding to the Phorbol-ester/DAG-type zinc- finger/C1 domain triggers the cooperative dissociation of these interactions, allowing the N-terminus to move out of the active site and thereby activating the enzyme. P52757; Q8NFD2: ANKK1; NbExp=3; IntAct=EBI-714925, EBI-13280688; P52757; P16333: NCK1; NbExp=3; IntAct=EBI-714925, EBI-389883; P52757; O43639: NCK2; NbExp=6; IntAct=EBI-714925, EBI-713635; P52757; P63000: RAC1; NbExp=4; IntAct=EBI-714925, EBI-413628; P52757; Q96LD8: SENP8; NbExp=3; IntAct=EBI-714925, EBI-1041210; P52757; Q8N9I8: SHF; NbExp=3; IntAct=EBI-714925, EBI-14328833; Membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=9; Name=Beta-2; IsoId=P52757-1; Sequence=Displayed; Name=Beta-1; IsoId=P52757-2; Sequence=Not described; Name=3; IsoId=P52757-3; Sequence=VSP_046271, VSP_046272; Name=4; Synonyms=B1-CHNdel ex7p; IsoId=P52757-4; Sequence=VSP_047600, VSP_047601; Name=5; Synonyms=B1-CHNdel ex9; IsoId=P52757-5; Sequence=VSP_046271, VSP_046272, VSP_047602; Name=6; Synonyms=B1-CHNdel ex7p,11; IsoId=P52757-6; Sequence=VSP_047600, VSP_047601, VSP_047603; Name=7; IsoId=P52757-7; Sequence=VSP_046271, VSP_046272, VSP_047603; Name=8; IsoId=P52757-8; Sequence=VSP_053323; Name=Beta-3; IsoId=P52757-9; Sequence=VSP_053679; Highest levels in the brain and pancreas. Also expressed in the heart, placenta, and weakly in the kidney and liver. Expression is much reduced in the malignant gliomas, compared to normal brain or low-grade astrocytomas. SH3/SH2 adaptor activity GTPase activator activity protein binding cytosol signal transduction positive regulation of signal transduction membrane intracellular signal transduction regulation of GTPase activity positive regulation of GTPase activity metal ion binding regulation of small GTPase mediated signal transduction uc003szz.1 uc003szz.2 uc003szz.3 uc003szz.4 uc003szz.5 
ENST00000222800.8 ABHD11 ENST00000222800.8 abhydrolase domain containing 11, transcript variant 5 (from RefSeq NR_169872.1) ABHD11 ABHDB_HUMAN ENST00000222800.1 ENST00000222800.2 ENST00000222800.3 ENST00000222800.4 ENST00000222800.5 ENST00000222800.6 ENST00000222800.7 H7BYM8 NR_169872 PP1226 Q6PJU0 Q8N722 Q8N723 Q8NFV2 Q8NFV3 Q8NFV4 Q9HBS8 WBSCR21 uc003tzb.1 uc003tzb.2 uc003tzb.3 uc003tzb.4 uc003tzb.5 Catalyzes the hydrolysis of diacylglycerol in vitro and may function as a key regulator in lipid metabolism, namely by regulating the intracellular levels of diacylglycerol (PubMed:32579589). 1,2- diacyl-sn-glycerols are the preferred substrate over 1,3-diacyl-sn- glycerols (By similarity). The enzyme hydrolyzes stearate in preference to palmitate from the sn-1 position of 1,2-diacyl-sn-glycerols (By similarity). Maintains the functional lipoylation of the 2-oxoglutarate dehydrogenase complex (OGDHc) through its interaction with the OGDHc by preventing the formation of lipoyl adducts (PubMed:32792488). In addition, is also required for the expansion and differentiation of embryonic stem cells (ESCs) (By similarity). Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:38507, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:52392, ChEBI:CHEBI:75728; Evidence=; Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815, ChEBI:CHEBI:28868; EC=3.1.1.116; Evidence=; Reaction=a 1,3-diacyl-sn-glycerol + H2O = a 1-acyl-sn-glycerol + a fatty acid + H(+); Xref=Rhea:RHEA:38503, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64683, ChEBI:CHEBI:77272; Evidence=; Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H2O = 2-(9Z- octadecenoyl)-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:77103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:73990, ChEBI:CHEBI:75468; Evidence=; Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- glycerol + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:77107, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:77129, ChEBI:CHEBI:186738; Evidence=; Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol + H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605; Evidence=; Kinetic parameters: KM=18.6 uM for 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn- glycerol ; Vmax=2600 nmol/min/mg enzyme toward 1-octadecanoyl-2-(5Z,8Z,11Z,14Z- eicosatetraenoyl)-sn-glycerol ; Interacts with OGDH and DLST; this interaction maintains the functional lipoylation of the 2-oxoglutarate dehydrogenase complex. Q8NFV4-4; X5D778: ANKRD11; NbExp=3; IntAct=EBI-12318443, EBI-17183751; Q8NFV4-4; P33240: CSTF2; NbExp=3; IntAct=EBI-12318443, EBI-711360; Q8NFV4-4; Q6PKX4: DOK6; NbExp=3; IntAct=EBI-12318443, EBI-2880244; Q8NFV4-4; Q86UW9: DTX2; NbExp=3; IntAct=EBI-12318443, EBI-740376; Q8NFV4-4; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-12318443, EBI-10242151; Q8NFV4-4; P28676: GCA; NbExp=3; IntAct=EBI-12318443, EBI-947242; Q8NFV4-4; O43593: HR; NbExp=3; IntAct=EBI-12318443, EBI-2880706; Q8NFV4-4; Q99750: MDFI; NbExp=3; IntAct=EBI-12318443, EBI-724076; Q8NFV4-4; Q6PF18: MORN3; NbExp=3; IntAct=EBI-12318443, EBI-9675802; Q8NFV4-4; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-12318443, EBI-11022007; Q8NFV4-4; P78337: PITX1; NbExp=3; IntAct=EBI-12318443, EBI-748265; Q8NFV4-4; O43741: PRKAB2; NbExp=3; IntAct=EBI-12318443, EBI-1053424; Q8NFV4-4; O75360: PROP1; NbExp=3; IntAct=EBI-12318443, EBI-9027467; Q8NFV4-4; P0CG20: PRR35; NbExp=3; IntAct=EBI-12318443, EBI-11986293; Q8NFV4-4; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-12318443, EBI-6257312; Q8NFV4-4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12318443, EBI-739895; Q8NFV4-4; Q08AM6: VAC14; NbExp=3; IntAct=EBI-12318443, EBI-2107455; Q8NFV4-4; O95231: VENTX; NbExp=3; IntAct=EBI-12318443, EBI-10191303; Q8NFV4-4; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12318443, EBI-2559305; Q8NFV4-4; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-12318443, EBI-12040603; Q8NFV4-4; Q9BYJ9: YTHDF1; NbExp=3; IntAct=EBI-12318443, EBI-1051237; Q8NFV4-4; Q15915: ZIC1; NbExp=3; IntAct=EBI-12318443, EBI-11963196; Mitochondrion Mitochondrion matrix Event=Alternative splicing; Named isoforms=6; Name=1; Synonyms=A; IsoId=Q8NFV4-1; Sequence=Displayed; Name=2; Synonyms=B; IsoId=Q8NFV4-2; Sequence=VSP_023925, VSP_023928; Name=3; Synonyms=C; IsoId=Q8NFV4-3; Sequence=VSP_023926, VSP_023927; Name=4; Synonyms=D; IsoId=Q8NFV4-4; Sequence=VSP_023924; Name=5; Synonyms=E; IsoId=Q8NFV4-5; Sequence=VSP_023924, VSP_023929, VSP_023930; Name=6; IsoId=Q8NFV4-6; Sequence=VSP_046994; Ubiquitously expressed (PubMed:12073013). Highly expressed in small intestine, prostate and thyroid, while aorta and colon tissues exhibit weak expression levels (PubMed:32579589). Phosphorylated. Note=ABHD11 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. [Isoform 2]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. [Isoform 3]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the AB hydrolase superfamily. Sequence=AAG17214.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence=; Sequence=AAH08251.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAH11712.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAH67750.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAL14848.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAL14849.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAM62312.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAM62313.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAM62314.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=AAS07472.1; Type=Erroneous gene model prediction; Evidence=; molecular_function cellular_component mitochondrion biological_process hydrolase activity uc003tzb.1 uc003tzb.2 uc003tzb.3 uc003tzb.4 uc003tzb.5 
ENST00000222803.10 FKBP14 ENST00000222803.10 FKBP prolyl isomerase 14, transcript variant 3 (from RefSeq NR_046479.2) ENST00000222803.1 ENST00000222803.2 ENST00000222803.3 ENST00000222803.4 ENST00000222803.5 ENST00000222803.6 ENST00000222803.7 ENST00000222803.8 ENST00000222803.9 FKB14_HUMAN FKBP22 NR_046479 Q9NWM8 UNQ322/PRO381 uc003tal.1 uc003tal.2 uc003tal.3 uc003tal.4 The protein encoded by this gene is a member of the FK506-binding protein family of peptidyl-prolyl cis-trans isomerases. The encoded protein is found in the lumen of the endoplasmic reticulum, where it is thought to accelerate protein folding. Defects in this gene are a cause of a type of Ehlers-Danlos syndrome (EDS). Both a protein-coding variant and noncoding variants are transcribed from this gene. [provided by RefSeq, Mar 2012]. PPIase which accelerates the folding of proteins during protein synthesis. Has a preference for substrates containing 4- hydroxylproline modifications, including type III collagen. May also target type VI and type X collagens. Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence=; Inhibited by tacrolimus/FK506. Monomer (PubMed:24821723, PubMed:24272907). Homodimer (PubMed:24821723, PubMed:24272907). Interacts with type III, type IV and type X collagens (PubMed:24821723). Q9NWM8; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-2477093, EBI-10982110; Endoplasmic reticulum lumen Ehlers-Danlos syndrome, kyphoscoliotic type, 2 (EDSKSCL2) [MIM:614557]: A form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. EDSKSCL2 is an autosomal recessive form characterized by severe generalized hypotonia at birth, myopathy, early-onset progressive kyphoscoliosis, joint hypermobility without contractures, hyperelastic skin with follicular hyperkeratosis, easy bruising, and occasional abnormal scarring, sensorineural hearing impairment, and normal pyridinoline excretion in urine. Note=The disease is caused by variants affecting the gene represented in this entry. protein peptidyl-prolyl isomerization peptidyl-prolyl cis-trans isomerase activity calcium ion binding endoplasmic reticulum endoplasmic reticulum lumen isomerase activity IRE1-mediated unfolded protein response metal ion binding uc003tal.1 uc003tal.2 uc003tal.3 uc003tal.4 
ENST00000222812.8 STX1A ENST00000222812.8 syntaxin 1A, transcript variant 1 (from RefSeq NM_004603.4) ENST00000222812.1 ENST00000222812.2 ENST00000222812.3 ENST00000222812.4 ENST00000222812.5 ENST00000222812.6 ENST00000222812.7 NM_004603 Q75ME0 Q75ME0_HUMAN STX1A hCG_96107 uc003tyx.1 uc003tyx.2 uc003tyx.3 uc003tyx.4 uc003tyx.5 This gene encodes a member of the syntaxin superfamily. Syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. Syntaxins possess a single C-terminal transmembrane domain, a SNARE [Soluble NSF (N-ethylmaleimide-sensitive fusion protein)-Attachment protein REceptor] domain (known as H3), and an N-terminal regulatory domain (Habc). Syntaxins bind synaptotagmin in a calcium-dependent fashion and interact with voltage dependent calcium and potassium channels via the C-terminal H3 domain. This gene product is a key molecule in ion channel regulation and synaptic exocytosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Sep 2009]. Cell membrane Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Single-pass type IV membrane protein Membrane Belongs to the syntaxin family. SNARE binding positive regulation of neurotransmitter secretion SNAP receptor activity plasma membrane integral component of plasma membrane intracellular protein transport synaptic vesicle voltage-gated potassium channel complex response to gravity positive regulation of norepinephrine secretion regulation of synaptic vesicle priming postsynaptic density membrane integral component of membrane synaptic vesicle exocytosis synaptic vesicle docking vesicle-mediated transport myosin binding calcium ion regulated exocytosis regulation of exocytosis calcium channel inhibitor activity protein domain specific binding insulin secretion secretory granule integral component of synaptic vesicle membrane axon synaptic vesicle membrane protein binding, bridging synaptic vesicle fusion to presynaptic active zone membrane nuclear membrane myosin head/neck binding macromolecular complex positive regulation of catecholamine secretion SNARE complex assembly actomyosin presynaptic membrane neuron projection ATP-dependent protein binding intracellular organelle ion channel binding regulated exocytosis positive regulation of exocytosis positive regulation of calcium ion-dependent exocytosis hormone secretion protein heterodimerization activity protein N-terminus binding vesicle docking calcium-dependent protein binding presynaptic active zone membrane synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex synaptobrevin 2-SNAP-25-syntaxin-1a complex protein localization to membrane modulation of excitatory postsynaptic potential glutamatergic synapse integral component of presynaptic membrane positive regulation of excitatory postsynaptic potential uc003tyx.1 uc003tyx.2 uc003tyx.3 uc003tyx.4 uc003tyx.5 
ENST00000222823.9 NOD1 ENST00000222823.9 nucleotide binding oligomerization domain containing 1, transcript variant 1 (from RefSeq NM_006092.4) B4DTU3 CARD4 ENST00000222823.1 ENST00000222823.2 ENST00000222823.3 ENST00000222823.4 ENST00000222823.5 ENST00000222823.6 ENST00000222823.7 ENST00000222823.8 NM_006092 NOD1 NOD1_HUMAN Q549U4 Q8IWF5 Q9Y239 uc003tav.1 uc003tav.2 uc003tav.3 uc003tav.4 uc003tav.5 This gene encodes a member of the nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family of proteins. The encoded protein plays a role in innate immunity by acting as a pattern-recognition receptor (PRR) that binds bacterial peptidoglycans and initiates inflammation. This protein has also been implicated in the immune response to viral and parasitic infection. Major structural features of this protein include an N-terminal caspase recruitment domain (CARD), a centrally located nucleotide-binding domain (NBD), and 10 tandem leucine-rich repeats (LRRs) in its C terminus. The CARD is involved in apoptotic signaling, LRRs participate in protein-protein interactions, and mutations in the NBD may affect the process of oligomerization and subsequent function of the LRR domain. Mutations in this gene are associated with asthma, inflammatory bowel disease, Behcet disease and sarcoidosis in human patients. [provided by RefSeq, Aug 2017]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.197963.1, BC040339.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000222823.9/ ENSP00000222823.4 RefSeq Select criteria :: based on conservation, longest protein ##RefSeq-Attributes-END## Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses (PubMed:11058605, PubMed:12796777, PubMed:12791997, PubMed:15044951, PubMed:16172124, PubMed:19043560, PubMed:22672233, PubMed:27099311). Specifically recognizes and binds gamma-D-glutamyl-meso-diaminopimelic acid (iE- DAP), a dipeptide present in peptidoglycan of Gram-negative bacteria (PubMed:12871942, PubMed:12796777, PubMed:12791997, PubMed:16211083, PubMed:16172124). Preferentially binds iE-DAP in tripeptide-containing muropeptides (MurNAc-TriDAP or TriDAP) (PubMed:16211083). Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (PubMed:12796777, PubMed:12791997, PubMed:17054981). Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:10880512, PubMed:12791997, PubMed:19043560). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (PubMed:10880512, PubMed:19043560). Also acts as a regulator of antiviral response elicited by dsRNA and the expression of RLR pathway members by targeting IFIH1 and TRAF3 to modulate the formation of IFIH1-MAVS and TRAF3-MAVS complexes leading to increased transcription of type I IFNs (PubMed:32169843). Also acts as a regulator of autophagy via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling (PubMed:27007849, PubMed:33942347). In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner (By similarity). Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm (By similarity). [Isoform 3]: In contrast to isoform 1, does not efficiently recognize and bind gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) ligand. Homooligomer: homooligomerizes following ligand-binding, promoting RIPK2 recruitment (PubMed:10880512). Interacts (via CARD domain) with RIPK2 (via CARD domain) (PubMed:10880512, PubMed:30478312, PubMed:23300079, PubMed:17054981). Following RIPK2 recruitment, RIPK2 homooligomerizes via its CARD domain and forms long filaments named RIPosomes (PubMed:30478312). Interacts with ARHGEF2 (PubMed:19043560). Interacts (via CARD domain) with ubiquitin; inhibiting interaction with RIPK2 (PubMed:23300079, PubMed:25127239). Interacts with NLRP10 and recruits it to the cell membrane following invasive bacterial infection (PubMed:22672233). Interacts with IFIH1; this interaction promotes transcription of antiviral genes and inhibition of viral replication (PubMed:32169843). Interacts with IRGM; promoting NOD1 degradation (PubMed:36221902). Interacts with ATG16L1 (By similarity). Q9Y239; P02489: CRYAA; NbExp=3; IntAct=EBI-1051262, EBI-6875961; Q9Y239; P14136: GFAP; NbExp=3; IntAct=EBI-1051262, EBI-744302; Q9Y239; Q53GS7: GLE1; NbExp=3; IntAct=EBI-1051262, EBI-1955541; Q9Y239; P42858: HTT; NbExp=9; IntAct=EBI-1051262, EBI-466029; Q9Y239; Q92876: KLK6; NbExp=3; IntAct=EBI-1051262, EBI-2432309; Q9Y239; P02545: LMNA; NbExp=3; IntAct=EBI-1051262, EBI-351935; Q9Y239; Q9Y239: NOD1; NbExp=2; IntAct=EBI-1051262, EBI-1051262; Q9Y239; Q6UX06: OLFM4; NbExp=2; IntAct=EBI-1051262, EBI-2804156; Q9Y239; Q13153: PAK1; NbExp=3; IntAct=EBI-1051262, EBI-1307; Q9Y239; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1051262, EBI-5235340; Q9Y239; Q9Y2Z0: SUGT1; NbExp=5; IntAct=EBI-1051262, EBI-307008; Q9Y239; A0A0H3NF38: sspH2; Xeno; NbExp=4; IntAct=EBI-1051262, EBI-10689860; Cell membrane ; Lipid-anchor Apical cell membrane Basolateral cell membrane Cytoplasm te=Detected in the cytoplasm and at the cell membrane (PubMed:31649195). Following bacterial infection, localizes to bacterial entry sites in the cell membrane (PubMed:31649195). Recruited to the basolateral and apical membranes in polarized epithelial cells (PubMed:19043560). Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=Alpha; IsoId=Q9Y239-1; Sequence=Displayed; Name=2; IsoId=Q9Y239-2; Sequence=VSP_055825, VSP_055826; Name=3; Synonyms=Beta, delta10 ; IsoId=Q9Y239-3; Sequence=VSP_061942; Highly expressed in adult heart, skeletal muscle, pancreas, spleen and ovary (PubMed:10224040). Also detected in placenta, lung, liver, kidney, thymus, testis, small intestine and colon (PubMed:10224040). The LRR repeats recognize and bind gamma-D-glutamyl-meso- diaminopimelic acid (iE-DAP). Palmitoylated. Palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection. Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activation. Degraded via selective autophagy following interaction with IRGM (PubMed:36221902). IRGM promotes NOD1-RIPK2 RIPosome recruitment to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation (PubMed:36221902). Belongs to the NOD1-NOD2 family. Human and mouse NOD1 bind gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) in a different context (PubMed:16211083). do not detect the same muropeptide from bacterial peptidoglycan: while human NOD1 detects a tripeptide-containing muropeptide (MurNAc-TriDAP or TriDAP), mouse Nod1 needs a tetrapeptide structure for efficient sensing (MurNAc-tetraDAP or TetraDAP) (PubMed:16211083). nucleotide binding activation of MAPK activity immune system process positive regulation of dendritic cell antigen processing and presentation protein binding ATP binding cytoplasm cytosol plasma membrane apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process defense response inflammatory response signal transduction JNK cascade cysteine-type endopeptidase activator activity involved in apoptotic process detection of biotic stimulus positive regulation of cell death membrane detection of bacterium basolateral plasma membrane apical plasma membrane positive regulation of interleukin-1 beta production positive regulation of interleukin-6 production positive regulation of tumor necrosis factor production positive regulation of stress-activated MAPK cascade intracellular signal transduction interleukin-8 biosynthetic process defense response to bacterium identical protein binding protein homodimerization activity peptidoglycan binding regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of cysteine-type endopeptidase activity involved in apoptotic process macromolecular complex binding innate immune response positive regulation of JNK cascade CARD domain binding defense response to Gram-positive bacterium positive regulation of nitric-oxide synthase activity positive regulation of NF-kappaB transcription factor activity positive regulation of ERK1 and ERK2 cascade nucleotide-binding oligomerization domain containing signaling pathway interleukin-1-mediated signaling pathway cellular response to muramyl dipeptide positive regulation of NIK/NF-kappaB signaling positive regulation of xenophagy uc003tav.1 uc003tav.2 uc003tav.3 uc003tav.4 uc003tav.5 
ENST00000222902.7 CCL24 ENST00000222902.7 C-C motif chemokine ligand 24, transcript variant 2 (from RefSeq NM_002991.3) B2R5K2 CCL24 CCL24_HUMAN ENST00000222902.1 ENST00000222902.2 ENST00000222902.3 ENST00000222902.4 ENST00000222902.5 ENST00000222902.6 MPIF2 NM_002991 O00175 SCYA24 uc011kga.1 uc011kga.2 uc011kga.3 uc011kga.4 This gene belongs to the subfamily of small cytokine CC genes. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity on resting T lymphocytes, a minimal activity on neutrophils, and is negative on monocytes and activated T lymphocytes. The protein is also a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line. [provided by RefSeq, Jul 2008]. Chemotactic for resting T-lymphocytes, and eosinophils (PubMed:9104803, PubMed:9365122). Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes (PubMed:9104803, PubMed:9365122). Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line (PubMed:9104803, PubMed:9365122). Binds to CCR3 (PubMed:9104803, PubMed:9365122). O00175; P13501: CCL5; NbExp=3; IntAct=EBI-16803966, EBI-2848366; O00175; O14625: CXCL11; NbExp=2; IntAct=EBI-16803966, EBI-2871971; Secreted Activated monocytes and activated T lymphocytes. N-glycosylated. Belongs to the intercrine beta (chemokine CC) family. Name=Wikipedia; Note=CCL24 entry; URL="https://en.wikipedia.org/wiki/CCL24"; positive regulation of endothelial cell proliferation monocyte chemotaxis cytokine activity protein binding extracellular region extracellular space chemotaxis inflammatory response immune response cytoskeleton organization signal transduction G-protein coupled receptor signaling pathway cell-cell signaling chemokine activity regulation of cell shape positive regulation of cell migration neutrophil chemotaxis positive regulation of actin filament polymerization CCR3 chemokine receptor binding positive regulation of GTPase activity positive regulation of angiogenesis receptor agonist activity CCR chemokine receptor binding eosinophil chemotaxis lymphocyte chemotaxis positive regulation of inflammatory response chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor positive regulation of eosinophil migration uc011kga.1 uc011kga.2 uc011kga.3 uc011kga.4 
ENST00000222969.10 BUD31 ENST00000222969.10 BUD31 homolog, transcript variant 1 (from RefSeq NM_003910.4) A4D274 B7Z4S9 BUD31_HUMAN D6W5S6 EDG2 ENST00000222969.1 ENST00000222969.2 ENST00000222969.3 ENST00000222969.4 ENST00000222969.5 ENST00000222969.6 ENST00000222969.7 ENST00000222969.8 ENST00000222969.9 NM_003910 P41223 Q6IB53 Q9UDV1 uc003uqg.1 uc003uqg.2 uc003uqg.3 uc003uqg.4 uc003uqg.5 uc003uqg.6 Involved in the pre-mRNA splicing process (PubMed:28502770, PubMed:28076346). May play a role as regulator of AR transcriptional activity; may increase AR transcriptional activity (PubMed:25091737). Identified in the spliceosome C complex (PubMed:28502770, PubMed:28076346). May interact with AR (PubMed:25091737). P41223; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-3904603, EBI-724373; P41223; P49639: HOXA1; NbExp=3; IntAct=EBI-3904603, EBI-740785; P41223; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-3904603, EBI-10172290; P41223; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3904603, EBI-16439278; P41223; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3904603, EBI-79165; Nucleus Note=Detected in chromatin at the promoter of AR target genes. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P41223-1; Sequence=Displayed; Name=2; IsoId=P41223-2; Sequence=VSP_055558; Detected in epithelial and stromal cells in benign prostate hyperplasia tissue (at protein level). Contains a short sequence motif (Phe-Xaa-Xaa-Phe-Tyr) that can bind to AR and may modulate AR activity. Belongs to the BUD31 (G10) family. mRNA splicing, via spliceosome protein binding nucleus nucleoplasm spliceosomal complex mRNA processing RNA splicing ligand-dependent nuclear receptor transcription coactivator activity nuclear hormone receptor binding U2-type catalytic step 2 spliceosome positive regulation of nucleic acid-templated transcription positive regulation of androgen receptor activity nuclear chromatin uc003uqg.1 uc003uqg.2 uc003uqg.3 uc003uqg.4 uc003uqg.5 uc003uqg.6 
ENST00000222982.8 CYP3A5 ENST00000222982.8 cytochrome P450 family 3 subfamily A member 5, transcript variant 5 (from RefSeq NM_001291830.2) A4D289 B7Z5I7 CP3A5_HUMAN CYP3A5 ENST00000222982.1 ENST00000222982.2 ENST00000222982.3 ENST00000222982.4 ENST00000222982.5 ENST00000222982.6 ENST00000222982.7 NM_001291830 P20815 Q53WY8 Q75MV0 Q9HB56 uc003urq.1 uc003urq.2 uc003urq.3 uc003urq.4 This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The encoded protein metabolizes drugs as well as the steroid hormones testosterone and progesterone. This gene is part of a cluster of cytochrome P450 genes on chromosome 7q21.1. Two pseudogenes of this gene have been identified within this cluster on chromosome 7. Expression of this gene is widely variable among populations, and a single nucleotide polymorphism that affects transcript splicing has been associated with susceptibility to hypertensions. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2014]. A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins (PubMed:2732228, PubMed:10681376, PubMed:11093772, PubMed:12865317). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds (PubMed:12865317, PubMed:2732228, PubMed:10681376, PubMed:11093772). Exhibits high catalytic activity for the formation of catechol estrogens from 17beta- estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2 (PubMed:12865317). Catalyzes 6beta-hydroxylation of the steroid hormones testosterone, progesterone, and androstenedione (PubMed:2732228). Catalyzes the oxidative conversion of all-trans- retinol to all-trans-retinal, a rate-limiting step for the biosynthesis of all-trans-retinoic acid (atRA) (PubMed:10681376). Further metabolizes all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in hepatic atRA clearance (PubMed:11093772). Also involved in the oxidative metabolism of xenobiotics, including calcium channel blocking drug nifedipine and immunosuppressive drug cyclosporine (PubMed:2732228). Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence= Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213; Evidence=; Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281; Evidence=; Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2- hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; Evidence=; Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4- hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87602; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293; Evidence=; Reaction=O2 + reduced [NADPH--hemoprotein reductase] + testosterone = 6beta,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46296, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17347, ChEBI:CHEBI:34477, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46297; Evidence=; Reaction=androst-4-ene-3,17-dione + O2 + reduced [NADPH--hemoprotein reductase] = 6beta-hydroxyandrost-4-ene-3,17-dione + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47256, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87571; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47257; Evidence=; Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 6beta-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47252, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17026, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62117; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47253; Evidence=; Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093; Evidence=; Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Kinetic parameters: KM=52.47 uM for 17beta-estradiol (2-hydroxylation) ; KM=46.03 uM for 17beta-estradiol (4-hydroxylation) ; KM=15.04 uM for estrone (2-hydroxylation) ; KM=27.75 uM for estrone (4-hydroxylation) ; KM=44 uM for all-trans-retinoate (4-hydroxylation) ; Vmax=627.4 pmol/min/nmol enzyme toward 17beta-estradiol (2- hydroxylation) ; Vmax=297.8 pmol/min/nmol enzyme toward 17beta-estradiol (4- hydroxylation) ; Vmax=102.6 pmol/min/nmol enzyme toward estrone (2-hydroxylation) ; Vmax=156.3 pmol/min/nmol enzyme toward estrone (4-hydroxylation) ; Vmax=1124 pmol/min/nmol enzyme toward all-trans-retinoate (4- hydroxylation) ; Steroid hormone biosynthesis. Cofactor metabolism; retinol metabolism. P20815; P42858: HTT; NbExp=3; IntAct=EBI-3908011, EBI-466029; Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P20815-1; Sequence=Displayed; Name=2; IsoId=P20815-2; Sequence=VSP_042734, VSP_042735; By glucocorticoids, such as dexamethesone. Chimeric transcripts, characterized by CYP3A43 exon 1 joined at canonical splice sites to distinct sets of CYP3A5 exons, have been detected. All are possibly produced by trans-splicing. The chimeric transcripts exist in 2 different combinations: CYP3A43 exon 1 joined in frame to CYP3A5 exon 11-13 and CYP3A43 exon 1 joined in frame to CYP3A5 exon 12-13. All chimeric transcripts are expressed at very low levels in the liver (PubMed:11726664). Belongs to the cytochrome P450 family. Name=PharmVar Pharmacogen Variation Consortium; Note=CYP3A5 alleles; URL="https://www.pharmvar.org/gene/CYP3A5"; lipid hydroxylation monooxygenase activity iron ion binding endoplasmic reticulum endoplasmic reticulum membrane lipid metabolic process xenobiotic metabolic process steroid metabolic process estrogen metabolic process steroid hydroxylase activity retinoic acid 4-hydroxylase activity alkaloid catabolic process membrane oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen oxygen binding heme binding organelle membrane retinol metabolic process retinoic acid metabolic process drug catabolic process intracellular membrane-bounded organelle metal ion binding testosterone 6-beta-hydroxylase activity oxidation-reduction process aromatase activity oxidative demethylation estrogen 16-alpha-hydroxylase activity uc003urq.1 uc003urq.2 uc003urq.3 uc003urq.4 
ENST00000222990.8 SNX8 ENST00000222990.8 sorting nexin 8 (from RefSeq NM_013321.4) A4D207 ENST00000222990.1 ENST00000222990.2 ENST00000222990.3 ENST00000222990.4 ENST00000222990.5 ENST00000222990.6 ENST00000222990.7 NM_013321 Q96I67 Q9Y5X2 SNX8_HUMAN uc003slw.1 uc003slw.2 uc003slw.3 uc003slw.4 May be involved in several stages of intracellular trafficking. May play a role in intracellular protein transport from early endosomes to the trans-Golgi network. Q9Y5X2; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-1752557, EBI-714543; Q9Y5X2; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-1752557, EBI-725606; Q9Y5X2; P16333: NCK1; NbExp=2; IntAct=EBI-1752557, EBI-389883; Q9Y5X2; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-1752557, EBI-712367; Q9Y5X2; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-1752557, EBI-14065960; Q9Y5X2; Q9Y5X2: SNX8; NbExp=2; IntAct=EBI-1752557, EBI-1752557; Early endosome membrane ; Peripheral membrane protein ; Cytoplasmic side Note=Colocalizes with retromer components. Belongs to the sorting nexin family. protein binding endosome cytosol intracellular protein transport lipid binding protein transport membrane early endosome membrane early endosome to Golgi transport phosphatidylinositol binding retrograde transport, endosome to Golgi identical protein binding intracellular membrane-bounded organelle retromer complex uc003slw.1 uc003slw.2 uc003slw.3 uc003slw.4 
ENST00000223023.5 WASL ENST00000223023.5 WASP like actin nucleation promoting factor (from RefSeq NM_003941.4) A1JUI9 ENST00000223023.1 ENST00000223023.2 ENST00000223023.3 ENST00000223023.4 NM_003941 O00401 Q7Z746 WASL_HUMAN uc003vkz.1 uc003vkz.2 uc003vkz.3 uc003vkz.4 uc003vkz.5 uc003vkz.6 This gene encodes a member of the Wiskott-Aldrich syndrome (WAS) protein family. Wiskott-Aldrich syndrome proteins share similar domain structure, and associate with a variety of signaling molecules to alter the actin cytoskeleton. The encoded protein is highly expressed in neural tissues, and interacts with several proteins involved in cytoskeletal organization, including cell division control protein 42 (CDC42) and the actin-related protein-2/3 (ARP2/3) complex. The encoded protein may be involved in the formation of long actin microspikes, and in neurite extension. [provided by RefSeq, Jul 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC052955.1, SRR1660805.240690.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223023.5/ ENSP00000223023.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Regulates actin polymerization by stimulating the actin- nucleating activity of the Arp2/3 complex (PubMed:9422512, PubMed:16767080, PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828). Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization (PubMed:9422512, PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828). Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia (PubMed:9422512). In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (PubMed:16767080). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression (By similarity). Plays a role in dendrite spine morphogenesis (By similarity). Decreasing levels of DNMBP (using antisense RNA) alters apical junction morphology in cultured enterocytes, junctions curve instead of being nearly linear (PubMed:19767742). Binds actin and the Arp2/3 complex (PubMed:22847007). Interacts with CDC42 (PubMed:9422512). Interacts with FCHSD1 (By similarity). Interacts with FCHSD2 (PubMed:29887380). Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP (PubMed:19767742, PubMed:24332715, PubMed:17015620). Interacts with SNX9 (By similarity). Interacts with the WW domains of PRPF40A/FBP11 (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with NOSTRIN (PubMed:16234328). Binds to TNK2 (PubMed:16257963). Interacts with SNX33 (PubMed:19487689). Interacts with NONO (via second RRM domain); the interaction is direct (PubMed:16767080). Component of a multiprotein complex with NONO and SFPQ; associates with the complex via direct interaction with NONO (PubMed:16767080). (Microbial infection) Interacts with E.coli effector protein EspF(U) (PubMed:19366662, PubMed:22921828). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U) (PubMed:22921828). (Microbial infection) Interacts with Shigella flexneri protein IcsA (PubMed:9582270, PubMed:10491394). The interaction with IcsA enhances the affinity of WASL for Arp2/3, thus assembling a tight complex which has maximal activity in actin assembly (PubMed:9582270, PubMed:10491394). O00401; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-957615, EBI-11096309; O00401; Q8IWW6-4: ARHGAP12; NbExp=3; IntAct=EBI-957615, EBI-11959591; O00401; O15145: ARPC3; NbExp=6; IntAct=EBI-957615, EBI-351829; O00401; P59998: ARPC4; NbExp=3; IntAct=EBI-957615, EBI-351872; O00401; P60953: CDC42; NbExp=3; IntAct=EBI-957615, EBI-81752; O00401; Q99828: CIB1; NbExp=7; IntAct=EBI-957615, EBI-372594; O00401; Q6XZF7-1: DNMBP; NbExp=2; IntAct=EBI-957615, EBI-16085546; O00401; P62993: GRB2; NbExp=11; IntAct=EBI-957615, EBI-401755; O00401; A0A0S2Z4D7: NCK1; NbExp=3; IntAct=EBI-957615, EBI-16429340; O00401; P16333: NCK1; NbExp=2; IntAct=EBI-957615, EBI-389883; O00401; P16333-1: NCK1; NbExp=2; IntAct=EBI-957615, EBI-15578122; O00401; E7ERP6: NCK2; NbExp=3; IntAct=EBI-957615, EBI-16429362; O00401; O43639: NCK2; NbExp=7; IntAct=EBI-957615, EBI-713635; O00401; Q9UNF0: PACSIN2; NbExp=3; IntAct=EBI-957615, EBI-742503; O00401; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-957615, EBI-77926; O00401; O96013: PAK4; NbExp=8; IntAct=EBI-957615, EBI-713738; O00401; Q13882: PTK6; NbExp=3; IntAct=EBI-957615, EBI-1383632; O00401; Q9H4E5: RHOJ; NbExp=6; IntAct=EBI-957615, EBI-6285694; O00401; O76064: RNF8; NbExp=8; IntAct=EBI-957615, EBI-373337; O00401; O00560: SDCBP; NbExp=6; IntAct=EBI-957615, EBI-727004; O00401; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-957615, EBI-77848; O00401; O94875-10: SORBS2; NbExp=3; IntAct=EBI-957615, EBI-12037893; O00401; O60504-2: SORBS3; NbExp=3; IntAct=EBI-957615, EBI-1222956; O00401; Q15642-2: TRIP10; NbExp=5; IntAct=EBI-957615, EBI-6550597; O00401; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-957615, EBI-7353612; O00401; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-957615, EBI-1380492; O00401; O43516: WIPF1; NbExp=8; IntAct=EBI-957615, EBI-346356; O00401; Q8TF74: WIPF2; NbExp=5; IntAct=EBI-957615, EBI-2850112; O00401; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-957615, EBI-367540; O00401; P61157: ACTR3; Xeno; NbExp=3; IntAct=EBI-957615, EBI-351419; O00401; P0DJ88: espF(U); Xeno; NbExp=2; IntAct=EBI-957615, EBI-10039462; O00401; Q8X482: espF(U); Xeno; NbExp=5; IntAct=EBI-957615, EBI-22229752; O00401; Q8R511: Fnbp1; Xeno; NbExp=2; IntAct=EBI-957615, EBI-1111424; Cytoplasm, cytoskeleton Nucleus Cytoplasm Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (By similarity). Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity. actin cortical patch assembly actin binding protein binding nucleus cytoplasm cytosol cytoskeleton actin filament plasma membrane endocytosis membrane budding actin filament organization cell cycle actin polymerization or depolymerization response to bacterium actin cytoskeleton vesicle organization lamellipodium actin cytoskeleton organization actin filament polymerization actin filament-based movement vesicle transport along actin filament actin cap actin cortical patch endocytic vesicle membrane GTPase regulator activity cytoplasmic vesicle regulation of protein localization cellular protein complex localization Fc-gamma receptor signaling pathway involved in phagocytosis positive regulation of transcription from RNA polymerase II promoter ephrin receptor signaling pathway regulation of nitric-oxide synthase activity actin filament binding cell division positive regulation of filopodium assembly spindle localization actin cortical patch localization dendritic spine morphogenesis membrane organization macromolecular complex assembly extracellular exosome negative regulation of membrane tubulation positive regulation of clathrin-dependent endocytosis negative regulation of lymphocyte migration positive regulation of Arp2/3 complex-mediated actin nucleation uc003vkz.1 uc003vkz.2 uc003vkz.3 uc003vkz.4 uc003vkz.5 uc003vkz.6 
ENST00000223026.9 HYAL4 ENST00000223026.9 hyaluronidase 4 (from RefSeq NM_012269.3) D0VXG1 ENST00000223026.1 ENST00000223026.2 ENST00000223026.3 ENST00000223026.4 ENST00000223026.5 ENST00000223026.6 ENST00000223026.7 ENST00000223026.8 HYAL4_HUMAN NM_012269 Q2M3T9 Q9UL99 Q9Y6T9 uc003vlc.1 uc003vlc.2 uc003vlc.3 uc003vlc.4 uc003vlc.5 This gene encodes a protein which is similar in structure to hyaluronidases but lacks hyaluronidase activity. The encoded protein acts as a chondroitin-sulfate-specific endo-beta-N-acetylgalactosaminidase; that is, it exhibits hydrolytic activity toward chondroitin sulfate chains and degrades them into oligosaccharides. Proteoglycans are formed by the covalent linkage of chondroitin sulfate chains to protein. Proteoglycans are ubiquitous components of the extracellular matrix of connective tissues and are also found at the surface of many cell types where they participate in a variety of cellular processes such as cell proliferation, differentiation, migration, cell-cell recognition, extracellular matrix deposition, and tissue morphogenesis. The expression of this gene is highest in testes and placenta. [provided by RefSeq, Apr 2019]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by transcript alignments. ##Evidence-Data-START## CDS exon combination :: AB470346.1, BC104790.1 [ECO:0000331] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223026.9/ ENSP00000223026.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide. Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D- glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; pH dependence: Optimum pH is 4.5-5 (for chondroitin sulfate hydrolase activity). ; Temperature dependence: Optimum temperature is 37 degrees Celsius. ; Membrane ; Multi-pass membrane protein Detected in placenta and skeletal muscle. Belongs to the glycosyl hydrolase 56 family. catalytic activity hyalurononglucosaminidase activity carbohydrate metabolic process glycosaminoglycan catabolic process metabolic process cell surface membrane integral component of membrane hydrolase activity hydrolase activity, acting on glycosyl bonds chondroitin sulfate catabolic process uc003vlc.1 uc003vlc.2 uc003vlc.3 uc003vlc.4 uc003vlc.5 
ENST00000223029.8 AIMP2 ENST00000223029.8 aminoacyl tRNA synthetase complex interacting multifunctional protein 2, transcript variant 1 (from RefSeq NM_006303.4) AIMP2_HUMAN ENST00000223029.1 ENST00000223029.2 ENST00000223029.3 ENST00000223029.4 ENST00000223029.5 ENST00000223029.6 ENST00000223029.7 F8W950 JTV1 NM_006303 PRO0992 Q13155 Q75MR1 Q96CZ5 Q9P1L2 uc003spo.1 uc003spo.2 uc003spo.3 uc003spo.4 uc003spo.5 The protein encoded by this gene is part of the aminoacyl-tRNA synthetase complex, which contains nine different aminoacyl-tRNA synthetases and three non-enzymatic factors. The encoded protein is one of the non-enzymatic factors and is required for assembly and stability of the complex. [provided by RefSeq, May 2016]. Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:19131329). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor. Part of the multisynthetase complex (MSC), a multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:24312579, PubMed:19131329, PubMed:19289464). Interacts (via N-terminus) with KARS1 (PubMed:9878398, PubMed:15220430, PubMed:18029264, PubMed:23159739, PubMed:26074468). Interacts with EPRS1 (PubMed:26472928). Forms a linear complex that contains MARS1, EEF1E1, EPRS1 and AIMP2 that is at the core of the multisubunit complex (PubMed:26472928). Binds FUBP1 (via C-terminus). Interacts in both its unphosphorylated and phosphorylated forms with p53/TP53 (via N-terminus) in the nucleus following UV irradiation. Interacts (via N-terminus) with PRKN/parkin (via first RING-type domain) (PubMed:16135753). Interacts with TARS3 (PubMed:24312579). Q13155; Q12904: AIMP1; NbExp=4; IntAct=EBI-745226, EBI-1045802; Q13155; Q12904-2: AIMP1; NbExp=5; IntAct=EBI-745226, EBI-12412735; Q13155; P05067: APP; NbExp=3; IntAct=EBI-745226, EBI-77613; Q13155; O75934: BCAS2; NbExp=12; IntAct=EBI-745226, EBI-1050106; Q13155; Q0VDD7: BRME1; NbExp=8; IntAct=EBI-745226, EBI-741210; Q13155; Q13895: BYSL; NbExp=5; IntAct=EBI-745226, EBI-358049; Q13155; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-745226, EBI-747505; Q13155; Q8NA61-2: CBY2; NbExp=5; IntAct=EBI-745226, EBI-11524851; Q13155; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-745226, EBI-11974185; Q13155; Q96L14: CEP170P1; NbExp=5; IntAct=EBI-745226, EBI-743488; Q13155; P14868: DARS1; NbExp=10; IntAct=EBI-745226, EBI-358730; Q13155; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-745226, EBI-11988027; Q13155; Q8IYI6: EXOC8; NbExp=5; IntAct=EBI-745226, EBI-742102; Q13155; Q13643: FHL3; NbExp=13; IntAct=EBI-745226, EBI-741101; Q13155; Q96AE4: FUBP1; NbExp=4; IntAct=EBI-745226, EBI-711404; Q13155; P13807: GYS1; NbExp=3; IntAct=EBI-745226, EBI-740553; Q13155; Q15046: KARS1; NbExp=21; IntAct=EBI-745226, EBI-356367; Q13155; Q15046-1: KARS1; NbExp=2; IntAct=EBI-745226, EBI-21457670; Q13155; Q15323: KRT31; NbExp=3; IntAct=EBI-745226, EBI-948001; Q13155; Q14525: KRT33B; NbExp=3; IntAct=EBI-745226, EBI-1049638; Q13155; O76011: KRT34; NbExp=3; IntAct=EBI-745226, EBI-1047093; Q13155; O76013-2: KRT36; NbExp=3; IntAct=EBI-745226, EBI-11958506; Q13155; P25791: LMO2; NbExp=3; IntAct=EBI-745226, EBI-739696; Q13155; P25791-3: LMO2; NbExp=6; IntAct=EBI-745226, EBI-11959475; Q13155; Q8TBB1: LNX1; NbExp=8; IntAct=EBI-745226, EBI-739832; Q13155; Q9NYP9: MIS18A; NbExp=6; IntAct=EBI-745226, EBI-1104552; Q13155; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-745226, EBI-928842; Q13155; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-745226, EBI-10172876; Q13155; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-745226, EBI-741158; Q13155; P22061: PCMT1; NbExp=3; IntAct=EBI-745226, EBI-353343; Q13155; O15212: PFDN6; NbExp=3; IntAct=EBI-745226, EBI-356973; Q13155; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-745226, EBI-742388; Q13155; P54646: PRKAA2; NbExp=3; IntAct=EBI-745226, EBI-1383852; Q13155; Q15276: RABEP1; NbExp=3; IntAct=EBI-745226, EBI-447043; Q13155; P0C264: SBK3; NbExp=3; IntAct=EBI-745226, EBI-17181801; Q13155; O95391: SLU7; NbExp=3; IntAct=EBI-745226, EBI-750559; Q13155; Q8TC71: SPATA18; NbExp=3; IntAct=EBI-745226, EBI-11334239; Q13155; Q8WWU5-7: TCP11; NbExp=3; IntAct=EBI-745226, EBI-17721485; Q13155; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-745226, EBI-750109; Q13155; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-745226, EBI-12090309; Q13155; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-745226, EBI-1105213; Q13155; P04637: TP53; NbExp=6; IntAct=EBI-745226, EBI-366083; Q13155; A0A0S2Z6H0: ZGPAT; NbExp=3; IntAct=EBI-745226, EBI-16428984; Q13155; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-745226, EBI-3439227; Q13155; Q8N5A5-2: ZGPAT; NbExp=12; IntAct=EBI-745226, EBI-10183064; Q13155; PRO_0000038593 [P04591]: gag; Xeno; NbExp=3; IntAct=EBI-745226, EBI-6179719; Cytoplasm, cytosol Nucleus Note=Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13155-1; Sequence=Displayed; Name=2; Synonyms=DX2 ; IsoId=Q13155-2; Sequence=VSP_059914; Phosphorylated on serine residues in response to UV irradiation. Ubiquitinated by PRKN, leading to its degradation by the proteasome. Mutant PRKN fails to ubiquitinate AIMP2 efficiently, allowing its accumulation which may contribute to neurodegeneration associated with Parkinson disease. Leukodystrophy, hypomyelinating, 17 (HLD17) [MIM:618006]: An autosomal recessive neurodevelopmental disorder characterized by atrophy of cerebral cortex, spinal cord and cerebellum, thin corpus callosum, abnormal signals in the basal ganglia, and features suggesting hypo- or demyelination observed on brain imaging. Clinical manifestations include lack of development, absent speech, microcephaly, spasticity, seizures, and contractures. Note=The disease may be caused by variants affecting the gene represented in this entry. Accumulates in brains affected by autosomal-recessive juvenile parkinsonism, idiopathic Parkinson disease and diffuse Lewy body disease. Sequence=AAC50391.1; Type=Frameshift; Evidence=; protein binding nucleus cytoplasm cytosol translation tRNA aminoacylation for protein translation apoptotic process multicellular organism development negative regulation of cell proliferation membrane aminoacyl-tRNA synthetase multienzyme complex cell differentiation positive regulation of protein ubiquitination binding, bridging Type II pneumocyte differentiation macromolecular complex assembly positive regulation of neuron death positive regulation of aminoacyl-tRNA ligase activity uc003spo.1 uc003spo.2 uc003spo.3 uc003spo.4 uc003spo.5 
ENST00000223051.8 TFR2 ENST00000223051.8 transferrin receptor 2, transcript variant 1 (from RefSeq NM_003227.4) A6NGM7 ENST00000223051.1 ENST00000223051.2 ENST00000223051.3 ENST00000223051.4 ENST00000223051.5 ENST00000223051.6 ENST00000223051.7 NM_003227 O75422 Q1HE13 Q9HA99 Q9NX67 Q9UP52 TFR2_HUMAN uc003uvv.1 uc003uvv.2 uc003uvv.3 This gene encodes a single-pass type II membrane protein, which is a member of the transferrin receptor-like family. This protein mediates cellular uptake of transferrin-bound iron, and may be involved in iron metabolism, hepatocyte function and erythrocyte differentiation. Mutations in this gene have been associated with hereditary hemochromatosis type III. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, May 2011]. Mediates cellular uptake of transferrin-bound iron in a non- iron dependent manner. May be involved in iron metabolism, hepatocyte function and erythrocyte differentiation. Homodimer. Q9UP52; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-3934135, EBI-2804156; Q9UP52; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-3934135, EBI-8652744; Cell membrane; Single-pass type II membrane protein. [Isoform Beta]: Cytoplasm Note=Lacks the transmembrane domain. Probably intracellular. Event=Alternative splicing; Named isoforms=3; Name=Alpha; IsoId=Q9UP52-1; Sequence=Displayed; Name=Beta; IsoId=Q9UP52-2; Sequence=VSP_005354; Name=Gamma; IsoId=Q9UP52-3; Sequence=VSP_005355; Predominantly expressed in liver. While the alpha form is also expressed in spleen, lung, muscle, prostate and peripheral blood mononuclear cells, the beta form is expressed in all tissues tested, albeit weakly. Hemochromatosis 3 (HFE3) [MIM:604250]: A disorder of iron metabolism characterized by iron overload. Excess iron is deposited in a variety of organs leading to their failure, and resulting in serious illnesses including cirrhosis, hepatomas, diabetes, cardiomyopathy, arthritis, and hypogonadotropic hypogonadism. Severe effects of the disease usually do not appear until after decades of progressive iron loading. te=The disease is caused by variants affecting the gene represented in this entry. The variant Lys-172 found in hereditary hemochromatosis type III affects the putative initiation codon of the beta isoform thus preventing its translation. Belongs to the peptidase M28 family. M28B subfamily. Sequence=BAA91153.1; Type=Erroneous initiation; Evidence=; transferrin receptor activity protein binding cytoplasm plasma membrane integral component of plasma membrane iron ion transport cellular iron ion homeostasis receptor-mediated endocytosis acute-phase response external side of plasma membrane response to iron ion membrane integral component of membrane cytoplasmic vesicle transferrin transport co-receptor binding positive regulation of endocytosis positive regulation of transcription from RNA polymerase II promoter iron ion homeostasis cellular response to iron ion positive regulation of peptide hormone secretion positive regulation of protein maturation HFE-transferrin receptor complex uc003uvv.1 uc003uvv.2 uc003uvv.3 
ENST00000223061.6 PCOLCE ENST00000223061.6 procollagen C-endopeptidase enhancer (from RefSeq NM_002593.4) B2R9E1 ENST00000223061.1 ENST00000223061.2 ENST00000223061.3 ENST00000223061.4 ENST00000223061.5 NM_002593 O14550 PCOC1_HUMAN PCPE1 Q15113 uc003uvo.1 uc003uvo.2 uc003uvo.3 uc003uvo.4 uc003uvo.5 uc003uvo.6 Fibrillar collagen types I-III are synthesized as precursor molecules known as procollagens. These precursors contain amino- and carboxyl-terminal peptide extensions known as N- and C-propeptides, respectively, which are cleaved, upon secretion of procollagen from the cell, to yield the mature triple helical, highly structured fibrils. This gene encodes a glycoprotein which binds and drives the enzymatic cleavage of type I procollagen and heightens C-proteinase activity. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189664.72099.1, BC000574.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223061.6/ ENSP00000223061.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. C-terminal processed part of PCPE (CT-PCPE) may have an metalloproteinase inhibitory activity. Interacts with EFEMP2. Q15113; PRO_0000000092 [P05067]: APP; NbExp=4; IntAct=EBI-8869614, EBI-821758; Q15113; P13497: BMP1; NbExp=3; IntAct=EBI-8869614, EBI-489827; Q15113; PRO_0000005794 [P39060]: COL18A1; NbExp=4; IntAct=EBI-8869614, EBI-2566375; Q15113; P20908: COL5A1; NbExp=2; IntAct=EBI-8869614, EBI-2464511; Q15113; P07996: THBS1; NbExp=3; IntAct=EBI-8869614, EBI-2530274; Q15113; P07589: FN1; Xeno; NbExp=2; IntAct=EBI-8869614, EBI-11147184; Q15113; P18828: Sdc1; Xeno; NbExp=4; IntAct=EBI-8869614, EBI-9985816; Q15113; P43407: Sdc2; Xeno; NbExp=4; IntAct=EBI-8869614, EBI-11578890; Q15113; O35988: Sdc4; Xeno; NbExp=2; IntAct=EBI-8869614, EBI-9986850; Secreted. C-terminally processed at multiple positions. extracellular matrix structural constituent protein binding collagen binding extracellular region extracellular space proteolysis multicellular organism development heparin binding positive regulation of peptidase activity peptidase activator activity extracellular exosome cellular response to leukemia inhibitory factor uc003uvo.1 uc003uvo.2 uc003uvo.3 uc003uvo.4 uc003uvo.5 uc003uvo.6 
ENST00000223073.6 RBM28 ENST00000223073.6 RNA binding motif protein 28, transcript variant 1 (from RefSeq NM_018077.3) A4D100 B4DU52 E9PDD9 ENST00000223073.1 ENST00000223073.2 ENST00000223073.3 ENST00000223073.4 ENST00000223073.5 NM_018077 Q53H65 Q96CV3 Q9NW13 RBM28_HUMAN uc031szb.1 uc031szb.2 The protein encoded by this gene is a specific nucleolar component of the spliceosomal small nuclear ribonucleoprotein (snRNP)complexes . It specifically associates with U1, U2, U4, U5, and U6 small nuclear RNAs (snRNAs), possibly coordinating their transition through the nucleolus. Mutation in this gene causes alopecia, progressive neurological defects, and endocrinopathy (ANE syndrome), a pleiotropic and clinically heterogeneous disorder. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2009]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK001239.1, SRR3476690.231180.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223073.6/ ENSP00000223073.1 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Nucleolar component of the spliceosomal ribonucleoprotein complexes. Interacts with U1, U2, U4, U5, and U6 spliceosomal small nuclear RNAs (snRNAs). Nucleus, nucleolus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NW13-1; Sequence=Displayed; Name=2; IsoId=Q9NW13-2; Sequence=VSP_046111; Ubiquitously expressed. Alopecia, neurologic defects, and endocrinopathy syndrome (ANES) [MIM:612079]: Affected individuals have hair loss of variable severity, ranging from complete alopecia to near-normal scalp hair with absence of body hair. All have moderate to severe intellectual disability, progressive motor deterioration and central hypogonadotropic hypogonadism with delayed or absent puberty and central adrenal insufficiency. Additional features included short stature, microcephaly, gynecomastia, pigmentary anomalies, hypodontia, kyphoscoliosis, ulnar deviation of the hands, and loss of subcutaneous fat. Note=The disease is caused by variants affecting the gene represented in this entry. nucleic acid binding RNA binding nucleus spliceosomal complex nucleolus mRNA processing RNA splicing ribonucleoprotein complex uc031szb.1 uc031szb.2 
ENST00000223095.5 SERPINE1 ENST00000223095.5 serpin family E member 1, transcript variant 12 (from RefSeq NM_001386466.1) B7Z4S0 ENST00000223095.1 ENST00000223095.2 ENST00000223095.3 ENST00000223095.4 F8WD53 NM_001386466 P05121 PAI1 PAI1_HUMAN PLANH1 uc003uxt.1 uc003uxt.2 uc003uxt.3 uc003uxt.4 uc003uxt.5 Serine protease inhibitor. Inhibits TMPRSS7 (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots (PubMed:8481516, PubMed:9207454, PubMed:17912461). As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading (PubMed:9175705). Acts as a regulator of cell migration, independently of its role as protease inhibitor (PubMed:15001579, PubMed:9168821). It is required for stimulation of keratinocyte migration during cutaneous injury repair (PubMed:18386027). It is involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (PubMed:25808697, PubMed:27046084). Forms a heterodimer with TMPRSS7 (PubMed:15853774). Interacts with VTN (PubMed:7522053). Binds LRP1B; binding is followed by internalization and degradation (PubMed:11384978). Interacts with PPP1CB (PubMed:28296156). In complex with PLAU/uPA, interacts with PLAUR/uPAR (PubMed:15053742). Interacts with SORL1 and LRP1, either alone or in complex with PLAU; these interactions are abolished in the presence of LRPAP1/RAP (PubMed:15053742). The ternary complex composed of PLAUR-PLAU-PAI1 also interacts with SORL1 (PubMed:15053742). Also interacts with SORL1, when complexed to PLAT/tPA (PubMed:15053742). P05121; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-953978, EBI-1052304; P05121; P02763: ORM1; NbExp=4; IntAct=EBI-953978, EBI-976767; P05121; P78337: PITX1; NbExp=3; IntAct=EBI-953978, EBI-748265; P05121; O43765: SGTA; NbExp=6; IntAct=EBI-953978, EBI-347996; P05121; Q96EQ0: SGTB; NbExp=6; IntAct=EBI-953978, EBI-744081; P05121; O43711: TLX3; NbExp=3; IntAct=EBI-953978, EBI-3939165; P05121; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-953978, EBI-10982110; P05121; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-953978, EBI-741480; P05121; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-953978, EBI-10173939; P05121; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-953978, EBI-947187; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P05121-1; Sequence=Displayed; Name=2; IsoId=P05121-2; Sequence=VSP_045493; Expressed in endothelial cells (PubMed:2430793, PubMed:3097076). Found in plasma, platelets, and hepatoma and fibrosarcoma cells. Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond. Plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:613329]: A hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen. Note=The disease is caused by variants affecting the gene represented in this entry. A rare PAI-1D mutation resulting in a frameshift and protein truncation has been found in an Old Order Amish community. Homozygous mutation carriers suffer from episodes of major hemorrhage, while heterozygous carriers do not manifest abnormal bleeding (PubMed:9207454). Heterozygosity for the mutation is associated with longer leukocyte telomere length, lower fasting insulin levels, lower prevalence of diabetes mellitus, and a longer life span (PubMed:29152572). Belongs to the serpin family. Name=Wikipedia; Note=Plasminogen activator inhibitor-1 entry; URL="https://en.wikipedia.org/wiki/Plasminogen_activator_inhibitor-1"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/serpine1/"; Name=Protein Spotlight; Note=Giving in to time - Issue 203 of May 2018; URL="https://web.expasy.org/spotlight/back_issues/203/"; chronological cell aging angiogenesis protease binding platelet degranulation serine-type endopeptidase inhibitor activity receptor binding protein binding extracellular region extracellular space plasma membrane circadian rhythm negative regulation of peptidase activity regulation of receptor activity negative regulation of plasminogen activation negative regulation of endopeptidase activity negative regulation of smooth muscle cell migration positive regulation of blood coagulation negative regulation of blood coagulation extracellular matrix organization negative regulation of cell migration peptidase inhibitor activity platelet alpha granule lumen positive regulation of interleukin-8 production negative regulation of cell adhesion mediated by integrin positive regulation of leukotriene production involved in inflammatory response fibrinolysis positive regulation of angiogenesis positive regulation of transcription from RNA polymerase II promoter positive regulation of receptor-mediated endocytosis positive regulation of inflammatory response defense response to Gram-negative bacterium negative regulation of fibrinolysis negative regulation of vascular wound healing negative regulation of wound healing extracellular exosome cellular response to lipopolysaccharide positive regulation of monocyte chemotaxis replicative senescence dentinogenesis positive regulation of odontoblast differentiation negative regulation of extrinsic apoptotic signaling pathway via death domain receptors negative regulation of smooth muscle cell-matrix adhesion negative regulation of endothelial cell apoptotic process uc003uxt.1 uc003uxt.2 uc003uxt.3 uc003uxt.4 uc003uxt.5 
ENST00000223114.9 MOGAT3 ENST00000223114.9 monoacylglycerol O-acyltransferase 3, transcript variant 1 (from RefSeq NM_178176.4) DC7 DGAT2L7 ENST00000223114.1 ENST00000223114.2 ENST00000223114.3 ENST00000223114.4 ENST00000223114.5 ENST00000223114.6 ENST00000223114.7 ENST00000223114.8 MOGAT3 MOGT3_HUMAN NM_178176 Q496A6 Q496A7 Q496A8 Q86VF5 Q9UDW7 UNQ9383/PRO34208 uc003uyc.1 uc003uyc.2 uc003uyc.3 uc003uyc.4 uc003uyc.5 uc003uyc.6 Acyl-CoA:monoacylglycerol acyltransferase (MOGAT; EC 2.3.1.22) catalyzes the synthesis of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA (Cheng et al., 2003 [PubMed 12618427]).[supplied by OMIM, Mar 2008]. Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705). Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacylglycerol + CoA; Xref=Rhea:RHEA:16741, ChEBI:CHEBI:17389, ChEBI:CHEBI:49172, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16742; Evidence=; Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di- (9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73990; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1- hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:73990, ChEBI:CHEBI:75466; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl- CoA = 1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:38299, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75466, ChEBI:CHEBI:75688; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38300; Evidence=; Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O- (9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:197429; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecyl)-3-(9Z- octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z- octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:55344, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:138735, ChEBI:CHEBI:197429; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345; Evidence=; Kinetic parameters: Vmax=9.3 nmol/min/mg enzyme with diacylglycerol as substrate ; Vmax=22.8 nmol/min/mg enzyme with 2-monoacylglycerol as substrate ; Glycerolipid metabolism; triacylglycerol biosynthesis. Q86VF5-3; P07339: CTSD; NbExp=3; IntAct=EBI-25840143, EBI-2115097; Q86VF5-3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-25840143, EBI-10976677; Q86VF5-3; P28799: GRN; NbExp=3; IntAct=EBI-25840143, EBI-747754; Q86VF5-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25840143, EBI-5235340; Q86VF5-3; O76024: WFS1; NbExp=3; IntAct=EBI-25840143, EBI-720609; Endoplasmic reticulum membrane ; Multi-pass membrane protein Cytoplasm, perinuclear region Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q86VF5-1; Sequence=Displayed; Name=2; IsoId=Q86VF5-2; Sequence=VSP_020361, VSP_020362; Name=3; IsoId=Q86VF5-3; Sequence=VSP_020363; Selectively expressed in the digestive system. Highly expressed in the ileum, and at lower level in jejunum, duodenum, colon, cecum and the rectum. Not expressed in the stomach and the esophagus and trachea. Expressed at very low level in liver. Ubiquitinated. Ubiquitination leads to proteasomal degradation. Belongs to the diacylglycerol acyltransferase family. Sequence=AAD45832.1; Type=Erroneous gene model prediction; Evidence=; 2-acylglycerol O-acyltransferase activity diacylglycerol O-acyltransferase activity cytoplasm endoplasmic reticulum endoplasmic reticulum membrane glycerol metabolic process lipid metabolic process membrane integral component of membrane transferase activity transferase activity, transferring acyl groups transferase activity, transferring acyl groups other than amino-acyl groups triglyceride biosynthetic process perinuclear region of cytoplasm perinuclear endoplasmic reticulum membrane uc003uyc.1 uc003uyc.2 uc003uyc.3 uc003uyc.4 uc003uyc.5 uc003uyc.6 
ENST00000223127.8 PLOD3 ENST00000223127.8 procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (from RefSeq NM_001084.5) B2R6W6 ENST00000223127.1 ENST00000223127.2 ENST00000223127.3 ENST00000223127.4 ENST00000223127.5 ENST00000223127.6 ENST00000223127.7 NM_001084 O60568 PLOD3_HUMAN Q540C3 uc003uyd.1 uc003uyd.2 uc003uyd.3 uc003uyd.4 uc003uyd.5 The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC011674.2, AK075338.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223127.8/ ENSP00000223127.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:9582318, PubMed:9724729, PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:10934207, PubMed:11896059, PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen- like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5- hydroxylysine residues (PubMed:25419660). Essential for normal biosynthesis and secretion of type IV collagens (PubMed:18834968) (Probable). Essential for normal formation of basement membranes (By similarity). Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L- lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA- COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4; Evidence= Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP; Xref=Rhea:RHEA:12637, Rhea:RHEA-COMP:12752, Rhea:RHEA- COMP:12753, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:133442, ChEBI:CHEBI:133443; EC=2.4.1.50; Evidence= Reaction=(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-glucose = (5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D- galactosyl]-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP; Xref=Rhea:RHEA:12576, Rhea:RHEA-COMP:12753, Rhea:RHEA-COMP:12754, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:133443, ChEBI:CHEBI:133452; EC=2.4.1.66; Evidence= Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence=; Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Lysyl hydroxylase activity is strongly inhibited by imidazole. Kinetic parameters: KM=35 uM for UDP-galactose ; KM=17 uM for UDP-glucose ; KM=100 uM for 2-oxoglutarate KM=300 uM for ascorbate ; KM=350 uM for ascorbate ; Homodimer. O60568; P38432: COIL; NbExp=3; IntAct=EBI-741582, EBI-945751; O60568; Q9UMD9: COL17A1; NbExp=3; IntAct=EBI-741582, EBI-2528742; O60568; Q6Q6R5-3: CRIP3; NbExp=3; IntAct=EBI-741582, EBI-12925520; O60568; Q5JST6: EFHC2; NbExp=12; IntAct=EBI-741582, EBI-2349927; O60568; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-741582, EBI-10174566; O60568; Q96KQ7: EHMT2; NbExp=8; IntAct=EBI-741582, EBI-744366; O60568; Q9UHH9: IP6K2; NbExp=3; IntAct=EBI-741582, EBI-747509; O60568; Q7L273: KCTD9; NbExp=3; IntAct=EBI-741582, EBI-4397613; O60568; O15037: KHNYN; NbExp=3; IntAct=EBI-741582, EBI-6148525; O60568; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-741582, EBI-11985629; O60568; Q15742: NAB2; NbExp=3; IntAct=EBI-741582, EBI-8641936; O60568; Q96QF0: RAB3IP; NbExp=4; IntAct=EBI-741582, EBI-747844; O60568; Q96QF0-2: RAB3IP; NbExp=3; IntAct=EBI-741582, EBI-747865; O60568; Q53GL6: RALY; NbExp=3; IntAct=EBI-741582, EBI-9512693; O60568; Q9BQY4: RHOXF2; NbExp=2; IntAct=EBI-741582, EBI-372094; O60568; O60504: SORBS3; NbExp=3; IntAct=EBI-741582, EBI-741237; O60568; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-741582, EBI-4395669; Rough endoplasmic reticulum Endoplasmic reticulum lumen Endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side Secreted Secreted, extracellular space Note=The majority of the secreted protein is associated with the extracellular matrix. Ubiquitous (PubMed:9724729). Detected in heart, placenta and pancreas and at lower levels in lung, liver and skeletal muscle (PubMed:9582318, PubMed:9724729). The N-terminal domain mediates glycosyltransferase activity. The C-terminal domain that mediates lysyl hydroxylase activity is also important for homodimerization. Bone fragility with contractures, arterial rupture, and deafness (BCARD) [MIM:612394]: An autosomal recessive connective tissue disorder, secondary to lysyl hydroxylase 3 deficiency. It is characterized by congenital malformations severely affecting multiple tissues and organs. Clinical features include growth retardation, craniofacial dysmorphism, popliteal and cerebral aneurysm, cerebral arterial hemorrhage, skin blistering and easy bruisability, and osteopenia. te=The disease is caused by variants affecting the gene represented in this entry. in utero embryonic development endothelial cell morphogenesis catalytic activity iron ion binding protein binding extracellular region extracellular space endoplasmic reticulum endoplasmic reticulum lumen endoplasmic reticulum membrane rough endoplasmic reticulum Golgi apparatus trans-Golgi network protein O-linked glycosylation protein localization metabolic process procollagen-lysine 5-dioxygenase activity membrane oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen transferase activity transferase activity, transferring glycosyl groups peptidyl-lysine hydroxylation neural tube development collagen fibril organization L-ascorbic acid binding cellular response to hormone stimulus collagen metabolic process procollagen glucosyltransferase activity vasodilation metal ion binding hydroxylysine biosynthetic process epidermis morphogenesis procollagen galactosyltransferase activity dioxygenase activity oxidation-reduction process lung morphogenesis extracellular exosome basement membrane assembly uc003uyd.1 uc003uyd.2 uc003uyd.3 uc003uyd.4 uc003uyd.5 
ENST00000223129.8 RPA3 ENST00000223129.8 replication protein A3 (from RefSeq NM_002947.5) ENST00000223129.1 ENST00000223129.2 ENST00000223129.3 ENST00000223129.4 ENST00000223129.5 ENST00000223129.6 ENST00000223129.7 NM_002947 P35244 Q549U6 REPA3 RFA3_HUMAN RPA14 uc003sri.1 uc003sri.2 uc003sri.3 uc003sri.4 As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Also plays a role in base excision repair (BER), probably through interaction with UNG (PubMed:9765279). Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51- dependent strand exchange (PubMed:19996105). Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. Also a component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2. P35244; P43351: RAD52; NbExp=3; IntAct=EBI-621428, EBI-706448; P35244; P27694: RPA1; NbExp=11; IntAct=EBI-621428, EBI-621389; P35244; P15927: RPA2; NbExp=12; IntAct=EBI-621428, EBI-621404; Nucleus Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination (PubMed:26474068). Belongs to the replication factor A protein 3 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rpa3/"; G1/S transition of mitotic cell cycle telomere maintenance double-strand break repair via homologous recombination DNA binding damaged DNA binding single-stranded DNA binding protein binding nucleus nucleoplasm DNA replication factor A complex DNA replication DNA repair transcription-coupled nucleotide-excision repair base-excision repair nucleotide-excision repair nucleotide-excision repair, preincision complex stabilization nucleotide-excision repair, preincision complex assembly nucleotide-excision repair, DNA incision, 3'-to lesion nucleotide-excision repair, DNA incision, 5'-to lesion nucleotide-excision repair, DNA gap filling mismatch repair DNA recombination cellular response to DNA damage stimulus regulation of mitotic cell cycle translesion synthesis telomere maintenance via semi-conservative replication nucleotide-excision repair, DNA incision site of double-strand break interstrand cross-link repair regulation of cell proliferation error-prone translesion synthesis DNA damage response, detection of DNA damage error-free translesion synthesis regulation of cellular response to heat regulation of signal transduction by p53 class mediator uc003sri.1 uc003sri.2 uc003sri.3 uc003sri.4 
ENST00000223136.5 FIS1 ENST00000223136.5 fission, mitochondrial 1 (from RefSeq NM_016068.3) CGI-135 ENST00000223136.1 ENST00000223136.2 ENST00000223136.3 ENST00000223136.4 FIS1_HUMAN NM_016068 Q9BTP3 Q9Y3D6 TTC11 uc003uyj.1 uc003uyj.2 uc003uyj.3 uc003uyj.4 uc003uyj.5 uc003uyj.6 The balance between fission and fusion regulates the morphology of mitochondria. TTC11 is a component of a mitochondrial complex that promotes mitochondrial fission (James et al., 2003 [PubMed 12783892]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.347142.1, SRR1163655.172599.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN03465403 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000223136.5/ ENSP00000223136.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Involved in the fragmentation of the mitochondrial network and its perinuclear clustering (PubMed:12783892, PubMed:12861026, PubMed:14996942, PubMed:23283981). Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission (PubMed:12861026, PubMed:16118244, PubMed:23283981, PubMed:23530241, PubMed:24196833). May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event (PubMed:23530241, PubMed:24196833). Also mediates peroxisomal fission (PubMed:16107562). May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis (PubMed:24196833). Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis (PubMed:12783892). Interacts with DNM1L/DLP1 through the TPR region; may form part of a larger protein complex at the endoplasmic reticulum- mitochondrial interface during mitochondrial fission (PubMed:12861026, PubMed:16118244, PubMed:24196833). Interacts with MARCHF5 (PubMed:16874301). Interacts with MIEF1 (PubMed:21701560). Interacts with PEX11A, PEX11B and PEX11G (PubMed:20826455). Q9Y3D6; Q9BV23: ABHD6; NbExp=3; IntAct=EBI-3385283, EBI-3916106; Q9Y3D6; Q96BI3: APH1A; NbExp=3; IntAct=EBI-3385283, EBI-2606935; Q9Y3D6; P51572: BCAP31; NbExp=8; IntAct=EBI-3385283, EBI-77683; Q9Y3D6; O00429: DNM1L; NbExp=2; IntAct=EBI-3385283, EBI-724571; Q9Y3D6; Q15125: EBP; NbExp=3; IntAct=EBI-3385283, EBI-3915253; Q9Y3D6; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3385283, EBI-781551; Q9Y3D6; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-3385283, EBI-18304435; Q9Y3D6; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-3385283, EBI-18938272; Q9Y3D6; O15552: FFAR2; NbExp=3; IntAct=EBI-3385283, EBI-2833872; Q9Y3D6; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3385283, EBI-10266796; Q9Y3D6; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-3385283, EBI-749265; Q9Y3D6; P48051: KCNJ6; NbExp=3; IntAct=EBI-3385283, EBI-12017638; Q9Y3D6; Q9NQG6: MIEF1; NbExp=4; IntAct=EBI-3385283, EBI-740987; Q9Y3D6; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-3385283, EBI-6163737; Q9Y3D6; Q9HC29: NOD2; NbExp=2; IntAct=EBI-3385283, EBI-7445625; Q9Y3D6; P57054: PIGP; NbExp=3; IntAct=EBI-3385283, EBI-17630288; Q9Y3D6; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-3385283, EBI-18397230; Q9Y3D6; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-3385283, EBI-17247926; Q9Y3D6; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3385283, EBI-18159983; Q9Y3D6; Q13336-2: SLC14A1; NbExp=3; IntAct=EBI-3385283, EBI-19141793; Q9Y3D6; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3385283, EBI-8638294; Q9Y3D6; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-3385283, EBI-11724433; Mitochondrion outer membrane ingle-pass membrane protein Peroxisome membrane ; Single-pass membrane protein The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L. Ubiquitinated by MARCHF5. Belongs to the FIS1 family. mitochondrial fission mitophagy release of cytochrome c from mitochondria protein binding mitochondrion mitochondrial outer membrane peroxisome peroxisomal membrane integral component of peroxisomal membrane endoplasmic reticulum protein targeting to mitochondrion apoptotic process positive regulation of cytosolic calcium ion concentration mitochondrial fusion regulation of mitochondrion organization response to muscle activity membrane integral component of membrane peroxisome fission integral component of mitochondrial outer membrane response to nutrient levels negative regulation of endoplasmic reticulum calcium ion concentration macromolecular complex calcium-mediated signaling using intracellular calcium source positive regulation of cysteine-type endopeptidase activity involved in apoptotic process positive regulation of neuron apoptotic process mitochondrial fragmentation involved in apoptotic process macromolecular complex binding protein homooligomerization positive regulation of mitochondrial calcium ion concentration mitochondrion morphogenesis cellular response to glucose stimulus cellular response to lipid positive regulation of mitochondrial fission positive regulation of protein targeting to membrane cellular response to toxic substance cellular response to peptide response to fluoride cellular response to thapsigargin response to flavonoid response to hypobaric hypoxia positive regulation of intrinsic apoptotic signaling pathway uc003uyj.1 uc003uyj.2 uc003uyj.3 uc003uyj.4 uc003uyj.5 uc003uyj.6 
ENST00000223145.10 GLCCI1 ENST00000223145.10 glucocorticoid induced 1 (from RefSeq NM_138426.4) A4D103 ENST00000223145.1 ENST00000223145.2 ENST00000223145.3 ENST00000223145.4 ENST00000223145.5 ENST00000223145.6 ENST00000223145.7 ENST00000223145.8 ENST00000223145.9 GLCI1_HUMAN NM_138426 Q86VQ1 Q96FD0 uc003srk.1 uc003srk.2 uc003srk.3 uc003srk.4 uc003srk.5 uc003srk.6 This gene encodes a protein of unknown function. Expression of this gene is induced by glucocorticoids and may be an early marker for glucocorticoid-induced apoptosis. Single nucleotide polymorphisms in this gene are associated with a decreased response to inhaled glucocorticoids in asthmatic patients. [provided by RefSeq, Feb 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC050291.1, SRR1163657.376342.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223145.10/ ENSP00000223145.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Predominantly expressed in lung, spleen, thymus and testis and, at lower levels, in brain, bone marrow, peripheral leukocytes, skin and trachea. Polymorphisms dbSNP:rs37972 and dbSNP:rs37973, located in GLCCI1 promoter region, are associated with a decreased response to glucorticoid treatment [MIM:614400] in asthma patients (PubMed:21991891), as well as in chronic obstructive pulmonary disease patients (PubMed:22187997). The mean increase in forced expiratory volume in 1 second in glucorticoid treated subjects who are homozygous for the mutant (G) rs37973 allele is only about one-third of that seen in similarly treated subjects who are homozygous for the wild-type allele (A) (PubMed:21991891). These polymorphisms affect GLCCI1 transcription level. cytoplasm uc003srk.1 uc003srk.2 uc003srk.3 uc003srk.4 uc003srk.5 uc003srk.6 
ENST00000223167.5 MYL10 ENST00000223167.5 myosin light chain 10 (from RefSeq NM_138403.5) ENST00000223167.1 ENST00000223167.2 ENST00000223167.3 ENST00000223167.4 MYL10_HUMAN MYLC2PL NM_138403 PLRLC Q9BUA6 uc003uyr.1 uc003uyr.2 uc003uyr.3 uc003uyr.4 Myosin is a hexamer of 2 heavy chains and 4 light chains. Q9BUA6; P36508: ZNF76; NbExp=3; IntAct=EBI-17561739, EBI-7254550; This chain binds calcium. calcium ion binding mitochondrion cytosol muscle contraction metal ion binding uc003uyr.1 uc003uyr.2 uc003uyr.3 uc003uyr.4 
ENST00000223208.10 CEP41 ENST00000223208.10 centrosomal protein 41, transcript variant 5 (from RefSeq NR_046443.2) A4D1M0 B4DQ35 CEP41_HUMAN ENST00000223208.1 ENST00000223208.2 ENST00000223208.3 ENST00000223208.4 ENST00000223208.5 ENST00000223208.6 ENST00000223208.7 ENST00000223208.8 ENST00000223208.9 F5H0V6 NR_046443 Q7Z496 Q86TM1 Q8NFU8 Q9BYV8 Q9H6A3 Q9NPV3 TSGA14 uc003vpz.1 uc003vpz.2 uc003vpz.3 uc003vpz.4 uc003vpz.5 uc003vpz.6 This gene encodes a centrosomal and microtubule-binding protein which is predicted to have two coiled-coil domains and a rhodanese domain. In human retinal pigment epithelial cells the protein localized to centrioles and cilia. Mutations in this gene have been associated with Joubert Syndrome 15; an autosomal recessive ciliopathy and neurological disorder. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2012]. Required during ciliogenesis for tubulin glutamylation in cilium. Probably acts by participating in the transport of TTLL6, a tubulin polyglutamylase, between the basal body and the cilium. Found in a complex with TTLL6. Q9BYV8-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-25843412, EBI-10976677; Q9BYV8-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25843412, EBI-5235340; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes mainly to the cilium basal body and in primary cilia. Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=L-type; IsoId=Q9BYV8-1; Sequence=Displayed; Name=2; IsoId=Q9BYV8-2; Sequence=VSP_012248; Name=3; Synonyms=S-type; IsoId=Q9BYV8-4; Sequence=VSP_012246, VSP_012247; Name=4; IsoId=Q9BYV8-5; Sequence=VSP_042579, VSP_012248; [Isoform 1]: Expressed in testis and fetal tissues. [Isoform 3]: Expressed in testis and fetal tissues. Although it contains a rhodanese domain, does not display phosphatase activity, suggesting that the protein is enzymatically inactive. Joubert syndrome 15 (JBTS15) [MIM:614464]: An autosomal recessive disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy, renal disease, liver fibrosis and polydactyly. Note=The disease is caused by variants affecting the gene represented in this entry. Note=Genetic variations in CEP41 may be associated with susceptibility to autism (PubMed:21438139). Belongs to the CEP41 family. Sequence=AAO31692.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence=; G2/M transition of mitotic cell cycle protein binding cytoplasm centrosome centriole microtubule organizing center cytosol cytoskeleton cilium regulation of G2/M transition of mitotic cell cycle protein transport membrane protein polyglutamylation cell projection organization ciliary basal body cell projection cilium assembly ciliary basal body docking uc003vpz.1 uc003vpz.2 uc003vpz.3 uc003vpz.4 uc003vpz.5 uc003vpz.6 
ENST00000223210.5 ZNF862 ENST00000223210.5 zinc finger protein 862 (from RefSeq NM_001099220.3) A0AUL8 ENST00000223210.1 ENST00000223210.2 ENST00000223210.3 ENST00000223210.4 KIAA0543 NM_001099220 O60290 ZN862_HUMAN uc010lpn.1 uc010lpn.2 uc010lpn.3 uc010lpn.4 uc010lpn.5 May be involved in transcriptional regulation. Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O60290-1; Sequence=Displayed; Name=2; IsoId=O60290-2; Sequence=VSP_031702, VSP_031703; molecular_function nucleic acid binding cellular_component nucleus regulation of transcription, DNA-templated biological_process metal ion binding protein dimerization activity uc010lpn.1 uc010lpn.2 uc010lpn.3 uc010lpn.4 uc010lpn.5 
ENST00000223215.10 MEST ENST00000223215.10 mesoderm specific transcript, transcript variant 1 (from RefSeq NM_002402.4) B2R6S1 ENST00000223215.1 ENST00000223215.2 ENST00000223215.3 ENST00000223215.4 ENST00000223215.5 ENST00000223215.6 ENST00000223215.7 ENST00000223215.8 ENST00000223215.9 MEST_HUMAN NM_002402 O14973 O15007 PEG1 Q5EB52 Q6AI49 Q92571 uc003vqg.1 uc003vqg.2 uc003vqg.3 uc003vqg.4 uc003vqg.5 uc003vqg.6 This gene encodes a member of the alpha/beta hydrolase superfamily. It is imprinted, exhibiting preferential expression from the paternal allele in fetal tissues, and isoform-specific imprinting in lymphocytes. The loss of imprinting of this gene has been linked to certain types of cancer and may be due to promotor switching. The encoded protein may play a role in development. Alternatively spliced transcript variants encoding multiple isoforms have been identified for this gene. Pseudogenes of this gene are located on the short arm of chromosomes 3 and 4, and the long arm of chromosomes 6 and 15. [provided by RefSeq, Dec 2011]. Q5EB52; O95873: C6orf47; NbExp=3; IntAct=EBI-1050204, EBI-719613; Q5EB52; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-1050204, EBI-752069; Q5EB52; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-1050204, EBI-7062247; Q5EB52; Q05329: GAD2; NbExp=3; IntAct=EBI-1050204, EBI-9304251; Q5EB52; Q9H400: LIME1; NbExp=3; IntAct=EBI-1050204, EBI-2830566; Q5EB52; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-1050204, EBI-2466594; Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q5EB52-1; Sequence=Displayed; Name=2; Synonyms=Isoform b; IsoId=Q5EB52-2; Sequence=VSP_024532; Name=3; IsoId=Q5EB52-3; Sequence=VSP_024532, VSP_024533; Highly expressed in hydatidiform moles, but barely expressed in dermoid cysts. Biallelic expression is detected in blood lymphocytes. Seems to imprinted in an isoform-specific manner rather than in a tissue-specific manner in lymphocytes. Isoform 1 is expressed only from the paternal allele. Isoform 2 is expressed from both the paternal allele and the maternal allele. Monoallelic expression of paternally derived allele was observed in all fetal tissues examined, including brain, skeletal muscle, kidney, adrenal, tongue, heart, skin and placenta. In 75-day fetus, expressed in the amnion, brain, heart, lung, stomach, gut, adrenal, kidney, muscle and liver. Belongs to the AB hydrolase superfamily. catalytic activity endoplasmic reticulum endoplasmic reticulum membrane mesoderm development regulation of lipid storage membrane integral component of membrane hydrolase activity extracellular exosome uc003vqg.1 uc003vqg.2 uc003vqg.3 uc003vqg.4 uc003vqg.5 uc003vqg.6 
ENST00000223271.8 RARRES2 ENST00000223271.8 retinoic acid receptor responder 2 (from RefSeq NM_002889.4) ENST00000223271.1 ENST00000223271.2 ENST00000223271.3 ENST00000223271.4 ENST00000223271.5 ENST00000223271.6 ENST00000223271.7 NM_002889 Q7LE02 Q99969 RARR2_HUMAN TIG2 uc003wha.1 uc003wha.2 uc003wha.3 uc003wha.4 uc003wha.5 This gene encodes a secreted chemotactic protein that initiates chemotaxis via the ChemR23 G protein-coupled seven-transmembrane domain ligand. Expression of this gene is upregulated by the synthetic retinoid tazarotene and occurs in a wide variety of tissues. The active protein has several roles, including that as an adipokine and as an antimicrobial protein with activity against bacteria and fungi. [provided by RefSeq, Nov 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U77594.2, BI824025.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223271.8/ ENSP00000223271.3 Protein has antimicrobial activity :: PMID: 24660117 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Acts also as a ligand for CMKLR2. Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a lower affinity than it does to CMKLR1 or CMKLR2 (PubMed:27716822). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a pro-inflammatory adipokine, causing an increase in secretion of pro-inflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti- inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Its dual role in inflammation and metabolism might provide a link between chronic inflammation and obesity, as well as obesity-related disorders such as type 2 diabetes and cardiovascular disease. Exhibits an antimicrobial function in the skin. Secreted Expressed at the highest levels in placenta, liver, and white adipose tissue (WAT), and to a lesser extent in many other tissues such as lung, brown adipose tissue, heart, ovary, kidney, skeletal muscle and pancreas. Within WAT, expression is enriched in adipocytes as compared to the stromal vascular fraction. Expression and secretion increases dramatically with adipogenesis. Highly expressed in skin (basal and suprabasal layers of the epidermis, hair follicles and endothelial cells). Expression is elevated in numerous metabolic and inflammatory diseases including psoriasis, obesity, type 2 diabetes, metabolic syndrome and cardiovascular disease. Inhibited in psoriatic lesions. Activated by tazarotene in skin rafts and in the epidermis of psoriatic lesions. Secreted in an inactive precursor form, prochemerin, which is proteolytically processed by a variety of extracellular proteases to generate forms with differing levels of bioactivity. For example, the removal of six amino acids results in chemerin-157, which exhibits the highest activity, while removal of seven amino acids results in chemerin-156 which has slightly less activity. Some proteases are able to cleave at more than one site and chemerin forms may be sequentially processed by different enzymes to modulate activity levels. The coordinated expression and activity of chemerin-modifying enzymes is essential for regulating its bioactivation, inactivation and, consequently, biological function. Cathepsin G cleaves seven C-terminal amino acids from prochemerin (chemerin-156), elastase is able to cleave six (chemerin-157), eight (chemerin-155) or eleven (chemerin-152), plasmin cleaves five amino acids (chemerin-158), and tryptase cleaves five (chemerin-158) or eight (chemerin-155). Multiple cleavages might be required to fully activate chemerin, with an initial tryptase cleavage resulting in chemerin with low activity (chemerin-158), and a second cleavage by carboxypeptidase N or B producing highly active chemerin (chemerin-157). retinoid metabolic process positive regulation of protein phosphorylation platelet degranulation receptor binding protein binding extracellular region extracellular space chemotaxis inflammatory response insulin receptor signaling pathway positive regulation of macrophage chemotaxis antifungal humoral response cell differentiation platelet dense granule lumen innate immune response positive regulation of fat cell differentiation embryonic digestive tract development defense response to Gram-negative bacterium defense response to Gram-positive bacterium positive regulation of chemotaxis regulation of lipid catabolic process antifungal innate immune response uc003wha.1 uc003wha.2 uc003wha.3 uc003wha.4 uc003wha.5 
ENST00000223273.7 YAE1 ENST00000223273.7 YAE1 maturation factor of ABCE1, transcript variant 1 (from RefSeq NM_020192.5) A4D1W4 B4DE83 C7orf36 ENST00000223273.1 ENST00000223273.2 ENST00000223273.3 ENST00000223273.4 ENST00000223273.5 ENST00000223273.6 GK003 NM_020192 Q6IAF7 Q8WVZ5 Q9NRH1 YAE1 YAE1D1 YAE1_HUMAN uc003thc.1 uc003thc.2 uc003thc.3 uc003thc.4 uc003thc.5 uc003thc.6 The complex LTO1:YAE1 functions as a target specific adapter that probably recruits apo-ABCE1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery (PubMed:26182403). May be required for biogenesis of the large ribosomal subunit and initiation of translation (PubMed:26182403). Forms a complex with LTO1. Q9NRH1; Q9UPT5-1: EXOC7; NbExp=3; IntAct=EBI-712905, EBI-6251402; Q9NRH1; Q8WV07: LTO1; NbExp=8; IntAct=EBI-712905, EBI-12249832; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NRH1-1; Sequence=Displayed; Name=2; IsoId=Q9NRH1-2; Sequence=VSP_055295, VSP_055296; nucleus cytoplasm uc003thc.1 uc003thc.2 uc003thc.3 uc003thc.4 uc003thc.5 uc003thc.6 
ENST00000223293.10 GIMAP2 ENST00000223293.10 GTPase, IMAP family member 2 (from RefSeq NM_015660.3) ENST00000223293.1 ENST00000223293.2 ENST00000223293.3 ENST00000223293.4 ENST00000223293.5 ENST00000223293.6 ENST00000223293.7 ENST00000223293.8 ENST00000223293.9 GIMA2_HUMAN IMAP2 NM_015660 Q96L25 Q9UG22 uc003who.1 uc003who.2 uc003who.3 uc003who.4 uc003who.5 This gene encodes a protein belonging to the GTP-binding superfamily and to the immuno-associated nucleotide (IAN) subfamily of nucleotide-binding proteins. In humans, the IAN subfamily genes are located in a cluster at 7q36.1. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1163658.375681.1, SRR1163655.551100.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223293.10/ ENSP00000223293.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## The heterodimer formed by GIMAP2 and GIMAP7 has GTPase activity. In contrast, GIMAP2 has no GTPase activity by itself. Monomer in the presence of bound GDP and in the absence of bound nucleotide. Homodimer in the presence of bound GTP. Can form linear oligomers. Heterodimer with GIMAP7. Q9UG22; Q9UG22: GIMAP2; NbExp=4; IntAct=EBI-15891037, EBI-15891037; Q9UG22; Q8NHV1: GIMAP7; NbExp=2; IntAct=EBI-15891037, EBI-16039011; Q9UG22; P42858: HTT; NbExp=6; IntAct=EBI-15891037, EBI-466029; Lipid droplet Detected in T-cells. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family. IAN subfamily. nucleotide binding protein binding GTP binding endoplasmic reticulum lipid particle identical protein binding uc003who.1 uc003who.2 uc003who.3 uc003who.4 uc003who.5 
ENST00000223321.9 PSMA2 ENST00000223321.9 proteasome 20S subunit alpha 2 (from RefSeq NM_002787.5) ENST00000223321.1 ENST00000223321.2 ENST00000223321.3 ENST00000223321.4 ENST00000223321.5 ENST00000223321.6 ENST00000223321.7 ENST00000223321.8 HC3 NM_002787 P25787 PSA2_HUMAN PSC3 Q6ICS6 Q9BU45 uc003thy.1 uc003thy.2 uc003thy.3 uc003thy.4 uc003thy.5 uc003thy.6 The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1082236.1, SRR3476690.13824.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223321.9/ ENSP00000223321.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP- dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin- independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. P25787; P25786: PSMA1; NbExp=12; IntAct=EBI-603262, EBI-359352; P25787; P25789: PSMA4; NbExp=8; IntAct=EBI-603262, EBI-359310; P25787; P60900: PSMA6; NbExp=6; IntAct=EBI-603262, EBI-357793; P25787; O14818: PSMA7; NbExp=6; IntAct=EBI-603262, EBI-603272; P25787; Q6S8E0: ORF9b; Xeno; NbExp=2; IntAct=EBI-603262, EBI-25489144; Cytoplasm cleus te=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9 (PubMed:34711951). Colocalizes with TRIM5 in cytoplasmic bodies (By similarity). Down-regulated by antioxidants BO-653 and probucol. Down- regulated in response to enterovirus 71 (EV71) infection (at protein level). Phosphorylated on tyrosine residues; which may be important for nuclear import. Belongs to the peptidase T1A family. MAPK cascade protein polyubiquitination proteasome complex P-body stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent endopeptidase activity threonine-type endopeptidase activity protein binding extracellular region nucleus nucleoplasm cytoplasm cytosol proteasome core complex proteolysis ubiquitin-dependent protein catabolic process regulation of cellular amino acid metabolic process peptidase activity response to virus proteasomal protein catabolic process proteasomal ubiquitin-independent protein catabolic process negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination hydrolase activity proteasome core complex, alpha-subunit complex anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway secretory granule lumen NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process neutrophil degranulation regulation of mRNA stability post-translational protein modification T cell receptor signaling pathway proteolysis involved in cellular protein catabolic process transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia extracellular exosome interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation ficolin-1-rich granule lumen uc003thy.1 uc003thy.2 uc003thy.3 uc003thy.4 uc003thy.5 uc003thy.6 
ENST00000223324.3 MRPL32 ENST00000223324.3 mitochondrial ribosomal protein L32, transcript variant 2 (from RefSeq NR_156497.1) ENST00000223324.1 ENST00000223324.2 HSPC283 NR_156497 Q96Q68 Q9BYC8 Q9P098 RM32_HUMAN uc003tia.1 uc003tia.2 uc003tia.3 uc003tia.4 uc003tia.5 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein that belongs to the L32 ribosomal protein family. A pseudogene corresponding to this gene is found on chromosome Xp. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR5189664.50406.1, AW379023.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta ##RefSeq-Attributes-END## Component of the mitochondrial large ribosomal subunit (mt- LSU) (PubMed:25278503, PubMed:25838379, PubMed:28892042). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins. bL32m has a zinc binding site. Q9BYC8; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-7825220, EBI-3957793; Mitochondrion Belongs to the bacterial ribosomal protein bL32 family. RNA binding structural constituent of ribosome mitochondrion mitochondrial inner membrane mitochondrial ribosome mitochondrial large ribosomal subunit ribosome translation large ribosomal subunit mitochondrial translational elongation mitochondrial translational termination uc003tia.1 uc003tia.2 uc003tia.3 uc003tia.4 uc003tia.5 
ENST00000223336.11 COA1 ENST00000223336.11 cytochrome c oxidase assembly factor 1, transcript variant 39 (from RefSeq NR_163915.1) A6NJU8 A8KAH8 C7orf44 COA1 COA1_HUMAN ENST00000223336.1 ENST00000223336.10 ENST00000223336.2 ENST00000223336.3 ENST00000223336.4 ENST00000223336.5 ENST00000223336.6 ENST00000223336.7 ENST00000223336.8 ENST00000223336.9 MITRAC15 NR_163915 Q9GZY4 Q9HAB7 Q9NVD2 uc003tin.1 uc003tin.2 uc003tin.3 Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for assembly of mitochondrial respiratory chain complex I and complex IV (PubMed:23260140). As part of the MCIA complex, required for efficient assembly of the mitochondrial complex I (PubMed:32320651). Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, the core components of this complex being COA3/MITRAC12 and COX14. Interacts with COX17 and COA6. Part of the mitochondrial complex I assembly/MCIA complex that comprises at least the core subunits TMEM126B, NDUFAF1, ECSIT and ACAD9 and complement subunits such as COA1 and TMEM186 (PubMed:32320651). Mitochondrion inner membrane ; Single-pass membrane protein Belongs to the COA1 family. mitochondrion mitochondrial inner membrane cytosol membrane integral component of membrane integral component of mitochondrial inner membrane mitochondrial respiratory chain complex I assembly mitochondrial respiratory chain complex IV assembly uc003tin.1 uc003tin.2 uc003tin.3 
ENST00000223357.8 AEBP1 ENST00000223357.8 AE binding protein 1 (from RefSeq NM_001129.5) ACLP AEBP1_HUMAN ENST00000223357.1 ENST00000223357.2 ENST00000223357.3 ENST00000223357.4 ENST00000223357.5 ENST00000223357.6 ENST00000223357.7 NM_001129 Q14113 Q59ER7 Q6ZSC7 Q7KZ79 Q8IUX7 uc003tkb.1 uc003tkb.2 uc003tkb.3 uc003tkb.4 uc003tkb.5 uc003tkb.6 This gene encodes a member of carboxypeptidase A protein family. The encoded protein may function as a transcriptional repressor and play a role in adipogenesis and smooth muscle cell differentiation. Studies in mice suggest that this gene functions in wound healing and abdominal wall development. Overexpression of this gene is associated with glioblastoma. [provided by RefSeq, May 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC038588.1, AB209744.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223357.8/ ENSP00000223357.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## [Isoform 1]: As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix. [Isoform 2]: May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor. Isoform 1: Interacts with different types of collagen, including collagens I, III, and V (PubMed:29606302). Isoform 2: Interacts with GNG5, NFKBIA, MAPK1, MAPK3 and PTEN. Interaction with MAPK1 may stimulate DNA-binding. May interact with calmodulin. Binds to DNA in vitro. [Isoform 1]: Secreted [Isoform 2]: Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8IUX7-1; Sequence=Displayed; Name=2; IsoId=Q8IUX7-2; Sequence=VSP_033467, VSP_033468, VSP_033469; Expressed in osteoblast and visceral fat. [Isoform 1]: The F5/8 type C domain binds to different types of collagen, including collagens I, III, and V. Phosphorylated by MAPK1 in vitro. Ehlers-Danlos syndrome, classic-like, 2 (EDSCLL2) [MIM:618000]: A variant form of Ehlers-Danlos syndrome, a connective tissue disorder. EDSCLL2 patients show severe joint and skin laxity, osteoporosis affecting the hips and spine, osteoarthritis, soft redundant skin that can be acrogeria-like, delayed wound healing with abnormal atrophic scarring, and shoulder, hip, knee, and ankle dislocations. Additional variable features include gastrointestinal and genitourinary manifestations (bowel rupture, gut dysmotility, cryptorchidism, and hernias), vascular complications (mitral valve prolapse and aortic root dilation), and skeletal anomalies. EDSCLL2 inheritance is autosomal recessive. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the peptidase M14 family. Although related to peptidase M14 family, lacks the active site residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity. Sequence=BAD92981.1; Type=Erroneous initiation; Evidence=; negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription corepressor activity carboxypeptidase activity metallocarboxypeptidase activity extracellular matrix structural constituent calmodulin binding collagen binding extracellular region extracellular space nucleus cytoplasm regulation of transcription, DNA-templated proteolysis peptide metabolic process zinc ion binding protein processing extracellular exosome regulation of collagen fibril organization uc003tkb.1 uc003tkb.2 uc003tkb.3 uc003tkb.4 uc003tkb.5 uc003tkb.6 
ENST00000223364.7 MYL7 ENST00000223364.7 myosin light chain 7 (from RefSeq NM_021223.3) B2R4L3 ENST00000223364.1 ENST00000223364.2 ENST00000223364.3 ENST00000223364.4 ENST00000223364.5 ENST00000223364.6 MLRA_HUMAN MYL2A MYLC2A NM_021223 Q01449 uc003tkg.1 uc003tkg.2 uc003tkg.3 uc003tkg.4 Myosin is a hexamer of 2 heavy chains and 4 light chains. Q01449; P59942: MCCD1; NbExp=3; IntAct=EBI-10222416, EBI-11987923; Q01449; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10222416, EBI-16439278; Q01449; P78424: POU6F2; NbExp=3; IntAct=EBI-10222416, EBI-12029004; Q01449; O75688-3: PPM1B; NbExp=3; IntAct=EBI-10222416, EBI-17715099; Q01449; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-10222416, EBI-11974061; Q01449; P51687: SUOX; NbExp=3; IntAct=EBI-10222416, EBI-3921347; Q01449; O94842: TOX4; NbExp=3; IntAct=EBI-10222416, EBI-948613; Predominantly expressed in adult atrial muscle. This chain binds calcium. calcium ion binding protein binding cytosol muscle contraction myosin complex A band dendritic spine metal ion binding uc003tkg.1 uc003tkg.2 uc003tkg.3 uc003tkg.4 
ENST00000223368.7 BCL7B ENST00000223368.7 BAF chromatin remodeling complex subunit BCL7B, transcript variant 1 (from RefSeq NM_001707.4) A8K226 BCL7B_HUMAN C9JWD3 D3DXF0 ENST00000223368.1 ENST00000223368.2 ENST00000223368.3 ENST00000223368.4 ENST00000223368.5 ENST00000223368.6 NM_001707 O43769 Q13845 Q6ZW75 Q9BQE9 uc003tyf.1 uc003tyf.2 uc003tyf.3 uc003tyf.4 This gene encodes a member of the BCL7 family including BCL7A, BCL7B and BCL7C proteins. This member is BCL7B, which contains a region that is highly similar to the N-terminal segment of BCL7A or BCL7C proteins. The BCL7A protein is encoded by the gene known to be directly involved in a three-way gene translocation in a Burkitt lymphoma cell line. This gene is located at a chromosomal region commonly deleted in Williams syndrome. This gene is highly conserved from C. elegans to human. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Oct 2010]. Positive regulator of apoptosis. Plays a role in the Wnt signaling pathway, negatively regulating the expression of Wnt signaling components CTNNB1 and HMGA1 (PubMed:25569233). Involved in cell cycle progression, maintenance of the nuclear structure and stem cell differentiation (PubMed:25569233). May play a role in lung tumor development or progression (By similarity). Q9BQE9; P43357: MAGEA3; NbExp=3; IntAct=EBI-2560588, EBI-5651459; Q9BQE9; P43360: MAGEA6; NbExp=6; IntAct=EBI-2560588, EBI-1045155; Q9BQE9; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2560588, EBI-750109; Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9BQE9-1; Sequence=Displayed; Name=2; IsoId=Q9BQE9-2; Sequence=VSP_019276, VSP_019277; Name=3; IsoId=Q9BQE9-3; Sequence=VSP_019278, VSP_019279; Name=4; IsoId=Q9BQE9-4; Sequence=VSP_045923; Ubiquitous. Note=BCL7B is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BCL7B may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. Causes an allergic reaction in human. Binds to IgE from atopic dermatitis (AD) patients. Identified as an IgE autoantigen in atopic dermatitis (AD) patients with severe skin manifestations. Belongs to the BCL7 family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/779/BCL7B"; actin binding protein binding cellular_component apoptotic process biological_process Wnt signaling pathway cell differentiation uc003tyf.1 uc003tyf.2 uc003tyf.3 uc003tyf.4 
ENST00000223369.3 YKT6 ENST00000223369.3 YKT6 v-SNARE homolog, transcript variant 1 (from RefSeq NM_006555.4) B4DR94 ENST00000223369.1 ENST00000223369.2 NM_006555 O15498 Q53F01 Q6FGU9 Q6IB15 YKT6_HUMAN uc003tkm.1 uc003tkm.2 uc003tkm.3 uc003tkm.4 uc003tkm.5 This gene product is one of the SNARE recognition molecules implicated in vesicular transport between secretory compartments. It is a membrane associated, isoprenylated protein that functions at the endoplasmic reticulum-Golgi transport step. This protein is highly conserved from yeast to human and can functionally complement the loss of the yeast homolog in the yeast secretory pathway. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.938251.1, SRR3476690.962189.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223369.3/ ENSP00000223369.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity. Identified in 2 different SNARE complexes; the first one composed of GOSR1, GOSR2 and STX5 and the second one composed of BET1L, GOSR1 and STX5. Cytoplasm, cytosol. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Note=Probably cycles through vesicles between Golgi and endosomes. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O15498-1; Sequence=Displayed; Name=2; IsoId=O15498-2; Sequence=VSP_056071; The longin domain regulates palmitoylation and membrane targeting. Palmitoylated; catalyzes its own palmitoylation. Palmitoylation is required for Golgi targeting. Farnesylation is required for Golgi targeting. Belongs to the synaptobrevin family. Golgi membrane SNAP receptor activity cytoplasm mitochondrion endosome endoplasmic reticulum Golgi apparatus cytosol integral component of plasma membrane ER to Golgi vesicle-mediated transport vesicle targeting vesicle docking involved in exocytosis protein transport membrane integral component of membrane vesicle-mediated transport transferase activity protein-cysteine S-palmitoyltransferase activity transport vesicle cytoplasmic vesicle membrane SNARE complex cytoplasmic vesicle endoplasmic reticulum-Golgi intermediate compartment membrane retrograde transport, endosome to Golgi neuronal cell body cadherin binding membrane fusion apical dendrite basilar dendrite uc003tkm.1 uc003tkm.2 uc003tkm.3 uc003tkm.4 uc003tkm.5 
ENST00000223398.11 CLIP2 ENST00000223398.11 CAP-Gly domain containing linker protein 2, transcript variant 1 (from RefSeq NM_003388.5) CLIP2_HUMAN CYLN2 ENST00000223398.1 ENST00000223398.10 ENST00000223398.2 ENST00000223398.3 ENST00000223398.4 ENST00000223398.5 ENST00000223398.6 ENST00000223398.7 ENST00000223398.8 ENST00000223398.9 KIAA0291 NM_003388 O14527 O43611 Q9UDT6 WBSCR3 WBSCR4 WSCR4 uc003uam.1 uc003uam.2 uc003uam.3 uc003uam.4 The protein encoded by this gene belongs to the family of cytoplasmic linker proteins, which have been proposed to mediate the interaction between specific membranous organelles and microtubules. This protein was found to associate with both microtubules and an organelle called the dendritic lamellar body. This gene is hemizygously deleted in Williams syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at 7q11.23. Alternative splicing of this gene generates 2 transcript variants. [provided by RefSeq, Jul 2008]. Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). Interacts with CLASP1 and CLASP2 (PubMed:11290329). Binds preferentially to tyrosinated microtubules, and only marginally to detyrosinated microtubules (By similarity). Cytoplasm Cytoplasm, cytoskeleton Note=Localizes preferentially to the ends of tyrosinated microtubules. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UDT6-1; Sequence=Displayed; Name=2; IsoId=Q9UDT6-2; Sequence=VSP_015682; Note=CLIP2 is located in the Williams-Beuren syndrome (WBS) critical region (PubMed:9799601). WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of CLIP2 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. However, it has been demonstrated that haploinsufficiency of this gene alone is not sufficient to cause any of the cognitive or facial features of WBS (PubMed:22608712). Sequence=BAA22960.2; Type=Erroneous initiation; Evidence=; cytoplasm cytoskeleton microtubule microtubule associated complex cytoplasmic microtubule microtubule binding microtubule plus-end microtubule plus-end binding uc003uam.1 uc003uam.2 uc003uam.3 uc003uam.4 
ENST00000223428.9 ZNF510 ENST00000223428.9 zinc finger protein 510, transcript variant 2 (from RefSeq NM_014930.3) ENST00000223428.1 ENST00000223428.2 ENST00000223428.3 ENST00000223428.4 ENST00000223428.5 ENST00000223428.6 ENST00000223428.7 ENST00000223428.8 KIAA0972 NM_014930 Q5SZP5 Q9Y2H8 ZN510_HUMAN uc004awn.1 uc004awn.2 This gene encodes a krueppel C2H2-type zinc-finger protein family member. The encoded protein is expressed in several cancer cell types and may be a biomarker for early diagnosis of these cancers. [provided by RefSeq, Sep 2015]. May be involved in transcriptional regulation. Nucleus Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=BAA76816.2; Type=Erroneous initiation; Evidence=; nucleic acid binding DNA binding nucleus regulation of transcription, DNA-templated metal ion binding uc004awn.1 uc004awn.2 
ENST00000223459.11 ZNF688 ENST00000223459.11 zinc finger protein 688, transcript variant 1 (from RefSeq NM_145271.4) A8MV39 B3KV51 ENST00000223459.1 ENST00000223459.10 ENST00000223459.2 ENST00000223459.3 ENST00000223459.4 ENST00000223459.5 ENST00000223459.6 ENST00000223459.7 ENST00000223459.8 ENST00000223459.9 NM_145271 O75701 P0C7X2 Q8IW91 Q8WV14 Q96MN0 ZN688_HUMAN uc002dyt.1 uc002dyt.2 uc002dyt.3 uc002dyt.4 uc002dyt.5 May be involved in transcriptional regulation. P0C7X2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-4395732, EBI-11096309; P0C7X2; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-4395732, EBI-8643161; P0C7X2; X5D778: ANKRD11; NbExp=3; IntAct=EBI-4395732, EBI-17183751; P0C7X2; A0A087WZT3: BOLA2-SMG1P6; NbExp=3; IntAct=EBI-4395732, EBI-12006120; P0C7X2; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-4395732, EBI-11530605; P0C7X2; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-4395732, EBI-744545; P0C7X2; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-4395732, EBI-10171570; P0C7X2; P24863: CCNC; NbExp=3; IntAct=EBI-4395732, EBI-395261; P0C7X2; P55273: CDKN2D; NbExp=3; IntAct=EBI-4395732, EBI-745859; P0C7X2; Q86X02: CDR2L; NbExp=3; IntAct=EBI-4395732, EBI-11063830; P0C7X2; Q96Q77: CIB3; NbExp=3; IntAct=EBI-4395732, EBI-10292696; P0C7X2; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-4395732, EBI-745369; P0C7X2; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-4395732, EBI-6658203; P0C7X2; P55040: GEM; NbExp=3; IntAct=EBI-4395732, EBI-744104; P0C7X2; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-4395732, EBI-748515; P0C7X2; O95872: GPANK1; NbExp=3; IntAct=EBI-4395732, EBI-751540; P0C7X2; P49639: HOXA1; NbExp=3; IntAct=EBI-4395732, EBI-740785; P0C7X2; O75031: HSF2BP; NbExp=3; IntAct=EBI-4395732, EBI-7116203; P0C7X2; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-4395732, EBI-11955401; P0C7X2; P25800: LMO1; NbExp=3; IntAct=EBI-4395732, EBI-8639312; P0C7X2; P25791-3: LMO2; NbExp=3; IntAct=EBI-4395732, EBI-11959475; P0C7X2; Q13064: MKRN3; NbExp=3; IntAct=EBI-4395732, EBI-2340269; P0C7X2; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-4395732, EBI-5662487; P0C7X2; O43639: NCK2; NbExp=3; IntAct=EBI-4395732, EBI-713635; P0C7X2; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-4395732, EBI-11750983; P0C7X2; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-4395732, EBI-725252; P0C7X2; P16118: PFKFB1; NbExp=3; IntAct=EBI-4395732, EBI-709807; P0C7X2; O43189: PHF1; NbExp=3; IntAct=EBI-4395732, EBI-530034; P0C7X2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-4395732, EBI-10232538; P0C7X2; O15160: POLR1C; NbExp=3; IntAct=EBI-4395732, EBI-1055079; P0C7X2; P20618: PSMB1; NbExp=3; IntAct=EBI-4395732, EBI-372273; P0C7X2; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-4395732, EBI-1504830; P0C7X2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-4395732, EBI-748391; P0C7X2; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-4395732, EBI-358436; P0C7X2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-4395732, EBI-11955057; P0C7X2; Q8WWU5-7: TCP11; NbExp=3; IntAct=EBI-4395732, EBI-17721485; P0C7X2; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-4395732, EBI-750487; P0C7X2; Q96A09: TENT5B; NbExp=3; IntAct=EBI-4395732, EBI-752030; P0C7X2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-4395732, EBI-11741437; P0C7X2; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-4395732, EBI-948354; P0C7X2; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-4395732, EBI-10183064; P0C7X2; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-4395732, EBI-373456; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P0C7X2-1; Sequence=Displayed; Name=2; IsoId=P0C7X2-5; Sequence=VSP_046955; Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=AAC31673.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: ZNF688 and ZNF785.; Evidence=; molecular_function nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding cellular_component nucleus regulation of transcription, DNA-templated biological_process sequence-specific DNA binding metal ion binding uc002dyt.1 uc002dyt.2 uc002dyt.3 uc002dyt.4 uc002dyt.5 
ENST00000223500.9 CHMP5 ENST00000223500.9 charged multivesicular body protein 5, transcript variant 1 (from RefSeq NM_016410.6) B2RD95 B4DIR6 C9orf83 CGI-34 CHMP5_HUMAN ENST00000223500.1 ENST00000223500.2 ENST00000223500.3 ENST00000223500.4 ENST00000223500.5 ENST00000223500.6 ENST00000223500.7 ENST00000223500.8 HSPC177 NM_016410 PNAS-114 PNAS-2 Q5VXW2 Q96AV2 Q9HB68 Q9NYS4 Q9NZZ3 Q9Y323 SNF7DC2 uc003zsm.1 uc003zsm.2 uc003zsm.3 uc003zsm.4 uc003zsm.5 uc003zsm.6 CHMP5 belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (MIM 164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006 [PubMed 16730941]).[supplied by OMIM, Mar 2008]. Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses) (PubMed:14519844). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release (PubMed:14519844). Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with VTA1; the interaction involves soluble CHMP5 (PubMed:15644320, PubMed:17261583, PubMed:21543490). Interacts with CHMP2A (PubMed:14519844). Interacts with NOD2 (PubMed:27812135). Interacts with BROX (PubMed:22484091). Q9NZZ3; Q9H444: CHMP4B; NbExp=4; IntAct=EBI-751303, EBI-749627; Q9NZZ3; Q8WV92: MITD1; NbExp=3; IntAct=EBI-751303, EBI-2691489; Q9NZZ3; O95630: STAMBP; NbExp=2; IntAct=EBI-751303, EBI-396676; Q9NZZ3; O75351: VPS4B; NbExp=6; IntAct=EBI-751303, EBI-2514459; Q9NZZ3; Q9NP79: VTA1; NbExp=3; IntAct=EBI-751303, EBI-740160; Q9NZZ3-1; Q5VW32: BROX; NbExp=6; IntAct=EBI-15979532, EBI-6286053; Cytoplasm, cytosol Endosome membrane ; Peripheral membrane protein Midbody Note=Localizes to the midbody of dividing cells (PubMed:17853893). Localized in two distinct rings on either side of the Flemming body (PubMed:17853893). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NZZ3-1; Sequence=Displayed; Name=2; IsoId=Q9NZZ3-2; Sequence=VSP_042556; Up-regulated by muramyl-dipeptide and lipopolysaccharide. (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty acyltransferase IcsB, promoting S.flexneri evasion of autophagy. ISGylated. Isgylation inhibits its interaction with VTA1. Belongs to the SNF7 family. Sequence=AAG23821.1; Type=Erroneous initiation; Evidence=; regulation of receptor recycling protein binding nucleus cytoplasm endosome cytosol nucleus organization vacuolar transport lysosome organization mitotic metaphase plate congression endosome to lysosome transport endosome membrane regulation of centrosome duplication protein transport membrane endosomal transport viral life cycle multivesicular body assembly cadherin binding viral budding extracellular exosome cellular response to lipopolysaccharide cellular response to muramyl dipeptide multivesicular body sorting pathway regulation of mitotic spindle assembly ESCRT III complex disassembly uc003zsm.1 uc003zsm.2 uc003zsm.3 uc003zsm.4 uc003zsm.5 uc003zsm.6 
ENST00000223641.5 SEC61B ENST00000223641.5 SEC61 translocon subunit beta (from RefSeq NM_006808.3) ENST00000223641.1 ENST00000223641.2 ENST00000223641.3 ENST00000223641.4 NM_006808 P38390 P38391 P60468 Q6IBC1 SC61B_HUMAN SEC61B uc004azh.1 uc004azh.2 uc004azh.3 uc004azh.4 uc004azh.5 The Sec61 complex is the central component of the protein translocation apparatus of the endoplasmic reticulum (ER) membrane. Oligomers of the Sec61 complex form a transmembrane channel where proteins are translocated across and integrated into the ER membrane. This complex consists of three membrane proteins- alpha, beta, and gamma. This gene encodes the beta-subunit protein. The Sec61 subunits are also observed in the post-ER compartment, suggesting that these proteins can escape the ER and recycle back. There is evidence for multiple polyadenylated sites for this transcript. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: ERR279854.286.1, SRR1660807.58439.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223641.5/ ENSP00000223641.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed:12475939). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:12475939). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (PubMed:19121997). The SEC61 channel-forming translocon complex consists of channel-forming core components SEC61A1, SEC61B and SEC61G and different auxiliary components such as SEC62 and SEC63 (By similarity). The SEC61 channel associates with the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522). Interacts with TRAM1 (PubMed:19121997). P60468; P51572: BCAP31; NbExp=7; IntAct=EBI-1788819, EBI-77683; P60468; P0DTD8: 7b; Xeno; NbExp=3; IntAct=EBI-1788819, EBI-25475914; P60468; Q12154: GET3; Xeno; NbExp=4; IntAct=EBI-1788819, EBI-2989; Endoplasmic reticulum membrane ; Single-pass membrane protein Note=Loss-of-function SEC61B variations may cause autosomal dominant polycystic liver disease (PCLD) in patients that lack variations in known causative genes, such as PRKCSH and SEC63. Belongs to the SEC61-beta family. RNA binding ARF guanyl-nucleotide exchange factor activity protein binding endoplasmic reticulum Sec61 translocon complex endoplasmic reticulum membrane cytosol SRP-dependent cotranslational protein targeting to membrane, translocation intracellular protein transport protein transport membrane integral component of membrane ER-associated ubiquitin-dependent protein catabolic process retrograde protein transport, ER to cytosol posttranslational protein targeting to membrane, translocation endoplasmic reticulum Sec complex epidermal growth factor binding P-P-bond-hydrolysis-driven protein transmembrane transporter activity uc004azh.1 uc004azh.2 uc004azh.3 uc004azh.4 uc004azh.5 
ENST00000223642.3 C5 ENST00000223642.3 complement C5, transcript variant 1 (from RefSeq NM_001735.3) CO5_HUMAN CPAMD4 ENST00000223642.1 ENST00000223642.2 NM_001735 P01031 Q14CJ0 Q27I61 uc004bkv.1 uc004bkv.2 uc004bkv.3 uc004bkv.4 uc004bkv.5 This gene encodes a component of the complement system, a part of the innate immune system that plays an important role in inflammation, host homeostasis, and host defense against pathogens. The encoded preproprotein is proteolytically processed to generate multiple protein products, including the C5 alpha chain, C5 beta chain, C5a anaphylatoxin and C5b. The C5 protein is comprised of the C5 alpha and beta chains, which are linked by a disulfide bridge. Cleavage of the alpha chain by a convertase enzyme results in the formation of the C5a anaphylatoxin, which possesses potent spasmogenic and chemotactic activity, and the C5b macromolecular cleavage product, a subunit of the membrane attack complex (MAC). Mutations in this gene cause complement component 5 deficiency, a disease characterized by recurrent bacterial infections. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2015]. Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. [C5a anaphylatoxin]: Derived from proteolytic degradation of complement C5, C5a anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes (PubMed:8182049). C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. C5 precursor is first processed by the removal of 4 basic residues, forming two chains, beta and alpha, linked by a disulfide bond. C5 convertase activates C5 by cleaving the alpha chain, releasing C5a anaphylatoxin and generating C5b (beta chain + alpha' chain). Interacts with the tick complement inhibitors OmCI, RaCI1 and CirpT1 (PubMed:18536718, PubMed:27018802, PubMed:31871188). Interacts with cobra venom factor (CVF) (PubMed:21217642). [C5a anaphylatoxin]: Interacts with C5AR1. (Microbial infection) Interacts with Staphylococcus aureus protein SSL5. P01031; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-8558308, EBI-7054139; P01031; Q13520: AQP6; NbExp=3; IntAct=EBI-8558308, EBI-13059134; P01031; Q03591: CFHR1; NbExp=3; IntAct=EBI-8558308, EBI-3935840; P01031; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-8558308, EBI-18013275; P01031; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-8558308, EBI-6942903; P01031; Q15125: EBP; NbExp=3; IntAct=EBI-8558308, EBI-3915253; P01031; P23276: KEL; NbExp=3; IntAct=EBI-8558308, EBI-746662; P01031; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-8558308, EBI-17272405; P01031; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-8558308, EBI-6163737; P01031; O14524-2: NEMP1; NbExp=3; IntAct=EBI-8558308, EBI-10969203; P01031; O15173: PGRMC2; NbExp=3; IntAct=EBI-8558308, EBI-1050125; P01031; P78424: POU6F2; NbExp=3; IntAct=EBI-8558308, EBI-12029004; P01031; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-8558308, EBI-17280858; P01031; Q91132; Xeno; NbExp=2; IntAct=EBI-8558308, EBI-7081824; Secreted. C5 variants are responsible for poor response to eculizumab [MIM:615749]. Eculizumab is a monoclonal antibody highly effective in reducing intravascular hemolysis in patients with paroxysmal nocturnal hemoglobinuria. It specifically binds to the terminal complement protein C5, inhibits its cleavage into C5a and C5b, and prevents the formations of the cytolytic complement pore (PubMed:24521109). Complement component 5 deficiency (C5D) [MIM:609536]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note=The disease is caused by variants affecting the gene represented in this entry. Note=An association study of C5 haplotypes and genotypes in individuals with chronic hepatitis C virus infection shows that individuals homozygous for the C5_1 haplotype have a significantly higher stage of liver fibrosis than individuals carrying at least 1 other allele. Name=C5base; Note=C5 mutation db; URL="http://structure.bmc.lu.se/idbase/C5base/"; Name=Wikipedia; Note=Complement C5 entry; URL="https://en.wikipedia.org/wiki/Complement_component_5"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/c5/"; activation of MAPK activity immune system process endopeptidase inhibitor activity receptor binding protein binding extracellular region membrane attack complex extracellular space chemotaxis inflammatory response complement activation complement activation, alternative pathway complement activation, classical pathway cell surface receptor signaling pathway G-protein coupled receptor signaling pathway chemokine activity positive regulation of vascular endothelial growth factor production negative regulation of macrophage chemotaxis negative regulation of endopeptidase activity cytolysis regulation of complement activation innate immune response cell chemotaxis extracellular exosome positive regulation of chemokine secretion uc004bkv.1 uc004bkv.2 uc004bkv.3 uc004bkv.4 uc004bkv.5 
ENST00000223795.3 TNFSF8 ENST00000223795.3 TNF superfamily member 8, transcript variant 1 (from RefSeq NM_001244.4) ENST00000223795.1 ENST00000223795.2 NM_001244 Q52M88 Q52M88_HUMAN TNFSF8 TNLG3A hCG_29853 uc004bji.1 uc004bji.2 uc004bji.3 uc004bji.4 The protein encoded by this gene is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The engagement of this cytokine expressed on B cell surface plays an inhibitory role in modulating Ig class switch. This cytokine was shown to enhance cell proliferation of some lymphoma cell lines, while to induce cell death and reduce cell proliferation of other lymphoma cell lines. The pleiotropic biologic activities of this cytokine on different CD30+ lymphoma cell lines may play a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2011]. Belongs to the tumor necrosis factor family. cytokine activity tumor necrosis factor receptor binding extracellular space immune response signal transduction membrane integral component of membrane CD8-positive, alpha-beta T cell differentiation positive regulation of transcription from RNA polymerase II promoter defense response to Gram-positive bacterium uc004bji.1 uc004bji.2 uc004bji.3 uc004bji.4 
ENST00000223862.2 RLN1 ENST00000223862.2 relaxin 1 (from RefSeq NM_006911.4) ENST00000223862.1 NM_006911 P04808 Q99936 Q9UQJ1 REL1_HUMAN uc003zjb.1 uc003zjb.2 uc003zjb.3 uc003zjb.4 Relaxins are known endocrine and autocrine/paracrine hormones, belonging to the insulin gene superfamily. In humans there are three non-allelic relaxin genes, RLN1, RLN2 and RLN3, where RLN1 and RLN2 share high sequence homology. The protein encoded by this gene is synthesized as a single-chain polypeptide but the active form consists of an A chain and a B chain linked by disulfide bonds. Relaxin is produced by the ovary, and targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may have additional roles in enhancing sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. [provided by RefSeq, Jan 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC005956.1, X00949.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145240, SAMEA2153427 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000223862.2/ ENSP00000223862.1 RefSeq Select criteria :: based on expression, longest protein ##RefSeq-Attributes-END## Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix. Heterodimer of a B chain and an A chain linked by two disulfide bonds. P04808; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12071382, EBI-5916454; P04808; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-12071382, EBI-10172526; Secreted. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P04808-1; Sequence=Displayed; Name=2; IsoId=P04808-2; Sequence=VSP_002709, VSP_002710; Prostate. Not expressed in placenta, decidua or ovary. Belongs to the insulin family. hormone activity extracellular region signal transduction female pregnancy uc003zjb.1 uc003zjb.2 uc003zjb.3 uc003zjb.4 
ENST00000223864.7 PLGRKT ENST00000223864.7 plasminogen receptor with a C-terminal lysine (from RefSeq NM_018465.4) AD025 B2R6W0 C9orf46 ENST00000223864.1 ENST00000223864.2 ENST00000223864.3 ENST00000223864.4 ENST00000223864.5 ENST00000223864.6 MDS030 NM_018465 PLRKT_HUMAN Q9HBL7 Q9NZ44 uc003zjc.1 uc003zjc.2 uc003zjc.3 uc003zjc.4 uc003zjc.5 uc003zjc.6 Receptor for plasminogen. Regulates urokinase plasminogen activator-dependent and stimulates tissue-type plasminogen activator- dependent cell surface plasminogen activation. Proposed to be part of a local catecholaminergic cell plasminogen activation system that regulates neuroendocrine prohormone processing. Involved in regulation of inflammatory response; regulates monocyte chemotactic migration and matrix metalloproteinase activation, such as of MMP2 and MMP9. Interacts with PLAT and PLAUR. Q9HBL7; P26641-2: EEF1G; NbExp=3; IntAct=EBI-714824, EBI-10177695; Cell membrane ; Multi-pass membrane protein Note=Colocalizes on the cell surface with urokinase plasminogen activator surface receptor/PLAUR. Expressed in peripheral blood cells and monocytes. Expressed in adrenal medulla. protein binding plasma membrane integral component of plasma membrane chemotaxis inflammatory response positive regulation of plasminogen activation membrane integral component of membrane uc003zjc.1 uc003zjc.2 uc003zjc.3 uc003zjc.4 uc003zjc.5 uc003zjc.6 
ENST00000224073.6 EDF1 ENST00000224073.6 endothelial differentiation related factor 1, transcript variant alpha (from RefSeq NM_003792.4) EDF1_HUMAN ENST00000224073.1 ENST00000224073.2 ENST00000224073.3 ENST00000224073.4 ENST00000224073.5 NM_003792 O60869 Q5T5T2 Q9UIM1 uc004cjt.1 uc004cjt.2 uc004cjt.3 uc004cjt.4 This gene encodes a protein that may regulate endothelial cell differentiation, lipid metabolism, and hormone-induced cardiomyocyte hypertrophy. The encoded protein has also been found to act as a transcriptional coactivator by interconnecting the general transcription factor TATA element-binding protein (TBP) and gene-specific activators. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]. Transcriptional coactivator stimulating NR5A1 and ligand- dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone- induced cardiomyocytes hypertrophy and lipid metabolism. Interacts with TBP and the transcription factor IID (TFIID) complex, NR5A2, NR1H3 and PPARG. Interaction with TBP is regulated by phosphorylation. Binds NR5A1, ATF1, FOS and JUN via their conserved basic region. Binding to calmodulin is regulated by calcium and phosphorylation of the IQ motif. O60869; P13569: CFTR; NbExp=3; IntAct=EBI-781301, EBI-349854; O60869; P03372: ESR1; NbExp=3; IntAct=EBI-781301, EBI-78473; O60869; P42858: HTT; NbExp=6; IntAct=EBI-781301, EBI-466029; O60869; P50222: MEOX2; NbExp=3; IntAct=EBI-781301, EBI-748397; O60869; Q13133: NR1H3; NbExp=4; IntAct=EBI-781301, EBI-781356; O60869; O00482: NR5A2; NbExp=2; IntAct=EBI-781301, EBI-781320; O60869; P37231: PPARG; NbExp=4; IntAct=EBI-781301, EBI-781384; O60869; P03495: NS; Xeno; NbExp=2; IntAct=EBI-781301, EBI-2548993; O60869-1; P20226: TBP; NbExp=2; IntAct=EBI-781310, EBI-355371; O60869-1; Q04752: NR5A1; Xeno; NbExp=4; IntAct=EBI-781310, EBI-850837; Cytoplasm. Nucleus. Note=Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin. Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=Alpha; IsoId=O60869-1; Sequence=Displayed; Name=2; Synonyms=Beta; IsoId=O60869-2; Sequence=VSP_013336; Name=3; IsoId=O60869-3; Sequence=VSP_054701; Expressed in brain, liver, lung, kidney and heart (at protein level). Ubiquitously expressed. More abundant in heart, pancreas, liver, intestine and adipose tissues. Expressed in fetal tissues. More abundant in kidney. Down-regulated by HIV-1 Tat or phorbol ester (TPA) treatment in endothelial cells (at mRNA and protein levels). The IQ motif, which is involved in calmodulin binding, overlaps with the binding domain for nuclear receptors and transcription factors. Its phosphorylation probably allows a switch between the two activities of the protein (By similarity). Phosphorylated (by PKA and PKC). TFIID-class transcription factor binding DNA binding transcription coactivator activity RNA binding protein binding calmodulin binding intracellular nucleus nucleolus cytoplasm cytosol regulation of transcription, DNA-templated multicellular organism development regulation of lipid metabolic process cell differentiation positive regulation of DNA binding endothelial cell differentiation positive regulation of transcription, DNA-templated uc004cjt.1 uc004cjt.2 uc004cjt.3 uc004cjt.4 
ENST00000224140.6 SETX ENST00000224140.6 senataxin, transcript variant 1 (from RefSeq NM_015046.7) A2A396 ALS4 B2RPB2 B5ME16 C9JQ10 ENST00000224140.1 ENST00000224140.2 ENST00000224140.3 ENST00000224140.4 ENST00000224140.5 KIAA0625 NM_015046 O75120 Q3KQX4 Q5JUJ1 Q68DW5 Q6AZD7 Q7Z333 Q7Z3J6 Q8WX33 Q9H9D1 Q9NVP9 SCAR1 SETX SETX_HUMAN uc004cbk.1 uc004cbk.2 uc004cbk.3 uc004cbk.4 uc004cbk.5 This gene encodes a protein named for its homology to the Sen1p protein of fungi which has RNA helicase activity encoded by a domain at the C-terminal end of the protein. The protein encoded by this gene contains a DNA/RNA helicase domain at its C-terminal end which suggests that it may be involved in both DNA and RNA processing. Mutations in this gene have been associated with ataxia-ocular apraxia-2 (AOA2) and an autosomal dominant form of juvenile amyotrophic lateral sclerosis (ALS4). [provided by RefSeq, Jul 2008]. Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription (PubMed:19515850, PubMed:21700224). Contributes to the mRNA splicing efficiency and splice site selection (PubMed:19515850). Required for the resolution of R-loop RNA-DNA hybrid formation at G- rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (PubMed:19515850, PubMed:21700224, PubMed:26700805). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress (PubMed:17562789). In association with RRP45, targets the RNA exosome complex to sites of transcription- induced DNA damage (PubMed:24105744). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (By similarity). May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (PubMed:21112256). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis (PubMed:21576111). Homodimer (PubMed:24244371). Interacts with PER2; the interaction inhibits termination of circadian target genes (By similarity). Interacts with CHD4, POLR2A, PRKDC and TRIM28 (PubMed:23149945). Does not interact with C14orf178 (PubMed:24244371). Interacts with UBE2I (PubMed:24105744). Interacts (via N-terminus domain) with EXOSC9 (via C-terminus region); the interaction enhances SETX sumoylation (PubMed:24105744). Interacts with NCL (via N-terminus domain) (PubMed:19515850). Interacts with PABPN1, PABPC1 and SF3B1 (PubMed:19515850). Interacts with SMN1/SMN2 and POLR2A; SMN1/SMN2 recruits SETX to POLR2A (PubMed:19515850, PubMed:26700805). Q7Z333; P24928: POLR2A; NbExp=7; IntAct=EBI-1220123, EBI-295301; Q7Z333; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-1220123, EBI-11528848; Q7Z333; Q7Z333: SETX; NbExp=4; IntAct=EBI-1220123, EBI-1220123; Q7Z333; Q9GZS3: SKIC8; NbExp=3; IntAct=EBI-1220123, EBI-358545; Q7Z333; Q16637: SMN2; NbExp=3; IntAct=EBI-1220123, EBI-395421; Q7Z333; P63279: UBE2I; NbExp=3; IntAct=EBI-1220123, EBI-80168; Q7Z333; O75604-3: USP2; NbExp=3; IntAct=EBI-1220123, EBI-10696113; Nucleus cleus, nucleoplasm Nucleus, nucleolus Cytoplasm romosome Chromosome, telomere Cell projection, axon Cell projection, growth cone Note=May be detected in the nucleolus only in cycling cells. At pachytene stage, colocalizes predominantly to the heterochromatic XY-body of sex chromosomes with DNA damage response proteins in a BRCA1-dependent manner (By similarity). Localizes with telomeric DNA in a transcription-dependent manner (PubMed:21112256). Under replication stress, colocalizes with a variety of DNA damage signaling and repair response proteins at distinct nuclear foci in mitotic S/G2- and G1-phase cells in a transcription- and RNA/DNA hybrid-dependent manner (PubMed:23149945). Localizes at limited number of nuclear foci (PubMed:24105744). Colocalizes with EXOSC9 in nuclear foci upon induction of transcription-related DNA damage at the S phase (PubMed:24105744). Most abundant in the nucleus. Detected in granules. Colocalized in cycling cells with FBL in the nucleolus. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q7Z333-1; Sequence=Displayed; Name=3; IsoId=Q7Z333-3; Sequence=VSP_017124; Name=4; IsoId=Q7Z333-4; Sequence=VSP_028826; Highly expressed in skeletal muscle. Expressed in heart, fibroblast, placenta and liver. Weakly expressed in brain and lung. Expressed in the cortex of the kidney (highly expressed in tubular epithelial cells but low expression in the glomerulus). The N-terminus domain is necessary for S/G2 nuclear foci localization (PubMed:23149945). Ubiquitinated. Sumoylated preferentially with SUMO2 or SUMO3 (PubMed:24105744, PubMed:24244371). Spinocerebellar ataxia, autosomal recessive, with axonal neuropathy 2 (SCAN2) [MIM:606002]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAN2 is an autosomal recessive form associated with peripheral neuropathy and elevated serum alpha-fetoprotein, immunoglobulins and, less commonly, creatine kinase levels. Some SCAN2 patients manifest oculomotor apraxia. te=The disease is caused by variants affecting the gene represented in this entry. Amyotrophic lateral sclerosis 4 (ALS4) [MIM:602433]: A form of amyotrophic lateral sclerosis with childhood- or adolescent-onset, and characterized by slow disease progression and the sparing of bulbar and respiratory muscles. Amyotrophic lateral sclerosis is a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the DNA2/NAM7 helicase family. Sequence=BAA91701.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAB14299.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=CAD97857.1; Type=Frameshift; Evidence=; MAPK cascade nucleotide binding nuclear chromosome chromosome, telomeric region transcription termination site sequence-specific DNA binding DNA binding DNA helicase activity RNA binding helicase activity protein binding ATP binding nucleus nucleoplasm chromosome nucleolus cytoplasm DNA repair double-strand break repair DNA recombination DNA-templated transcription, termination termination of RNA polymerase II transcription mRNA splice site selection RNA processing cellular response to DNA damage stimulus spermatogenesis nervous system development circadian rhythm fibroblast growth factor receptor signaling pathway positive regulation of neuron projection development nuclear body hydrolase activity cell differentiation axon growth cone DNA duplex unwinding positive regulation of RNA splicing cellular response to oxidative stress identical protein binding cell projection negative regulation of apoptotic process protein kinase B signaling cellular response to fibroblast growth factor stimulus intercellular bridge positive regulation of transcription from RNA polymerase II promoter rhythmic process positive regulation of DNA-templated transcription, termination cellular response to hydrogen peroxide cellular response to retinoic acid positive regulation of DNA-templated transcription, initiation positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled uc004cbk.1 uc004cbk.2 uc004cbk.3 uc004cbk.4 uc004cbk.5 
ENST00000224337.10 BLNK ENST00000224337.10 B cell linker, transcript variant 1 (from RefSeq NM_013314.4) BASH BLNK_HUMAN ENST00000224337.1 ENST00000224337.2 ENST00000224337.3 ENST00000224337.4 ENST00000224337.5 ENST00000224337.6 ENST00000224337.7 ENST00000224337.8 ENST00000224337.9 NM_013314 O75498 O75499 Q2MD49 Q8WV28 SLP65 uc001kls.1 uc001kls.2 uc001kls.3 uc001kls.4 uc001kls.5 uc001kls.6 This gene encodes a cytoplasmic linker or adaptor protein that plays a critical role in B cell development. This protein bridges B cell receptor-associated kinase activation with downstream signaling pathways, thereby affecting various biological functions. The phosphorylation of five tyrosine residues is necessary for this protein to nucleate distinct signaling effectors following B cell receptor activation. Mutations in this gene cause hypoglobulinemia and absent B cells, a disease in which the pro- to pre-B-cell transition is developmentally blocked. Deficiency in this protein has also been shown in some cases of pre-B acute lymphoblastic leukemia. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, May 2012]. Functions as a central linker protein, downstream of the B- cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR- mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR- induced B-cell apoptosis. Associates with PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with VAV3, PLCG2 and GRB2. Interacts through its SH2 domain with CD79A. Interacts (via SH2 domain) with SYK; phosphorylated and activated by SYK. Interacts (via SH2 domain) with SCIMP; this interaction is dependent on phosphorylation of SCIMP 'Tyr-131' (PubMed:21930792). Q8WV28; P10275: AR; NbExp=2; IntAct=EBI-2623522, EBI-608057; Q8WV28; Q06187: BTK; NbExp=2; IntAct=EBI-2623522, EBI-624835; Q8WV28; Q9Y5K6: CD2AP; NbExp=2; IntAct=EBI-2623522, EBI-298152; Q8WV28; P62993: GRB2; NbExp=4; IntAct=EBI-2623522, EBI-401755; Q8WV28; P10721: KIT; NbExp=2; IntAct=EBI-2623522, EBI-1379503; Q8WV28; Q5ZMQ7: RCJMB04_1g20; Xeno; NbExp=3; IntAct=EBI-2623522, EBI-7061433; Cytoplasm Cell membrane Note=BCR activation results in the translocation to membrane fraction. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q8WV28-1; Sequence=Displayed; Name=2; IsoId=Q8WV28-2; Sequence=VSP_016178; Name=3; IsoId=Q8WV28-3; Sequence=VSP_045324; Expressed in B-cell lineage and fibroblast cell lines (at protein level). Highest levels of expression in the spleen, with lower levels in the liver, kidney, pancreas, small intestines and colon. Following BCR activation, phosphorylated on tyrosine residues by SYK and LYN. When phosphorylated, serves as a scaffold to assemble downstream targets of antigen activation, including PLCG1, VAV1, GRB2 and NCK1. Phosphorylation of Tyr-84, Tyr-178 and Tyr-189 facilitates PLCG1 binding. Phosphorylation of Tyr-96 facilitates BTK binding. Phosphorylation of Tyr-72 facilitates VAV1 and NCK1 binding. Phosphorylation is required for both Ca(2+) and MAPK signaling pathways. Agammaglobulinemia 4, autosomal recessive (AGM4) [MIM:613502]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. Note=The disease is caused by variants affecting the gene represented in this entry. Name=BLNKbase; Note=BLNK mutation db; URL="http://structure.bmc.lu.se/idbase/BLNKbase/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/804/BLNK"; transmembrane receptor protein tyrosine kinase adaptor activity SH3/SH2 adaptor activity protein binding cytoplasm cytosol plasma membrane inflammatory response humoral immune response transmembrane receptor protein tyrosine kinase signaling pathway positive regulation of signal transduction membrane B cell differentiation intracellular signal transduction cytoplasmic ribonucleoprotein granule B cell activation uc001kls.1 uc001kls.2 uc001kls.3 uc001kls.4 uc001kls.5 uc001kls.6 
ENST00000224356.5 CYP26A1 ENST00000224356.5 cytochrome P450 family 26 subfamily A member 1, transcript variant 1 (from RefSeq NM_000783.4) B3KNI4 CP26A_HUMAN CYP26 CYP26A1 ENST00000224356.1 ENST00000224356.2 ENST00000224356.3 ENST00000224356.4 NM_000783 O43174 P450RAI1 Q5VXH9 Q5VXI0 uc001kil.1 uc001kil.2 uc001kil.3 uc001kil.4 This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This endoplasmic reticulum protein acts on retinoids, including all-trans-retinoic acid (RA), with both 4-hydroxylation and 18-hydroxylation activities. This enzyme regulates the cellular level of retinoic acid which is involved in regulation of gene expression in both embryonic and adult tissues. Two alternatively spliced transcript variants of this gene, which encode the distinct isoforms, have been reported. [provided by RefSeq, Jul 2008]. A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:22020119, PubMed:9228017, PubMed:9716180). RAs exist as at least four different isomers: all- trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (Probable). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (PubMed:22020119, PubMed:9228017, PubMed:9716180). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (Probable). Involved in the convertion of atRA to all-trans-4-oxo-RA. Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA (By similarity) (PubMed:9228017). Can oxidize all-trans-13,14- dihydroretinoate (DRA) to metabolites which could include all-trans-4- oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all- trans-18-hydroxy-DRA (By similarity). May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (PubMed:26937021). Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S)-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51492, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51493; Evidence=; Reaction=all-trans-(4S)-hydroxyretinoate + O2 + reduced [NADPH-- hemoprotein reductase] = all-trans-(4S,16)-dihydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51632, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185, ChEBI:CHEBI:134233; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51633; Evidence=; Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-18-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55856, Rhea:RHEA- COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:139258; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55857; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Kinetic parameters: KM=50.1 nM for all-trans-retinoate (4-hydroxylation) ; KM=48.9 nM for all-trans-retinoate (18-hydroxylation) ; KM=0.24 uM for tazarotenic acid (tazarotenic acid sulfoxide formation) ; KM=0.39 uM for tazarotenic acid (hydroxytazarotenic acid formation) ; Vmax=9.5 pmol/min/pmol enzyme toward all-trans-retinoate (4- hydroxylation) ; Vmax=5.0 pmol/min/pmol enzyme toward all-trans-retinoate (18- hydroxylation) ; Endoplasmic reticulum membrane ; Peripheral membrane protein. Microsome membrane ; Peripheral membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43174-1; Sequence=Displayed; Name=2; IsoId=O43174-2; Sequence=VSP_045087; Expressed in most fetal and adult tissues with highest levels in adult liver, heart, pituitary gland, adrenal gland, placenta and regions of the brain (PubMed:9826557). Expressed at high levels in lung, pancreas, skin and uterus (at protein level) (PubMed:22020119). Lower expression level is detected in spleen, kidney, intestine and adipose tissue (at protein level) (PubMed:22020119). By retinoic acid. Belongs to the cytochrome P450 family. C-22 sterol desaturase activity kidney development retinoic acid binding monooxygenase activity iron ion binding endoplasmic reticulum endoplasmic reticulum membrane ergosterol biosynthetic process vitamin metabolic process xenobiotic metabolic process retinoic acid 4-hydroxylase activity membrane sterol metabolic process oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen oxygen binding heme binding organelle membrane response to retinoic acid response to vitamin A retinoic acid catabolic process retinoic acid metabolic process intracellular membrane-bounded organelle metal ion binding negative regulation of retinoic acid receptor signaling pathway oxidation-reduction process uc001kil.1 uc001kil.2 uc001kil.3 uc001kil.4 
ENST00000224652.12 ATE1 ENST00000224652.12 arginyltransferase 1, transcript variant 1 (from RefSeq NM_001001976.3) ATE1 ATE1_HUMAN ENST00000224652.1 ENST00000224652.10 ENST00000224652.11 ENST00000224652.2 ENST00000224652.3 ENST00000224652.4 ENST00000224652.5 ENST00000224652.6 ENST00000224652.7 ENST00000224652.8 ENST00000224652.9 NM_001001976 O95260 O95261 Q5SQQ3 Q8WW04 uc001lfq.1 uc001lfq.2 uc001lfq.3 uc001lfq.4 uc001lfq.5 uc001lfq.6 This gene encodes an arginyltransferase, an enzyme that is involved in posttranslational conjugation of arginine to N-terminal aspartate or glutamate residues. Conjugation of arginine to the N-terminal aspartate or glutamate targets proteins for ubiquitin-dependent degradation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2013]. Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues. Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl- tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] + tRNA(Arg); Xref=Rhea:RHEA:10208, Rhea:RHEA-COMP:9658, Rhea:RHEA- COMP:9673, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10638, ChEBI:CHEBI:15378, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:78597, ChEBI:CHEBI:83562; EC=2.3.2.8; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10209; Evidence=; Monomer. Interacts with LIAT1; LIAT1 is not a substrate of ATE1, the interaction takes place in the cytoplasm and seems to increase ATE1 arginyltransferase activity. O95260; O43463: SUV39H1; NbExp=2; IntAct=EBI-1043378, EBI-349968; [Isoform ATE1-1]: Nucleus Cytoplasm [Isoform ATE1-2]: Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=ATE1-1; IsoId=O95260-1; Sequence=Displayed; Name=ATE1-2; IsoId=O95260-2; Sequence=VSP_000336; Belongs to the R-transferase family. It is uncertain whether Met-1 or Met-37 is the initiator. arginyltransferase activity protein binding nucleus cytoplasm proteasomal protein catabolic process protein arginylation transferase activity transferase activity, transferring acyl groups uc001lfq.1 uc001lfq.2 uc001lfq.3 uc001lfq.4 uc001lfq.5 uc001lfq.6 
ENST00000224721.12 CDH23 ENST00000224721.12 cadherin related 23, transcript variant 1 (from RefSeq NM_022124.6) C4IXS9 CAD23_HUMAN CDH23 ENST00000224721.1 ENST00000224721.10 ENST00000224721.11 ENST00000224721.2 ENST00000224721.3 ENST00000224721.4 ENST00000224721.5 ENST00000224721.6 ENST00000224721.7 ENST00000224721.8 ENST00000224721.9 F6U049 KIAA1774 KIAA1812 NM_022124 Q5QGS1 Q5QGS2 Q5QGS5 Q5QGS6 Q5XKN2 Q6UWW1 Q96JL3 Q9H251 Q9H4K9 UNQ1894/PRO4340 uc285hzv.1 uc285hzv.2 This gene is a member of the cadherin superfamily, whose genes encode calcium dependent cell-cell adhesion glycoproteins. The encoded protein is thought to be involved in stereocilia organization and hair bundle formation. The gene is located in a region containing the human deafness loci DFNB12 and USH1D. Usher syndrome 1D and nonsyndromic autosomal recessive deafness DFNB12 are caused by allelic mutations of this cadherin-like gene. Upregulation of this gene may also be associated with breast cancer. Alternative splice variants encoding different isoforms have been described. [provided by RefSeq, May 2013]. Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells. CDH23 is required for establishing and/or maintaining the proper organization of the stereocilia bundle of hair cells in the cochlea and the vestibule during late embryonic/early postnatal development. It is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. antiparallel heterodimer with PCDH15 (By similarity). Interacts with USH1C and USH1G (PubMed:19297620, PubMed:21436032). Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=11; Comment=Additional isoforms seem to exist.; Name=1; IsoId=Q9H251-1; Sequence=Displayed; Name=2; IsoId=Q9H251-2; Sequence=VSP_000645; Name=3; IsoId=Q9H251-3; Sequence=VSP_000646; Name=4; IsoId=Q9H251-4; Sequence=VSP_000647; Name=5; IsoId=Q9H251-5; Sequence=VSP_013268, VSP_013269; Name=6; IsoId=Q9H251-6; Sequence=VSP_035289, VSP_035290; Name=7; Synonyms=B1; IsoId=Q9H251-7; Sequence=VSP_044260; Name=8; IsoId=Q9H251-8; Sequence=VSP_044261, VSP_000645; Name=9; Synonyms=B2; IsoId=Q9H251-9; Sequence=VSP_044260, VSP_000647; Name=10; Synonyms=C1; IsoId=Q9H251-10; Sequence=VSP_047923, VSP_047924; Name=11; Synonyms=C2; IsoId=Q9H251-11; Sequence=VSP_047923, VSP_047924, VSP_000647; Particularly strong expression in the retina (PubMed:11138009). Found also in the cochlea. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic interaction with PCDH15. Usher syndrome 1D (USH1D) [MIM:601067]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness. te=The disease is caused by variants affecting the gene represented in this entry. Usher syndrome 1D/F (USH1DF) [MIM:601067]: A digenic recessive form of Usher syndrome, a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. Deafness, autosomal recessive, 12 (DFNB12) [MIM:601386]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. te=The disease is caused by variants affecting the gene represented in this entry. Pituitary adenoma 5, multiple types (PITA5) [MIM:617540]: A form of pituitary adenoma, a neoplasm of the pituitary gland and one of the most common neuroendocrine tumors. Pituitary adenomas are clinically classified as functional and non-functional tumors, and manifest with a variety of features, including local invasion of surrounding structures and excessive hormone secretion. Functional pituitary adenomas are further classified by the type of hormone they secrete: growth hormone (GH)-secreting, prolactin (PRL)-secreting, adrenocorticotropin (ACTH)-secreting, thyroid-stimulating hormone (TSH)-secreting, and plurihormonal (GH and TSH) tumors. Familial and sporadic forms have been reported. The transmission pattern of familial PITA5 is consistent with autosomal dominant inheritance with reduced penetrance. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Name=Mutations of the CDH23 gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/cdh23mut.htm"; cell morphogenesis calcium ion binding protein binding plasma membrane cell-cell adherens junction calcium ion transport cell-cell junction assembly cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules visual perception sensory perception of sound locomotory behavior cytoskeletal protein binding cell surface membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules catenin complex stereocilium adherens junction organization protein homodimerization activity cell-cell adhesion mediated by cadherin cadherin binding photoreceptor cell maintenance metal ion binding response to stimulus sensory perception of light stimulus equilibrioception regulation of cytosolic calcium ion concentration inner ear receptor stereocilium organization cell-cell adhesion uc285hzv.1 uc285hzv.2 
ENST00000224784.10 ACTA2 ENST00000224784.10 actin alpha 2, smooth muscle, transcript variant 2 (from RefSeq NM_001613.4) ACTA_HUMAN ACTSA ACTVS B2R8A4 ENST00000224784.1 ENST00000224784.2 ENST00000224784.3 ENST00000224784.4 ENST00000224784.5 ENST00000224784.6 ENST00000224784.7 ENST00000224784.8 ENST00000224784.9 GIG46 NM_001613 P03996 P04108 P62736 Q6FI19 uc001kfp.1 uc001kfp.2 uc001kfp.3 uc001kfp.4 This gene encodes one of six different actin proteins. Actins are highly conserved proteins that are involved in cell motility, structure, integrity, and intercellular signaling. The encoded protein is a smooth muscle actin that is involved in vascular contractility and blood pressure homeostasis. Mutations in this gene cause a variety of vascular diseases, such as thoracic aortic disease, coronary artery disease, stroke, and Moyamoya disease, as well as multisystemic smooth muscle dysfunction syndrome. [provided by RefSeq, Sep 2017]. Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence=; Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Cytoplasm, cytoskeleton. Up-regulated in response to enterovirus 71 (EV71) infection. Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. Methylated at His-75 by SETD3. [Actin, aortic smooth muscle, intermediate form]: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. (Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-52 of one monomer and Glu-272 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin- dependent and independent manners (PubMed:26228148). Note=ACTA2 mutations predispose patients to a variety of diffuse and diverse vascular diseases, premature onset coronary artery disease (CAD), premature ischemic strokes and Moyamoya disease. Aortic aneurysm, familial thoracic 6 (AAT6) [MIM:611788]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. te=The disease is caused by variants affecting the gene represented in this entry. Moyamoya disease 5 (MYMY5) [MIM:614042]: A progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults. Note=The disease is caused by variants affecting the gene represented in this entry. Multisystemic smooth muscle dysfunction syndrome (MSMDS) [MIM:613834]: A syndrome characterized by dysfunction of smooth muscle cells throughout the body, leading to aortic and cerebrovascular disease, fixed dilated pupils, hypotonic bladder, malrotation, and hypoperistalsis of the gut and pulmonary hypertension. Note=The disease is caused by variants affecting the gene represented in this entry. In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. Belongs to the actin family. nucleotide binding ATP binding extracellular space cytoplasm cytosol cytoskeleton muscle contraction regulation of blood pressure response to virus positive regulation of gene expression vascular smooth muscle contraction actin cytoskeleton protein kinase binding lamellipodium filopodium smooth muscle contractile fiber macromolecular complex cell body positive regulation of transcription, DNA-templated extracellular exosome glomerular mesangial cell development mesenchyme migration uc001kfp.1 uc001kfp.2 uc001kfp.3 uc001kfp.4 
ENST00000224949.9 PITRM1 ENST00000224949.9 pitrilysin metallopeptidase 1, transcript variant 2 (from RefSeq NM_014889.4) B3KMJ6 B4E0J8 C9JSL2 E7ES23 ENST00000224949.1 ENST00000224949.2 ENST00000224949.3 ENST00000224949.4 ENST00000224949.5 ENST00000224949.6 ENST00000224949.7 ENST00000224949.8 KIAA1104 MP1 NM_014889 O95204 PITRM1 PREP PREP_HUMAN Q2M2G6 Q4VBR1 Q5JRW7 Q5JRX3 Q7L5Z7 Q9BSI6 Q9BVJ5 Q9UPP8 uc001igt.1 uc001igt.2 uc001igt.3 uc001igt.4 The protein encoded by this gene is an ATP-dependent metalloprotease that degrades post-cleavage mitochondrial transit peptides. The encoded protein binds zinc and can also degrade amyloid beta A4 protein, suggesting a possible role in Alzheimer's disease. [provided by RefSeq, Dec 2016]. Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing (PubMed:10360838, PubMed:16849325, PubMed:19196155, PubMed:24931469). Has an ATP-independent activity (PubMed:16849325). Specifically cleaves peptides in the range of 5 to 65 residues (PubMed:19196155). Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference (PubMed:10360838, PubMed:19196155, PubMed:24931469). Degrades the transit peptides of mitochondrial proteins after their cleavage (PubMed:19196155). Also degrades other unstructured peptides (PubMed:19196155). It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion (PubMed:16849325, PubMed:24931469, PubMed:26697887). It is a highly efficient protease, at least toward amyloid-beta protein 40 (PubMed:24931469, PubMed:29764912, PubMed:29383861). Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently (PubMed:24931469). It is also able to degrade amyloid-beta protein 42 (PubMed:29764912). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Mainly exists in a closed and catalytically competent conformation but a closed-to-open switch allows substrate entry into the catalytic chamber (PubMed:24931469). Substrate binding induces closure and dimerization (PubMed:24931469). A disulfide bond may lock the enzyme in a closed conformation preventing substrate entry into the catalytic chamber, participating in redox regulation of the enzyme (Probable). Inhibited by metal-chelating agents (PubMed:10360838). Inhibited by nickel and zinc excess, and slightly activated by manganese (PubMed:19196155). Kinetic parameters: KM=1.07 uM for leumorphin ARG-ARG-GLN-PHE-LYS-VAL-VAL-THR-ARG-SER-GLN peptide (at pH 7.5) ; KM=0.5 uM for TYR-GLY-GLY-LEU-ARG-ARG-GLY-GLN peptide (at pH 7.5) ; pH dependence: Optimum pH is 7.7. ; Monomer and homodimer; homodimerization is induced by binding of the substrate. Q5JRX3-1; PRO_0000000093 [P05067]: APP; NbExp=3; IntAct=EBI-16109799, EBI-2431589; Mitochondrion Mitochondrion matrix Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q5JRX3-1; Sequence=Displayed; Name=2; IsoId=Q5JRX3-2; Sequence=VSP_020597; Name=3; IsoId=Q5JRX3-3; Sequence=VSP_046494, VSP_046495; Widely expressed. Expressed at higher level in muscle and heart compared to brain, pancreas, liver, lung and placenta. A disulfide bond locks the enzyme in the closed conformation preventing substrate entry into the catalytic chamber. Spinocerebellar ataxia, autosomal recessive, 30 (SCAR30) [MIM:619405]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR30 is a progressive disease characterized by childhood-onset global developmental delay with variably impaired intellectual development, motor dysfunction, and cerebellar ataxia. Affected individuals may also have psychiatric abnormalities. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the peptidase M16 family. PreP subfamily. Sequence=AAH01150.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=CAI39997.1; Type=Erroneous gene model prediction; Evidence=; catalytic activity metalloendopeptidase activity protein binding mitochondrion mitochondrial matrix proteolysis protein targeting to mitochondrion enzyme activator activity peptidase activity metallopeptidase activity zinc ion binding hydrolase activity positive regulation of catalytic activity metal ion binding uc001igt.1 uc001igt.2 uc001igt.3 uc001igt.4 
ENST00000224950.8 STN1 ENST00000224950.8 STN1 subunit of CST complex (from RefSeq NM_024928.5) D3DR99 ENST00000224950.1 ENST00000224950.2 ENST00000224950.3 ENST00000224950.4 ENST00000224950.5 ENST00000224950.6 ENST00000224950.7 NM_024928 OBFC1 Q5TCZ0 Q9H668 STN1 STN1_HUMAN uc001kxm.1 uc001kxm.2 uc001kxm.3 uc001kxm.4 uc001kxm.5 OBFC1 and C17ORF68 (MIM 613129) are subunits of an alpha accessory factor (AAF) that stimulates the activity of DNA polymerase-alpha-primase (see MIM 176636), the enzyme that initiates DNA replication (Casteel et al., 2009 [PubMed 19119139]). OBFC1 also appears to function in a telomere-associated complex with C17ORF68 and TEN1 (C17ORF106; MIM 613130) (Miyake et al., 2009 [PubMed 19854130]).[supplied by OMIM, Nov 2009]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.1243.1, SRR1803615.185582.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000224950.8/ ENSP00000224950.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22964711, PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097). Required for efficicient replication of the duplex region of the telomere. Promotes efficient replication of lagging-strand telomeres (PubMed:22863775, PubMed:22964711). Promotes general replication start following replication-fork stalling implicating new origin firing (PubMed:22863775). May be in involved in C-strand fill-in during late S/G2 phase independent of its role in telomere duplex replication (PubMed:23142664). Component of the CST complex, a complex that binds to single- stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. In addition to telomere protection, the CST complex has probably a more general role in DNA metabolism at non- telomeric sites. Component of the CST complex, composed of TEN1/C17orf106, CTC1/C17orf68 and STN1; in the complex interacts directly with TEN1 and CTC1. Interacts with ACD/TPP1, POT1 and POLA1. Q9H668; Q96AP0: ACD; NbExp=4; IntAct=EBI-746930, EBI-717666; Q9H668; Q9NX04: AIRIM; NbExp=5; IntAct=EBI-746930, EBI-8643161; Q9H668; Q9NWQ9: C14orf119; NbExp=4; IntAct=EBI-746930, EBI-725606; Q9H668; Q2NKJ3: CTC1; NbExp=7; IntAct=EBI-746930, EBI-2562802; Q9H668; Q2NKJ3-1: CTC1; NbExp=5; IntAct=EBI-746930, EBI-15994382; Q9H668; P42858: HTT; NbExp=3; IntAct=EBI-746930, EBI-466029; Q9H668; Q5SW96: LDLRAP1; NbExp=12; IntAct=EBI-746930, EBI-747813; Q9H668; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-746930, EBI-10274069; Q9H668; Q13064: MKRN3; NbExp=3; IntAct=EBI-746930, EBI-2340269; Q9H668; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746930, EBI-741158; Q9H668; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-746930, EBI-1504830; Q9H668; P51687: SUOX; NbExp=3; IntAct=EBI-746930, EBI-3921347; Q9H668; Q9BT92: TCHP; NbExp=3; IntAct=EBI-746930, EBI-740781; Q9H668; Q86WV5: TEN1; NbExp=11; IntAct=EBI-746930, EBI-2562799; Q9H668; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-746930, EBI-74615; Q9H668; O14773-1: TPP1; NbExp=2; IntAct=EBI-746930, EBI-15619703; Q9H668; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-746930, EBI-11059915; Q9H668; Q99757: TXN2; NbExp=3; IntAct=EBI-746930, EBI-2932492; Nucleus Chromosome, telomere Cerebroretinal microangiopathy with calcifications and cysts 2 (CRMCC2) [MIM:617341]: An autosomal recessive, multisystemic disorder characterized by intrauterine growth retardation and, later in life, premature aging symptoms, including poor growth, graying hair, liver fibrosis, portal hypertension, esophageal varices, osteopenia, pancytopenia, hypocellular bone marrow, and vascular telangiectasia resulting in gastrointestinal bleeding. Brain calcifications and white matter changes are responsible for signs including spasticity, ataxia, or dystonia observed in some patients. Note=The disease is caused by variants affecting the gene represented in this entry. Cells expressing STN1 mutants defective for dimerization with TEN1 display elongated telomeres and telomere defects associated with telomere uncapping. Belongs to the STN1 family. telomere maintenance double-strand break repair via homologous recombination chromosome, telomeric region nuclear chromosome, telomeric region fibrillar center nucleic acid binding DNA binding single-stranded DNA binding protein binding nucleus nucleoplasm DNA replication factor A complex chromosome DNA replication DNA repair nucleotide-excision repair telomere maintenance via telomere lengthening telomere capping negative regulation of telomere maintenance via telomerase site of double-strand break telomeric DNA binding single-stranded telomeric DNA binding intracellular membrane-bounded organelle intermediate filament cytoskeleton positive regulation of DNA replication CST complex uc001kxm.1 uc001kxm.2 uc001kxm.3 uc001kxm.4 uc001kxm.5 
ENST00000225171.7 DNAJC12 ENST00000225171.7 DnaJ heat shock protein family (Hsp40) member C12, transcript variant 1 (from RefSeq NM_021800.3) DJC12_HUMAN ENST00000225171.1 ENST00000225171.2 ENST00000225171.3 ENST00000225171.4 ENST00000225171.5 ENST00000225171.6 JDP1 NM_021800 Q5JVQ1 Q9UKB2 Q9UKB3 uc001jnb.1 uc001jnb.2 uc001jnb.3 uc001jnb.4 uc001jnb.5 This gene encodes a member of a subclass of the HSP40/DnaJ protein family. Members of this family of proteins are associated with complex assembly, protein folding, and export. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]. Interacts with HSPA8. [Isoform a]: Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=a; Synonyms=JDP1a; IsoId=Q9UKB3-1; Sequence=Displayed; Name=B; Synonyms=JDP1b; IsoId=Q9UKB3-2; Sequence=VSP_001295, VSP_001296; Expressed at high levels in brain, heart, and testis, and at reduced levels in kidney and stomach. Up-regulated by ER stress. Hyperphenylalaninemia, mild, non-BH4-deficient (HPANBH4) [MIM:617384]: An autosomal recessive disorder characterized by increased serum phenylalanine, normal BH4 metabolism, and highly variable neurologic defects, including movement abnormalities and intellectual disability. Note=The disease is caused by variants affecting the gene represented in this entry. protein binding cytoplasm uc001jnb.1 uc001jnb.2 uc001jnb.3 uc001jnb.4 uc001jnb.5 
ENST00000225174.8 PPIF ENST00000225174.8 peptidylprolyl isomerase F (from RefSeq NM_005729.4) CYP3 ENST00000225174.1 ENST00000225174.2 ENST00000225174.3 ENST00000225174.4 ENST00000225174.5 ENST00000225174.6 ENST00000225174.7 NM_005729 P30405 PPIF_HUMAN Q2YDB7 Q5W131 uc001kai.1 uc001kai.2 uc001kai.3 uc001kai.4 uc001kai.5 The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is part of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163658.241077.1, SRR1803613.160048.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000225174.8/ ENSP00000225174.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:26387735). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691). Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence=; Inhibited by cyclosporin A (CsA) (PubMed:20676357). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP. Associates with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase; the association is increased by inorganic phosphate (Pi) and decreased by cyclosporin A (CsA) (By similarity). Interacts with ATP5F1B; ATP5PD and ATP5PO (By similarity). Interacts with SLC25A3; the interaction is impaired by CsA (By similarity). Interacts with BCL2; the interaction is impaired by CsA (PubMed:19228691). Interacts with TP53; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by CsA (PubMed:22726440). Interacts with C1QBP (PubMed:20950273). Interacts with MCUR1 (PubMed:26976564). Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF (PubMed:26387735). Interacts with SPG7 (PubMed:26387735). P30405; Q9NYB9: ABI2; NbExp=4; IntAct=EBI-5544229, EBI-743598; P30405; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-5544229, EBI-11096309; P30405; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-5544229, EBI-11522760; P30405; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-5544229, EBI-821758; P30405; P53365: ARFIP2; NbExp=3; IntAct=EBI-5544229, EBI-638194; P30405; Q8N9N5: BANP; NbExp=3; IntAct=EBI-5544229, EBI-744695; P30405; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-5544229, EBI-7062247; P30405; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-5544229, EBI-2548702; P30405; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-5544229, EBI-14240149; P30405; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-5544229, EBI-3918971; P30405; P43364: MAGEA11; NbExp=3; IntAct=EBI-5544229, EBI-739552; P30405; P15941-11: MUC1; NbExp=3; IntAct=EBI-5544229, EBI-17263240; P30405; Q04118: PRB3; NbExp=3; IntAct=EBI-5544229, EBI-13360404; P30405; P08247: SYP; NbExp=5; IntAct=EBI-5544229, EBI-9071725; P30405; Q16563: SYPL1; NbExp=3; IntAct=EBI-5544229, EBI-2800683; P30405; P04637: TP53; NbExp=4; IntAct=EBI-5544229, EBI-366083; P30405; O95070: YIF1A; NbExp=3; IntAct=EBI-5544229, EBI-2799703; Mitochondrion matrix Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P30405-1; Sequence=Displayed; Name=2; IsoId=P30405-2; Sequence=VSP_056286; Acetylated at Lys-167; deacetylated at Lys-167 by SIRT3. Belongs to the cyclophilin-type PPIase family. protein peptidyl-prolyl isomerization response to ischemia peptidyl-prolyl cis-trans isomerase activity protein binding mitochondrion mitochondrial inner membrane mitochondrial permeability transition pore complex mitochondrial matrix protein folding apoptotic process response to oxidative stress apoptotic mitochondrial changes regulation of proton-transporting ATPase activity, rotational mechanism regulation of necrotic cell death programmed cell death cyclosporin A binding membrane isomerase activity negative regulation of ATPase activity protein refolding peptide binding regulation of apoptotic process negative regulation of apoptotic process regulation of mitochondrial membrane permeability unfolded protein binding necroptotic process cellular response to hydrogen peroxide cellular response to arsenic-containing substance cellular response to calcium ion positive regulation of release of cytochrome c from mitochondria negative regulation of release of cytochrome c from mitochondria negative regulation of oxidative phosphorylation regulation of mitochondrial membrane permeability involved in programmed necrotic cell death mitochondrial outer membrane permeabilization involved in programmed cell death negative regulation of oxidative phosphorylation uncoupler activity negative regulation of intrinsic apoptotic signaling pathway mitochondrial proton-transporting ATP synthase complex uc001kai.1 uc001kai.2 uc001kai.3 uc001kai.4 uc001kai.5 
ENST00000225235.5 TBC1D12 ENST00000225235.5 TBC1 domain family member 12 (from RefSeq NM_015188.2) ENST00000225235.1 ENST00000225235.2 ENST00000225235.3 ENST00000225235.4 KIAA0608 NM_015188 O60347 Q5VYA6 Q8WX26 Q8WX59 Q9UG83 TBC12_HUMAN uc001kjr.1 uc001kjr.2 uc001kjr.3 uc001kjr.4 RAB11A-binding protein that plays a role in neurite outgrowth. Interacts with RAB11A; this interaction recruits TBC1D12 to RAB11A-positive recycling endosomes. Endosome Sequence=BAA25534.1; Type=Erroneous initiation; Evidence=; Sequence=CAB43225.2; Type=Erroneous initiation; Evidence=; GTPase activator activity autophagosome intracellular protein transport Rab GTPase binding recycling endosome activation of GTPase activity regulation of autophagosome assembly uc001kjr.1 uc001kjr.2 uc001kjr.3 uc001kjr.4 
ENST00000225275.4 MPO ENST00000225275.4 myeloperoxidase (from RefSeq NM_000250.2) A1L4B8 ENST00000225275.1 ENST00000225275.2 ENST00000225275.3 NM_000250 P05164 PERM_HUMAN Q14862 Q4PJH5 Q9UCL7 uc002ivu.1 uc002ivu.2 Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of neutrophils. [provided by RefSeq, Nov 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M19507.1, X04876.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2149004, SAMEA2154529 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: inferred from homology MANE Ensembl match :: ENST00000225275.4/ ENSP00000225275.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity (PubMed:9922160). Mediates the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low-density lipoprotein particles and limits vascular damage (PubMed:25698971). Reaction=chloride + H(+) + H2O2 = H2O + hypochlorous acid; Xref=Rhea:RHEA:28218, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17996, ChEBI:CHEBI:24757; EC=1.11.2.2; Evidence=; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per monomer.; Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer.; Homodimer; disulfide-linked. Each monomer consists of a light and a heavy chain. P05164; P27918: CFP; NbExp=4; IntAct=EBI-2556173, EBI-9038570; P05164; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-2556173, EBI-357085; Lysosome. Event=Alternative splicing; Named isoforms=3; Name=H17; Synonyms=B; IsoId=P05164-1; Sequence=Displayed; Name=H14; IsoId=P05164-2; Sequence=VSP_007206; Name=H7; Synonyms=A; IsoId=P05164-3; Sequence=VSP_007207; Myeloperoxidase deficiency (MPOD) [MIM:254600]: A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the peroxidase family. XPO subfamily. Name=MPObase; Note=MPO mutation db; URL="http://structure.bmc.lu.se/idbase/MPObase/"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mpo/"; Name=Wikipedia; Note=Myeloperoxidase entry; URL="https://en.wikipedia.org/wiki/Myeloperoxidase"; response to yeast hypochlorous acid biosynthetic process respiratory burst involved in defense response chromatin binding peroxidase activity extracellular region extracellular space nucleus cytoplasm lysosome defense response response to oxidative stress aging heparin binding response to mechanical stimulus oxidoreductase activity removal of superoxide radicals heme binding secretory granule response to food response to lipopolysaccharide low-density lipoprotein particle remodeling azurophil granule lumen azurophil granule defense response to bacterium hydrogen peroxide catabolic process negative regulation of apoptotic process intracellular membrane-bounded organelle neutrophil degranulation cell redox homeostasis metal ion binding defense response to fungus oxidation-reduction process extracellular exosome phagocytic vesicle lumen response to gold nanoparticle uc002ivu.1 uc002ivu.2 
ENST00000225276.10 ST6GALNAC2 ENST00000225276.10 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (from RefSeq NM_006456.3) ENST00000225276.1 ENST00000225276.2 ENST00000225276.3 ENST00000225276.4 ENST00000225276.5 ENST00000225276.6 ENST00000225276.7 ENST00000225276.8 ENST00000225276.9 NM_006456 Q12971 Q9UJ37 SIA7B_HUMAN SIAT7B SIATL1 STHM uc002jsg.1 uc002jsg.2 uc002jsg.3 uc002jsg.4 uc002jsg.5 uc002jsg.6 ST6GALNAC2 belongs to a family of sialyltransferases that add sialic acids to the nonreducing ends of glycoconjugates. At the cell surface, these modifications have roles in cell-cell and cell-substrate interactions, bacterial adhesion, and protein targeting (Samyn-Petit et al., 2000 [PubMed 10742600]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803616.255230.1, SRR1660809.201916.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2162841 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225276.10/ ENSP00000225276.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins (PubMed:10742600, PubMed:29251719). Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage (PubMed:10742600). Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl- (1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D- galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:11136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:133470, ChEBI:CHEBI:140764; EC=2.4.3.3; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11137; Evidence=; Kinetic parameters: KM=130 uM for CMP-N-acetylneuraminate ; KM=104 uM for CMP-N-acetylneuraminate ; Protein modification; protein glycosylation. Golgi apparatus membrane ; Single- pass type II membrane protein Expressed in skeletal muscle, heart, kidney, placenta, lung and leukocytes. Aberrant O-galactosylation of IgA1 molecules plays a role in the development and progression of IgA nephropathy (IgAN). Genetic interactions of C1GALT1 and ST6GALNAC2 variants influence IgA1 O-glycosylation, disease predisposition, and disease severity, and may contribute to the polygenic nature of IgAN. Belongs to the glycosyltransferase 29 family. Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc II; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_631"; Golgi membrane alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity Golgi apparatus protein glycosylation protein O-linked glycosylation sialyltransferase activity membrane integral component of membrane O-glycan processing transferase activity transferase activity, transferring glycosyl groups protein sialylation uc002jsg.1 uc002jsg.2 uc002jsg.3 uc002jsg.4 uc002jsg.5 uc002jsg.6 
ENST00000225296.8 DHX33 ENST00000225296.8 DEAH-box helicase 33, transcript variant 1 (from RefSeq NM_020162.4) B4DHF9 DDX33 DHX33 DHX33_HUMAN ENST00000225296.1 ENST00000225296.2 ENST00000225296.3 ENST00000225296.4 ENST00000225296.5 ENST00000225296.6 ENST00000225296.7 NM_020162 Q4G149 Q5CZ73 Q9H5M9 Q9H6R0 uc002gca.1 uc002gca.2 uc002gca.3 uc002gca.4 This gene encodes a member of the DEAD box protein family. The DEAD box proteins are characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2010]. Implicated in nucleolar organization, ribosome biogenesis, protein synthesis and cytoplasmic dsRNA sensing (By similarity) (PubMed:21930779, PubMed:23871209, PubMed:26100019). Stimulates RNA polymerase I transcription of the 47S precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment (PubMed:21930779). In the cytoplasm, promotes elongation-competent 80S ribosome assembly at the late stage of mRNA translation initiation (PubMed:26100019). Senses cytosolic dsRNA mediating NLRP3 inflammasome formation in macrophages and type I interferon production in myeloid dendritic cells (PubMed:23871209). Required for NLRP3 activation induced by viral dsRNA and bacterial RNA (PubMed:23871209). In dendritic cells, required for induction of type I interferon production induced by cytoplasmic dsRNA via the activation of MAPK and NF-kappa-B signaling pathways (By similarity). Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Interacts with UBTF (PubMed:21930779). Interacts with DDX3X, EIF3G and EIF3H; the interaction is independent of RNA (PubMed:26100019). Interacts (via HA2 region and Helicase C-terminal domain) with the components of the large ribosomal subunit RPL3, RPL7, RPL26 and RPL27 (PubMed:26100019). Interacts (via DEAH box) with NLRP3 (via NACHT domain) (PubMed:23871209). Binds to mRNA (PubMed:26100019). Binds to double-stranded RNA (via the helicase C-terminal domain) (PubMed:23871209). Interacts (via the helicase C-terminal domain) with MAVS (By similarity). Nucleus, nucleolus cleus, nucleoplasm Cytoplasm cleus Inflammasome Note=Predominantly in the nucleolus. During mitosis, localizes with the nucleolar organizing regions (PubMed:21930779). Upon dsRNA-binding, localizes in the inflammasome (PubMed:23871209). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H6R0-1; Sequence=Displayed; Name=2; IsoId=Q9H6R0-2; Sequence=VSP_016256; Ubiquitinated, leading to its degradation by the proteasome. Deubiquitinated by USP36. Belongs to the DEAD box helicase family. DEAH subfamily. Sequence=AAH30017.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleotide binding rDNA binding nucleic acid binding RNA binding RNA helicase activity double-stranded RNA binding mRNA binding helicase activity protein binding ATP binding nucleus nucleoplasm nucleolus cytoplasm translational initiation hydrolase activity positive regulation of type I interferon production activating transcription factor binding ribosomal large subunit binding positive regulation of MAPK cascade positive regulation of transcription from RNA polymerase I promoter positive regulation of NF-kappaB transcription factor activity inflammasome complex NLRP3 inflammasome complex positive regulation of NLRP3 inflammasome complex assembly uc002gca.1 uc002gca.2 uc002gca.3 uc002gca.4 
ENST00000225298.12 UTP18 ENST00000225298.12 UTP18 small subunit processome component (from RefSeq NM_016001.3) CDABP0061 CGI-48 ENST00000225298.1 ENST00000225298.10 ENST00000225298.11 ENST00000225298.2 ENST00000225298.3 ENST00000225298.4 ENST00000225298.5 ENST00000225298.6 ENST00000225298.7 ENST00000225298.8 ENST00000225298.9 NM_016001 Q9H4N6 Q9Y5J1 UTP18 UTP18_HUMAN WDR50 uc002its.1 uc002its.2 uc002its.3 uc002its.4 uc002its.5 Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre- rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre- ribosomal RNA by the RNA exosome. Involved in nucleolar processing of pre-18S ribosomal RNA. Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. Nucleus, nucleolus Belongs to the WD repeat UTP18 family. Sequence=AAD34043.1; Type=Frameshift; Evidence=; Sequence=AAG01999.1; Type=Erroneous initiation; Evidence=; RNA binding nucleus nucleoplasm nucleolus rRNA processing nuclear membrane small-subunit processome Pwp2p-containing subcomplex of 90S preribosome uc002its.1 uc002its.2 uc002its.3 uc002its.4 uc002its.5 
ENST00000225328.10 P2RX5 ENST00000225328.10 purinergic receptor P2X 5, transcript variant 1 (from RefSeq NM_002561.4) ENST00000225328.1 ENST00000225328.2 ENST00000225328.3 ENST00000225328.4 ENST00000225328.5 ENST00000225328.6 ENST00000225328.7 ENST00000225328.8 ENST00000225328.9 G5E981 NM_002561 O43450 O75540 P2RX5_HUMAN P2X5 Q308M5 Q59F38 Q8IXW4 Q93086 Q93087 Q9NZV0 uc002fwi.1 uc002fwi.2 uc002fwi.3 uc002fwi.4 uc002fwi.5 The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream gene, TAX1BP3 (Tax1 binding protein 3). [provided by RefSeq, Mar 2011]. Receptor for ATP that acts as a ligand-gated ion channel. Functional P2XRs are organized as homomeric and heteromeric trimers. Membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q93086-3; Sequence=Displayed; Name=2; Synonyms=A; IsoId=Q93086-1; Sequence=VSP_035587; Name=3; Synonyms=B; IsoId=Q93086-2; Sequence=VSP_004503, VSP_035587; Name=4; IsoId=Q93086-4; Sequence=VSP_035588; Name=5; IsoId=Q93086-5; Sequence=VSP_004503; Expressed at high levels in brain and immune system. [Isoform 4]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the P2X receptor family. Sequence=AAF43106.1; Type=Erroneous gene model prediction; Evidence=; Sequence=AK307959; Type=Frameshift; Evidence=; Sequence=BAD92860.1; Type=Frameshift; Evidence=; Sequence=BC028084; Type=Frameshift; Evidence=; Name=Wikipedia; Note=P2X receptor entry; URL="https://en.wikipedia.org/wiki/P2X_receptor"; purinergic nucleotide receptor activity transmembrane signaling receptor activity extracellular ATP-gated cation channel activity ion channel activity ATP binding integral component of nuclear inner membrane cytosol plasma membrane integral component of plasma membrane ion transport signal transduction nervous system development blood coagulation positive regulation of calcium ion transport into cytosol membrane integral component of membrane response to ATP purinergic nucleotide receptor signaling pathway positive regulation of calcium-mediated signaling excitatory postsynaptic potential cation transmembrane transport postsynapse uc002fwi.1 uc002fwi.2 uc002fwi.3 uc002fwi.4 uc002fwi.5 
ENST00000225371.6 EPX ENST00000225371.6 eosinophil peroxidase (from RefSeq NM_000502.6) ENST00000225371.1 ENST00000225371.2 ENST00000225371.3 ENST00000225371.4 ENST00000225371.5 EPER EPO EPP NM_000502 P11678 PERE_HUMAN Q4TVP3 uc002ivq.1 uc002ivq.2 uc002ivq.3 uc002ivq.4 uc002ivq.5 This gene is a member of the peroxidase gene family and is expressed in eosinophils. The encoded preproprotein is proteolytically processed into covalently attached heavy and light chains to form the mature enzyme, which functions as an oxidant. The enzyme is released at sites of parasitic infection or allergen stimulation to mediate lysis of protozoa or parasitic worms. The gene is found in a gene cluster with other peroxidase genes on chromosome 17. Mutations in this gene result in eosinophil peroxidase deficiency. [provided by RefSeq, Feb 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## RNAseq introns :: single sample supports all introns SAMEA2149004, SAMEA2153307 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225371.6/ ENSP00000225371.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis. Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Note=Binds 1 Ca(2+) ion per heterodimer. Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) covalently through ester linkages to hydroxylated methyl groups formed auto-catalytically with hydrogen peroxide at the heme C-1 and C-5 positions. The ester linkage to Asp-232 was observed in 30% of the chains.; Tetramer of two light chains and two heavy chains. Cytoplasmic granule. Note=Cytoplasmic granules of eosinophils. Eosinophil peroxidase deficiency (EPXD) [MIM:261500]: A rare abnormality without clinical symptoms characterized by decreased or absent peroxidase activity and decreased volume of the granule matrix in eosinophils. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the peroxidase family. XPO subfamily. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/epx/"; defense response to nematode peroxidase activity extracellular region extracellular space cytoplasm defense response response to oxidative stress oxidoreductase activity heme binding negative regulation of interleukin-10 production negative regulation of interleukin-5 production positive regulation of interleukin-4 production secretory granule lumen defense response to bacterium hydrogen peroxide catabolic process neutrophil degranulation metal ion binding oxidation-reduction process extracellular exosome eosinophil migration cellular oxidant detoxification uc002ivq.1 uc002ivq.2 uc002ivq.3 uc002ivq.4 uc002ivq.5 
ENST00000225387.8 CRYBA1 ENST00000225387.8 crystallin beta A1 (from RefSeq NM_005208.5) CRBA1_HUMAN CRYB1 CRYBA1 ENST00000225387.1 ENST00000225387.2 ENST00000225387.3 ENST00000225387.4 ENST00000225387.5 ENST00000225387.6 ENST00000225387.7 NM_005208 P05813 Q13633 Q14CM9 uc002hdw.1 uc002hdw.2 uc002hdw.3 uc002hdw.4 uc002hdw.5 Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: EB361356.1, EB361468.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression ##RefSeq-Attributes-END## Crystallins are the dominant structural components of the vertebrate eye lens. Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). Interacts with CRYBA1 (PubMed:28083894). P05813; Q03989: ARID5A; NbExp=3; IntAct=EBI-7043337, EBI-948603; P05813; Q9H503-2: BANF2; NbExp=3; IntAct=EBI-7043337, EBI-11977289; P05813; Q96J87-2: CELF6; NbExp=3; IntAct=EBI-7043337, EBI-12832044; P05813; Q8TCT0: CERK; NbExp=3; IntAct=EBI-7043337, EBI-10274247; P05813; Q9Y6H1: CHCHD2; NbExp=3; IntAct=EBI-7043337, EBI-2321769; P05813; P02511: CRYAB; NbExp=2; IntAct=EBI-7043337, EBI-739060; P05813; P53674: CRYBB1; NbExp=9; IntAct=EBI-7043337, EBI-7519424; P05813; P43320: CRYBB2; NbExp=3; IntAct=EBI-7043337, EBI-974082; P05813; P26998: CRYBB3; NbExp=6; IntAct=EBI-7043337, EBI-1965681; P05813; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7043337, EBI-3867333; P05813; O75593: FOXH1; NbExp=3; IntAct=EBI-7043337, EBI-1759806; P05813; P31273: HOXC8; NbExp=3; IntAct=EBI-7043337, EBI-1752118; P05813; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-7043337, EBI-1052037; P05813; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-7043337, EBI-11953846; P05813; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-7043337, EBI-10241252; P05813; Q14847-2: LASP1; NbExp=3; IntAct=EBI-7043337, EBI-9088686; P05813; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-7043337, EBI-12025760; P05813; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-7043337, EBI-742388; P05813; O75360: PROP1; NbExp=3; IntAct=EBI-7043337, EBI-9027467; P05813; Q93062: RBPMS; NbExp=3; IntAct=EBI-7043337, EBI-740322; P05813; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-7043337, EBI-372094; P05813; Q08AM6: VAC14; NbExp=3; IntAct=EBI-7043337, EBI-2107455; Event=Alternative initiation; Named isoforms=2; Name=A3; IsoId=P05813-1; Sequence=Displayed; Name=A1; IsoId=P05813-2; Sequence=VSP_018710; Has a two-domain beta-structure, folded into four very similar Greek key motifs. Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility. S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental. [Beta-crystallin A3]: Mass=25192; Mass_error=3; Method=Electrospray; Evidence=; [Beta-crystallin A3]: Mass=25192; Method=Electrospray; Evidence=; [Beta-crystallin A3, isoform A1, Delta4 form]: Mass=22646; Method=Electrospray; Evidence=; [Beta-crystallin A3, isoform A1, Delta7 form]: Mass=22351; Method=Electrospray; Evidence=; [Beta-crystallin A3, isoform A1, Delta8 form]: Mass=22294; Method=Electrospray; Evidence=; Cataract 10, multiple types (CTRCT10) [MIM:600881]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT10 includes congenital zonular with sutural opacities, among others. This is a form of zonular cataract with an erect Y-shaped anterior and an inverted Y-shaped posterior sutural opacities. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the beta/gamma-crystallin family. Name=Eye disease Crystallin, beta-A1 (CRYBA1); Note=Leiden Open Variation Database (LOVD); URL="https://databases.lovd.nl/shared/genes/CRYBA1"; negative regulation of cytokine production lens development in camera-type eye molecular_function structural constituent of eye lens protein binding nucleus cytoplasm visual perception negative regulation of phosphatidylinositol 3-kinase signaling negative regulation of TOR signaling negative regulation of protein kinase B signaling negative regulation of ERK1 and ERK2 cascade positive regulation of anoikis uc002hdw.1 uc002hdw.2 uc002hdw.3 uc002hdw.4 uc002hdw.5 
ENST00000225388.9 NUFIP2 ENST00000225388.9 nuclear FMR1 interacting protein 2 (from RefSeq NM_020772.3) A1L3A6 A1L3A7 ENST00000225388.1 ENST00000225388.2 ENST00000225388.3 ENST00000225388.4 ENST00000225388.5 ENST00000225388.6 ENST00000225388.7 ENST00000225388.8 KIAA1321 NM_020772 NUFIP2 NUFP2_HUMAN PIG1 Q7Z417 Q9P2M5 uc002hdy.1 uc002hdy.2 uc002hdy.3 uc002hdy.4 uc002hdy.5 uc002hdy.6 Binds RNA. Interacts with FMR1 (via N-terminus). Interacts with DDX6 (PubMed:26184334). Q7Z417; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1210753, EBI-10173507; Q7Z417; A2BDD9: AMOT; NbExp=3; IntAct=EBI-1210753, EBI-17286414; Q7Z417; Q66GS9: CEP135; NbExp=3; IntAct=EBI-1210753, EBI-1046993; Q7Z417; Q96MT8: CEP63; NbExp=3; IntAct=EBI-1210753, EBI-741977; Q7Z417; P49747: COMP; NbExp=3; IntAct=EBI-1210753, EBI-2531022; Q7Z417; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1210753, EBI-3867333; Q7Z417; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1210753, EBI-10976677; Q7Z417; O95967: EFEMP2; NbExp=6; IntAct=EBI-1210753, EBI-743414; Q7Z417; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-1210753, EBI-12260294; Q7Z417; Q9UBX5: FBLN5; NbExp=4; IntAct=EBI-1210753, EBI-947897; Q7Z417; Q5TD97: FHL5; NbExp=3; IntAct=EBI-1210753, EBI-750641; Q7Z417; Q06787: FMR1; NbExp=3; IntAct=EBI-1210753, EBI-366305; Q7Z417; Q9BTY2: FUCA2; NbExp=3; IntAct=EBI-1210753, EBI-9050116; Q7Z417; Q9UN86-2: G3BP2; NbExp=4; IntAct=EBI-1210753, EBI-11035716; Q7Z417; P28799: GRN; NbExp=10; IntAct=EBI-1210753, EBI-747754; Q7Z417; P42858: HTT; NbExp=6; IntAct=EBI-1210753, EBI-466029; Q7Z417; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1210753, EBI-10975473; Q7Z417; Q5T749: KPRP; NbExp=5; IntAct=EBI-1210753, EBI-10981970; Q7Z417; Q15323: KRT31; NbExp=3; IntAct=EBI-1210753, EBI-948001; Q7Z417; O76014: KRT37; NbExp=3; IntAct=EBI-1210753, EBI-1045716; Q7Z417; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1210753, EBI-11749135; Q7Z417; Q9BYS1: KRTAP1-5; NbExp=5; IntAct=EBI-1210753, EBI-11741292; Q7Z417; P60370: KRTAP10-5; NbExp=6; IntAct=EBI-1210753, EBI-10172150; Q7Z417; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-1210753, EBI-10172290; Q7Z417; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-1210753, EBI-10171774; Q7Z417; P60411: KRTAP10-9; NbExp=8; IntAct=EBI-1210753, EBI-10172052; Q7Z417; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-1210753, EBI-1052037; Q7Z417; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-1210753, EBI-11953334; Q7Z417; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-1210753, EBI-14065470; Q7Z417; Q9BYR7: KRTAP3-2; NbExp=6; IntAct=EBI-1210753, EBI-751260; Q7Z417; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-1210753, EBI-3957694; Q7Z417; Q9BYQ7: KRTAP4-1; NbExp=3; IntAct=EBI-1210753, EBI-34579671; Q7Z417; Q9BYQ6: KRTAP4-11; NbExp=6; IntAct=EBI-1210753, EBI-10302392; Q7Z417; Q9BQ66: KRTAP4-12; NbExp=8; IntAct=EBI-1210753, EBI-739863; Q7Z417; Q9BYR5: KRTAP4-2; NbExp=6; IntAct=EBI-1210753, EBI-10172511; Q7Z417; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-1210753, EBI-11958132; Q7Z417; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-1210753, EBI-11993254; Q7Z417; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-1210753, EBI-11993296; Q7Z417; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-1210753, EBI-11958178; Q7Z417; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-1210753, EBI-11974251; Q7Z417; Q6L8H1: KRTAP5-4; NbExp=3; IntAct=EBI-1210753, EBI-11963072; Q7Z417; Q6L8G9: KRTAP5-6; NbExp=6; IntAct=EBI-1210753, EBI-10250562; Q7Z417; P26371: KRTAP5-9; NbExp=5; IntAct=EBI-1210753, EBI-3958099; Q7Z417; Q9BYQ4: KRTAP9-2; NbExp=6; IntAct=EBI-1210753, EBI-1044640; Q7Z417; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-1210753, EBI-1043191; Q7Z417; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-1210753, EBI-10185730; Q7Z417; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-1210753, EBI-11958364; Q7Z417; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-1210753, EBI-10245913; Q7Z417; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-1210753, EBI-11973993; Q7Z417; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-1210753, EBI-10246750; Q7Z417; Q9UHV8: LGALS13; NbExp=3; IntAct=EBI-1210753, EBI-3957707; Q7Z417; Q99750: MDFI; NbExp=3; IntAct=EBI-1210753, EBI-724076; Q7Z417; A6BM72: MEGF11; NbExp=3; IntAct=EBI-1210753, EBI-947743; Q7Z417; P07196: NEFL; NbExp=3; IntAct=EBI-1210753, EBI-475646; Q7Z417; Q99435: NELL2; NbExp=2; IntAct=EBI-1210753, EBI-946274; Q7Z417; Q5BJF6: ODF2; NbExp=3; IntAct=EBI-1210753, EBI-8744243; Q7Z417; Q92824: PCSK5; NbExp=3; IntAct=EBI-1210753, EBI-751290; Q7Z417; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-1210753, EBI-11956269; Q7Z417; Q5VY43: PEAR1; NbExp=3; IntAct=EBI-1210753, EBI-1249608; Q7Z417; O15162: PLSCR1; NbExp=2; IntAct=EBI-1210753, EBI-740019; Q7Z417; P30044: PRDX5; NbExp=3; IntAct=EBI-1210753, EBI-722161; Q7Z417; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-1210753, EBI-3918154; Q7Z417; P49795: RGS19; NbExp=3; IntAct=EBI-1210753, EBI-874907; Q7Z417; O76081-6: RGS20; NbExp=3; IntAct=EBI-1210753, EBI-10178530; Q7Z417; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1210753, EBI-5235340; Q7Z417; Q13077: TRAF1; NbExp=3; IntAct=EBI-1210753, EBI-359224; Q7Z417; O76024: WFS1; NbExp=3; IntAct=EBI-1210753, EBI-720609; Nucleus toplasm toplasm, Stress granule Note=Distribution is cell cycle- modulated, being cytoplasmic in the G2/M phase and accumulating in nucleus during the G1 phase (PubMed:12837692). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q7Z417-1; Sequence=Displayed; Name=2; IsoId=Q7Z417-2; Sequence=VSP_056177; Sequence=BAA92559.1; Type=Erroneous initiation; Evidence=; RNA binding protein binding nucleus nucleoplasm cytoplasm cytosol cytoplasmic stress granule membrane nuclear body polysomal ribosome uc002hdy.1 uc002hdy.2 uc002hdy.3 uc002hdy.4 uc002hdy.5 uc002hdy.6 
ENST00000225394.8 GIT1 ENST00000225394.8 GIT ArfGAP 1, transcript variant 2 (from RefSeq NM_014030.4) B4DGU9 B4DSV3 ENST00000225394.1 ENST00000225394.2 ENST00000225394.3 ENST00000225394.4 ENST00000225394.5 ENST00000225394.6 ENST00000225394.7 GIT1_HUMAN NM_014030 Q86SS0 Q9BRJ4 Q9Y2X7 uc002hef.1 uc002hef.2 uc002hef.3 uc002hef.4 GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). Forms homodimers and possibly oligomers (By similarity). May forms heterooligomers with GIT2 (By similarity). Interacts with G protein-coupled receptor kinases, including GRK2, GRK3, GRK5 and GRK6 (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA4 (By similarity). Interacts with GRIP1 and forms a ternary complex with PPFIA1 and GRIP1 (By similarity). Directly interacts with ARHGEF7/beta- PIX, forming in vitro a heptameric complex made of a GIT1 dimer and an ARHGEF7 trimer (PubMed:10896954, PubMed:27012601). Directly interacts with PXN/paxillin; this interaction is enhanced in the presence of ARHGEF7 (PubMed:10896954, PubMed:10938112, PubMed:27012601). Directly interacts (via C-terminus) with TGFB1I1/Hic-5 (via LD motif 3) (PubMed:12153727). Directly interacts with PTK2/FAK1 (By similarity). May interact with PTK2B/PYK2; this interaction may be indirect (By similarity). Interacts with AMPA receptors GRIA2/3 (By similarity). Directly interacts with protein Piccolo/PCLO (By similarity). Forms a complex with Ephrin-B1/EFNB1 and NCK2/GRB4 (via SH2); this interaction is important for spine morphogenesis and synapse formation. Interaction with NCK2 is transient and depends upon GIT1 phosphorylation at Tyr-383 (By similarity). Interacts with GRIN3A/GluN3A (via C-terminus); this interaction competes with GIT1 interaction with ARHGEF7 and limits synaptic localization of GIT1 (By similarity). Interacts with IKBKG/NEMO in resting bone mesenchymal stem cells, as well as in TNF- stimulated cells; this interaction may increase IKBKG affinity for 'Lys-63'-linked polyubiquitin chains (PubMed:31502302). Interacts with GABA(A) receptors, including GABRB3 and GABRG2 (By similarity). Interacts with SCRIB (PubMed:15182672, PubMed:19041750). Interacts (via N- and C-terminus) with ENTR1/SDCCAG3 (via N-terminus); this interaction is direct (PubMed:23108400). May form a tripartite complex with ENTR1 and PTPN13 (PubMed:23108400). Interacts with YWHAZ (By similarity). Interacts with PAK1 (PubMed:27012601). Interacts with PAK3 (PubMed:10896954). Directly interacts (via N-terminus) with gamma- tubulin (PubMed:27012601). Interacts with MAPK1 and MAPK3; this interaction is required for MAPK1/3 recruitment to focal adhesions (By similarity). Q9Y2X7; Q14155: ARHGEF7; NbExp=4; IntAct=EBI-466061, EBI-717515; Q9Y2X7; Q99728: BARD1; NbExp=2; IntAct=EBI-466061, EBI-473181; Q9Y2X7; Q9P2H0: CEP126; NbExp=2; IntAct=EBI-466061, EBI-473176; Q9Y2X7; Q12873: CHD3; NbExp=2; IntAct=EBI-466061, EBI-523590; Q9Y2X7; P62993: GRB2; NbExp=4; IntAct=EBI-466061, EBI-401755; Q9Y2X7; P25098: GRK2; NbExp=5; IntAct=EBI-466061, EBI-3904795; Q9Y2X7; P42858: HTT; NbExp=10; IntAct=EBI-466061, EBI-466029; Q9Y2X7; Q5T3J3: LRIF1; NbExp=2; IntAct=EBI-466061, EBI-473196; Q9Y2X7; Q13153: PAK1; NbExp=5; IntAct=EBI-466061, EBI-1307; Q9Y2X7; P49023: PXN; NbExp=3; IntAct=EBI-466061, EBI-702209; Q9Y2X7; P49024: PXN; Xeno; NbExp=3; IntAct=EBI-466061, EBI-2896280; Cytoplasm Synapse Presynapse Postsynapse Postsynaptic density Cell junction, focal adhesion ll projection, lamellipodium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome toplasm, cytoskeleton, spindle pole Note=Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytosolic complexes, containing at least PXN/paxillin, ARHGEF7 and PAK1, and membrane protrusions. During cell migration, moves from the disassembling adhesions into the cytosol and towards the leading edge. In adherent cells, localizes to adhesions. Recruitment to adhesions may be mediated by RAC and active tyrosine-phosphorylated PXN (PubMed:11896197). May be present in both excitatory and inhibitory synapses. In hippocampal neurons, recruitment of GIT1 to synapses is regulated by ephrinB activation and ephrinB downstream effector GRB4/NCK2. In hippocampal neurons, partially colocalizes with PCLO (By similarity). Interaction with GRIN3A limits GIT1 synaptic localization (By similarity). Localization to the centrosome does not depend upon the presence of gamma-tubulin (PubMed:27012601). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9Y2X7-1; Sequence=Displayed; Name=2; IsoId=Q9Y2X7-2; Sequence=VSP_009666, VSP_009667; Name=3; IsoId=Q9Y2X7-3; Sequence=VSP_040984; Up-regulated at the transcriptional level by MYC. The coiled coil region mediates dimerization. Phosphorylated by PAK1 (PubMed:27012601). Phosphorylation on tyrosine residues may be catalyzed by PTK2/FAK1 and SRC in growing fibroblasts. Phosphorylation at Tyr-383 is induced by activation of Ephrin-B1/EFNB1 and catalyzed by SRC family kinases. It is required for the interaction with NCK2 and for GIT1 recruitment to synapses in hippocampal neurons (By similarity). Sequence=AAH48196.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; GTPase activator activity protein binding cytoplasm cytosol focal adhesion regulation of G-protein coupled receptor protein signaling pathway membrane regulation of cytokinesis positive regulation of GTPase activity calyx of Held macromolecular complex binding metal ion binding ephrin receptor signaling pathway regulation of synaptic vesicle exocytosis uc002hef.1 uc002hef.2 uc002hef.3 uc002hef.4 
ENST00000225430.9 RPL19 ENST00000225430.9 ribosomal protein L19, transcript variant 1 (from RefSeq NM_000981.4) B2R4K2 ENST00000225430.1 ENST00000225430.2 ENST00000225430.3 ENST00000225430.4 ENST00000225430.5 ENST00000225430.6 ENST00000225430.7 ENST00000225430.8 NM_000981 P14118 P22908 P84098 Q502Y6 Q7Z6E4 RL19_HUMAN uc002hrq.1 uc002hrq.2 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L19E family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC095445.1, SRR5189664.134613.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225430.9/ ENSP00000225430.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:32669547). Component of the large ribosomal subunit. P84098; P54253: ATXN1; NbExp=3; IntAct=EBI-916524, EBI-930964; P84098; P42858: HTT; NbExp=6; IntAct=EBI-916524, EBI-466029; P84098; P54274: TERF1; NbExp=2; IntAct=EBI-916524, EBI-710997; Cytoplasm Citrullinated by PADI4. Belongs to the eukaryotic ribosomal protein eL19 family. Sequence=CAD97677.1; Type=Erroneous initiation; Evidence=; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay cytoplasmic translation RNA binding structural constituent of ribosome protein binding cytosol ribosome focal adhesion translation translational initiation SRP-dependent cotranslational protein targeting to membrane membrane viral transcription cytosolic large ribosomal subunit polysomal ribosome synapse uc002hrq.1 uc002hrq.2 
ENST00000225504.8 SUPT4H1 ENST00000225504.8 SPT4 homolog, DSIF elongation factor subunit, transcript variant 2 (from RefSeq NR_073470.2) B2R4X8 D3DTZ4 ENST00000225504.1 ENST00000225504.2 ENST00000225504.3 ENST00000225504.4 ENST00000225504.5 ENST00000225504.6 ENST00000225504.7 NR_073470 P63272 Q16550 Q62387 Q6ZP89 SPT4H SPT4H_HUMAN SUPT4H uc002iwe.1 uc002iwe.2 uc002iwe.3 uc002iwe.4 This gene encodes the small subunit of DRB (5,6-dichloro-1-beta-d-ribofuranosylbenzimidazole) sensitivity-inducing factor (DSIF) complex, which regulates mRNA processing and transcription elongation by RNA polymerase II. The encoded protein is localized to the nucleus and interacts with the large subunit (SUPT5H) to form the DSIF complex. Related pseudogenes have been identified on chromosomes 2 and 12. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Nov 2012]. Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. Interacts with SUPT5H to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of NELFA, NELFB, NELFD and NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. DSIF also interacts with PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1. P63272; O00267: SUPT5H; NbExp=15; IntAct=EBI-727250, EBI-710464; Nucleus Widely expressed. Belongs to the SPT4 family. negative regulation of transcription from RNA polymerase II promoter RNA polymerase II core binding transcription factor activity, sequence-specific DNA binding single-stranded RNA binding protein binding nucleus nucleoplasm chromatin organization chromatin remodeling regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter transcription from RNA polymerase II promoter transcription elongation from RNA polymerase II promoter zinc ion binding DSIF complex negative regulation of DNA-templated transcription, elongation positive regulation of DNA-templated transcription, elongation negative regulation of transcription elongation from RNA polymerase II promoter positive regulation of transcription from RNA polymerase II promoter metal ion binding protein heterodimerization activity positive regulation of viral transcription uc002iwe.1 uc002iwe.2 uc002iwe.3 uc002iwe.4 
ENST00000225512.6 WNT3 ENST00000225512.6 Wnt family member 3 (from RefSeq NM_030753.5) ENST00000225512.1 ENST00000225512.2 ENST00000225512.3 ENST00000225512.4 ENST00000225512.5 INT4 NM_030753 P56703 Q2M237 Q9H1J9 WNT3_HUMAN uc002ikv.1 uc002ikv.2 uc002ikv.3 uc002ikv.4 The WNT gene family consists of structurally related genes which encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It encodes a protein which shows 98% amino acid identity to mouse Wnt3 protein, and 84% to human WNT3A protein, another WNT gene product. The mouse studies show the requirement of Wnt3 in primary axis formation in the mouse. Studies of the gene expression suggest that this gene may play a key role in some cases of human breast, rectal, lung, and gastric cancer through activation of the WNT-beta-catenin-TCF signaling pathway. This gene is clustered with WNT15, another family member, in the chromosome 17q21 region. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC114219.1, SRR1803616.121826.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1970526, SAMEA2145893 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225512.6/ ENSP00000225512.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (PubMed:26902720). Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis. Required for normal formation of the apical ectodermal ridge (By similarity). Required for normal embryonic development, and especially for limb development (PubMed:14872406). Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity (PubMed:26902720). The complex with AFM may represent the physiological form in body fluids (PubMed:26902720).Interacts with PORCN. Interacts with WLS (By similarity). P56703; P43652: AFM; NbExp=3; IntAct=EBI-3644922, EBI-20737924; P56703; O75084: FZD7; NbExp=3; IntAct=EBI-3644922, EBI-746917; P56703; Q61091: Fzd8; Xeno; NbExp=2; IntAct=EBI-3644922, EBI-6171689; Secreted, extracellular space, extracellular matrix Secreted Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. Tetraamelia syndrome 1 (TETAMS1) [MIM:273395]: A form of tetraamelia, a rare disease characterized by rudimentary appendages or complete absence of all four limbs, and other anomalies such as craniofacial, nervous system, pulmonary, skeletal and urogenital defects. TETAMS1 patients manifest complete limb agenesis without defects of scapulae or clavicles. Other features include bilateral cleft lip/palate, diaphragmatic defect with bilobar right lung, renal and adrenal agenesis, pelvic hypoplasia, and urogenital defects. TETAMS1 transmission pattern is consistent with autosomal recessive inheritance. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the Wnt family. cell morphogenesis mesoderm formation receptor binding frizzled binding protein binding extracellular region extracellular space cytoplasm endoplasmic reticulum lumen Golgi lumen plasma membrane multicellular organism development gamete generation axon guidance anterior/posterior axis specification dorsal/ventral axis specification anterior/posterior pattern specification positive regulation of gene expression Wnt signaling pathway protein domain specific binding positive regulation of Wnt signaling pathway neuron differentiation endocytic vesicle membrane extracellular matrix embryonic forelimb morphogenesis embryonic hindlimb morphogenesis canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation canonical Wnt signaling pathway involved in osteoblast differentiation cell fate commitment receptor agonist activity anatomical structure formation involved in morphogenesis positive regulation of collateral sprouting in absence of injury negative regulation of axon extension involved in axon guidance regulation of neurogenesis Spemann organizer formation at the anterior end of the primitive streak canonical Wnt signaling pathway limb development limb bud formation head morphogenesis mammary gland epithelium development extracellular exosome cellular response to retinoic acid stem cell proliferation canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation canonical Wnt signaling pathway involved in stem cell proliferation Wnt signalosome uc002ikv.1 uc002ikv.2 uc002ikv.3 uc002ikv.4 
ENST00000225519.5 SHPK ENST00000225519.5 sedoheptulokinase (from RefSeq NM_013276.4) B2R640 CARKL ENST00000225519.1 ENST00000225519.2 ENST00000225519.3 ENST00000225519.4 NM_013276 Q8WUH3 Q9UHJ6 SHPK SHPK_HUMAN uc002fvz.1 uc002fvz.2 uc002fvz.3 The protein encoded by this gene has weak homology to several carbohydrate kinases, a class of proteins involved in the phosphorylation of sugars as they enter a cell, inhibiting return across the cell membrane. Sequence variation between this novel gene and known carbohydrate kinases suggests the possibility of a different substrate, cofactor or changes in kinetic properties distinguishing it from other carbohydrate kinases. The gene resides in a region commonly deleted in cystinosis patients, suggesting a role as a modifier for the cystinosis phenotype. The genomic region is also rich in Alu repetitive sequences, frequently involved in chromosomal rearrangements. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AF163573.1, BC020543.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225519.5/ ENSP00000225519.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as a modulator of macrophage activation through control of glucose metabolism. Reaction=ATP + sedoheptulose = ADP + D-sedoheptulose 7-phosphate + H(+); Xref=Rhea:RHEA:23844, ChEBI:CHEBI:15378, ChEBI:CHEBI:16802, ChEBI:CHEBI:30616, ChEBI:CHEBI:57483, ChEBI:CHEBI:456216; EC=2.7.1.14; Evidence=; Kinetic parameters: KM=0.06 mM for sedoheptulose ; pH dependence: Optimum pH is 8.5. ; Cytoplasm Strongly expressed in liver, kidney and pancreas. Expressed at lower levels in placenta and heart. Very weakly expressed in lung and brain. Down-regulated by LPS. Sedoheptulokinase deficiency (SHPKD) [MIM:617213]: An autosomal recessive metabolic disease characterized by increased urinary erythritol and sedoheptulose. Neonatal cholestasis, hypoglycemia, anemia, congenital arthrogryposis multiplex, multiple contractures and dysmorphisms have been reported in SHPKD patients, but the relationship of these features to the SHPKD is unclear. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the FGGY kinase family. nucleotide binding ATP binding cytoplasm cytosol carbohydrate metabolic process pentose-phosphate shunt pentose-phosphate shunt, non-oxidative branch kinase activity phosphorylation transferase activity phosphotransferase activity, alcohol group as acceptor cellular response to interleukin-13 regulation of macrophage activation sedoheptulokinase activity regulation of inflammatory response cellular response to lipopolysaccharide cellular response to interleukin-4 uc002fvz.1 uc002fvz.2 uc002fvz.3 
ENST00000225525.4 TAX1BP3 ENST00000225525.4 Tax1 binding protein 3, transcript variant 1 (from RefSeq NM_014604.4) B2RD53 D3DTJ6 ENST00000225525.1 ENST00000225525.2 ENST00000225525.3 NM_014604 O14907 Q7LCQ4 TAX1BP3 TIP1 TX1B3_HUMAN uc002fwc.1 uc002fwc.2 uc002fwc.3 uc002fwc.4 uc002fwc.5 This gene encodes a small, highly conserved protein with a single PDZ domain. PDZ (PSD-95/Discs large/ZO-1 homologous) domains promote protein-protein interactions that affect cell signaling, adhesion, protein scaffolding, and receptor and ion transporter functions. The encoded protein interacts with a large number of target proteins that play roles in signaling pathways; for example, it interacts with Rho A and glutaminase L and also acts as a negative regulator of the Wnt/beta-catenin signaling pathway. This protein was first identified as binding to the T-cell leukaemia virus (HTLV1) Tax oncoprotein. Overexpression of this gene has been implicated in altered cancer cell adhesion, migration and metastasis. The encoded protein also modulates the localization and density of inwardly rectifying potassium channel 2.3 (Kir2.3). To date, this protein has been shown to play a role in cell proliferation, development, stress response, and polarization. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Apr 2017]. May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6. Interacts (via its PDZ domain) with GLS2. Interacts (via its PDZ domain) with RTKN (via the C-terminal region); this interaction facilitates Rho-mediated activation of the FOS serum response element (SRE). Interacts (via its PDZ domain) with CTNNB1; this interaction inhibits the transcriptional activity of CTNNB1. Interacts with HTLV-1 TAX protein. Interacts (via PDZ domain) with ARHGEF16. Interacts (via PDZ domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4 binding. Interacts with ADGRB2 (PubMed:21787750). O14907; Q96D59: RNF183; NbExp=3; IntAct=EBI-723259, EBI-743938; O14907; P03126: E6; Xeno; NbExp=2; IntAct=EBI-723259, EBI-1177242; Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Recruited to the cell membrane by interaction with membrane proteins. Ubiquitous. Detected in brain, heart, kidney, lung, small intestine and skeletal muscle. Detected in various cell lines including HeLa. Weakly expressed in peripheral blood leukocytes. Sequence=AAF43104.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; fibrillar center protein binding nucleus cytoplasm cytosol plasma membrane Rho protein signal transduction beta-catenin binding protein C-terminus binding negative regulation of cell proliferation actin cytoskeleton membrane Wnt signaling pathway negative regulation of Wnt signaling pathway intracellular membrane-bounded organelle extracellular exosome activation of GTPase activity negative regulation of protein localization to cell surface uc002fwc.1 uc002fwc.2 uc002fwc.3 uc002fwc.4 uc002fwc.5 
ENST00000225538.4 P2RX1 ENST00000225538.4 purinergic receptor P2X 1 (from RefSeq NM_002558.4) ENST00000225538.1 ENST00000225538.2 ENST00000225538.3 NM_002558 P2RX1_HUMAN P2X1 P51575 Q9UK84 uc002fww.1 uc002fww.2 uc002fww.3 uc002fww.4 uc002fww.5 The protein encoded by this gene belongs to the P2X family of G-protein-coupled receptors. These proteins can form homo-and heterotimers and function as ATP-gated ion channels and mediate rapid and selective permeability to cations. This protein is primarily localized to smooth muscle where binds ATP and mediates synaptic transmission between neurons and from neurons to smooth muscle and may being responsible for sympathetic vasoconstriction in small arteries, arterioles and vas deferens. Mouse studies suggest that this receptor is essential for normal male reproductive function. This protein may also be involved in promoting apoptosis. [provided by RefSeq, Jun 2013]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC044657.1, U45448.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2147975, SAMEA2159764 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225538.4/ ENSP00000225538.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity). Homo- or heteropolymers. P51575; Q9BQA9: CYBC1; NbExp=5; IntAct=EBI-11599725, EBI-2680384; Membrane; Multi-pass membrane protein. Belongs to the P2X receptor family. Name=Wikipedia; Note=P2X receptor entry; URL="https://en.wikipedia.org/wiki/P2X_receptor"; Name=Wikipedia; Note=P2RX1 entry; URL="https://en.wikipedia.org/wiki/P2RX1"; purinergic nucleotide receptor activity serotonin secretion by platelet regulation of vascular smooth muscle contraction extracellular ATP-gated cation channel activity ion channel activity cation channel activity ATP binding integral component of nuclear inner membrane plasma membrane integral component of plasma membrane ion transport apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process regulation of smooth muscle contraction signal transduction insemination blood coagulation drug binding regulation of blood pressure zinc ion binding external side of plasma membrane response to organic substance membrane integral component of membrane neuronal action potential regulation of vasoconstriction platelet activation secretory granule membrane macromolecular complex response to ATP synaptic transmission, glutamatergic specific granule membrane purinergic nucleotide receptor signaling pathway neuron projection positive regulation of ion transport neutrophil degranulation membrane raft postsynaptic membrane ceramide biosynthetic process protein homooligomerization protein heterooligomerization regulation of calcium ion transport excitatory postsynaptic potential cation transmembrane transport glutamatergic synapse integral component of postsynaptic membrane integral component of presynaptic active zone membrane regulation of presynaptic cytosolic calcium ion concentration regulation of synaptic vesicle exocytosis uc002fww.1 uc002fww.2 uc002fww.3 uc002fww.4 uc002fww.5 
ENST00000225550.4 KRT37 ENST00000225550.4 keratin 37 (from RefSeq NM_003770.5) ENST00000225550.1 ENST00000225550.2 ENST00000225550.3 HHA7 HKA7 KRT37_HUMAN KRTHA7 NM_003770 O76014 uc002hwp.1 uc002hwp.2 uc002hwp.3 The protein encoded by this gene is a member of the keratin gene family. As a type I hair keratin, it is an acidic protein which heterodimerizes with type II keratins to form hair and nails. The type I hair keratins are clustered in a region of chromosome 17q12-q21 and have the same direction of transcription. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AJ786655.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA2155974 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225550.4/ ENSP00000225550.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## O76014; P21549: AGXT; NbExp=3; IntAct=EBI-1045716, EBI-727098; O76014; P29972: AQP1; NbExp=3; IntAct=EBI-1045716, EBI-745213; O76014; O75934: BCAS2; NbExp=3; IntAct=EBI-1045716, EBI-1050106; O76014; Q13515: BFSP2; NbExp=3; IntAct=EBI-1045716, EBI-10229433; O76014; Q0VAL7: C21orf58; NbExp=3; IntAct=EBI-1045716, EBI-10226774; O76014; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-1045716, EBI-10181422; O76014; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-1045716, EBI-11980535; O76014; P27658: COL8A1; NbExp=3; IntAct=EBI-1045716, EBI-747133; O76014; P17661: DES; NbExp=3; IntAct=EBI-1045716, EBI-1055572; O76014; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-1045716, EBI-1752811; O76014; Q969U6: FBXW5; NbExp=3; IntAct=EBI-1045716, EBI-741068; O76014; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-1045716, EBI-11427343; O76014; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-1045716, EBI-11956675; O76014; O14964: HGS; NbExp=3; IntAct=EBI-1045716, EBI-740220; O76014; P49639: HOXA1; NbExp=3; IntAct=EBI-1045716, EBI-740785; O76014; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-1045716, EBI-12056251; O76014; P04264: KRT1; NbExp=3; IntAct=EBI-1045716, EBI-298429; O76014; P12035: KRT3; NbExp=3; IntAct=EBI-1045716, EBI-2430095; O76014; P19013: KRT4; NbExp=3; IntAct=EBI-1045716, EBI-2371606; O76014; P04259: KRT6B; NbExp=3; IntAct=EBI-1045716, EBI-740907; O76014; P48668: KRT6C; NbExp=3; IntAct=EBI-1045716, EBI-2564105; O76014; Q3SY84: KRT71; NbExp=3; IntAct=EBI-1045716, EBI-2952676; O76014; Q7RTS7: KRT74; NbExp=7; IntAct=EBI-1045716, EBI-968660; O76014; O95678: KRT75; NbExp=3; IntAct=EBI-1045716, EBI-2949715; O76014; Q01546: KRT76; NbExp=3; IntAct=EBI-1045716, EBI-2952745; O76014; Q14533: KRT81; NbExp=5; IntAct=EBI-1045716, EBI-739648; O76014; P78385: KRT83; NbExp=3; IntAct=EBI-1045716, EBI-10221390; O76014; P78386: KRT85; NbExp=5; IntAct=EBI-1045716, EBI-1049371; O76014; O43790: KRT86; NbExp=3; IntAct=EBI-1045716, EBI-9996498; O76014; Q9BT17: MTG1; NbExp=3; IntAct=EBI-1045716, EBI-2602570; O76014; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-1045716, EBI-1210753; O76014; O43482: OIP5; NbExp=3; IntAct=EBI-1045716, EBI-536879; O76014; P32242: OTX1; NbExp=3; IntAct=EBI-1045716, EBI-740446; O76014; Q13526: PIN1; NbExp=3; IntAct=EBI-1045716, EBI-714158; O76014; Q16512: PKN1; NbExp=3; IntAct=EBI-1045716, EBI-602382; O76014; P25786: PSMA1; NbExp=3; IntAct=EBI-1045716, EBI-359352; O76014; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-1045716, EBI-358489; O76014; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-1045716, EBI-455078; O76014; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-1045716, EBI-12018146; O76014; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-1045716, EBI-6116822; O76014; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1045716, EBI-739895; There are two types of hair/microfibrillar keratin, I (acidic) and II (neutral to basic). Belongs to the intermediate filament family. structural molecule activity cytosol intermediate filament keratinization extracellular exosome cornification uc002hwp.1 uc002hwp.2 uc002hwp.3 
ENST00000225577.9 RPS6KB1 ENST00000225577.9 ribosomal protein S6 kinase B1, transcript variant 23 (from RefSeq NR_161462.1) B2R779 B4DLT4 B4DTG1 E7ESB8 ENST00000225577.1 ENST00000225577.2 ENST00000225577.3 ENST00000225577.4 ENST00000225577.5 ENST00000225577.6 ENST00000225577.7 ENST00000225577.8 F6UYM1 KS6B1_HUMAN NR_161462 P23443 Q7Z721 STK14A uc002ixy.1 uc002ixy.2 uc002ixy.3 uc002ixy.4 uc002ixy.5 uc002ixy.6 This gene encodes a member of the ribosomal S6 kinase family of serine/threonine kinases. The encoded protein responds to mTOR (mammalian target of rapamycin) signaling to promote protein synthesis, cell growth, and cell proliferation. Activity of this gene has been associated with human cancer. Alternatively spliced transcript variants have been observed. The use of alternative translation start sites results in isoforms with longer or shorter N-termini which may differ in their subcellular localizations. There are two pseudogenes for this gene on chromosome 17. [provided by RefSeq, Jan 2013]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803616.170503.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142853, SAMEA2144120 [ECO:0000348] ##Evidence-Data-END## Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:23429703, PubMed:28178239, PubMed:22017876). Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:23429703, PubMed:28178239, PubMed:22017876). Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex (PubMed:16286006). Upon mitogenic stimulation, phosphorylation by the mechanistic target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation (PubMed:16286006). The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B (PubMed:16286006). Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis (PubMed:17053147). Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR (PubMed:15341740). In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2 (PubMed:11500364). Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling (PubMed:19720745, PubMed:19935711, PubMed:19995915). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed:22017876). Mediates cell survival by phosphorylating the pro- apoptotic protein BAD and suppressing its pro-apoptotic function (By similarity). Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex (PubMed:17936702). The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function (PubMed:17936702). Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1 (PubMed:18952604). In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B (PubMed:17052453). May be involved in cytoskeletal rearrangement through binding to neurabin (By similarity). Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (PubMed:23429703). Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition (PubMed:28178239). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence= Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence= Activation requires multiple phosphorylation events on serine/threonine residues. Activation appears to be first mediated by phosphorylation of multiple sites in the autoinhibitory domain, which facilitates phosphorylation at Thr-412, disrupting the autoinhibitory mechanism and allowing phosphorylation of Thr-252 by PDPK1. The active conformation of the kinase is believed to be stabilized by a mechanism involving three conserved phosphorylation sites located in the kinase domain activation loop (Thr-252) and in the AGC-kinase C-terminal domain (Ser-394 in the middle of the tail/linker region and Thr-412 within a hydrophobic motif at its end). Activated by mTORC1; isoform Alpha I and isoform Alpha II are sensitive to rapamycin, which inhibits activating phosphorylation at Thr-412. Activated by PDPK1. Interacts with PPP1R9A/neurabin-1 (By similarity). Interacts with RPTOR (PubMed:12150926). Interacts with IRS1 (PubMed:18952604). Interacts with EIF3B and EIF3C (PubMed:16286006). Interacts with TRAF4 (PubMed:12801526). Interacts with POLDIP3 (PubMed:15341740). Interacts (via N-terminus) with IER5 (PubMed:26496226). P23443; Q06481-5: APLP2; NbExp=3; IntAct=EBI-1775921, EBI-25646567; P23443; P55884: EIF3B; NbExp=3; IntAct=EBI-1775921, EBI-366696; P23443; P08151: GLI1; NbExp=4; IntAct=EBI-1775921, EBI-308084; P23443; Q5VY09: IER5; NbExp=2; IntAct=EBI-1775921, EBI-1774000; P23443; Q00005: PPP2R2B; NbExp=2; IntAct=EBI-1775921, EBI-1052159; P23443; P13051-2: UNG; NbExp=3; IntAct=EBI-1775921, EBI-25834258; P23443-2; P08151: GLI1; NbExp=2; IntAct=EBI-6093204, EBI-308084; P23443-4; P05067: APP; NbExp=3; IntAct=EBI-25882353, EBI-77613; P23443-4; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-25882353, EBI-9090282; Synapse, synaptosome Mitochondrion outer membrane. Mitochondrion. Note=Colocalizes with URI1 at mitochondrion. [Isoform Alpha I]: Nucleus. Cytoplasm. [Isoform Alpha II]: Cytoplasm. Event=Alternative splicing, Alternative initiation; Named isoforms=5; Comment=Additional isoforms seem to exist.; Name=Alpha I; Synonyms=p80-S6K 1; IsoId=P23443-1; Sequence=Displayed; Name=Alpha II; IsoId=P23443-2; Sequence=VSP_018839; Name=2; IsoId=P23443-3; Sequence=VSP_054613; Name=4; IsoId=P23443-5; Sequence=VSP_055026; Name=3; IsoId=P23443-4; Sequence=VSP_054614; Widely expressed. The autoinhibitory domain is believed to block phosphorylation within the AGC-kinase C-terminal domain and the activation loop. The TOS (TOR signaling) motif is essential for activation by mTORC1. Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism (PubMed:29236692, PubMed:18925875, PubMed:19085255, PubMed:22017876, PubMed:23429703). Activated by phosphorylation at Thr-252 by PDPK1 (PubMed:9445476, PubMed:19864428). Dephosphorylation by PPP1CC at Thr-412 in mitochondrion (PubMed:17936702). Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily. G1/S transition of mitotic cell cycle nucleotide binding protein kinase activity protein serine/threonine kinase activity ribosomal protein S6 kinase activity protein serine/threonine/tyrosine kinase activity protein binding ATP binding nucleus nucleoplasm cytoplasm mitochondrion mitochondrial outer membrane cytosol regulation of translation protein phosphorylation apoptotic process cell cycle signal transduction membrane kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation cell junction response to nutrient levels TOR signaling cellular response to insulin stimulus intracellular signal transduction neuron projection negative regulation of apoptotic process long-chain fatty acid import synapse positive regulation of translation positive regulation of mitotic cell cycle positive regulation of translational initiation negative regulation of insulin receptor signaling pathway phosphatidylinositol-mediated signaling cellular response to growth factor stimulus uc002ixy.1 uc002ixy.2 uc002ixy.3 uc002ixy.4 uc002ixy.5 uc002ixy.6 
ENST00000225603.9 CBX1 ENST00000225603.9 chromobox 1, transcript variant 2 (from RefSeq NM_001127228.2) CBX1 ENST00000225603.1 ENST00000225603.2 ENST00000225603.3 ENST00000225603.4 ENST00000225603.5 ENST00000225603.6 ENST00000225603.7 ENST00000225603.8 NM_001127228 Q6IBN6 Q6IBN6_HUMAN hCG_2000655 uc002ine.1 uc002ine.2 uc002ine.3 uc002ine.4 uc002ine.5 This gene encodes a highly conserved nonhistone protein, which is a member of the heterochromatin protein family . The protein is enriched in the heterochromatin and associated with centromeres. The protein has a single N-terminal chromodomain which can bind to histone proteins via methylated lysine residues, and a C-terminal chromo shadow-domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated nonhistone proteins. The protein may play an important role in the epigenetic control of chromatin structure and gene expression. Several related pseudogenes are located on chromosomes 1, 3, and X. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jul 2008]. chromatin female pronucleus male pronucleus nucleus pericentric heterochromatin chromocenter identical protein binding protein homodimerization activity negative regulation of transcription, DNA-templated uc002ine.1 uc002ine.2 uc002ine.3 uc002ine.4 uc002ine.5 
ENST00000225609.10 PIGL ENST00000225609.10 phosphatidylinositol glycan anchor biosynthesis class L, transcript variant 1 (from RefSeq NM_004278.4) A8KA67 B4DYN4 ENST00000225609.1 ENST00000225609.2 ENST00000225609.3 ENST00000225609.4 ENST00000225609.5 ENST00000225609.6 ENST00000225609.7 ENST00000225609.8 ENST00000225609.9 NM_004278 PIGL PIGL_HUMAN Q9Y2B2 uc002gpv.1 uc002gpv.2 uc002gpv.3 uc002gpv.4 uc002gpv.5 This gene encodes an enzyme that catalyzes the second step of glycosylphosphatidylinositol (GPI) biosynthesis, which is the de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI). Study of a similar rat enzyme suggests that this protein localizes to the endoplasmic reticulum. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AK292932.1, SRR1660809.72037.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1968189 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225609.10/ ENSP00000225609.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Catalyzes the second step of glycosylphosphatidylinositol (GPI) biosynthesis, which is the de-N-acetylation of N- acetylglucosaminyl-phosphatidylinositol. Reaction=a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo- inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn- glycero-3-phospho)-1D-myo-inositol; Xref=Rhea:RHEA:11660, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57265, ChEBI:CHEBI:57997; EC=3.5.1.89; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11661; Evidence=; Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. Endoplasmic reticulum membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y2B2-1; Sequence=Displayed; Name=2; IsoId=Q9Y2B2-2; Sequence=VSP_056886; Retained in the ER by two retention signals, one located in cytoplasmic domain, and a second signal in transmembrane domain that is functional in the presence of membrane proximal residues of the cytoplasmic tail. Coloboma, congenital heart disease, ichthyosiform dermatosis, impaired intellectual development, and ear anomalies syndrome (CHIME) [MIM:280000]: An extremely rare autosomal recessive multisystem disorder clinically characterized by colobomas, congenital heart defects, migratory ichthyosiform dermatosis, intellectual disability, and ear anomalies including conductive hearing loss. Other clinical features include distinctive facial features, abnormal growth, genitourinary abnormalities, seizures, and feeding difficulties. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the PIGL family. N-acetylglucosaminylphosphatidylinositol deacetylase activity endoplasmic reticulum endoplasmic reticulum membrane GPI anchor biosynthetic process membrane integral component of membrane preassembly of GPI anchor in ER membrane hydrolase activity uc002gpv.1 uc002gpv.2 uc002gpv.3 uc002gpv.4 uc002gpv.5 
ENST00000225648.4 HOXB6 ENST00000225648.4 homeobox B6, transcript variant 1 (from RefSeq NM_018952.5) A8K835 D3DTV5 ENST00000225648.1 ENST00000225648.2 ENST00000225648.3 HOX2B HXB6_HUMAN NM_018952 P09068 P17509 Q9HB11 Q9UGH2 uc002ins.1 uc002ins.2 uc002ins.3 This gene is a member of the Antp homeobox family and encodes a protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded protein functions as a sequence-specific transcription factor that is involved in development, including that of lung and skin, and has been localized to both the nucleus and cytoplasm. Altered expression of this gene or a change in the subcellular localization of its protein is associated with some cases of acute myeloid leukemia and colorectal cancer. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC014651.1, BG332853.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2144335 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225648.4/ ENSP00000225648.3 RefSeq Select criteria :: based on conservation ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. P17509; P49761: CLK3; NbExp=6; IntAct=EBI-741308, EBI-745579; P17509; P13807: GYS1; NbExp=3; IntAct=EBI-741308, EBI-740553; P17509; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-741308, EBI-11750983; P17509; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-741308, EBI-741158; P17509; P78362: SRPK2; NbExp=3; IntAct=EBI-741308, EBI-593303; P17509; Q96M29: TEKT5; NbExp=3; IntAct=EBI-741308, EBI-10239812; Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P17509-1; Sequence=Displayed; Name=2; Synonyms=Homeobox-less; IsoId=P17509-2; Sequence=VSP_002388, VSP_002389; Belongs to the Antp homeobox family. nuclear chromatin RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding RNA binding protein binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development anterior/posterior pattern specification erythrocyte homeostasis sequence-specific DNA binding embryonic skeletal system morphogenesis embryonic skeletal system development uc002ins.1 uc002ins.2 uc002ins.3 
ENST00000225655.6 PFN1 ENST00000225655.6 profilin 1, transcript variant 2 (from RefSeq NM_005022.4) ENST00000225655.1 ENST00000225655.2 ENST00000225655.3 ENST00000225655.4 ENST00000225655.5 NM_005022 P07737 PROF1_HUMAN Q53Y44 uc002gaa.1 uc002gaa.2 uc002gaa.3 uc002gaa.4 uc002gaa.5 uc002gaa.6 This gene encodes a member of the profilin family of small actin-binding proteins. The encoded protein plays an important role in actin dynamics by regulating actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome, and the encoded protein may also play a role in Huntington disease. Multiple pseudogenes of this gene are located on chromosome 1. [provided by RefSeq, Jul 2012]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189658.11029.1, SRR1163657.160382.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225655.6/ ENSP00000225655.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR. Found in a complex with XPO6, Ran, ACTB and PFN1 (PubMed:14592989). Interacts with VASP (PubMed:17914456, PubMed:18689676). Interacts with HTT (PubMed:18573880). Interacts with SH3BGRL (PubMed:34331014). Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio (PubMed:17914456, PubMed:18689676). Interacts with ACTMAP (PubMed:36173861). P07737; P60709: ACTB; NbExp=2; IntAct=EBI-713780, EBI-353944; P07737; Q92558: WASF1; NbExp=2; IntAct=EBI-713780, EBI-1548747; P07737; P07830: act21; Xeno; NbExp=3; IntAct=EBI-713780, EBI-7195234; P07737; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-713780, EBI-367540; P07737; O08816: Wasl; Xeno; NbExp=4; IntAct=EBI-713780, EBI-6142604; Cytoplasm, cytoskeleton. Expressed in epididymis (at protein level). Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation. Amyotrophic lateral sclerosis 18 (ALS18) [MIM:614808]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the profilin family. adenyl-nucleotide exchange factor activity neural tube closure RNA binding actin binding actin monomer binding protein binding phosphatidylinositol-4,5-bisphosphate binding nucleus cytoplasm cytosol cytoskeleton focal adhesion cell cortex regulation of transcription from RNA polymerase II promoter positive regulation of epithelial cell migration membrane Rho GTPase binding actin cytoskeleton organization regulation of actin filament polymerization negative regulation of actin filament polymerization positive regulation of actin filament polymerization negative regulation of actin filament bundle assembly positive regulation of actin filament bundle assembly positive regulation of ATPase activity cadherin binding protein stabilization negative regulation of stress fiber assembly Wnt signaling pathway, planar cell polarity pathway synapse maturation extracellular exosome proline-rich region binding blood microparticle modification of postsynaptic actin cytoskeleton glutamatergic synapse positive regulation of ruffle assembly uc002gaa.1 uc002gaa.2 uc002gaa.3 uc002gaa.4 uc002gaa.5 uc002gaa.6 
ENST00000225665.12 SLC25A11 ENST00000225665.12 solute carrier family 25 member 11, transcript variant 1 (from RefSeq NM_003562.5) ENST00000225665.1 ENST00000225665.10 ENST00000225665.11 ENST00000225665.2 ENST00000225665.3 ENST00000225665.4 ENST00000225665.5 ENST00000225665.6 ENST00000225665.7 ENST00000225665.8 ENST00000225665.9 NM_003562 Q6IBH0 Q6IBH0_HUMAN SLC25A11 hCG_32694 uc002fzo.1 uc002fzo.2 uc002fzo.3 uc002fzo.4 The oxoglutarate/malate carrier transports 2-oxoglutarate across the inner membranes of mitochondria in an electroneutral exchange for malate or other dicarboxylic acids (summary by Iacobazzi et al., 1992 [PubMed 1457818]).[supplied by OMIM, Jan 2011]. Reaction=(S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2- oxoglutarate(in); Xref=Rhea:RHEA:71587, ChEBI:CHEBI:15589, ChEBI:CHEBI:16810; Evidence=; Reaction=2-oxoglutarate(out) + maleate(in) = 2-oxoglutarate(in) + maleate(out); Xref=Rhea:RHEA:71599, ChEBI:CHEBI:16810, ChEBI:CHEBI:30780; Evidence=; Reaction=2-oxoglutarate(out) + malonate(in) = 2-oxoglutarate(in) + malonate(out); Xref=Rhea:RHEA:71591, ChEBI:CHEBI:15792, ChEBI:CHEBI:16810; Evidence=; Reaction=2-oxoglutarate(out) + oxaloacetate(in) = 2-oxoglutarate(in) + oxaloacetate(out); Xref=Rhea:RHEA:71603, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810; Evidence=; Reaction=2-oxoglutarate(out) + succinate(in) = 2-oxoglutarate(in) + succinate(out); Xref=Rhea:RHEA:71595, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031; Evidence=; Membrane ; Multi- pass membrane protein Belongs to the mitochondrial carrier (TC 2.A.29) family. membrane integral component of membrane uc002fzo.1 uc002fzo.2 uc002fzo.3 uc002fzo.4 
ENST00000225688.4 RASD1 ENST00000225688.4 ras related dexamethasone induced 1, transcript variant 1 (from RefSeq NM_016084.5) AGS1 B2R709 B4DFF4 DEXRAS1 ENST00000225688.1 ENST00000225688.2 ENST00000225688.3 NM_016084 Q9NYB4 Q9Y272 RASD1_HUMAN uc002gri.1 uc002gri.2 uc002gri.3 uc002gri.4 uc002gri.5 This gene encodes a member of the Ras superfamily of small GTPases and is induced by dexamethasone. The encoded protein is an activator of G-protein signaling and acts as a direct nucleotide exchange factor for Gi-Go proteins. This protein interacts with the neuronal nitric oxide adaptor protein CAPON, and a nuclear adaptor protein FE65, which interacts with the Alzheimer's disease amyloid precursor protein. This gene may play a role in dexamethasone-induced alterations in cell morphology, growth and cell-extracellular matrix interactions. Epigenetic inactivation of this gene is closely correlated with resistance to dexamethasone in multiple myeloma cells. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Sep 2011]. Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). Forms a ternary complex with CAPON and NOS1. Component of a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts with APBB1/FE65 (By similarity). Q9Y272; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-740818, EBI-11096309; Q9Y272; P05067: APP; NbExp=3; IntAct=EBI-740818, EBI-77613; Q9Y272; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-740818, EBI-10961624; Q9Y272; Q86X02: CDR2L; NbExp=3; IntAct=EBI-740818, EBI-11063830; Q9Y272; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-740818, EBI-3867333; Q9Y272; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-740818, EBI-371922; Q9Y272; P61978: HNRNPK; NbExp=6; IntAct=EBI-740818, EBI-304185; Q9Y272; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-740818, EBI-7060731; Q9Y272; O43390-2: HNRNPR; NbExp=3; IntAct=EBI-740818, EBI-12236340; Q9Y272; O75525: KHDRBS3; NbExp=3; IntAct=EBI-740818, EBI-722504; Q9Y272; O76011: KRT34; NbExp=3; IntAct=EBI-740818, EBI-1047093; Q9Y272; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-740818, EBI-11749135; Q9Y272; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-740818, EBI-10171774; Q9Y272; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-740818, EBI-10172052; Q9Y272; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-740818, EBI-3957672; Q9Y272; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-740818, EBI-3958099; Q9Y272; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-740818, EBI-11962084; Q9Y272; P43243: MATR3; NbExp=6; IntAct=EBI-740818, EBI-352602; Q9Y272; Q99750: MDFI; NbExp=5; IntAct=EBI-740818, EBI-724076; Q9Y272; Q13064: MKRN3; NbExp=3; IntAct=EBI-740818, EBI-2340269; Q9Y272; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-740818, EBI-11522433; Q9Y272; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-740818, EBI-22310682; Q9Y272; Q9NQX1-2: PRDM5; NbExp=3; IntAct=EBI-740818, EBI-12859340; Q9Y272; Q16825: PTPN21; NbExp=3; IntAct=EBI-740818, EBI-2860264; Q9Y272; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-740818, EBI-3437896; Q9Y272; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-740818, EBI-11994018; Q9Y272; Q15415: RBMY1J; NbExp=6; IntAct=EBI-740818, EBI-8642021; Q9Y272; O94972: TRIM37; NbExp=3; IntAct=EBI-740818, EBI-741602; Q9Y272; O00308: WWP2; NbExp=3; IntAct=EBI-740818, EBI-743923; Cell membrane ; Lipid-anchor ; Cytoplasmic side Cytoplasm, perinuclear region Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y272-1; Sequence=Displayed; Name=2; IsoId=Q9Y272-2; Sequence=VSP_046431, VSP_046432; Expressed in a variety of tissues including heart, cardiovascular tissues, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, gastrointestinal and reproductive tissues. By dexamethasone. S-nitrosylation stimulates guanine-nucleotide exchange activity. Belongs to the small GTPase superfamily. RasD family. nucleotide binding GTPase activity protein binding GTP binding nucleus cytoplasm plasma membrane signal transduction G-protein coupled receptor signaling pathway nitric oxide mediated signal transduction membrane sarcoplasmic reticulum negative regulation of transcription, DNA-templated perinuclear region of cytoplasm uc002gri.1 uc002gri.2 uc002gri.3 uc002gri.4 uc002gri.5 
ENST00000225698.8 C1QBP ENST00000225698.8 complement C1q binding protein (from RefSeq NM_001212.4) C1QBP_HUMAN ENST00000225698.1 ENST00000225698.2 ENST00000225698.3 ENST00000225698.4 ENST00000225698.5 ENST00000225698.6 ENST00000225698.7 GC1QBP HABP1 NM_001212 Q07021 Q2HXR8 Q9NNY8 SF2P32 uc002gby.1 uc002gby.2 The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system. The protein encoded by this gene is known to bind to the globular heads of C1q molecules and inhibit C1 activation. This protein has also been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.675649.1, SRR1163655.239161.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN03267753, SAMN03267760 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000225698.8/ ENSP00000225698.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria (PubMed:28942965). In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex- mediated transcription. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting RIGI- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. (Microbial infection) Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA. (Microbial infection) In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B (InlB) and Staphylococcus aureus protein A. (Microbial infection) Involved in replication of Rubella virus. Homotrimer; three monomers form a donut-shaped structure with an unusually asymmetric charge distribution on the surface. Interacts with CDK13, HRK, VTN, NFYB, ADRA1B, FOXC1, DDX21, DDX50, NCL, SRSF1, SRSF9 and CDKN2A isoform smARF. Interacts with CD93; the association may represent a cell surface C1q receptor. Interacts with KRT1; the association represents a cell surface kininogen receptor. Interacts with CD209; the interaction is indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with FBL and RRP1; the respective interactions with C1QBP are competitive. Probably associates with the mitoribosome. Interacts with MAVS; the interaction occurs upon viral transfection. Interacts with PPIF. Interacts with U2AF1L4. Interacts with PLEKHN1 (PubMed:18191643). Interacts with VGF-derived peptide TLQP-21 (By similarity). Interacts with POLGARF which is produced from an alternative reading frame of the POLG gene; the interaction results in nucleolar localization of C1QBP, probably due to prevention of C1QBP maturation and redirection from mitochondria to nucleoli (PubMed:32958672). (Microbial infection) Interacts with Rubella virus capsid protein; the interaction occurs in mitochondria (PubMed:10823864, PubMed:12034482). Interacts with Rubella virus protease/methyltransferase p150 (PubMed:22238231). (Microbial infection) Interacts with Staphylococcus aureus protein A/spa. (Microbial infection) Interacts with Staphylococcus aureus protein A/spa, HIV-1 Tat and HCV core protein. (Microbial infection) Interacts with HIV-1 Tat and HCV core protein. (Microbial infection) Interacts with L.monocytogenes internalin B. (Microbial infection) Interacts with Epstein-Barr virus EBNA1. Q07021; P02647: APOA1; NbExp=2; IntAct=EBI-347528, EBI-701692; Q07021; Q14004-2: CDK13; NbExp=6; IntAct=EBI-347528, EBI-6375898; Q07021; Q8N726: CDKN2A; NbExp=3; IntAct=EBI-347528, EBI-625922; Q07021; P00748: F12; NbExp=2; IntAct=EBI-347528, EBI-6378830; Q07021; Q12948: FOXC1; NbExp=6; IntAct=EBI-347528, EBI-1175253; Q07021; O00198: HRK; NbExp=7; IntAct=EBI-347528, EBI-701322; Q07021; Q13351: KLF1; NbExp=3; IntAct=EBI-347528, EBI-8284732; Q07021; P01042: KNG1; NbExp=4; IntAct=EBI-347528, EBI-6378713; Q07021; Q7Z434: MAVS; NbExp=5; IntAct=EBI-347528, EBI-995373; Q07021; Q05513: PRKCZ; NbExp=4; IntAct=EBI-347528, EBI-295351; Q07021; Q15139: PRKD1; NbExp=9; IntAct=EBI-347528, EBI-1181072; Q07021; Q8N3Z0: PRSS35; NbExp=4; IntAct=EBI-347528, EBI-20628340; Q07021; P04004: VTN; NbExp=9; IntAct=EBI-347528, EBI-1036653; Q07021; P67809: YBX1; NbExp=11; IntAct=EBI-347528, EBI-354065; Q07021; Q64364: Cdkn2a; Xeno; NbExp=4; IntAct=EBI-347528, EBI-1202287; Q07021; PRO_0000240177 [O40955]; Xeno; NbExp=2; IntAct=EBI-347528, EBI-6383633; Q07021; PRO_0000041308 [P07566]; Xeno; NbExp=3; IntAct=EBI-347528, EBI-6377932; Q07021; PRO_0000041302 [P08563]; Xeno; NbExp=3; IntAct=EBI-347528, EBI-11478341; Q07021; PRO_0000037566 [P27958]; Xeno; NbExp=4; IntAct=EBI-347528, EBI-6377335; PRO_0000018590; P02745: C1QA; NbExp=6; IntAct=EBI-14032968, EBI-1220209; PRO_0000018590; P02746: C1QB; NbExp=4; IntAct=EBI-14032968, EBI-2813376; PRO_0000018590; P02747: C1QC; NbExp=4; IntAct=EBI-14032968, EBI-1220222; PRO_0000018590; P0DTC4: E; Xeno; NbExp=2; IntAct=EBI-14032968, EBI-25475850; PRO_0000018590; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-14032968, EBI-25474821; Mitochondrion matrix cleus Nucleus, nucleolus Cell membrane eripheral membrane protein xtracellular side. Secreted. Cytoplasm te=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes. Localizes to the nucleolus when coexpressed with POLGARF (PubMed:32958672). Interaction with POLGARF is likely to result in prevention of C1QBP maturation and redirection from mitochondria to nucleoli (PubMed:32958672). Expressed on cell surface of peripheral blood cells (at protein level); Surface expression is reported for macrophages and monocyte-derived dendritic cells. Enhanced cell surface expression upon platelet and monocyte activation. Combined oxidative phosphorylation deficiency 33 (COXPD33) [MIM:617713]: An autosomal recessive disorder caused by multiple mitochondrial respiratory chain defects and impaired mitochondrial energy metabolism. Clinical manifestations are highly variable. Affected infants present with cardiomyopathy accompanied by multisystemic features involving liver, kidney, and brain. Death in infancy is observed in some patients. Children and adults present with myopathy and progressive external ophthalmoplegia. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the MAM33 family. The subcellular location has been matter of debate. After being reported to be exclusively localized to mitochondria, demonstrations of promiscuous associations and locations were considered as artifactual due to the extremely acidic character and the use of different tagged versions of the protein (PubMed:9305894, PubMed:11493647). However, its location to multiple compartments linked to diverse functions is now accepted. The N-termini of the surface and secreted forms are identical to the reported processed mitochondrial form. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/c1qbp/"; negative regulation of transcription from RNA polymerase II promoter complement component C1q binding adaptive immune response immune system process transcription corepressor activity mRNA binding protein kinase C binding protein binding hyaluronic acid binding extracellular region extracellular space nucleus nucleolus cytoplasm mitochondrion mitochondrial matrix cytosol plasma membrane mRNA processing apoptotic process immune response complement activation, classical pathway blood coagulation, intrinsic pathway transcription factor binding RNA splicing translation activator activity cell surface phosphatidylinositol 3-kinase signaling membrane viral process regulation of complement activation kininogen binding adrenergic receptor binding negative regulation of interferon-gamma production negative regulation of interleukin-12 production negative regulation of MDA-5 signaling pathway negative regulation of RIG-I signaling pathway ribosome biogenesis mature ribosome assembly positive regulation of apoptotic process innate immune response positive regulation of cell adhesion negative regulation of mRNA splicing, via spliceosome presynaptic active zone negative regulation of defense response to virus positive regulation of protein kinase B signaling positive regulation of mitochondrial translation positive regulation of neutrophil chemotaxis mitochondrial ribosome binding presynapse glutamatergic synapse GABA-ergic synapse positive regulation of substrate adhesion-dependent cell spreading positive regulation of trophoblast cell migration positive regulation of dendritic cell chemotaxis uc002gby.1 uc002gby.2 
ENST00000225719.9 CPD ENST00000225719.9 carboxypeptidase D, transcript variant 1 (from RefSeq NM_001304.5) B7Z7T9 B7ZAU4 CBPD_HUMAN ENST00000225719.1 ENST00000225719.2 ENST00000225719.3 ENST00000225719.4 ENST00000225719.5 ENST00000225719.6 ENST00000225719.7 ENST00000225719.8 F5GZH6 NM_001304 O15377 O75976 Q86SH9 Q86XE6 uc002hfb.1 uc002hfb.2 uc002hfb.3 uc002hfb.4 The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities. The pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus-binding protein. Transcript variants utilizing alternative polyadenylation signals exist for this gene. [provided by RefSeq, Jul 2008]. Reaction=Releases C-terminal Arg and Lys from polypeptides.; EC=3.4.17.22; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 2 Zn(2+) ions per subunit. ; pH dependence: Optimum pH is 6.0-6.5.; Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75976-1; Sequence=Displayed; Name=2; IsoId=O75976-2; Sequence=VSP_045833, VSP_045834; Highly expressed in placenta, pancreas and hepatoma cells. Lower levels found in skeletal muscle, heart and colon carcinoma and melanoma cell lines. There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity. Belongs to the peptidase M14 family. carboxypeptidase activity metallocarboxypeptidase activity serine-type carboxypeptidase activity extracellular space plasma membrane proteolysis peptide metabolic process peptidase activity metallopeptidase activity zinc ion binding membrane integral component of membrane protein processing hydrolase activity metal ion binding extracellular exosome uc002hfb.1 uc002hfb.2 uc002hfb.3 uc002hfb.4 
ENST00000225726.10 CCDC47 ENST00000225726.10 coiled-coil domain containing 47 (from RefSeq NM_020198.3) B2RAS8 CCD47_HUMAN CCDC47 D3DU20 ENST00000225726.1 ENST00000225726.2 ENST00000225726.3 ENST00000225726.4 ENST00000225726.5 ENST00000225726.6 ENST00000225726.7 ENST00000225726.8 ENST00000225726.9 GK001 MSTP041 NM_020198 PSEC0077 Q96A33 Q96D00 Q96JZ7 Q9H3E4 Q9NRG3 uc002jbs.1 uc002jbs.2 uc002jbs.3 uc002jbs.4 uc002jbs.5 uc002jbs.6 Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (PubMed:32814900, PubMed:32820719, PubMed:36261522). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (PubMed:36261522). Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein (By similarity). Within the PAT subcomplex, CCDC47 occludes the lateral gate of the SEC61 complex (By similarity). Involved in the regulation of calcium ion homeostasis in the ER (PubMed:30401460). Required for proper protein degradation via the ERAD (ER-associated degradation) pathway (PubMed:25009997). Has an essential role in the maintenance of ER organization during embryogenesis (By similarity). Component of the PAT complex, composed of WDR83OS/Asterix and CCDC47 (PubMed:32814900, PubMed:36261522). The PAT complex is part of the multi-pass translocon (MPT) complex, composed of three subcomplexes, the GEL complex (composed of RAB5IF/OPTI and TMCO1), the BOS complex (composed of NCLN/Nicalin, NOMO and TMEM147) and the PAT complex (composed of WDR83OS/Asterix and CCDC47) (PubMed:32820719, PubMed:36261522). The MPT complex associates with the SEC61 complex (PubMed:32820719, PubMed:36261522). Interacts with VCP, HSPA5, DERL1, DERL2 and SELENOS (By similarity). Q96A33; Q92985: IRF7; NbExp=2; IntAct=EBI-720151, EBI-968267; Q96A33; Q92993: KAT5; NbExp=3; IntAct=EBI-720151, EBI-399080; Q96A33; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-720151, EBI-11742507; Q96A33; P17252: PRKCA; NbExp=3; IntAct=EBI-720151, EBI-1383528; Q96A33; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-720151, EBI-9090795; Q96A33; Q86WV6: STING1; NbExp=2; IntAct=EBI-720151, EBI-2800345; Q96A33; P58753: TIRAP; NbExp=2; IntAct=EBI-720151, EBI-528644; Q96A33; Q9Y284: WDR83OS; NbExp=2; IntAct=EBI-720151, EBI-6309120; Q96A33; P61981: YWHAG; NbExp=3; IntAct=EBI-720151, EBI-359832; Q96A33; Q99J34: Irak1; Xeno; NbExp=2; IntAct=EBI-720151, EBI-6117042; Q96A33; Q6PDS3: Sarm1; Xeno; NbExp=2; IntAct=EBI-720151, EBI-6117196; Endoplasmic reticulum membrane ingle-pass type I membrane protein Rough endoplasmic reticulum membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96A33-1; Sequence=Displayed; Name=2; IsoId=Q96A33-2; Sequence=VSP_018478; Trichohepatoneurodevelopmental syndrome (THNS) [MIM:618268]: An autosomal recessive complex multisystem disorder characterized by woolly or coarse hair, liver dysfunction, pruritus, dysmorphic features, hypotonia, and global developmental delay. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the CCDC47 family. Sequence=AAG39292.1; Type=Frameshift; Evidence=; osteoblast differentiation RNA binding calcium ion binding protein binding endoplasmic reticulum endoplasmic reticulum membrane rough endoplasmic reticulum ER overload response endoplasmic reticulum organization post-embryonic development membrane integral component of membrane ER-associated ubiquitin-dependent protein catabolic process rough endoplasmic reticulum membrane endoplasmic reticulum calcium ion homeostasis ERAD pathway calcium ion homeostasis uc002jbs.1 uc002jbs.2 uc002jbs.3 uc002jbs.4 uc002jbs.5 uc002jbs.6 
ENST00000225728.8 MED31 ENST00000225728.8 mediator complex subunit 31 (from RefSeq NM_016060.3) B2R4L9 CGI-125 ENST00000225728.1 ENST00000225728.2 ENST00000225728.3 ENST00000225728.4 ENST00000225728.5 ENST00000225728.6 ENST00000225728.7 MED31_HUMAN NM_016060 Q9Y3C7 SOH1 uc002gdg.1 uc002gdg.2 uc002gdg.3 uc002gdg.4 uc002gdg.5 uc002gdg.6 Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Q9Y3C7; O95257: GADD45G; NbExp=2; IntAct=EBI-394707, EBI-448202; Q9Y3C7; P42858: HTT; NbExp=9; IntAct=EBI-394707, EBI-466029; Q9Y3C7; O43513: MED7; NbExp=3; IntAct=EBI-394707, EBI-394632; Q9Y3C7; Q96HR8: NAF1; NbExp=3; IntAct=EBI-394707, EBI-2515597; Nucleus Belongs to the Mediator complex subunit 31 family. ubiquitin ligase complex transcription cofactor activity transcription coactivator activity protein binding nucleus nucleoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter transcription initiation from RNA polymerase II promoter protein ubiquitination mediator complex negative regulation of fibroblast proliferation limb development ubiquitin protein ligase activity core mediator complex positive regulation of nucleic acid-templated transcription uc002gdg.1 uc002gdg.2 uc002gdg.3 uc002gdg.4 uc002gdg.5 uc002gdg.6 
ENST00000225729.8 DRG2 ENST00000225729.8 developmentally regulated GTP binding protein 2, transcript variant 1 (from RefSeq NM_001388.5) B2R8G5 DRG2 DRG2_HUMAN ENST00000225729.1 ENST00000225729.2 ENST00000225729.3 ENST00000225729.4 ENST00000225729.5 ENST00000225729.6 ENST00000225729.7 NM_001388 P55039 Q53Y50 Q9BWB2 uc002gsh.1 uc002gsh.2 uc002gsh.3 uc002gsh.4 This gene encodes a GTP-binding protein known to function in the regulation of cell growth and differentiation. Read-through transcripts containing this gene and a downstream gene have been identified, but they are not thought to encode a fusion protein. This gene is located within the Smith-Magenis syndrome region on chromosome 17. [provided by RefSeq, Jan 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.932256.1, SRR3476690.882587.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225729.8/ ENSP00000225729.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21' by JMJD7, may bind to RNA and play a role in translation. Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Interacts with RWDD1; this interaction confers protection to polyubiquitination and proteolytic degradation (By similarity). Interacts with JMJD7; this interaction is direct (PubMed:29915238). P55039; P38919: EIF4A3; NbExp=3; IntAct=EBI-750565, EBI-299104; P55039; P0C870: JMJD7; NbExp=3; IntAct=EBI-750565, EBI-9090173; P55039; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-750565, EBI-1055254; P55039; Q15742: NAB2; NbExp=3; IntAct=EBI-750565, EBI-8641936; P55039; Q9H446: RWDD1; NbExp=8; IntAct=EBI-750565, EBI-748952; P55039; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-750565, EBI-5235340; P55039; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-750565, EBI-3918381; Nucleus Cytoplasm Highest levels in skeletal muscle, heart and kidney. Low levels in colon, thymus, spleen, small intestine, lung and Leukocytes. Hydroxylated (with S stereochemistry) at C-3 of Lys-21 by JMJD7; this modification hinders trypsin-catalyzed proteolysis in vitro. Polyubiquitinated. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. nucleotide binding cytoplasmic translation RNA binding GTPase activity protein binding GTP binding nucleus nucleoplasm cytoplasm cytosol signal transduction membrane hydrolase activity intracellular membrane-bounded organelle metal ion binding uc002gsh.1 uc002gsh.2 uc002gsh.3 uc002gsh.4 
ENST00000225737.11 AKAP10 ENST00000225737.11 A-kinase anchoring protein 10, transcript variant 1 (from RefSeq NM_007202.4) AKA10_HUMAN B2R650 ENST00000225737.1 ENST00000225737.10 ENST00000225737.2 ENST00000225737.3 ENST00000225737.4 ENST00000225737.5 ENST00000225737.6 ENST00000225737.7 ENST00000225737.8 ENST00000225737.9 NM_007202 O43572 Q96AJ7 uc002gwo.1 uc002gwo.2 uc002gwo.3 uc002gwo.4 uc002gwo.5 uc002gwo.6 This gene encodes a member of the A-kinase anchor protein family. A-kinase anchor proteins bind to the regulatory subunits of protein kinase A (PKA) and confine the holoenzyme to discrete locations within the cell. The encoded protein is localized to mitochondria and interacts with both the type I and type II regulatory subunits of PKA. Polymorphisms in this gene may be associated with increased risk of arrhythmias and sudden cardiac death. [provided by RefSeq, May 2012]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660807.256198.1, SRR1803612.244754.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000225737.11/ ENSP00000225737.6 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G- alpha proteins, providing a link between the signaling machinery and the downstream kinase (By similarity). O43572; P00514: PRKAR1A; Xeno; NbExp=2; IntAct=EBI-752153, EBI-1041635; Mitochondrion Membrane Cytoplasm Note=Predominantly mitochondrial but also membrane associated and cytoplasmic. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. protein binding cytoplasm mitochondrion cytosol plasma membrane signal transduction blood coagulation protein localization membrane macromolecular complex protein kinase A binding uc002gwo.1 uc002gwo.2 uc002gwo.3 uc002gwo.4 uc002gwo.5 uc002gwo.6 
ENST00000225740.11 ALDH3A1 ENST00000225740.11 aldehyde dehydrogenase 3 family member A1, transcript variant 2 (from RefSeq NM_000691.5) A8K828 AL3A1_HUMAN ALDH3 ENST00000225740.1 ENST00000225740.10 ENST00000225740.2 ENST00000225740.3 ENST00000225740.4 ENST00000225740.5 ENST00000225740.6 ENST00000225740.7 ENST00000225740.8 ENST00000225740.9 NM_000691 P30838 Q9BT37 uc002gwj.1 uc002gwj.2 uc002gwj.3 uc002gwj.4 uc002gwj.5 Aldehyde dehydrogenases oxidize various aldehydes to the corresponding acids. They are involved in the detoxification of alcohol-derived acetaldehyde and in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. The enzyme encoded by this gene forms a cytoplasmic homodimer that preferentially oxidizes aromatic and medium-chain (6 carbons or more) saturated and unsaturated aldehyde substrates. It is thought to promote resistance to UV and 4-hydroxy-2-nonenal-induced oxidative damage in the cornea. The gene is located within the Smith-Magenis syndrome region on chromosome 17. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Sep 2008]. ALDHs play a major role in the detoxification of alcohol- derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:1737758). Preferentially oxidizes aromatic aldehyde substrates (PubMed:1737758). Comprises about 50 percent of corneal epithelial soluble proteins (By similarity). May play a role in preventing corneal damage caused by ultraviolet light (By similarity). Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.5; Evidence= Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate; Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; Kinetic parameters: Note=Has a high Km for acetaldehyde.; Homodimer. P30838; O75344: FKBP6; NbExp=3; IntAct=EBI-3905126, EBI-744771; P30838; Q9NUX5: POT1; NbExp=2; IntAct=EBI-3905126, EBI-752420; Cytoplasm High levels in stomach, esophagus and lung; low level in the liver and kidney. Belongs to the aldehyde dehydrogenase family. response to hypoxia 3-chloroallyl aldehyde dehydrogenase activity aldehyde dehydrogenase (NAD) activity aldehyde dehydrogenase [NAD(P)+] activity protein binding extracellular space cytoplasm endoplasmic reticulum cytosol plasma membrane cellular aldehyde metabolic process xenobiotic metabolic process aging response to nutrient alcohol dehydrogenase (NADP+) activity positive regulation of cell proliferation response to organic cyclic compound integral component of membrane oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor benzaldehyde dehydrogenase (NAD+) activity response to drug response to glucocorticoid response to cAMP oxidation-reduction process uc002gwj.1 uc002gwj.2 uc002gwj.3 uc002gwj.4 uc002gwj.5 
ENST00000225777.8 SYNGR2 ENST00000225777.8 synaptogyrin 2, transcript variant 1 (from RefSeq NM_004710.7) ENST00000225777.1 ENST00000225777.2 ENST00000225777.3 ENST00000225777.4 ENST00000225777.5 ENST00000225777.6 ENST00000225777.7 NM_004710 O43760 O43762 Q3KQZ2 Q658S7 SNG2_HUMAN SYNGR2 UNQ352/PRO615 uc002juu.1 uc002juu.2 uc002juu.3 This gene encodes an integral membrane protein containing four transmembrane regions and a C-terminal cytoplasmic tail that is tyrosine phosphorylated. The exact function of this protein is unclear, but studies of a similar rat protein suggest that it may play a role in regulating membrane traffic in non-neuronal cells. The gene belongs to the synaptogyrin gene family. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. ##Evidence-Data-START## Transcript exon combination :: BC029755.1, AY358916.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane. (Microbial infection) May play a role in the assembly of cytoplasmic inclusion bodies required for SFTS phlebovirus replication. (Microbial infection) Interacts with SFTS phlebovirus protein NSs; may be involved in virus replication. O43760; Q6AZY7: SCARA3; NbExp=3; IntAct=EBI-2826419, EBI-8657660; Cytoplasmic vesicle membrane ; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Multi-pass membrane protein Note=Localizes to cytoplasmic vesicles associated with the recycling endosomes. Lipid droplet. Note=(Microbial infection) Upon SFTS phlebovirus infection, the protein localizes in lipid droplets and inclusion bodies. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43760-1; Sequence=Displayed; Name=2; IsoId=O43760-2; Sequence=VSP_056179; Ubiquitous; low expression in brain. (Microbial infection) Up-regulated upon SFTS phlebovirus infection (at protein level). May be tyrosine phosphorylated by Src. Belongs to the synaptogyrin family. protein binding lipid particle synaptic vesicle membrane integral component of membrane cell junction cytoplasmic vesicle membrane synaptic vesicle membrane cytoplasmic vesicle neuromuscular junction regulated exocytosis synapse synaptic vesicle membrane organization extracellular exosome uc002juu.1 uc002juu.2 uc002juu.3 
ENST00000225792.10 DDX5 ENST00000225792.10 DEAD-box helicase 5, transcript variant 2 (from RefSeq NM_004396.5) B4DLW8 B5BU21 D3DU32 DDX5_HUMAN E7ETL9 ENST00000225792.1 ENST00000225792.2 ENST00000225792.3 ENST00000225792.4 ENST00000225792.5 ENST00000225792.6 ENST00000225792.7 ENST00000225792.8 ENST00000225792.9 G17P1 HELR HLR1 NM_004396 O75681 P17844 Q53Y61 uc002jek.1 uc002jek.2 uc002jek.3 uc002jek.4 This gene encodes a member of the DEAD box family of RNA helicases that are involved in a variety of cellular processes as a result of its role as an adaptor molecule, promoting interactions with a large number of other factors. This protein is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. Members of this family contain nine conserved motifs, including the conserved Asp-Glu-Ala-Asp (DEAD) motif, important to ATP binding and hydrolysis as well as RNA binding and unwinding activities. Dysregulation of this gene may play a role in cancer development. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2017]. Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre- mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53- dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as a transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Identified in the spliceosome C complex (PubMed:11991638). Component of a ribonucleoprotein complex containing mRNAs and RNA- binding proteins including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF (PubMed:24644279). Interacts with RBM4; the interaction occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. Interacts with ESR1, AR, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with DDX17. Interacts with BRDT. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts with DHX36; this interaction occurs in a RNA- dependent manner (PubMed:18279852). Interacts with NUPR1 (By similarity). Interacts with ERCC6 (PubMed:26030138). Interacts with DDX3X in the cytoplasm; this interaction may be more efficient when both proteins are unphosphorylated (PubMed:22034099). P17844; Q12873: CHD3; NbExp=4; IntAct=EBI-351962, EBI-523590; P17844; Q92841: DDX17; NbExp=3; IntAct=EBI-351962, EBI-746012; P17844; Q9NRR4: DROSHA; NbExp=6; IntAct=EBI-351962, EBI-528367; P17844; Q09472: EP300; NbExp=4; IntAct=EBI-351962, EBI-447295; P17844; Q01780: EXOSC10; NbExp=3; IntAct=EBI-351962, EBI-358236; P17844; P22087: FBL; NbExp=6; IntAct=EBI-351962, EBI-358318; P17844; Q13547: HDAC1; NbExp=4; IntAct=EBI-351962, EBI-301834; P17844; O95983: MBD3; NbExp=4; IntAct=EBI-351962, EBI-1783068; P17844; O94916: NFAT5; NbExp=4; IntAct=EBI-351962, EBI-308320; P17844; P24928: POLR2A; NbExp=3; IntAct=EBI-351962, EBI-295301; P17844; Q15637: SF1; NbExp=3; IntAct=EBI-351962, EBI-744603; P17844; Q15797: SMAD1; NbExp=4; IntAct=EBI-351962, EBI-1567153; P17844; P84022: SMAD3; NbExp=2; IntAct=EBI-351962, EBI-347161; P17844; Q99717: SMAD5; NbExp=3; IntAct=EBI-351962, EBI-6391136; P17844; Q13148: TARDBP; NbExp=3; IntAct=EBI-351962, EBI-372899; P17844; P04637: TP53; NbExp=6; IntAct=EBI-351962, EBI-366083; P17844; P04637-1: TP53; NbExp=2; IntAct=EBI-351962, EBI-3895849; P17844; P04637-7: TP53; NbExp=2; IntAct=EBI-351962, EBI-3895873; P17844; P45481: Crebbp; Xeno; NbExp=3; IntAct=EBI-351962, EBI-296306; P17844; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-351962, EBI-1185167; P17844; P10085: Myod1; Xeno; NbExp=3; IntAct=EBI-351962, EBI-4405734; P17844; Q1K9H5: PB1; Xeno; NbExp=2; IntAct=EBI-351962, EBI-6050669; P17844; P04618: rev; Xeno; NbExp=2; IntAct=EBI-351962, EBI-6164309; P17844; Q08775-3: Runx2; Xeno; NbExp=2; IntAct=EBI-351962, EBI-6119991; P17844; PRO_0000037577 [P27958]; Xeno; NbExp=12; IntAct=EBI-351962, EBI-6904388; P17844; PRO_0000308465 [P29991]; Xeno; NbExp=3; IntAct=EBI-351962, EBI-8826747; Nucleus Nucleus, nucleolus Nucleus speckle Cytoplasm Note=During the G0 phase, predominantly located in the nucleus. Cytoplasmic levels increase during the G1/S phase. During the M phase, located at the vicinity of the condensed chromosomes. At G1, localizes in the cytoplasm. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P17844-1; Sequence=Displayed; Name=2; IsoId=P17844-2; Sequence=VSP_056154; Arg-502 is dimethylated, probably to asymmetric dimethylarginine. Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination. Polyubiquitinated, leading to proteasomal degradation. Weakly phosphorylated in the G1/S phase of the cell cycle and much more at G2/M, especially at Thr and Tyr residues. Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily. DDX5 was reported to be a transcriptional coactivator of ESR1. However, this study has been retracted due to concerns of image manipulation. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40290/DDX5"; negative regulation of transcription from RNA polymerase II promoter nucleotide binding alternative mRNA splicing, via spliceosome regulation of alternative mRNA splicing, via spliceosome mRNA splicing, via spliceosome nuclear-transcribed mRNA catabolic process epithelial to mesenchymal transition nucleic acid binding RNA binding RNA helicase activity mRNA 3'-UTR binding helicase activity protein binding calmodulin binding ATP binding nucleus nucleoplasm spliceosomal complex nucleolus cytoplasm regulation of transcription from RNA polymerase II promoter mRNA processing RNA splicing mRNA transcription membrane hydrolase activity enzyme binding BMP signaling pathway intracellular estrogen receptor signaling pathway androgen receptor signaling pathway MH2 domain binding pre-mRNA binding ribonucleoprotein complex binding positive regulation of DNA damage response, signal transduction by p53 class mediator regulation of viral genome replication myoblast differentiation regulation of osteoblast differentiation SMAD binding calcium-dependent protein binding rhythmic process androgen receptor binding regulation of androgen receptor signaling pathway pri-miRNA transcription from RNA polymerase II promoter extracellular exosome R-SMAD binding primary miRNA binding catalytic step 2 spliceosome intrinsic apoptotic signaling pathway by p53 class mediator positive regulation of production of miRNAs involved in gene silencing by miRNA promoter-specific chromatin binding ribonucleoprotein complex regulation of skeletal muscle cell differentiation regulation of pri-miRNA transcription from RNA polymerase II promoter uc002jek.1 uc002jek.2 uc002jek.3 uc002jek.4 
ENST00000225823.7 ASIC2 ENST00000225823.7 acid sensing ion channel subunit 2, transcript variant MDEG2 (from RefSeq NM_183377.2) ACCN ACCN1 ASIC2_HUMAN BNAC1 E9PBX2 ENST00000225823.1 ENST00000225823.2 ENST00000225823.3 ENST00000225823.4 ENST00000225823.5 ENST00000225823.6 MDEG NM_183377 Q13553 Q16515 Q6DJU1 Q8N3E2 uc002hht.1 uc002hht.2 uc002hht.3 uc002hht.4 uc002hht.5 This gene encodes a member of the degenerin/epithelial sodium channel (DEG/ENaC) superfamily. The members of this family are amiloride-sensitive sodium channels that contain intracellular N and C termini, 2 hydrophobic transmembrane regions, and a large extracellular loop, which has many cysteine residues with conserved spacing. The member encoded by this gene may play a role in neurotransmission. In addition, a heteromeric association between this member and acid-sensing (proton-gated) ion channel 3 has been observed to co-assemble into proton-gated channels sensitive to gadolinium. Alternative splicing has been observed at this locus and two variants, encoding distinct isoforms, have been identified. [provided by RefSeq, Feb 2012]. Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Heteromeric channel assembly seems to modulate. Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with STOM; this regulates channel activity (By similarity). Interacts with PRKCABP and ASIC3. Heterotrimer of Asic1a- Asic2a interacts with the snake venom mambalgin-1 (PubMed:23034652). Heterotrimer of Asic1a-Asic2a interacts with the snake venom mambalgin- 2 and mambalgin-3 (By similarity). Heterotrimer of Asic1a-Asic2b interacts with the snake venom mambalgin-1 and mambalgin-2 (By similarity). Q16515; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-79149, EBI-79165; Cell membrane ; Multi-pass membrane protein Note=Localized at the plasma membrane of neurons, in the soma and punctated peripheral processes. Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Asic2a ; IsoId=Q16515-1; Sequence=Displayed; Name=2; Synonyms=Asic2b, MDEG2; IsoId=Q16515-2; Sequence=VSP_015590, VSP_015591; Brain and spinal cord. Isoform 1 is also detected in testis, liver, colon and ovary. Inhibited by anti-inflammatory drugs like salicylic acid (By similarity). Regulated by Zn(2+). Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC2 subfamily. regulation of systemic arterial blood pressure by aortic arch baroreceptor feedback ion channel activity cation channel activity sodium channel activity protein binding plasma membrane integral component of plasma membrane ion transport cation transport sodium ion transport chemical synaptic transmission central nervous system development peripheral nervous system development phototransduction sensory perception of sound response to mechanical stimulus response to acidic pH ligand-gated sodium channel activity monovalent inorganic cation transport membrane integral component of membrane regulation of vasoconstriction ion gated channel activity ion transmembrane transport regulation of ion transmembrane transport protein localization to synapse sodium ion transmembrane transport regulation of membrane potential neuron projection neuronal cell body negative regulation of apoptotic process dendritic spine synapse sensory perception of sour taste detection of mechanical stimulus involved in sensory perception positive regulation of synapse assembly cation transmembrane transport uc002hht.1 uc002hht.2 uc002hht.3 uc002hht.4 uc002hht.5 
ENST00000225831.4 CCL2 ENST00000225831.4 C-C motif chemokine ligand 2 (from RefSeq NM_002982.4) B2R4V3 CCL2_HUMAN ENST00000225831.1 ENST00000225831.2 ENST00000225831.3 MCP1 NM_002982 P13500 Q9UDF3 SCYA2 uc002hhy.1 uc002hhy.2 uc002hhy.3 uc002hhy.4 This gene is one of several cytokine genes clustered on the q-arm of chromosome 17. Chemokines are a superfamily of secreted proteins involved in immunoregulatory and inflammatory processes. The superfamily is divided into four subfamilies based on the arrangement of N-terminal cysteine residues of the mature peptide. This chemokine is a member of the CC subfamily which is characterized by two adjacent cysteine residues. This cytokine displays chemotactic activity for monocytes and basophils but not for neutrophils or eosinophils. It has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis and atherosclerosis. It binds to chemokine receptors CCR2 and CCR4. [provided by RefSeq, Jul 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189652.15518.1, SRR5189652.174085.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225831.4/ ENSP00000225831.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as a ligand for C-C chemokine receptor CCR2 (PubMed:9837883, PubMed:10587439, PubMed:10529171). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (PubMed:9837883, PubMed:10587439). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils (PubMed:8627182, PubMed:9792674, PubMed:8195247). May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis (PubMed:8107690). Monomer or homodimer; in equilibrium (PubMed:8898111, PubMed:9837883, PubMed:15033992, PubMed:8989326). Is tethered on endothelial cells by glycosaminoglycan (GAG) side chains of proteoglycans (PubMed:9792674). Interacts with TNFAIP6 (via Link domain). P13500; P13501: CCL5; NbExp=2; IntAct=EBI-1034732, EBI-2848366; P13500; P80075: CCL8; NbExp=2; IntAct=EBI-1034732, EBI-16803830; P13500; P02776: PF4; NbExp=2; IntAct=EBI-1034732, EBI-2565740; P13500; P78317: RNF4; NbExp=3; IntAct=EBI-1034732, EBI-2340927; P13500; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1034732, EBI-6447886; P13500; Q2F862; Xeno; NbExp=5; IntAct=EBI-1034732, EBI-16161937; PRO_0000005146; P98066: TNFAIP6; NbExp=2; IntAct=EBI-11711396, EBI-11700693; Secreted Expressed in the seminal plasma, endometrial fluid and follicular fluid (at protein level) (PubMed:23765988). Expressed in monocytes (PubMed:2513477). Up-regulated upon hypertonic conditions (PubMed:23233732). In pancreatic islets, secretion is stimulated by IL1B (PubMed:23955712). Processing at the N-terminus can regulate receptor and target cell selectivity (PubMed:8627182). Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant (PubMed:8627182). N-Glycosylated. Genetic variations in CCL2 determine Mycobacterium tuberculosis susceptibility [MIM:607948]. Belongs to the intercrine beta (chemokine CC) family. Name=Wikipedia; Note=CCL2 entry; URL="https://en.wikipedia.org/wiki/CCL2"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/scya2/"; MAPK cascade angiogenesis monocyte chemotaxis protein kinase activity receptor binding cytokine activity protein binding extracellular region extracellular space cell protein phosphorylation chemotaxis inflammatory response immune response humoral immune response cytoskeleton organization cell adhesion signal transduction cell surface receptor signaling pathway G-protein coupled receptor signaling pathway G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger JAK-STAT cascade chemokine activity regulation of cell shape response to bacterium animal organ morphogenesis viral genome replication cytokine-mediated signaling pathway sensory perception of pain cellular homeostasis neutrophil chemotaxis lipopolysaccharide-mediated signaling pathway CCR2 chemokine receptor binding negative regulation of glial cell apoptotic process helper T cell extravasation PERK-mediated unfolded protein response protein kinase B signaling negative regulation of neuron apoptotic process positive regulation of GTPase activity astrocyte cell migration cellular response to fibroblast growth factor stimulus CCR chemokine receptor binding eosinophil chemotaxis macrophage chemotaxis lymphocyte chemotaxis positive regulation of T cell activation positive regulation of nitric-oxide synthase biosynthetic process positive regulation of synaptic transmission, glutamatergic chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to lipopolysaccharide cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor cellular response to organic cyclic compound positive regulation of calcium ion import positive regulation of NMDA glutamate receptor activity negative regulation of vascular endothelial cell proliferation negative regulation of G1/S transition of mitotic cell cycle positive regulation of endothelial cell apoptotic process positive regulation of apoptotic cell clearance negative regulation of natural killer cell chemotaxis uc002hhy.1 uc002hhy.2 uc002hhy.3 uc002hhy.4 
ENST00000225842.4 CCL1 ENST00000225842.4 C-C motif chemokine ligand 1 (from RefSeq NM_002981.2) B2R5G9 CCL1_HUMAN ENST00000225842.1 ENST00000225842.2 ENST00000225842.3 NM_002981 P22362 Q2M309 SCYA1 uc002hid.1 uc002hid.2 uc002hid.3 uc002hid.4 This antimicrobial gene is one of several chemokine genes clustered on the q-arm of chromosome 17. Chemokines form a superfamily of secreted proteins involved in immunoregulatory and inflammatory processes. The superfamily is divided into four subfamilies based on the arrangement of the N-terminal cysteine residues of the mature peptide. This chemokine, a member of the CC subfamily, is secreted by activated T cells and displays chemotactic activity for monocytes but not for neutrophils. It binds to the chemokine (C-C motif) receptor 8. [provided by RefSeq, Sep 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DA620119.1, BX093610.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225842.4/ ENSP00000225842.3 Protein has antimicrobial activity :: PMID: 12949249 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cytokine that is chemotactic for monocytes but not for neutrophils. Binds to CCR8. Monomer. Secreted. By phorbol myristate acetate (PMA). Belongs to the intercrine beta (chemokine CC) family. Name=Wikipedia; Note=CCL1 entry; URL="https://en.wikipedia.org/wiki/CCL1"; monocyte chemotaxis cytokine activity extracellular region extracellular space cell cellular calcium ion homeostasis chemotaxis inflammatory response immune response signal transduction G-protein coupled receptor signaling pathway positive regulation of cytosolic calcium ion concentration chemokine activity viral process neutrophil chemotaxis killing of cells of other organism positive regulation of GTPase activity CCR chemokine receptor binding eosinophil chemotaxis lymphocyte chemotaxis positive regulation of inflammatory response chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor positive regulation of monocyte chemotaxis positive regulation of interleukin-17 secretion uc002hid.1 uc002hid.2 uc002hid.3 uc002hid.4 
ENST00000225844.7 CCL13 ENST00000225844.7 C-C motif chemokine ligand 13 (from RefSeq NM_005408.3) CCL13_HUMAN ENST00000225844.1 ENST00000225844.2 ENST00000225844.3 ENST00000225844.4 ENST00000225844.5 ENST00000225844.6 MCP4 NCC1 NM_005408 O95689 Q6ICQ6 Q99616 SCYA13 uc002hic.1 uc002hic.2 uc002hic.3 uc002hic.4 This antimicrobial gene is one of several Cys-Cys (CC) cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity for monocytes, lymphocytes, basophils and eosinophils, but not neutrophils. This chemokine plays a role in accumulation of leukocytes during inflammation. It may also be involved in the recruitment of monocytes into the arterial wall during artherosclerosis. [provided by RefSeq, Sep 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AJ001634.1, U59808.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225844.7/ ENSP00000225844.2 Protein has antimicrobial activity :: PMID: 12949249 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils, but not neutrophils. Signals through CCR2B and CCR3 receptors. Plays a role in the accumulation of leukocytes at both sides of allergic and non-allergic inflammation. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. May play a role in the monocyte attraction in tissues chronically exposed to exogenous pathogens. Q99616; O00585: CCL21; NbExp=2; IntAct=EBI-725342, EBI-953695; Q99616; Q9Y258: CCL26; NbExp=2; IntAct=EBI-725342, EBI-7783416; Q99616; P13501: CCL5; NbExp=3; IntAct=EBI-725342, EBI-2848366; Q99616; P02778: CXCL10; NbExp=2; IntAct=EBI-725342, EBI-7815386; Q99616; O14625: CXCL11; NbExp=2; IntAct=EBI-725342, EBI-2871971; Q99616; P48061: CXCL12; NbExp=2; IntAct=EBI-725342, EBI-3913254; Q99616; P02776: PF4; NbExp=2; IntAct=EBI-725342, EBI-2565740; Q99616; P47992: XCL1; NbExp=2; IntAct=EBI-725342, EBI-10209901; Secreted. Widely expressed. Found in small intestine, thymus, colon, lung, trachea, stomach and lymph node. Low levels seen in the pulmonary artery smooth muscle cells. By IL1/interleukin-1 and TNF. One major form (form long), and two minor forms (short chain and medium chain) are produced by differential signal peptide cleavage. The medium chain is about 30-fold less active than the long chain. [C-C motif chemokine 13, long chain]: Mass=9314; Mass_error=30; Method=MALDI; Evidence=; [C-C motif chemokine 13, medium chain]: Mass=8760; Mass_error=30; Method=MALDI; Evidence=; [C-C motif chemokine 13, short chain]: Mass=8575; Mass_error=30; Method=MALDI; Evidence=; This protein can bind heparin. Belongs to the intercrine beta (chemokine CC) family. Name=Wikipedia; Note=CCL13 entry; URL="https://en.wikipedia.org/wiki/CCL13"; monocyte chemotaxis receptor binding cytokine activity protein binding extracellular region extracellular space cell cellular calcium ion homeostasis chemotaxis inflammatory response immune response cytoskeleton organization signal transduction G-protein coupled receptor signaling pathway cell-cell signaling chemokine activity regulation of cell shape neutrophil chemotaxis killing of cells of other organism positive regulation of GTPase activity CCR chemokine receptor binding eosinophil chemotaxis lymphocyte chemotaxis chemokine-mediated signaling pathway positive regulation of ERK1 and ERK2 cascade cellular response to interferon-gamma cellular response to interleukin-1 cellular response to tumor necrosis factor uc002hic.1 uc002hic.2 uc002hic.3 uc002hic.4 
ENST00000225873.9 PEX12 ENST00000225873.9 peroxisomal biogenesis factor 12 (from RefSeq NM_000286.3) B2R6M2 ENST00000225873.1 ENST00000225873.2 ENST00000225873.3 ENST00000225873.4 ENST00000225873.5 ENST00000225873.6 ENST00000225873.7 ENST00000225873.8 NM_000286 O00623 PAF3 PEX12 PEX12_HUMAN uc002hjp.1 uc002hjp.2 uc002hjp.3 uc002hjp.4 uc002hjp.5 This gene belongs to the peroxin-12 family. Peroxins (PEXs) are proteins that are essential for the assembly of functional peroxisomes. The peroxisome biogenesis disorders (PBDs) are a group of genetically heterogeneous autosomal recessive, lethal diseases characterized by multiple defects in peroxisome function. The peroxisomal biogenesis disorders are a heterogeneous group with at least 14 complementation groups and with more than 1 phenotype being observed in cases falling into particular complementation groups. Although the clinical features of PBD patients vary, cells from all PBD patients exhibit a defect in the import of one or more classes of peroxisomal matrix proteins into the organelle. Defects in this gene are a cause of Zellweger syndrome (ZWS). [provided by RefSeq, Oct 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.856607.1, SRR1660805.145609.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225873.9/ ENSP00000225873.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:9354782, PubMed:9632816, PubMed:24662292). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (PubMed:24662292). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity). Protein modification; protein ubiquitination. Component of the PEX2-PEX10-PEX12 retrotranslocation channel, composed of PEX2, PEX10 and PEX12 (PubMed:24662292, PubMed:10562279). Interacts with PEX19 via its cytoplasmic domain (PubMed:10704444, PubMed:11390669). O00623; Q9ULC5: ACSL5; NbExp=3; IntAct=EBI-594836, EBI-2876927; O00623; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-594836, EBI-10827839; O00623; Q12982: BNIP2; NbExp=3; IntAct=EBI-594836, EBI-752094; O00623; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-594836, EBI-8648738; O00623; Q6UWT4: C5orf46; NbExp=3; IntAct=EBI-594836, EBI-11986083; O00623; P78369: CLDN10; NbExp=3; IntAct=EBI-594836, EBI-13372810; O00623; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-594836, EBI-10241815; O00623; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-594836, EBI-2680384; O00623; Q96LL9: DNAJC30; NbExp=3; IntAct=EBI-594836, EBI-8639143; O00623; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-594836, EBI-10976398; O00623; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-594836, EBI-11337888; O00623; Q14318: FKBP8; NbExp=3; IntAct=EBI-594836, EBI-724839; O00623; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-594836, EBI-713304; O00623; P29033: GJB2; NbExp=3; IntAct=EBI-594836, EBI-3905204; O00623; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-594836, EBI-725665; O00623; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-594836, EBI-10317612; O00623; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-594836, EBI-12866138; O00623; Q16617: NKG7; NbExp=3; IntAct=EBI-594836, EBI-3919611; O00623; Q8IXM6: NRM; NbExp=3; IntAct=EBI-594836, EBI-10262547; O00623; P40855: PEX19; NbExp=2; IntAct=EBI-594836, EBI-594747; O00623; P50542: PEX5; NbExp=4; IntAct=EBI-594836, EBI-597835; O00623; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-594836, EBI-8652812; O00623; P43378: PTPN9; NbExp=3; IntAct=EBI-594836, EBI-742898; O00623; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-594836, EBI-3232108; O00623; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-594836, EBI-8652744; O00623; P60059: SEC61G; NbExp=3; IntAct=EBI-594836, EBI-4402709; O00623; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-594836, EBI-8640191; O00623; P10124: SRGN; NbExp=3; IntAct=EBI-594836, EBI-744915; O00623; Q9UNK0: STX8; NbExp=3; IntAct=EBI-594836, EBI-727240; O00623; Q9C0I4: THSD7B; NbExp=3; IntAct=EBI-594836, EBI-311394; O00623; P17152: TMEM11; NbExp=3; IntAct=EBI-594836, EBI-723946; O00623; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-594836, EBI-347385; O00623; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-594836, EBI-16746122; O00623; P49638: TTPA; NbExp=3; IntAct=EBI-594836, EBI-10210710; Peroxisome membrane ; Multi-pass membrane protein The three subunits of the retrotranslocation channel (PEX2, PEX10 and PEX12) coassemble in the membrane into a channel with an open 10 Angstrom pore (By similarity). The RING-type zinc-fingers that catalyze PEX5 receptor ubiquitination are positioned above the pore on the cytosolic side of the complex (By similarity). The RING-type zinc-finger is degenerated and only coordinates one zinc ions, preventing E3 ubiquitin-protein ligase activity. Peroxisome biogenesis disorder complementation group 3 (PBD- CG3) [MIM:614859]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). Note=The disease is caused by variants affecting the gene represented in this entry. Peroxisome biogenesis disorder 3A (PBD3A) [MIM:614859]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. te=The disease is caused by variants affecting the gene represented in this entry. Peroxisome biogenesis disorder 3B (PBD3B) [MIM:266510]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the pex2/pex10/pex12 family. Name=dbPEX, PEX Gene Database; URL="https://databases.lovd.nl/shared/genes/PEX12"; ubiquitin-protein transferase activity protein binding peroxisome peroxisomal membrane integral component of peroxisomal membrane protein monoubiquitination protein targeting to peroxisome peroxisome organization protein C-terminus binding zinc ion binding membrane integral component of membrane protein import into peroxisome matrix protein ubiquitination metal ion binding peroxisomal importomer complex uc002hjp.1 uc002hjp.2 uc002hjp.3 uc002hjp.4 uc002hjp.5 
ENST00000225899.4 KRT32 ENST00000225899.4 keratin 32 (from RefSeq NM_002278.3) ENST00000225899.1 ENST00000225899.2 ENST00000225899.3 HHA2 HKA2 K1H2_HUMAN KRTHA2 NM_002278 Q14532 uc002hwr.1 uc002hwr.2 uc002hwr.3 uc002hwr.4 uc002hwr.5 The protein encoded by this gene is a member of the keratin gene family. As a type I hair keratin, it is an acidic protein which heterodimerizes with type II keratins to form hair and nails. The type I hair keratins are clustered in a region of chromosome 17q12-q21 and have the same direction of transcription. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: X81419.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2147975, SAMEA2156670 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Q14532; Q86YP4: GATAD2A; NbExp=3; IntAct=EBI-1044146, EBI-726224; Q14532; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-1044146, EBI-14069005; Q14532; Q14CN4: KRT72; NbExp=3; IntAct=EBI-1044146, EBI-1221280; Q14532; Q6KB66-2: KRT80; NbExp=4; IntAct=EBI-1044146, EBI-11999246; Q14532; O43790: KRT86; NbExp=3; IntAct=EBI-1044146, EBI-9996498; Q14532; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-1044146, EBI-14086479; Q14532; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-1044146, EBI-11746523; Q14532; Q9BT92: TCHP; NbExp=3; IntAct=EBI-1044146, EBI-740781; Q14532; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-1044146, EBI-7353612; Q14532; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-1044146, EBI-25492395; Restricted to the hair cuticle. There are two types of hair/microfibrillar keratin, I (acidic) and II (neutral to basic). Belongs to the intermediate filament family. Sequence=CAA57179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; structural molecule activity cytosol intermediate filament epidermis development keratinization extracellular exosome cornification uc002hwr.1 uc002hwr.2 uc002hwr.3 uc002hwr.4 uc002hwr.5 
ENST00000225916.10 KAT2A ENST00000225916.10 lysine acetyltransferase 2A, transcript variant 1 (from RefSeq NM_021078.3) ENST00000225916.1 ENST00000225916.2 ENST00000225916.3 ENST00000225916.4 ENST00000225916.5 ENST00000225916.6 ENST00000225916.7 ENST00000225916.8 ENST00000225916.9 GCN5 GCN5L2 KAT2A KAT2A_HUMAN NM_021078 Q8N1A2 Q92830 Q9UCW1 uc002hyx.1 uc002hyx.2 uc002hyx.3 uc002hyx.4 KAT2A, or GCN5, is a histone acetyltransferase (HAT) that functions primarily as a transcriptional activator. It also functions as a repressor of NF-kappa-B (see MIM 164011) by promoting ubiquitination of the NF-kappa-B subunit RELA (MIM 164014) in a HAT-independent manner (Mao et al., 2009 [PubMed 19339690]).[supplied by OMIM, Sep 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC039907.1, BC032743.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225916.10/ ENSP00000225916.5 RefSeq Select criteria :: based on conservation ##RefSeq-Attributes-END## Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferase, succinyltransferase or malonyltransferase, depending on the context (PubMed:29211711, PubMed:35995428). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes (PubMed:29211711). Succinylation of histones gives a specific tag for epigenetic transcription activation (PubMed:29211711). Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation (PubMed:29211711). In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase (PubMed:17301242, PubMed:19103755, PubMed:29211711). Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles (PubMed:17301242, PubMed:19103755). Acetylation of histones gives a specific tag for epigenetic transcription activation (PubMed:17301242, PubMed:19103755, PubMed:29211711). Recruited by the XPC complex at promoters, where it specifically mediates acetylation of histone variant H2A.Z.1/H2A.Z, thereby promoting expression of target genes (PubMed:29973595, PubMed:31527837). Involved in long-term memory consolidation and synaptic plasticity: acts by promoting expression of a hippocampal gene expression network linked to neuroactive receptor signaling (By similarity). Acts as a positive regulator of T-cell activation: upon TCR stimulation, recruited to the IL2 promoter following interaction with NFATC2 and catalyzes acetylation of histone H3 at 'Lys-9' (H3K9ac), leading to promote IL2 expression (By similarity). Required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac) (By similarity). Regulates embryonic stem cell (ESC) pluripotency and differentiation (By similarity). Also acetylates non-histone proteins, such as CEBPB, PPARGC1A, PLK4 and TBX5 (PubMed:17301242, PubMed:16753578, PubMed:27796307, PubMed:29174768). Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5 (PubMed:29174768). Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4 (PubMed:27796307). Acts as a negative regulator of gluconeogenesis by mediating acetylation and subsequent inactivation of PPARGC1A (PubMed:16753578, PubMed:23142079). Also acts as a histone glutaryltransferase: catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (PubMed:31542297). (Microbial infection) In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; Evidence= Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L- lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence= Reaction=L-lysyl-[protein] + succinyl-CoA = CoA + H(+) + N(6)-succinyl- L-lysyl-[protein]; Xref=Rhea:RHEA:16261, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:87830; Evidence=; Reaction=glutaryl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-glutaryl- L-lysyl-[protein]; Xref=Rhea:RHEA:18009, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378, ChEBI:CHEBI:87828; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18010; Evidence=; Kinetic parameters: KM=0.83 uM for acetyl-CoA ; KM=0.91 uM for acetyl-CoA ; KM=0.36 uM for succinyl-CoA ; KM=5.90 uM for acetyl-CoA (in the presence of H3K9 peptide) ; KM=45.1 uM for malonyl-CoA (in the presence of H3K9 peptide) ; Homooligomer; may form a tetramer of homodimers (PubMed:30109122). Interacts with EP300, CREBBP and ADA2. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, KAT2A/GCN5L2, TAF10 and TRRAP (PubMed:10373431, PubMed:10611234, PubMed:11438666). Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9 (PubMed:18206972). The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22 (PubMed:18206972). Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (PubMed:19103755). In the complex, it probably interacts directly with KAT14, MBIP and WDR5 (PubMed:19103755). Interacts with PML (By similarity). Interacts with CEBPB (PubMed:17301242). Interacts with TACC1, TACC2 and TACC3 (PubMed:14767476). Interacts with RELA (By similarity). Interacts with NFATC2 (By similarity). Interacts with TBX5 (PubMed:29174768). Interacts with PLK4 (PubMed:27796307). Associates with the 2- oxoglutarate dehydrogenase complex (PubMed:29211711). Interacts with XPC; leading to KAT2A recruitment to promoters and subsequent acetylation of histones (PubMed:29973595, PubMed:31527837). Interacts with ERCC3/XPB; leading to KAT2A recruitment to promoters and subsequent acetylation of histones (PubMed:30894545). Interacts with ISL1. Interactions of ISL1 with MLIP1 or KAT2A may be mutually exclusive (By similarity). (Microbial infection) Interacts with and acetylates HIV-1 Tat. Q92830; Q9NY61: AATF; NbExp=4; IntAct=EBI-477622, EBI-372428; Q92830; Q01094: E2F1; NbExp=3; IntAct=EBI-477622, EBI-448924; Q92830; O75717: WDHD1; NbExp=5; IntAct=EBI-477622, EBI-3951691; Q92830; Q8IYH5: ZZZ3; NbExp=2; IntAct=EBI-477622, EBI-2795524; Q92830; P0DTC9: N; Xeno; NbExp=2; IntAct=EBI-477622, EBI-25475856; Q92830; P59595: N; Xeno; NbExp=2; IntAct=EBI-477622, EBI-7602718; Nucleus romosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Mainly localizes to the nucleus (PubMed:27796307). Localizes to sites of DNA damage (PubMed:25593309). Also localizes to centrosomes in late G1 and around the G1/S transition, coinciding with the onset of centriole formation (PubMed:27796307). Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=GCN5-L; IsoId=Q92830-1; Sequence=Displayed; Name=2; Synonyms=GCN5-S; IsoId=Q92830-2; Sequence=VSP_000556; Expressed in all tissues tested. Loop3 is required for substrate specificity and adopts different structural conformations in succinyl-CoA-bound and acetyl- CoA-bound forms. Tyr-645 has an important role in the selective binding of succinyl-CoA over acetyl-CoA. Acetylated at Lys-549, inhibiting the protein acetyltransferase activity (PubMed:23142079). Deacetylation at Lys-549 by SIRT6 promotes phosphorylation at Ser-307 and Thr-735 and subsequent activation of the protein acetyltransferase activity, leading to acetylation and inactivation of PPARGC1A (PubMed:23142079). Belongs to the acetyltransferase family. GCN5 subfamily. According to a report, has weak protein acyltransferase activity compared to protein acetyltransferase activity (PubMed:27377381). These conclusions are however not supported by subsequent studies (PubMed:29211711, PubMed:31542297). histone acetyltransferase complex nuclear chromatin in utero embryonic development somitogenesis cytokine production neural tube closure chromatin binding transcription coactivator activity histone acetyltransferase activity protein binding extracellular space nucleus nucleoplasm Ada2/Gcn5/Ada3 transcription activator complex chromosome cytoplasm centrosome microtubule organizing center cytoskeleton chromatin remodeling regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter nervous system development heart development long-term memory N-acetyltransferase activity transcription factor binding cell proliferation H3 histone acetyltransferase activity response to organic cyclic compound viral process acetyltransferase activity histone acetylation histone deubiquitination protein deubiquitination transferase activity transferase activity, transferring acyl groups internal peptidyl-lysine acetylation protein phosphatase binding telencephalon development metencephalon development midbrain development STAGA complex positive regulation of cell projection organization regulation of protein stability response to nutrient levels transcription factor TFTC complex positive regulation of histone acetylation multicellular organism growth positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter histone deacetylase binding histone H3 acetylation histone H4-K12 acetylation histone acetyltransferase activity (H4-K12 specific) histone H3-K14 acetylation regulation of regulatory T cell differentiation positive regulation of gene expression, epigenetic positive regulation of transcription from RNA polymerase II promoter negative regulation of centriole replication regulation of synaptic plasticity intracellular distribution of mitochondria regulation of T cell activation limb development peptide-lysine-N-acetyltransferase activity cellular response to tumor necrosis factor alpha-tubulin acetylation mitotic spindle cellular response to nerve growth factor stimulus positive regulation of cardiac muscle cell differentiation oxoglutarate dehydrogenase complex uc002hyx.1 uc002hyx.2 uc002hyx.3 uc002hyx.4 
ENST00000225927.7 NAGLU ENST00000225927.7 N-acetyl-alpha-glucosaminidase (from RefSeq NM_000263.4) ANAG_HUMAN ENST00000225927.1 ENST00000225927.2 ENST00000225927.3 ENST00000225927.4 ENST00000225927.5 ENST00000225927.6 NM_000263 P54802 UFHSD1 uc002hzv.1 uc002hzv.2 uc002hzv.3 uc002hzv.4 uc002hzv.5 This gene encodes an enzyme that degrades heparan sulfate by hydrolysis of terminal N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. Defects in this gene are the cause of mucopolysaccharidosis type IIIB (MPS-IIIB), also known as Sanfilippo syndrome B. This disease is characterized by the lysosomal accumulation and urinary excretion of heparan sulfate. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: HM005331.1, U40846.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225927.7/ ENSP00000225927.1 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Involved in the degradation of heparan sulfate. Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.; EC=3.2.1.50; Monomer and homodimer. Lysosome. Liver, ovary, peripheral blood leukocytes, testis, prostate, spleen, colon, lung, placenta and kidney. Mucopolysaccharidosis 3B (MPS3B) [MIM:252920]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. te=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, axonal, 2V (CMT2V) [MIM:616491]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2V is an autosomal dominant sensory neuropathy with late onset. The main clinical feature is recurrent leg pain that progresses to constant painful paraesthesias in the feet and later the hands. As it evolves, some patients develop a mild sensory ataxia. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyl hydrolase 89 family. A MPS3B mutation at position 100 was erroneously reported (PubMed:9950362) as an amino acid change from Arg to His. The right amino acid change is from His to Arg. alpha-N-acetylglucosaminidase activity lysosome glycosaminoglycan catabolic process lysosome organization nervous system development metabolic process hydrolase activity hydrolase activity, acting on glycosyl bonds cerebellar Purkinje cell layer development middle ear morphogenesis lysosomal lumen locomotor rhythm retinal rod cell development inner ear receptor cell development extracellular exosome uc002hzv.1 uc002hzv.2 uc002hzv.3 uc002hzv.4 uc002hzv.5 
ENST00000225941.6 ABI3 ENST00000225941.6 ABI family member 3, transcript variant 1 (from RefSeq NM_016428.3) ABI3_HUMAN C9IZN8 ENST00000225941.1 ENST00000225941.2 ENST00000225941.3 ENST00000225941.4 ENST00000225941.5 NESH NM_016428 Q9H0P6 Q9P2A4 uc002iop.1 uc002iop.2 This gene encodes a member of an adaptor protein family. Members of this family encode proteins containing a homeobox homology domain, proline rich region and Src-homology 3 (SH3) domain, and are components of the Abi/WAVE complex which regulates actin polymerization. The encoded protein inhibits ectopic metastasis of tumor cells as well as cell migration. This may be accomplished through interaction with p21-activated kinase. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]. May inhibit tumor metastasis (By similarity). In vitro, reduces cell motility. May interact with PAK1 and PAK2. Probably interacts with TARSH. Q9P2A4; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-742038, EBI-11096309; Q9P2A4; Q9P2A4: ABI3; NbExp=4; IntAct=EBI-742038, EBI-742038; Q9P2A4; Q9BRR9: ARHGAP9; NbExp=3; IntAct=EBI-742038, EBI-750254; Q9P2A4; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-742038, EBI-742909; Q9P2A4; Q13515: BFSP2; NbExp=5; IntAct=EBI-742038, EBI-10229433; Q9P2A4; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-742038, EBI-465861; Q9P2A4; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-742038, EBI-2350265; Q9P2A4; Q9C0F1: CEP44; NbExp=9; IntAct=EBI-742038, EBI-744115; Q9P2A4; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-742038, EBI-2806959; Q9P2A4; O60941: DTNB; NbExp=3; IntAct=EBI-742038, EBI-740402; Q9P2A4; O15372: EIF3H; NbExp=6; IntAct=EBI-742038, EBI-709735; Q9P2A4; Q7L2H7: EIF3M; NbExp=3; IntAct=EBI-742038, EBI-353901; Q9P2A4; Q6IB98: EIF3S3; NbExp=3; IntAct=EBI-742038, EBI-10184995; Q9P2A4; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-742038, EBI-11748557; Q9P2A4; Q9UI08: EVL; NbExp=4; IntAct=EBI-742038, EBI-346653; Q9P2A4; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-742038, EBI-6448852; Q9P2A4; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-742038, EBI-11986315; Q9P2A4; Q9Y285: FARSA; NbExp=3; IntAct=EBI-742038, EBI-725361; Q9P2A4; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-742038, EBI-10244131; Q9P2A4; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-742038, EBI-11427343; Q9P2A4; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-742038, EBI-712073; Q9P2A4; P62993: GRB2; NbExp=3; IntAct=EBI-742038, EBI-401755; Q9P2A4; Q86YM7: HOMER1; NbExp=4; IntAct=EBI-742038, EBI-746815; Q9P2A4; Q9NSB8-2: HOMER2; NbExp=3; IntAct=EBI-742038, EBI-12017090; Q9P2A4; Q9NSC5: HOMER3; NbExp=8; IntAct=EBI-742038, EBI-748420; Q9P2A4; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-742038, EBI-9091197; Q9P2A4; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-742038, EBI-8638439; Q9P2A4; Q63ZY3: KANK2; NbExp=6; IntAct=EBI-742038, EBI-2556193; Q9P2A4; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-742038, EBI-739493; Q9P2A4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-742038, EBI-14069005; Q9P2A4; Q6P597: KLC3; NbExp=3; IntAct=EBI-742038, EBI-1643885; Q9P2A4; Q9NSK0: KLC4; NbExp=3; IntAct=EBI-742038, EBI-949319; Q9P2A4; A1A4E9: KRT13; NbExp=3; IntAct=EBI-742038, EBI-10171552; Q9P2A4; P02533: KRT14; NbExp=3; IntAct=EBI-742038, EBI-702178; Q9P2A4; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-742038, EBI-2952736; Q9P2A4; Q7Z3Y7: KRT28; NbExp=3; IntAct=EBI-742038, EBI-11980489; Q9P2A4; Q15323: KRT31; NbExp=3; IntAct=EBI-742038, EBI-948001; Q9P2A4; Q92764: KRT35; NbExp=3; IntAct=EBI-742038, EBI-1058674; Q9P2A4; O76013-2: KRT36; NbExp=3; IntAct=EBI-742038, EBI-11958506; Q9P2A4; O76015: KRT38; NbExp=3; IntAct=EBI-742038, EBI-1047263; Q9P2A4; P43365: MAGEA12; NbExp=3; IntAct=EBI-742038, EBI-749530; Q9P2A4; Q9NX70: MED29; NbExp=3; IntAct=EBI-742038, EBI-394656; Q9P2A4; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-742038, EBI-1104552; Q9P2A4; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-742038, EBI-995714; Q9P2A4; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-742038, EBI-748896; Q9P2A4; O43639: NCK2; NbExp=6; IntAct=EBI-742038, EBI-713635; Q9P2A4; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-742038, EBI-928842; Q9P2A4; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-742038, EBI-2859639; Q9P2A4; Q9BVL2: NUP58; NbExp=7; IntAct=EBI-742038, EBI-2811583; Q9P2A4; O43482: OIP5; NbExp=3; IntAct=EBI-742038, EBI-536879; Q9P2A4; P25786: PSMA1; NbExp=3; IntAct=EBI-742038, EBI-359352; Q9P2A4; Q7L099: RUFY3; NbExp=3; IntAct=EBI-742038, EBI-722392; Q9P2A4; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-742038, EBI-11984663; Q9P2A4; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-742038, EBI-10224192; Q9P2A4; Q9Y3L3: SH3BP1; NbExp=3; IntAct=EBI-742038, EBI-346869; Q9P2A4; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-742038, EBI-358489; Q9P2A4; Q16623: STX1A; NbExp=3; IntAct=EBI-742038, EBI-712466; Q9P2A4; P32856-2: STX2; NbExp=3; IntAct=EBI-742038, EBI-11956649; Q9P2A4; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-742038, EBI-740595; Q9P2A4; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-742038, EBI-3650647; Q9P2A4; Q99757: TXN2; NbExp=3; IntAct=EBI-742038, EBI-2932492; Q9P2A4; Q5ST30: VARS2; NbExp=3; IntAct=EBI-742038, EBI-2116622; Q9P2A4; P50552: VASP; NbExp=9; IntAct=EBI-742038, EBI-748201; Q9P2A4; P42768: WAS; NbExp=4; IntAct=EBI-742038, EBI-346375; Q9P2A4; Q92558: WASF1; NbExp=3; IntAct=EBI-742038, EBI-1548747; Q9P2A4; B2R8Y4; NbExp=3; IntAct=EBI-742038, EBI-10175581; Cytoplasm Note=Colocalizes with PAK2 at leading edge of cells. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9P2A4-1; Sequence=Displayed; Name=2; IsoId=Q9P2A4-2; Sequence=VSP_041467; Expressed in heart, lung, liver, pancreas, kidney, placenta and at low levels in brain and skeletal muscle. Belongs to the ABI family. protein binding cytoplasm membrane SH3 domain binding lamellipodium regulation of cell migration identical protein binding peptidyl-tyrosine phosphorylation uc002iop.1 uc002iop.2 
ENST00000225964.10 COL1A1 ENST00000225964.10 collagen type I alpha 1 chain (from RefSeq NM_000088.4) CO1A1_HUMAN ENST00000225964.1 ENST00000225964.2 ENST00000225964.3 ENST00000225964.4 ENST00000225964.5 ENST00000225964.6 ENST00000225964.7 ENST00000225964.8 ENST00000225964.9 NM_000088 O76045 P02452 P78441 Q13896 Q13902 Q13903 Q14037 Q14992 Q15176 Q15201 Q16050 Q59F64 Q7KZ30 Q7KZ34 Q8IVI5 Q8N473 Q9UML6 Q9UMM7 uc002iqm.1 uc002iqm.2 uc002iqm.3 uc002iqm.4 uc002iqm.5 This gene encodes the pro-alpha1 chains of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for platelet-derived growth factor beta are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from unregulated expression of the growth factor. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: Z74615.1, AB209597.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000225964.10/ ENSP00000225964.6 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Type I collagen is a member of group I collagen (fibrillar forming collagen). Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). Interacts with TRAM2 (PubMed:14749390). Interacts with MFAP4 in a Ca (2+)-dependent manner (By similarity). P02452; P08123: COL1A2; NbExp=5; IntAct=EBI-982999, EBI-983038; P02452; P02751: FN1; NbExp=3; IntAct=EBI-982999, EBI-1220319; P02452; Q14145: KEAP1; NbExp=3; IntAct=EBI-982999, EBI-751001; P02452; O01949: AAEL010235; Xeno; NbExp=5; IntAct=EBI-982999, EBI-7685554; Secreted, extracellular space, extracellular matrix Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. Caffey disease (CAFYD) [MIM:114000]: An autosomal dominant disorder characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. Note=The disease is caused by variants affecting the gene represented in this entry. Ehlers-Danlos syndrome, classic type, 1 (EDSCL1) [MIM:130000]: A form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. The main features of classic Ehlers-Danlos syndrome are joint hypermobility and dislocation, and fragile, bruisable skin. EDSCL1 inheritance is autosomal dominant. Note=The disease may be caused by variants affecting the gene represented in this entry. Ehlers-Danlos syndrome, arthrochalasia type, 1 (EDSARTH1) [MIM:130060]: A form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDSARTH1 is an autosomal dominant form characterized by frequent congenital hip dislocation and extreme joint laxity with recurrent joint subluxations and minimal skin involvement. te=The disease is caused by variants affecting the gene represented in this entry. Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta. te=The disease is caused by variants affecting the gene represented in this entry. Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. te=The disease is caused by variants affecting the gene represented in this entry. Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta. te=The disease is caused by variants affecting the gene represented in this entry. Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. te=The disease is caused by variants affecting the gene represented in this entry. Combined osteogenesis imperfecta and Ehlers-Danlos syndrome 1 (OIEDS1) [MIM:619115]: An autosomal dominant connective tissue disorder characterized by osteopenia, bone fragility, long bone fractures, blue sclerae, joint hyperextensibility, soft and hyperextensible skin, abnormal wound healing, easy bruising, and vascular fragility. te=The disease is caused by variants affecting the gene represented in this entry. Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF. Belongs to the fibrillar collagen family. Sequence=BAD92834.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=Osteogenesis imperfecta variant database; Note=The COL1A1 gene homepage; URL="https://www.LOVD.nl/COL1A1"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/186/COL1A1"; Name=Wikipedia; Note=Type-I collagen entry; URL="https://en.wikipedia.org/wiki/Type-I_collagen"; skeletal system development ossification blood vessel development osteoblast differentiation intramembranous ossification endochondral ossification protease binding extracellular matrix structural constituent protein binding extracellular region collagen trimer collagen type I trimer extracellular space cytoplasm endoplasmic reticulum endoplasmic reticulum lumen Golgi apparatus response to nutrient blood coagulation visual perception sensory perception of sound response to mechanical stimulus positive regulation of epithelial to mesenchymal transition negative regulation of cell-substrate adhesion protein transport extracellular matrix structural constituent conferring tensile strength secretory granule platelet activation extracellular matrix organization collagen fibril organization positive regulation of cell migration extracellular matrix response to nutrient levels response to corticosteroid response to estradiol collagen biosynthetic process protein localization to nucleus tooth mineralization collagen-activated tyrosine kinase receptor signaling pathway wound healing response to drug response to hydrogen peroxide identical protein binding response to peptide hormone skin development skin morphogenesis cellular response to fibroblast growth factor stimulus tooth eruption positive regulation of transcription, DNA-templated metal ion binding platelet-derived growth factor binding response to steroid hormone skeletal system morphogenesis embryonic skeletal system development regulation of immune response leukocyte migration response to cAMP response to hyperoxia face morphogenesis bone trabecula formation cartilage development involved in endochondral bone morphogenesis cellular response to amino acid stimulus cellular response to mechanical stimulus cellular response to retinoic acid cellular response to vitamin E cellular response to tumor necrosis factor cellular response to epidermal growth factor stimulus cellular response to transforming growth factor beta stimulus positive regulation of canonical Wnt signaling pathway response to fluoride cellular response to fluoride uc002iqm.1 uc002iqm.2 uc002iqm.3 uc002iqm.4 uc002iqm.5 
ENST00000225969.9 MRPL27 ENST00000225969.9 mitochondrial ribosomal protein L27 (from RefSeq NM_016504.3) B2RE14 ENST00000225969.1 ENST00000225969.2 ENST00000225969.3 ENST00000225969.4 ENST00000225969.5 ENST00000225969.6 ENST00000225969.7 ENST00000225969.8 HSPC250 NM_016504 Q9P0M9 RM27_HUMAN uc002iqq.1 uc002iqq.2 uc002iqq.3 uc002iqq.4 uc002iqq.5 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AF151084.1, SRR1163658.334646.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2153932, SAMN03267769 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000225969.9/ ENSP00000225969.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the mitochondrial large ribosomal subunit (mt- LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins. Q9P0M9; Q13643: FHL3; NbExp=6; IntAct=EBI-5325236, EBI-741101; Mitochondrion Belongs to the bacterial ribosomal protein bL27 family. RNA binding structural constituent of ribosome protein binding mitochondrion mitochondrial inner membrane mitochondrial large ribosomal subunit ribosome translation mitochondrial translational elongation mitochondrial translational termination uc002iqq.1 uc002iqq.2 uc002iqq.3 uc002iqq.4 uc002iqq.5 
ENST00000225972.8 LRRC59 ENST00000225972.8 leucine rich repeat containing 59 (from RefSeq NM_018509.4) B2RE83 D3DTX8 ENST00000225972.1 ENST00000225972.2 ENST00000225972.3 ENST00000225972.4 ENST00000225972.5 ENST00000225972.6 ENST00000225972.7 LRC59_HUMAN NM_018509 PRO1855 Q96AG4 Q9P189 uc002iqt.1 uc002iqt.2 uc002iqt.3 uc002iqt.4 uc002iqt.5 Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores. Can form homodimers. Interacts with SGO1. Interacts with FGF1. Q96AG4; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-358888, EBI-11522760; Q96AG4; P29972: AQP1; NbExp=3; IntAct=EBI-358888, EBI-745213; Q96AG4; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-358888, EBI-7247651; Q96AG4; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-358888, EBI-11522780; Q96AG4; O95406: CNIH1; NbExp=3; IntAct=EBI-358888, EBI-12172273; Q96AG4; Q15125: EBP; NbExp=3; IntAct=EBI-358888, EBI-3915253; Q96AG4; P56851: EDDM3B; NbExp=3; IntAct=EBI-358888, EBI-10215665; Q96AG4; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-358888, EBI-11978907; Q96AG4; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-358888, EBI-10485931; Q96AG4; Q6UX34: SNORC; NbExp=3; IntAct=EBI-358888, EBI-11957067; Q96AG4; P55061: TMBIM6; NbExp=3; IntAct=EBI-358888, EBI-1045825; Q96AG4; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-358888, EBI-347385; Q96AG4; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-358888, EBI-2852148; Q96AG4; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-358888, EBI-12111910; Q96AG4; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-358888, EBI-11996766; Q96AG4; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-358888, EBI-12195249; Microsome membrane ; Single-pass type II membrane protein Endoplasmic reticulum membrane; Single-pass type II membrane protein. Nucleus envelope. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1. Widely expressed. Sequence=AAF69611.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAG38180.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; RNA binding nucleus nuclear envelope endoplasmic reticulum endoplasmic reticulum membrane membrane integral component of membrane organelle membrane mitochondrial nucleoid intracellular membrane-bounded organelle cadherin binding uc002iqt.1 uc002iqt.2 uc002iqt.3 uc002iqt.4 uc002iqt.5 
ENST00000225992.8 PPY ENST00000225992.8 pancreatic polypeptide, transcript variant 1 (from RefSeq NM_002722.5) ENST00000225992.1 ENST00000225992.2 ENST00000225992.3 ENST00000225992.4 ENST00000225992.5 ENST00000225992.6 ENST00000225992.7 NM_002722 P01298 PAHO_HUMAN PNP PPY uc002iep.1 uc002iep.2 uc002iep.3 uc002iep.4 uc002iep.5 This gene encodes a member of the neuropeptide Y (NPY) family of peptides. The encoded 95 aa preproprotein is synthesized in the pancreatic islets of Langerhans and proteolytically processed to generate two peptide products. These products include the active pancreatic hormone of 36 aa and an icosapeptide of unknown function. This hormone acts as a regulator of pancreatic and gastrointestinal functions and may be important in the regulation of food intake. Plasma level of this hormone has been shown to be reduced in conditions associated with increased food intake and elevated in anorexia nervosa. In addition, infusion of this hormone in obese rodents has shown to decrease weight gain. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Jan 2016]. [Pancreatic polypeptide]: Hormone secreted by pancreatic cells that acts as a regulator of pancreatic and gastrointestinal functions probably by signaling through the G protein-coupled receptor NPY4R2. P01298; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12121422, EBI-3867333; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P01298-1; Sequence=Displayed; Name=2; IsoId=P01298-2; Sequence=VSP_057852; Released in circulation upon food intake (PubMed:828120). Also up-regulated by exercise (PubMed:514078). Obinepitide is under clinical trial by 7TM Pharma to be used for the treatment of obesity. Obinepitide is derived from pancreatic hormone residues 30 to 65 with a Gln at position 63. Belongs to the NPY family. G-protein coupled receptor binding hormone activity neuropeptide hormone activity extracellular region extracellular space cytoplasm G-protein coupled receptor signaling pathway neuropeptide signaling pathway protein secretion uc002iep.1 uc002iep.2 uc002iep.3 uc002iep.4 uc002iep.5 
ENST00000226004.8 DUSP3 ENST00000226004.8 dual specificity phosphatase 3 (from RefSeq NM_004090.4) D3DX45 DUS3_HUMAN ENST00000226004.1 ENST00000226004.2 ENST00000226004.3 ENST00000226004.4 ENST00000226004.5 ENST00000226004.6 ENST00000226004.7 NM_004090 P51452 Q5U0J1 Q8IYJ9 VHR uc002ied.1 uc002ied.2 uc002ied.3 uc002ied.4 uc002ied.5 uc002ied.6 The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.105724.1, SRR1803611.73793.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226004.8/ ENSP00000226004.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2. Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence= Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Interacts with VRK3, which seems to activate it's phosphatase activity. P51452; P50221: MEOX1; NbExp=3; IntAct=EBI-1049755, EBI-2864512; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P51452-1; Sequence=Displayed; Name=2; IsoId=P51452-2; Sequence=VSP_056284; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily. inactivation of MAPK activity immunological synapse phosphoprotein phosphatase activity protein tyrosine phosphatase activity nucleus nucleoplasm cytosol protein dephosphorylation cytoskeletal protein binding protein tyrosine/serine/threonine phosphatase activity dephosphorylation hydrolase activity phosphatase activity protein kinase binding negative regulation of cell migration receptor tyrosine kinase binding MAP kinase phosphatase activity peptidyl-tyrosine dephosphorylation negative regulation of epidermal growth factor receptor signaling pathway negative regulation of MAPK cascade positive regulation of mitotic cell cycle negative regulation of JNK cascade negative regulation of T cell receptor signaling pathway negative regulation of T cell activation negative regulation of chemotaxis regulation of focal adhesion assembly negative regulation of ERK1 and ERK2 cascade cellular response to epidermal growth factor stimulus peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity protein tyrosine kinase binding uc002ied.1 uc002ied.2 uc002ied.3 uc002ied.4 uc002ied.5 uc002ied.6 
ENST00000226021.5 CACNG1 ENST00000226021.5 calcium voltage-gated channel auxiliary subunit gamma 1 (from RefSeq NM_000727.4) B2R9N3 CACNLG CCG1_HUMAN ENST00000226021.1 ENST00000226021.2 ENST00000226021.3 ENST00000226021.4 NM_000727 Q06432 Q14D59 uc002jfu.1 uc002jfu.2 uc002jfu.3 uc002jfu.4 uc002jfu.5 Voltage-dependent calcium channels are composed of five subunits. The protein encoded by this gene represents one of these subunits, gamma, and is one of two known gamma subunit proteins. This particular gamma subunit is part of skeletal muscle 1,4-dihydropyridine-sensitive calcium channels and is an integral membrane protein that plays a role in excitation-contraction coupling. This gene is part of a functionally diverse eight-member protein subfamily of the PMP-22/EMP/MP20 family and is located in a cluster with two family members that function as transmembrane AMPA receptor regulatory proteins (TARPs). [provided by RefSeq, Dec 2010]. ##Evidence-Data-START## Transcript exon combination :: SRR5189667.187776.1, L07738.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2153427, SAMEA2158800 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226021.5/ ENSP00000226021.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics. Component of a calcium channel complex consisting of a pore- forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2. Q06432; Q13323: BIK; NbExp=3; IntAct=EBI-9686780, EBI-700794; Q06432; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-9686780, EBI-18013275; Q06432; P60508: ERVFRD-1; NbExp=3; IntAct=EBI-9686780, EBI-17973325; Q06432; O15552: FFAR2; NbExp=3; IntAct=EBI-9686780, EBI-2833872; Q06432; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-9686780, EBI-12142257; Q06432; Q05329: GAD2; NbExp=3; IntAct=EBI-9686780, EBI-9304251; Q06432; Q8TED1: GPX8; NbExp=3; IntAct=EBI-9686780, EBI-11721746; Q06432; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-9686780, EBI-18053395; Q06432; O14880: MGST3; NbExp=3; IntAct=EBI-9686780, EBI-724754; Q06432; P15941-11: MUC1; NbExp=3; IntAct=EBI-9686780, EBI-17263240; Q06432; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-9686780, EBI-12382569; Q06432; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-9686780, EBI-7545592; Q06432; Q8WY91: THAP4; NbExp=3; IntAct=EBI-9686780, EBI-726691; Q06432; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-9686780, EBI-12947623; Q06432; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-9686780, EBI-3923061; Q06432; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-9686780, EBI-1059156; Q06432; A8KA83; NbExp=3; IntAct=EBI-9686780, EBI-10174961; Cell membrane, sarcolemma ; Multi-pass membrane protein Skeletal muscle. N-glycosylated. Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily. voltage-gated ion channel activity voltage-gated calcium channel activity calcium channel regulator activity calcium channel activity protein binding plasma membrane integral component of plasma membrane voltage-gated calcium channel complex ion transport calcium ion transport membrane integral component of membrane T-tubule regulation of ion transmembrane transport sarcolemma cardiac conduction sarcoplasmic reticulum calcium ion transport calcium ion transmembrane transport regulation of calcium ion transmembrane transport via high voltage-gated calcium channel L-type voltage-gated calcium channel complex uc002jfu.1 uc002jfu.2 uc002jfu.3 uc002jfu.4 uc002jfu.5 
ENST00000226067.10 HLF ENST00000226067.10 HLF transcription factor, PAR bZIP family member, transcript variant 1 (from RefSeq NM_002126.5) A8K1X8 ENST00000226067.1 ENST00000226067.2 ENST00000226067.3 ENST00000226067.4 ENST00000226067.5 ENST00000226067.6 ENST00000226067.7 ENST00000226067.8 ENST00000226067.9 HLF_HUMAN NM_002126 Q16534 Q6FHS9 uc002iug.1 uc002iug.2 uc002iug.3 This gene encodes a member of the proline and acidic-rich (PAR) protein family, a subset of the bZIP transcription factors. The encoded protein forms homodimers or heterodimers with other PAR family members and binds sequence-specific promoter elements to activate transcription. Chromosomal translocations fusing portions of this gene with the E2A gene cause a subset of childhood B-lineage acute lymphoid leukemias. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.43262.1, SRR1660809.156869.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226067.10/ ENSP00000226067.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Binds DNA specifically as homodimer or heterodimer with other PAR factors. Q16534; Q16520: BATF; NbExp=2; IntAct=EBI-2798854, EBI-749503; Q16534; Q9NR55: BATF3; NbExp=2; IntAct=EBI-2798854, EBI-10312707; Q16534; Q10586: DBP; NbExp=3; IntAct=EBI-2798854, EBI-3908088; Q16534; P35638: DDIT3; NbExp=3; IntAct=EBI-2798854, EBI-742651; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q16534-1; Sequence=Displayed; Name=2; IsoId=Q16534-2; Sequence=VSP_053852; Highly expressed in liver; lower levels in lung and kidney. Accumulates according to a robust circadian rhythm. Note=A chromosomal aberration involving HLF is a cause of pre- B-cell acute lymphoblastic leukemia (B-ALL). Translocation t(17;19)(q22;p13.3) with TCF3. Belongs to the bZIP family. PAR subfamily. Sequence=AAA58445.1; Type=Erroneous initiation; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/47/HLF"; nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding double-stranded DNA binding transcription factor activity, sequence-specific DNA binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter transcription from RNA polymerase II promoter multicellular organism development skeletal muscle cell differentiation sequence-specific DNA binding positive regulation of transcription from RNA polymerase II promoter rhythmic process uc002iug.1 uc002iug.2 uc002iug.3 
ENST00000226091.3 EFNB3 ENST00000226091.3 ephrin B3 (from RefSeq NM_001406.4) B2RBW2 D3DTQ6 EFNB3_HUMAN ENST00000226091.1 ENST00000226091.2 EPLG8 LERK8 NM_001406 O00680 Q15768 Q8TBH7 Q92875 uc002gis.1 uc002gis.2 uc002gis.3 uc002gis.4 uc002gis.5 EFNB3, a member of the ephrin gene family, is important in brain development as well as in its maintenance. Moreover, since levels of EFNB3 expression were particularly high in several forebrain subregions compared to other brain subregions, it may play a pivotal role in forebrain function. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH Receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are similarly divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC042944.2, U66406.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226091.3/ ENSP00000226091.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity). (Microbial infection) Acts as a receptor for nipah virus and hendra virus. Interacts with GRIP1 and GRIP2. (Microbial infection) Interacts with nipah virus and hendra virus glycoprotein (PubMed:16477309, PubMed:17376907). Q15768; P54764: EPHA4; NbExp=2; IntAct=EBI-3908475, EBI-5773557; Membrane; Single-pass type I membrane protein. Highly expressed in brain; expressed in embryonic floor plate, roof plate and hindbrain segments. Belongs to the ephrin family. virus receptor activity transmembrane-ephrin receptor activity protein binding plasma membrane integral component of plasma membrane cell-cell signaling multicellular organism development nervous system development axon guidance adult walking behavior membrane integral component of membrane viral process axon choice point recognition cell differentiation T cell costimulation viral entry into host cell ephrin receptor binding ephrin receptor signaling pathway negative regulation of axonogenesis glutamatergic synapse integral component of presynaptic membrane integral component of postsynaptic density membrane trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission uc002gis.1 uc002gis.2 uc002gis.3 uc002gis.4 uc002gis.5 
ENST00000226105.11 RANGRF ENST00000226105.11 RAN guanine nucleotide release factor, transcript variant 1 (from RefSeq NM_016492.5) D3DTR6 ENST00000226105.1 ENST00000226105.10 ENST00000226105.2 ENST00000226105.3 ENST00000226105.4 ENST00000226105.5 ENST00000226105.6 ENST00000226105.7 ENST00000226105.8 ENST00000226105.9 HSPC165 HSPC236 MDS5 MOG1 MOG1_HUMAN NM_016492 Q68DI3 Q9BR68 Q9HD47 Q9HD48 Q9NRU9 Q9P001 Q9P0P2 RANGNRF uc002gkv.1 uc002gkv.2 uc002gkv.3 uc002gkv.4 uc002gkv.5 This gene encodes a protein that has been shown to function as a guanine nucleotide release factor in mouse and to regulate the expression and function of the Nav1.5 cardiac sodium channel in human. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2010]. May regulate the intracellular trafficking of RAN (PubMed:11290418). Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1 (PubMed:29040603). Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics (PubMed:29040603). Enhances the expression of SCN5A at the cell membrane in cardiomyocytes (PubMed:18184654, PubMed:23420830, PubMed:21621375). Monomer. Interacts with RAN, both RAN-GTP and RAN-GDP (PubMed:11290418, PubMed:29040603). Competes with RCC1 for a common binding site on RAN and thereby inhibits RCC1-mediated nucleotide exchange (PubMed:29040603). Forms a complex with RAN-GTP and RANBP1 (By similarity). Interacts with the cytoplasmic loop 2 of SCN5A (PubMed:18184654). Q9HD47-3; P55212: CASP6; NbExp=3; IntAct=EBI-9089733, EBI-718729; Q9HD47-3; P41091: EIF2S3; NbExp=3; IntAct=EBI-9089733, EBI-1054228; Q9HD47-3; P22607: FGFR3; NbExp=3; IntAct=EBI-9089733, EBI-348399; Q9HD47-3; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-9089733, EBI-10226858; Q9HD47-3; P06396: GSN; NbExp=3; IntAct=EBI-9089733, EBI-351506; Q9HD47-3; P54652: HSPA2; NbExp=3; IntAct=EBI-9089733, EBI-356991; Q9HD47-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9089733, EBI-21591415; Q9HD47-3; P62826: RAN; NbExp=3; IntAct=EBI-9089733, EBI-286642; Nucleus Cytoplasm, perinuclear region Cytoplasm Cell membrane ; Peripheral membrane protein ; Cytoplasmic side Note=May shuttle between the nucleus and cytoplasm. Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=MOG1a; IsoId=Q9HD47-1; Sequence=Displayed; Name=2; Synonyms=MOG1b; IsoId=Q9HD47-2; Sequence=VSP_033060; Name=3; IsoId=Q9HD47-3; Sequence=VSP_033059, VSP_033061; Name=4; IsoId=Q9HD47-4; Sequence=VSP_033057, VSP_033058; Isoform 1 and isoform 2 are ubiquitously expressed (PubMed:11290418). Detected in heart and brain (PubMed:21621375). Overexpression can rescue the trafficking defect caused by some SCN5A mutations that impair trafficking to the cell membrane. Belongs to the MOG1 family. Sequence=AAF29129.1; Type=Frameshift; Evidence=; Sequence=AAF87316.1; Type=Frameshift; Evidence=; regulation of heart rate regulation of membrane depolarization guanyl-nucleotide exchange factor activity Ran guanyl-nucleotide exchange factor activity nucleus nucleoplasm cytoplasm rough endoplasmic reticulum cytosol plasma membrane caveola ER to Golgi vesicle-mediated transport Ran GTPase binding intercalated disc protein transport membrane sodium channel regulator activity protein exit from endoplasmic reticulum regulation of membrane potential ion channel binding perinuclear region of cytoplasm regulation of microtubule nucleation by Ran protein signal transduction regulation of bundle of His cell action potential regulation of cardiac muscle cell action potential involved in regulation of contraction regulation of membrane depolarization during cardiac muscle cell action potential regulation of sodium ion transmembrane transport positive regulation of protein localization to plasma membrane positive regulation of protein localization to cell surface regulation of sodium ion transmembrane transporter activity uc002gkv.1 uc002gkv.2 uc002gkv.3 uc002gkv.4 uc002gkv.5 
ENST00000226193.6 RCVRN ENST00000226193.6 recoverin (from RefSeq NM_002903.3) ENST00000226193.1 ENST00000226193.2 ENST00000226193.3 ENST00000226193.4 ENST00000226193.5 NM_002903 P35243 Q53XL0 RCV1 RECO_HUMAN uc002gme.1 uc002gme.2 uc002gme.3 This gene encodes a member of the recoverin family of neuronal calcium sensors. The encoded protein contains three calcium-binding EF-hand domains and may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin may be the antigen responsible for cancer-associated retinopathy. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AL712005.1, S43855.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226193.6/ ENSP00000226193.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as a calcium sensor and regulates phototransduction of cone and rod photoreceptor cells (By similarity). Modulates light sensitivity of cone photoreceptor in dark and dim conditions (By similarity). In response to high Ca(2+) levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by binding to and inhibiting GRK1-mediated phosphorylation of RHO/rhodopsin (By similarity). Plays a role in scotopic vision/enhances vision in dim light by enhancing signal transfer between rod photoreceptors and rod bipolar cells (By similarity). Improves rod photoreceptor sensitivity in dim light and mediates response of rod photoreceptors to facilitate detection of change and motion in bright light (By similarity). Homodimer; disulfide-linked (By similarity). Homodimerization is caused by prolonged intense illumination (By similarity). May form a complex composed of RHO, GRK1 and RCVRN in a Ca(2+)-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (By similarity). Interacts (via C-terminus) with GRK1 (via N-terminus); the interaction is Ca(2+)-dependent (By similarity). Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Photoreceptor outer segment membrane ; Lipid-anchor ; Cytoplasmic side Perikaryon Note=Primarily expressed in the inner segments of light-adapted rod photoreceptors, approximately 10% of which translocates from photoreceptor outer segments upon light stimulation (By similarity). Targeting of myristoylated protein to rod photoreceptor outer segments is calcium dependent (By similarity). Retina and pineal gland. EF-hand 2 and EF-hand 3 domains are the low-affinity and the high-affinity calcium binding sites, respectively. EF-hand 1 and EF- hand 4 domains do not bind calcium due to substitutions that disrupt their respective Ca(2+) binding loops. The cooperative binding of calcium to the EF-hand 2 domain following EF-hand 3 domain calcium binding requires myristoylation (By similarity). Calcium binding to the 2 EF-hand domains induces exposure of the myristoyl group through a protein conformation change, this process known as the calcium- myristoyl switch facilitates binding to photoreceptor cell membranes (By similarity). The N-terminal glycine is linked to one of four different types of acyl groups. The most abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present (By similarity). The Ca(2+) induced exposure of the myristoyl group, known as the calcium-myristoyl switch, promotes RCVRN binding to the photoreceptor cell membranes only when intracellular Ca(2+) concentration is high (By similarity). Oxidation on Cys-39 occurs in response to prolonged intense illumination and results in the formation of disulfide homodimers, and to a lesser extent disulfide-linked heterodimers. Belongs to the recoverin family. calcium ion binding signal transduction visual perception phototransduction calcium sensitive guanylate cyclase activator activity dendrite positive regulation of guanylate cyclase activity metal ion binding response to stimulus regulation of calcium ion transport uc002gme.1 uc002gme.2 uc002gme.3 
ENST00000226207.6 MYH1 ENST00000226207.6 myosin heavy chain 1 (from RefSeq NM_005963.4) ENST00000226207.1 ENST00000226207.2 ENST00000226207.3 ENST00000226207.4 ENST00000226207.5 MYH1_HUMAN NM_005963 P12882 Q14CA4 Q9Y622 uc002gmo.1 uc002gmo.2 uc002gmo.3 uc002gmo.4 uc002gmo.5 Myosin is a major contractile protein which converts chemical energy into mechanical energy through the hydrolysis of ATP. Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. Myosin heavy chains are encoded by a multigene family. In mammals at least 10 different myosin heavy chain (MYH) isoforms have been described from striated, smooth, and nonmuscle cells. These isoforms show expression that is spatially and temporally regulated during development. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## CDS exon combination :: AF111785.1, EU794637.1 [ECO:0000331] RNAseq introns :: mixed/partial sample support SAMEA1968540, SAMEA1968968 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226207.6/ ENSP00000226207.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Muscle contraction. Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). P12882; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-366238, EBI-11977221; P12882; A1A4E9: KRT13; NbExp=3; IntAct=EBI-366238, EBI-10171552; Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils. Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. Represents a conventional myosin. This protein should not be confused with the unconventional myosin-1 (MYO1). nucleotide binding motor activity actin binding protein binding calmodulin binding ATP binding cytoplasm muscle myosin complex muscle contraction intercalated disc myosin complex myofibril A band myosin filament cytoplasmic ribonucleoprotein granule actin filament binding uc002gmo.1 uc002gmo.2 uc002gmo.3 uc002gmo.4 uc002gmo.5 
ENST00000226218.9 VTN ENST00000226218.9 vitronectin (from RefSeq NM_000638.4) B2R7G0 ENST00000226218.1 ENST00000226218.2 ENST00000226218.3 ENST00000226218.4 ENST00000226218.5 ENST00000226218.6 ENST00000226218.7 ENST00000226218.8 NM_000638 P01141 P04004 Q9BSH7 VTNC_HUMAN uc002hbc.1 uc002hbc.2 uc002hbc.3 uc002hbc.4 uc002hbc.5 The protein encoded by this gene is a member of the pexin family. It is found in serum and tissues and promotes cell adhesion and spreading, inhibits the membrane-damaging effect of the terminal cytolytic complement pathway, and binds to several serpin serine protease inhibitors. It is a secreted protein and exists in either a single chain form or a clipped, two chain form held together by a disulfide bond. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189655.110316.1, SRR5189664.122025.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145122, SAMEA2155590 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226218.9/ ENSP00000226218.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1, insulin and C1QBP. (Microbial infection) Interacts (via hemopexin repeat 2) with P.falciparum (isolate CDC / Honduras) SERA5 P47 (via C-terminus); may form heterotetramers of two VTN and SERA5 P47 heterodimers; the interaction may protect merozoites from phagocytosis by host monocytes; VTN glycosylation appears to be dispensable for the interaction. P04004; Q07021: C1QBP; NbExp=9; IntAct=EBI-1036653, EBI-347528; P04004; Q15700: DLG2; NbExp=3; IntAct=EBI-1036653, EBI-80426; P04004; Q92796: DLG3; NbExp=3; IntAct=EBI-1036653, EBI-80440; P04004; Q9HD26: GOPC; NbExp=4; IntAct=EBI-1036653, EBI-349832; P04004; Q9HD26-2: GOPC; NbExp=3; IntAct=EBI-1036653, EBI-11102276; P04004; Q9NSN8: SNTG1; NbExp=3; IntAct=EBI-1036653, EBI-19763427; P04004; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1036653, EBI-947187; P04004; P75358: gapA; Xeno; NbExp=3; IntAct=EBI-1036653, EBI-2259469; P04004; P75167: gpmI; Xeno; NbExp=2; IntAct=EBI-1036653, EBI-2259565; P04004; P78007: ldh; Xeno; NbExp=3; IntAct=EBI-1036653, EBI-2260877; P04004; A0A024A2C9: lph; Xeno; NbExp=7; IntAct=EBI-1036653, EBI-12498321; P04004; P75390: pdhA; Xeno; NbExp=3; IntAct=EBI-1036653, EBI-2259629; P04004; P75391: pdhB; Xeno; NbExp=3; IntAct=EBI-1036653, EBI-2259621; P04004; P78031: pyk; Xeno; NbExp=3; IntAct=EBI-1036653, EBI-2259473; P04004; P75611: tkt; Xeno; NbExp=3; IntAct=EBI-1036653, EBI-12654979; P04004; Q4KTX9; Xeno; NbExp=12; IntAct=EBI-1036653, EBI-12501515; Secreted, extracellular space Parasitophorous vacuole Note=(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995). Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995). Expressed in the retina pigment epithelium (at protein level) (PubMed:25136834). Expressed in plasma (at protein level) (PubMed:2448300). Expressed in serum (at protein level) (PubMed:29567995). The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin. Sulfated on tyrosine residues. N- and O-glycosylated. Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both. Phosphorylation sites are present in the extracellular medium. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/vtn/"; scavenger receptor activity integrin binding extracellular matrix structural constituent protein binding collagen binding extracellular region basement membrane extracellular space cytoplasm endoplasmic reticulum Golgi lumen endocytosis immune response cell adhesion cell-matrix adhesion heparin binding cell proliferation positive regulation of cell-substrate adhesion negative regulation of endopeptidase activity positive regulation of smooth muscle cell migration cell migration negative regulation of blood coagulation extracellular matrix organization polysaccharide binding regulation of complement activation positive regulation of vascular endothelial growth factor receptor signaling pathway extracellular matrix positive regulation of protein binding cell adhesion mediated by integrin endodermal cell differentiation identical protein binding intracellular membrane-bounded organelle rough endoplasmic reticulum lumen positive regulation of receptor-mediated endocytosis oligodendrocyte differentiation positive regulation of peptidyl-tyrosine phosphorylation extracellular matrix binding protein polymerization smooth muscle cell-matrix adhesion extracellular exosome alphav-beta3 integrin-vitronectin complex blood microparticle positive regulation of wound healing liver regeneration uc002hbc.1 uc002hbc.2 uc002hbc.3 uc002hbc.4 uc002hbc.5 
ENST00000226225.7 TNFAIP1 ENST00000226225.7 TNF alpha induced protein 1 (from RefSeq NM_021137.5) B7Z6M4 BACD2_HUMAN BACURD2 EDP1 ENST00000226225.1 ENST00000226225.2 ENST00000226225.3 ENST00000226225.4 ENST00000226225.5 ENST00000226225.6 NM_021137 Q13829 Q5TZQ1 uc002hay.1 uc002hay.2 uc002hay.3 uc002hay.4 uc002hay.5 This gene was identified as a gene whose expression can be induced by the tumor necrosis factor alpha (TNF) in umbilical vein endothelial cells. Studies of a similar gene in mouse suggest that the expression of this gene is developmentally regulated in a tissue-specific manner. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC003694.2, SRR1803611.75799.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226225.7/ ENSP00000226225.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA- dependent DNA polymerase delta activity. Protein modification; protein ubiquitination. Component of the BCR(TNFAIP1) E3 ubiquitin ligase complex, at least composed of CUL3, TNFAIP1/BACURD2 and RBX1. Interacts with RHOA; with a preference for RhoA-GDP. Interacts with RHOB. Interacts with PCNA. Interacts with CSNK2B. Q13829; P02649: APOE; NbExp=3; IntAct=EBI-2505861, EBI-1222467; Q13829; Q9H6L4: ARMC7; NbExp=6; IntAct=EBI-2505861, EBI-742909; Q13829; P54253: ATXN1; NbExp=3; IntAct=EBI-2505861, EBI-930964; Q13829; Q7Z479: CAPN7; NbExp=3; IntAct=EBI-2505861, EBI-10213454; Q13829; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-2505861, EBI-1765641; Q13829; Q9H257: CARD9; NbExp=3; IntAct=EBI-2505861, EBI-751319; Q13829; Q16543: CDC37; NbExp=3; IntAct=EBI-2505861, EBI-295634; Q13829; Q13618: CUL3; NbExp=5; IntAct=EBI-2505861, EBI-456129; Q13829; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-2505861, EBI-6255981; Q13829; Q9NQT4: EXOSC5; NbExp=6; IntAct=EBI-2505861, EBI-371876; Q13829; P01100: FOS; NbExp=3; IntAct=EBI-2505861, EBI-852851; Q13829; P50440: GATM; NbExp=3; IntAct=EBI-2505861, EBI-2552594; Q13829; P14136: GFAP; NbExp=3; IntAct=EBI-2505861, EBI-744302; Q13829; P62993: GRB2; NbExp=3; IntAct=EBI-2505861, EBI-401755; Q13829; O14929: HAT1; NbExp=3; IntAct=EBI-2505861, EBI-2339359; Q13829; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-2505861, EBI-5460660; Q13829; P42858: HTT; NbExp=3; IntAct=EBI-2505861, EBI-466029; Q13829; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2505861, EBI-1055254; Q13829; Q9H3F6: KCTD10; NbExp=6; IntAct=EBI-2505861, EBI-2505886; Q13829; Q8WZ19: KCTD13; NbExp=11; IntAct=EBI-2505861, EBI-742916; Q13829; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2505861, EBI-739832; Q13829; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2505861, EBI-741158; Q13829; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-2505861, EBI-398874; Q13829; O15160: POLR1C; NbExp=9; IntAct=EBI-2505861, EBI-1055079; Q13829; P54619: PRKAG1; NbExp=3; IntAct=EBI-2505861, EBI-1181439; Q13829; P25786: PSMA1; NbExp=3; IntAct=EBI-2505861, EBI-359352; Q13829; P62745: RHOB; NbExp=5; IntAct=EBI-2505861, EBI-602647; Q13829; P00441: SOD1; NbExp=3; IntAct=EBI-2505861, EBI-990792; Q13829; P12931: SRC; NbExp=3; IntAct=EBI-2505861, EBI-621482; Q13829; O75716: STK16; NbExp=3; IntAct=EBI-2505861, EBI-749295; Q13829; Q13829: TNFAIP1; NbExp=4; IntAct=EBI-2505861, EBI-2505861; Q13829; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-2505861, EBI-746595; Cytoplasm. Nucleus. Endosome. Note=Colocalizes with RHOB in endosomes. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13829-1; Sequence=Displayed; Name=2; IsoId=Q13829-2; Sequence=VSP_056029; By TNF, IL1B/interleukin-1 beta and bacterial lipopolysaccharides (LPS). Phosphorylation at Ser-280 by CK2 facilitates the nucleus localization and increases interaction with PCNA. Belongs to the BACURD family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/tnfaip1/"; protein binding nucleus nucleolus cytoplasm endosome DNA replication apoptotic process immune response cell migration protein ubiquitination GTP-Rho binding protein domain specific binding Cul3-RING ubiquitin ligase complex negative regulation of Rho protein signal transduction identical protein binding stress fiber assembly proteasome-mediated ubiquitin-dependent protein catabolic process positive regulation of DNA replication protein homooligomerization ubiquitin-protein transferase activity uc002hay.1 uc002hay.2 uc002hay.3 uc002hay.4 uc002hay.5 
ENST00000226230.8 TMEM97 ENST00000226230.8 transmembrane protein 97 (from RefSeq NM_014573.3) B4DS02 ENST00000226230.1 ENST00000226230.2 ENST00000226230.3 ENST00000226230.4 ENST00000226230.5 ENST00000226230.6 ENST00000226230.7 MAC30 NM_014573 Q07823 Q5BJF2 S2R SGMR2_HUMAN TMEM97 uc002hat.1 uc002hat.2 uc002hat.3 uc002hat.4 TMEM97 is a conserved integral membrane protein that plays a role in controlling cellular cholesterol levels (Bartz et al., 2009 [PubMed 19583955]).[supplied by OMIM, Aug 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.97499.1, SRR5189661.190685.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226230.8/ ENSP00000226230.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Intracellular sigma-2 receptor that binds histatin 1/HN1 (Hst 1) at the endoplasmic reticulun (ER) membrane, which is critical for mitochondrial-targeting and -activating properties of Hst1 (PubMed:34233061, PubMed:35970844). Thought to play important role in regulating cell survival, morphology and differentiation (PubMed:23922215, PubMed:25620095). May play a role as a regulator of cellular cholesterol homeostasis (PubMed:19583955). May function as sterol isomerase (PubMed:25566323). May alter the activity of some cytochrome P450 proteins (PubMed:22292588). Interacts with histatin 1/HTN1; the interaction induces HTN1- stimulating wound healing (PubMed:34233061). Interacts with NPC1. Q5BJF2; A6NM10-2: AQP12B; NbExp=3; IntAct=EBI-12111910, EBI-17265552; Q5BJF2; P41181: AQP2; NbExp=3; IntAct=EBI-12111910, EBI-12701138; Q5BJF2; Q13520: AQP6; NbExp=3; IntAct=EBI-12111910, EBI-13059134; Q5BJF2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12111910, EBI-11343438; Q5BJF2; Q8WWH4: ASZ1; NbExp=3; IntAct=EBI-12111910, EBI-12239061; Q5BJF2; O75787: ATP6AP2; NbExp=3; IntAct=EBI-12111910, EBI-2512037; Q5BJF2; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-12111910, EBI-747430; Q5BJF2; Q13323: BIK; NbExp=3; IntAct=EBI-12111910, EBI-700794; Q5BJF2; P19397: CD53; NbExp=3; IntAct=EBI-12111910, EBI-6657396; Q5BJF2; P04233-2: CD74; NbExp=3; IntAct=EBI-12111910, EBI-12222807; Q5BJF2; Q99675: CGRRF1; NbExp=3; IntAct=EBI-12111910, EBI-2130213; Q5BJF2; O95471: CLDN7; NbExp=3; IntAct=EBI-12111910, EBI-740744; Q5BJF2; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-12111910, EBI-11291074; Q5BJF2; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-12111910, EBI-18013275; Q5BJF2; Q15125: EBP; NbExp=3; IntAct=EBI-12111910, EBI-3915253; Q5BJF2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12111910, EBI-781551; Q5BJF2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12111910, EBI-18304435; Q5BJF2; O15552: FFAR2; NbExp=3; IntAct=EBI-12111910, EBI-2833872; Q5BJF2; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-12111910, EBI-3918971; Q5BJF2; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-12111910, EBI-6911547; Q5BJF2; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-12111910, EBI-12175685; Q5BJF2; O75712: GJB3; NbExp=3; IntAct=EBI-12111910, EBI-3908586; Q5BJF2; O95377: GJB5; NbExp=3; IntAct=EBI-12111910, EBI-3909454; Q5BJF2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12111910, EBI-13345167; Q5BJF2; O60883: GPR37L1; NbExp=3; IntAct=EBI-12111910, EBI-2927498; Q5BJF2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12111910, EBI-11721746; Q5BJF2; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-12111910, EBI-18053395; Q5BJF2; P38484: IFNGR2; NbExp=3; IntAct=EBI-12111910, EBI-3905457; Q5BJF2; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12111910, EBI-8632435; Q5BJF2; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12111910, EBI-17490413; Q5BJF2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12111910, EBI-2820517; Q5BJF2; Q9H400: LIME1; NbExp=3; IntAct=EBI-12111910, EBI-2830566; Q5BJF2; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-12111910, EBI-358888; Q5BJF2; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12111910, EBI-11956541; Q5BJF2; Q6IN84: MRM1; NbExp=3; IntAct=EBI-12111910, EBI-5454865; Q5BJF2; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-12111910, EBI-3923617; Q5BJF2; P15941-11: MUC1; NbExp=3; IntAct=EBI-12111910, EBI-17263240; Q5BJF2; Q9Y375: NDUFAF1; NbExp=3; IntAct=EBI-12111910, EBI-741874; Q5BJF2; Q8N183: NDUFAF2; NbExp=3; IntAct=EBI-12111910, EBI-2682365; Q5BJF2; O14524-2: NEMP1; NbExp=3; IntAct=EBI-12111910, EBI-10969203; Q5BJF2; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-12111910, EBI-16427978; Q5BJF2; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12111910, EBI-716063; Q5BJF2; P60201-2: PLP1; NbExp=3; IntAct=EBI-12111910, EBI-12188331; Q5BJF2; Q9H902: REEP1; NbExp=3; IntAct=EBI-12111910, EBI-1644241; Q5BJF2; Q9UBD6: RHCG; NbExp=3; IntAct=EBI-12111910, EBI-15853497; Q5BJF2; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-12111910, EBI-12055631; Q5BJF2; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-12111910, EBI-3920694; Q5BJF2; O95470: SGPL1; NbExp=3; IntAct=EBI-12111910, EBI-1046170; Q5BJF2; Q13336-2: SLC14A1; NbExp=3; IntAct=EBI-12111910, EBI-19141793; Q5BJF2; Q15849: SLC14A2; NbExp=4; IntAct=EBI-12111910, EBI-1573290; Q5BJF2; O43278-2: SPINT1; NbExp=3; IntAct=EBI-12111910, EBI-12078338; Q5BJF2; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12111910, EBI-17280858; Q5BJF2; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-12111910, EBI-2821497; Q5BJF2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12111910, EBI-8638294; Q5BJF2; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-12111910, EBI-3923061; Q5BJF2; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12111910, EBI-18178701; Q5BJF2; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-12111910, EBI-8649725; Q5BJF2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12111910, EBI-6447886; Q5BJF2; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-12111910, EBI-744988; Nucleus membrane ; Multi-pass membrane protein Rough endoplasmic reticulum membrane ; Multi-pass membrane protein Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. Widely expressed in normal tissues. Expressed in pancreatic, renal, breast, colon, ovarian surface epithelial (OSE) cells. Highly expressed in various proliferating cancer cells (PubMed:23922215). Up-regulated in ovarian surface epithelial (OSE) cells with progesterone. Binds numerous drugs and highly expressed in various proliferating cancer cells (PubMed:28559337). Under investigation for its potential diagnostic and therapeutic uses (PubMed:23922215, PubMed:25620095). Sigma receptors are classified into two subtypes (Sigma- 1 and Sigma-2) based on their different pharmacological profile. Sigma- 2 receptors are identified by radioligand-binding studies as a binding site with high affinity for di-o-tolylguanidine (DTG) and haloperidol. Potentially useful for cancer diagnostics or as target for anticancer therapeutics or adjuvant anticancer treatment agents (PubMed:23922215). Some exogenous ligands display a neuroprotective effect (PubMed:25620095). Belongs to the TMEM97/sigma-2 receptor family. The molecular identity of the sigma-2 receptor has been unclear for a long time. It is now identified as TMEM97 (PubMed:28559337). Previously identified as PGRMC1 (AC O00264) (PubMed:22292588, PubMed:28007569). Sequence=AAA16188.1; Type=Frameshift; Evidence=; regulation of cell growth protein binding nucleus lysosome endoplasmic reticulum rough endoplasmic reticulum cytosol plasma membrane membrane integral component of membrane rough endoplasmic reticulum membrane nuclear membrane cholesterol homeostasis uc002hat.1 uc002hat.2 uc002hat.3 uc002hat.4 
ENST00000226253.9 ALDOC ENST00000226253.9 aldolase, fructose-bisphosphate C (from RefSeq NM_005165.3) ALDC ALDOC_HUMAN B2R5R3 ENST00000226253.1 ENST00000226253.2 ENST00000226253.3 ENST00000226253.4 ENST00000226253.5 ENST00000226253.6 ENST00000226253.7 ENST00000226253.8 NM_005165 P09972 Q3SYL3 Q6FH94 Q6P0L5 uc002hbp.1 uc002hbp.2 uc002hbp.3 uc002hbp.4 uc002hbp.5 This gene encodes a member of the class I fructose-biphosphate aldolase gene family. Expressed specifically in the hippocampus and Purkinje cells of the brain, the encoded protein is a glycolytic enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehyde, respectively. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.124528.1, SRR3476690.1069107.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142586, SAMEA2146236 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226253.9/ ENSP00000226253.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence=; Kinetic parameters: KM=10.7 uM for fructose 1,6-bisphosphate ; KM=16 mM for fructose 1-phosphate ; Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 4/4. Homotetramer. Interacts with ATP6V1E1. May interact with PLD2. P09972; P04075: ALDOA; NbExp=3; IntAct=EBI-2952751, EBI-709613; P09972; P04075-2: ALDOA; NbExp=6; IntAct=EBI-2952751, EBI-10194102; P09972; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-2952751, EBI-11954519; P09972; P13569: CFTR; NbExp=8; IntAct=EBI-2952751, EBI-349854; P09972; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-2952751, EBI-739832; In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain. Belongs to the class I fructose-bisphosphate aldolase family. Sequence=AAI03761.1; Type=Erroneous initiation; Evidence=; catalytic activity fructose-bisphosphate aldolase activity protein binding extracellular region cytosol cytoskeleton fructose metabolic process gluconeogenesis glycolytic process cytoskeletal protein binding lyase activity fructose 1,6-bisphosphate metabolic process epithelial cell differentiation secretory granule lumen neutrophil degranulation canonical glycolysis extracellular exosome tertiary granule lumen ficolin-1-rich granule lumen uc002hbp.1 uc002hbp.2 uc002hbp.3 uc002hbp.4 uc002hbp.5 
ENST00000226279.8 CD38 ENST00000226279.8 CD38 molecule, transcript variant 2 (from RefSeq NR_132660.2) CD38_HUMAN ENST00000226279.1 ENST00000226279.2 ENST00000226279.3 ENST00000226279.4 ENST00000226279.5 ENST00000226279.6 ENST00000226279.7 NR_132660 O00121 O00122 P28907 Q96HY4 uc003gol.1 uc003gol.2 uc003gol.3 The protein encoded by this gene is a non-lineage-restricted, type II transmembrane glycoprotein that synthesizes and hydrolyzes cyclic adenosine 5'-diphosphate-ribose, an intracellular calcium ion mobilizing messenger. The release of soluble protein and the ability of membrane-bound protein to become internalized indicate both extracellular and intracellular functions for the protein. This protein has an N-terminal cytoplasmic tail, a single membrane-spanning domain, and a C-terminal extracellular region with four N-glycosylation sites. Crystal structure analysis demonstrates that the functional molecule is a dimer, with the central portion containing the catalytic site. It is used as a prognostic marker for patients with chronic lymphocytic leukemia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]. Synthesizes cyclic ADP-ribose (cADPR), a second messenger for glucose-induced insulin secretion (PubMed:8253715, PubMed:7961800). Synthesizes the Ca(2+) mobilizer nicotinate-adenine dinucleotide phosphate, NAADP(+), from 2'-phospho-cADPR and nicotinic acid, as well as from NADP(+) and nicotinic acid. At both pH 5.0 and pH 7.4 preferentially transforms 2'-phospho-cADPR into NAADP(+), while preferentially cleaving NADP(+) to cADPR and ADPRP rather than into NADDP(+) (PubMed:16690024). Has cADPR hydrolase activity (PubMed:8253715, PubMed:7961800). Reaction=2'-phospho-cyclic ADP-ribose + nicotinate = nicotinate-adenine dinucleotide phosphate; Xref=Rhea:RHEA:38607, ChEBI:CHEBI:32544, ChEBI:CHEBI:75967, ChEBI:CHEBI:75970; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38608; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38609; Evidence=; Reaction=NAD(+) = cyclic ADP-beta-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:73672; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38612; Evidence=; Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence=; Reaction=cyclic ADP-beta-D-ribose + H2O = ADP-D-ribose; Xref=Rhea:RHEA:38615, ChEBI:CHEBI:15377, ChEBI:CHEBI:57967, ChEBI:CHEBI:73672; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38616; Evidence=; Reaction=NADP(+) = 2'-phospho-cyclic ADP-ribose + nicotinamide; Xref=Rhea:RHEA:38603, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:75970; Evidence=; Reaction=NADP(+) + nicotinate = nicotinamide + nicotinate-adenine dinucleotide phosphate; Xref=Rhea:RHEA:38599, ChEBI:CHEBI:17154, ChEBI:CHEBI:32544, ChEBI:CHEBI:58349, ChEBI:CHEBI:75967; EC=2.4.99.20; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38600; Evidence=; ATP inhibits the cADPR hydrolyzing activity. pH dependence: Optimum pH for NAADP(+) production is 5.0 from either substrate, activity is much higher at pH 5.0 than 7.4. ; Homodimer. Cell surface Membrane ; Single-pass type II membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P28907-1; Sequence=Displayed; Name=2; IsoId=P28907-2; Sequence=VSP_000707, VSP_000708; Expressed at high levels in pancreas, liver, kidney, brain, testis, ovary, placenta, malignant lymphoma and neuroblastoma. Preferentially expressed at both early and late stages of the B and T-cell maturation. It is also detected on erythroid and myeloid progenitors in bone marrow, where the level of surface expression was shown to decrease during differentiation of blast- forming unit E to colony-forming unit E. A cell surface antigen recognized in lymophocytes by multiple mAbs. [Isoform 2]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the ADP-ribosyl cyclase family. Name=Wikipedia; Note=CD38 entry; URL="https://en.wikipedia.org/wiki/CD38"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/978/CD38"; response to hypoxia NAD+ nucleosidase activity nucleus plasma membrane signal transduction positive regulation of cytosolic calcium ion concentration female pregnancy positive regulation of cell proliferation response to hormone cell surface negative regulation of neuron projection development artery smooth muscle contraction membrane integral component of membrane basolateral plasma membrane transferase activity hydrolase activity hydrolase activity, acting on glycosyl bonds phosphorus-oxygen lyase activity NAD metabolic process positive regulation of cell growth secretory granule membrane positive regulation of B cell proliferation positive regulation of insulin secretion response to estradiol response to retinoic acid response to progesterone response to hydroperoxide response to cytokine response to drug identical protein binding negative regulation of apoptotic process intracellular membrane-bounded organelle negative regulation of bone resorption negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of vasoconstriction NAD(P)+ nucleosidase activity B cell receptor signaling pathway long term synaptic depression NAD+ nucleotidase, cyclic ADP-ribose generating extracellular exosome response to interleukin-1 apoptotic signaling pathway uc003gol.1 uc003gol.2 uc003gol.3 
ENST00000226284.7 IBSP ENST00000226284.7 integrin binding sialoprotein (from RefSeq NM_004967.4) BNSP ENST00000226284.1 ENST00000226284.2 ENST00000226284.3 ENST00000226284.4 ENST00000226284.5 ENST00000226284.6 NM_004967 P21815 SIAL_HUMAN uc003hqx.1 uc003hqx.2 uc003hqx.3 uc003hqx.4 uc003hqx.5 uc003hqx.6 The protein encoded by this gene is a major structural protein of the bone matrix. It constitutes approximately 12% of the noncollagenous proteins in human bone and is synthesized by skeletal-associated cell types, including hypertrophic chondrocytes, osteoblasts, osteocytes, and osteoclasts. The only extraskeletal site of its synthesis is the trophoblast. This protein binds to calcium and hydroxyapatite via its acidic amino acid clusters, and mediates cell attachment through an RGD sequence that recognizes the vitronectin receptor. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660805.193979.1, SRR1660807.136311.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145743, SAMEA2153307 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226284.7/ ENSP00000226284.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment. P21815; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-18400392, EBI-10175124; P21815; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-18400392, EBI-12175685; Secreted. N-glycosylated; glycans consist of sialylated and core-fucosylated bi-, tri- and tetraantennary chains. O-glycosylated at eight sites; mucin-type glycans contain Gal, GlcNAc, GalNAc and terminal NeuAc. Sulfated on either Tyr-313 or Tyr-314. It is possible that the segments of clustered carboxyl groups mediate the strong binding to hydroxyapatite. ossification osteoblast differentiation molecular_function integrin binding extracellular region extracellular space cell adhesion membrane extracellular matrix organization bone mineralization biomineral tissue development vesicle positive regulation of cell adhesion cellular response to growth factor stimulus uc003hqx.1 uc003hqx.2 uc003hqx.3 uc003hqx.4 uc003hqx.5 uc003hqx.6 
ENST00000226299.9 LAP3 ENST00000226299.9 leucine aminopeptidase 3 (from RefSeq NM_015907.3) AMPL_HUMAN B3KMQ3 ENST00000226299.1 ENST00000226299.2 ENST00000226299.3 ENST00000226299.4 ENST00000226299.5 ENST00000226299.6 ENST00000226299.7 ENST00000226299.8 LAP3 LAPEP NM_015907 P28838 PEPS Q6IAM6 Q6P0L6 Q9UQE3 uc062vle.1 uc062vle.2 Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S- conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status. Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence=; Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103; EC=3.4.13.23; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445; Evidence=; Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine; Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235, ChEBI:CHEBI:57305, ChEBI:CHEBI:61694; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784; Evidence=; Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L- cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:145802, ChEBI:CHEBI:145803; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569; Evidence=; Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Binds two metal ions per subunit. Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals: site 1 is occupied by Zn(2+), Mn(2+), Mg(2+) or Co(2+), while the tight binding site 2 can be occupied by only Zn(2+) or Co(2+). One Zn(2+) ion is tightly bound to site 2 and essential for enzyme activity in vivo, while site 1 can be occupied by different metals to give different enzymatic activities. Mn(2+) is required for Cys-Gly hydrolysis activity. A third metal binding site may serve a structural role, possibly stabilizing part of the interface between the N-terminal and the catalytic domain. ; Homohexamer. P28838; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-2339312, EBI-11524452; P28838; Q13185: CBX3; NbExp=6; IntAct=EBI-2339312, EBI-78176; P28838; P45973: CBX5; NbExp=3; IntAct=EBI-2339312, EBI-78219; P28838; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-2339312, EBI-726739; P28838; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-2339312, EBI-10232538; P28838; Q92569: PIK3R3; NbExp=3; IntAct=EBI-2339312, EBI-79893; P28838; P22415: USF1; NbExp=3; IntAct=EBI-2339312, EBI-1054489; P28838; P36508: ZNF76; NbExp=3; IntAct=EBI-2339312, EBI-7254550; P28838; Q15942: ZYX; NbExp=3; IntAct=EBI-2339312, EBI-444225; P28838; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-2339312, EBI-25492395; Cytoplasm Event=Alternative initiation; Named isoforms=2; Name=1; IsoId=P28838-1; Sequence=Displayed; Name=2; IsoId=P28838-2; Sequence=VSP_022631; Belongs to the peptidase M17 family. aminopeptidase activity nucleus nucleoplasm cytoplasm trans-Golgi network cytosol focal adhesion proteolysis peptidase activity metalloexopeptidase activity hydrolase activity protein metabolic process manganese ion binding midbody metal ion binding extracellular exosome uc062vle.1 uc062vle.2 
ENST00000226317.10 CXCL6 ENST00000226317.10 C-X-C motif chemokine ligand 6 (from RefSeq NM_002993.4) B2R4X3 CXCL6_HUMAN ENST00000226317.1 ENST00000226317.2 ENST00000226317.3 ENST00000226317.4 ENST00000226317.5 ENST00000226317.6 ENST00000226317.7 ENST00000226317.8 ENST00000226317.9 GCP2 NM_002993 P80162 Q4W5D4 SCYB6 uc003hhf.1 uc003hhf.2 uc003hhf.3 uc003hhf.4 uc003hhf.5 The protein encoded by this gene is a member CXC chemokine family. The encoded protein is a chemotactic for neutrophil granulocytes and has antibacterial action against gram-negative and gram-positive bacteria. This gene and other members of the CXC chemokine gene family form a gene cluster in a region of chromosome 4q. [provided by RefSeq, Jun 2020]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U81234.1, ERR279869.1807.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226317.10/ ENSP00000226317.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Chemotactic for neutrophil granulocytes. Signals through binding and activation of its receptors (CXCR1 and CXCR2). In addition to its chemotactic and angiogenic properties, it has strong antibacterial activity against Gram-positive and Gram-negative bacteria (90-fold-higher when compared to CXCL5 and CXCL7). P80162; P13501: CCL5; NbExp=2; IntAct=EBI-9214033, EBI-2848366; P80162; P48061: CXCL12; NbExp=2; IntAct=EBI-9214033, EBI-3913254; P80162; P02776: PF4; NbExp=2; IntAct=EBI-9214033, EBI-2565740; Secreted. Belongs to the intercrine alpha (chemokine CxC) family. Name=Wikipedia; Note=CXCL6 entry; URL="https://en.wikipedia.org/wiki/CXCL6"; leukocyte homeostasis cytokine activity protein binding extracellular region extracellular space chemotaxis defense response inflammatory response immune response signal transduction G-protein coupled receptor signaling pathway cell-cell signaling chemokine activity heparin binding neutrophil chemotaxis leukocyte chemotaxis response to lipopolysaccharide regulation of chemokine production neutrophil activation defense response to bacterium chemokine-mediated signaling pathway regulation of neutrophil mediated killing of gram-negative bacterium cellular response to lipopolysaccharide uc003hhf.1 uc003hhf.2 uc003hhf.3 uc003hhf.4 uc003hhf.5 
ENST00000226319.11 JADE1 ENST00000226319.11 jade family PHD finger 1, transcript variant 1 (from RefSeq NM_199320.4) D3DNY0 D3DNY1 ENST00000226319.1 ENST00000226319.10 ENST00000226319.2 ENST00000226319.3 ENST00000226319.4 ENST00000226319.5 ENST00000226319.6 ENST00000226319.7 ENST00000226319.8 ENST00000226319.9 JADE1_HUMAN KIAA1807 NM_199320 PHF17 Q4W5D5 Q6IE81 Q6ZSL7 Q8NC41 Q96JL8 Q96SQ1 Q9H692 uc003igk.1 uc003igk.2 uc003igk.3 uc003igk.4 uc003igk.5 Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity (PubMed:16387653, PubMed:19187766, PubMed:20129055, PubMed:24065767). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac), regulating DNA replication initiation, regulating DNA replication initiation (PubMed:20129055, PubMed:24065767). May also promote acetylation of nucleosomal histone H4 by KAT5 (PubMed:15502158). Promotes apoptosis (PubMed:16046545). May act as a renal tumor suppressor (PubMed:16046545). Negatively regulates canonical Wnt signaling; at least in part, cooperates with NPHP4 in this function (PubMed:22654112). Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3 (PubMed:16387653, PubMed:19187766, PubMed:20129055, PubMed:24065767, PubMed:29382722). Interacts with NPHP4 (PubMed:22654112). [Isoform 3]: Interacts with VHL and KAT5 (PubMed:12169691, PubMed:15502158). Does not associate with ING4 or ING5, and does not act as a component of the HBO1 complex (PubMed:19187766). Q6IE81; O95251: KAT7; NbExp=2; IntAct=EBI-954672, EBI-473199; Q6IE81; O75161: NPHP4; NbExp=4; IntAct=EBI-954672, EBI-4281852; Q6IE81; Q9BW85: YJU2; NbExp=3; IntAct=EBI-954672, EBI-10300345; Q6IE81-3; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12120084, EBI-748974; Q6IE81-3; Q9BW85: YJU2; NbExp=3; IntAct=EBI-12120084, EBI-10300345; Q6IE81-3; Q9UQR1-2: ZNF148; NbExp=3; IntAct=EBI-12120084, EBI-11742222; Nucleus romosome Cytoplasm Cytoplasm, cytoskeleton, cilium basal body Note=Localizes to the ciliary transition zone. Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=JADE1L; IsoId=Q6IE81-1; Sequence=Displayed; Name=2; IsoId=Q6IE81-2; Sequence=VSP_021045; Name=3; Synonyms=JADE1S; IsoId=Q6IE81-3; Sequence=VSP_021046, VSP_021047; Highly expressed in kidney. Also present in pancreas, liver and heart (at protein level). Down-regulated in renal cancer cells. The 2 PHD-type zinc fingers are required for transcriptional activity. Belongs to the JADE family. Sequence=BAB15371.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAC11335.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; histone acetyltransferase complex transcription coactivator activity protein binding nucleus nucleoplasm cytoplasm cytosol cytoskeleton plasma membrane apoptotic process nuclear speck negative regulation of cell growth ciliary basal body cell projection histone H3 acetylation histone H4-K5 acetylation histone H4-K8 acetylation histone H4-K12 acetylation metal ion binding negative regulation of canonical Wnt signaling pathway positive regulation of nucleic acid-templated transcription negative regulation of G1/S transition of mitotic cell cycle histone H4-K16 acetylation uc003igk.1 uc003igk.2 uc003igk.3 uc003igk.4 uc003igk.5 
ENST00000226355.5 AFM ENST00000226355.5 afamin (from RefSeq NM_001133.2) A8K3E1 AFAM_HUMAN ALB2 ALBA ENST00000226355.1 ENST00000226355.2 ENST00000226355.3 ENST00000226355.4 NM_001133 P43652 Q32MR3 Q4W5C5 uc003hhb.1 uc003hhb.2 uc003hhb.3 uc003hhb.4 uc003hhb.5 This gene is a member of the albumin gene family, which is comprised of four genes that localize to chromosome 4 in a tandem arrangement. These four genes encode structurally-related serum transport proteins that are known to be evolutionarily related. The protein encoded by this gene is regulated developmentally, expressed in the liver and secreted into the bloodstream. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK290556.1, BC109020.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1970526, SAMEA2145122 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226355.5/ ENSP00000226355.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Functions as a carrier for hydrophobic molecules in body fluids (Probable). Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (PubMed:26902720). Binds vitamin E (PubMed:15952736, PubMed:12463752). May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient (PubMed:15952736). May be involved in the transport of vitamin E across the blood-brain barrier (PubMed:19046407). Forms a 1:1 complex with Wnt family members; interacts with WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B. P43652; P56703: WNT3; NbExp=3; IntAct=EBI-20737924, EBI-3644922; P43652; P27467: Wnt3a; Xeno; NbExp=3; IntAct=EBI-20737924, EBI-2899665; Secreted High level detected in plasma but also in extravascular fluids such as follicular and cerebrospinal fluids (at protein level). The second albumin domain forms a deep binding pocket that contains palmitoleic acid (in vitro) (PubMed:29153507). Palmitoleic acid is most likely not the physiological ligand. Instead, this pocket may accomodate the covalently bound lipid moiety of Wnt family members (Probable). N-glycosylated; more than 90% of the glycans are sialylated. Belongs to the ALB/AFP/VDB family. fatty acid binding protein binding extracellular region extracellular space cytoplasm zinc ion binding vitamin E binding protein transport protein stabilization vitamin transport extracellular exosome protein transport within extracellular region blood microparticle uc003hhb.1 uc003hhb.2 uc003hhb.3 uc003hhb.4 uc003hhb.5 
ENST00000226382.4 PHOX2B ENST00000226382.4 paired like homeobox 2B (from RefSeq NM_003924.4) ENST00000226382.1 ENST00000226382.2 ENST00000226382.3 NM_003924 PHX2B_HUMAN PMX2B Q6PJD9 Q99453 uc003gwf.1 uc003gwf.2 uc003gwf.3 uc003gwf.4 uc003gwf.5 The DNA-associated protein encoded by this gene is a member of the paired family of homeobox proteins localized to the nucleus. The protein functions as a transcription factor involved in the development of several major noradrenergic neuron populations and the determination of neurotransmitter phenotype. The gene product is linked to enhancement of second messenger-mediated activation of the dopamine beta-hydroylase, c-fos promoters and several enhancers, including cyclic amp-response element and serum-response element. Expansion of a 20 amino acid polyalanine tract in this protein by 5-13 aa has been associated with congenital central hypoventilation syndrome. [provided by RefSeq, Jul 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by transcript alignments and orthologous data. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: D82344.1, BC017199.2 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226382.4/ ENSP00000226382.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Involved in the development of several major noradrenergic neuron populations, including the locus coeruleus. Transcription factor which could determine a neurotransmitter phenotype in vertebrates. Enhances second-messenger-mediated activation of the dopamine beta- hydrolase and c-fos promoters, and of several enhancers including cAMP- response element and serum-response element. Interacts with TRIM11. Nucleus Expressed in neuroblastoma, brain and adrenal gland. Central hypoventilation syndrome, congenital, 1 (CCHS1) [MIM:209880]: An autosomal dominant form of congenital central hypoventilation syndrome, a rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. te=The disease is caused by variants affecting the gene represented in this entry. Neuroblastoma 2 (NBLST2) [MIM:613013]: A common neoplasm of early childhood arising from embryonic cells that form the primitive neural crest and give rise to the adrenal medulla and the sympathetic nervous system. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the paired homeobox family. nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding neuron migration regulation of respiratory gaseous exchange by neurological system process noradrenergic neuron differentiation noradrenergic neuron development brainstem development DNA binding nucleus nucleoplasm regulation of transcription, DNA-templated multicellular organism development nervous system development negative regulation of cell proliferation glial cell differentiation regulation of gene expression positive regulation of G2/M transition of mitotic cell cycle cell differentiation in hindbrain medullary reticular formation development hindbrain tangential cell migration neuron differentiation skeletal muscle cell differentiation sequence-specific DNA binding negative regulation of neuron differentiation positive regulation of neuron differentiation positive regulation of transcription from RNA polymerase II promoter cell development autonomic nervous system development enteric nervous system development sympathetic nervous system development parasympathetic nervous system development inner ear development efferent axon development in a lateral line nerve respiratory system development retrotrapezoid nucleus neuron differentiation sympathetic ganglion development negative regulation of cell cycle arrest dopaminergic neuron differentiation cellular response to BMP stimulus neural crest cell migration involved in autonomic nervous system development uc003gwf.1 uc003gwf.2 uc003gwf.3 uc003gwf.4 uc003gwf.5 
ENST00000226413.5 GNRHR ENST00000226413.5 gonadotropin releasing hormone receptor, transcript variant 1 (from RefSeq NM_000406.3) ENST00000226413.1 ENST00000226413.2 ENST00000226413.3 ENST00000226413.4 GNRHR_HUMAN GRHR NM_000406 O75793 P30968 Q14D13 Q92644 uc003hdn.1 uc003hdn.2 uc003hdn.3 uc003hdn.4 uc003hdn.5 This gene encodes the receptor for type 1 gonadotropin-releasing hormone. This receptor is a member of the seven-transmembrane, G-protein coupled receptor (GPCR) family. It is expressed on the surface of pituitary gonadotrope cells as well as lymphocytes, breast, ovary, and prostate. Following binding of gonadotropin-releasing hormone, the receptor associates with G-proteins that activate a phosphatidylinositol-calcium second messenger system. Activation of the receptor ultimately causes the release of gonadotropic luteinizing hormone (LH) and follicle stimulating hormone (FSH). Defects in this gene are a cause of hypogonadotropic hypogonadism (HH). Alternative splicing results in multiple transcript variants encoding different isoforms. More than 18 transcription initiation sites in the 5' region and multiple polyA signals in the 3' region have been identified for this gene. [provided by RefSeq, Jul 2008]. Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G- proteins that activate a phosphatidylinositol-calcium second messenger system. Isoform 2 may act as an inhibitor of GnRH-R signaling. Cell membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P30968-1; Sequence=Displayed; Name=2; Synonyms=Truncated; IsoId=P30968-2; Sequence=VSP_001914; Pituitary, ovary, testis, breast and prostate but not in liver and spleen. Hypogonadotropic hypogonadism 7 with or without anosmia (HH7) [MIM:146110]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. In some cases, it is associated with non-reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). te=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in GNRHR as well as in other HH-associated genes including FGFR1 (PubMed:23643382). Belongs to the G-protein coupled receptor 1 family. G-protein coupled receptor activity gonadotropin-releasing hormone receptor activity plasma membrane integral component of plasma membrane signal transduction G-protein coupled receptor signaling pathway multicellular organism development membrane integral component of membrane protein-hormone receptor activity cellular response to hormone stimulus cellular response to gonadotropin-releasing hormone uc003hdn.1 uc003hdn.2 uc003hdn.3 uc003hdn.4 uc003hdn.5 
ENST00000226432.9 CWH43 ENST00000226432.9 cell wall biogenesis 43 C-terminal homolog, transcript variant 1 (from RefSeq NM_025087.3) B2RPD7 ENST00000226432.1 ENST00000226432.2 ENST00000226432.3 ENST00000226432.4 ENST00000226432.5 ENST00000226432.6 ENST00000226432.7 ENST00000226432.8 NM_025087 PG2IP_HUMAN PGAP2IP Q9H720 uc003gyv.1 uc003gyv.2 uc003gyv.3 uc003gyv.4 uc003gyv.5 Involved in lipid remodeling during GPI-anchor maturation. Interacts with PGAP2/FRAG1. Membrane ; Multi-pass membrane protein Belongs to the PGAP2IP family. endoplasmic reticulum GPI anchor biosynthetic process membrane integral component of membrane uc003gyv.1 uc003gyv.2 uc003gyv.3 uc003gyv.4 uc003gyv.5 
ENST00000226444.4 SULT1E1 ENST00000226444.4 sulfotransferase family 1E member 1 (from RefSeq NM_005420.3) ENST00000226444.1 ENST00000226444.2 ENST00000226444.3 NM_005420 Q53X91 Q53X91_HUMAN SULT1E1 hCG_38316 uc003heo.1 uc003heo.2 uc003heo.3 uc003heo.4 Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes a protein that transfers a sulfo moiety to and from estrone, which may control levels of estrogen receptors. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC027956.1, S77383.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN03267769 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226444.4/ ENSP00000226444.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Homodimer. Belongs to the sulfotransferase 1 family. cytosol sulfotransferase activity transferase activity nuclear membrane uc003heo.1 uc003heo.2 uc003heo.3 uc003heo.4 
ENST00000226460.5 SMR3A ENST00000226460.5 submaxillary gland androgen regulated protein 3A (from RefSeq NM_012390.4) ENST00000226460.1 ENST00000226460.2 ENST00000226460.3 ENST00000226460.4 NM_012390 PBI PROL5 Q99954 SMR3A_HUMAN uc003hfg.1 uc003hfg.2 uc003hfg.3 May play a role in protection or detoxification. Q99954; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-12067698, EBI-12020132; Q99954; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12067698, EBI-10261141; Q99954; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-12067698, EBI-12040603; Q99954; O00308: WWP2; NbExp=3; IntAct=EBI-12067698, EBI-743923; Secreted Belongs to the PROL1/PROL3 family. endopeptidase inhibitor activity extracellular region negative regulation of endopeptidase activity regulation of sensory perception of pain uc003hfg.1 uc003hfg.2 uc003hfg.3 
ENST00000226524.4 PF4V1 ENST00000226524.4 platelet factor 4 variant 1 (from RefSeq NM_002620.4) A1L4S0 CXCL4V1 ENST00000226524.1 ENST00000226524.2 ENST00000226524.3 NM_002620 P10720 PF4V_HUMAN SCYB4V1 uc003hhg.1 uc003hhg.2 uc003hhg.3 The protein encoded by this gene is a chemokine that is highly similar to platelet factor 4. The encoded protein displays a strong antiangiogenic function and is regulated by chemokine (C-X-C motif) receptor 3. This protein also impairs tumor growth and can protect against blood-retinal barrier breakdown in diabetes patients. [provided by RefSeq, Nov 2015]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189655.25447.1, ERR279829.555.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2144333, SAMEA2144335 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226524.4/ ENSP00000226524.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Inhibitor of angiogenesis. Inhibitor of endothelial cell chemotaxis (in vitro). Homotetramer. P10720; O00585: CCL21; NbExp=2; IntAct=EBI-1223944, EBI-953695; P10720; O15444: CCL25; NbExp=2; IntAct=EBI-1223944, EBI-7783341; P10720; O14625: CXCL11; NbExp=2; IntAct=EBI-1223944, EBI-2871971; P10720; P48061: CXCL12; NbExp=4; IntAct=EBI-1223944, EBI-3913254; P10720; P47992: XCL1; NbExp=2; IntAct=EBI-1223944, EBI-10209901; Secreted. The N-terminal processed forms of platelet factor 4 variant seems to be produced by proteolytic cleavage. The most abundant form is Platelet factor 4 variant(5-74). [Platelet factor 4 variant]: Mass=8250.9; Method=Electrospray; Note=Platelet factor 4 variant.; Evidence=; [Platelet factor 4 variant(4-74)]: Mass=7877.7; Method=Electrospray; Note=Platelet factor 4 variant(4-74).; Evidence=; [Platelet factor 4 variant(5-74)]: Mass=7805.8; Method=Electrospray; Note=Platelet factor 4 variant(5-74).; Evidence=; [Platelet factor 4 variant(6-74)]: Mass=7678.6; Method=Electrospray; Note=Platelet factor 4 variant(6-74).; Evidence=; Binding to heparin is much weaker than in the close homolog PF4/CXCL4. Belongs to the intercrine alpha (chemokine CxC) family. cytokine activity protein binding extracellular region extracellular space chemotaxis defense response inflammatory response immune response chemokine activity heparin binding platelet activation neutrophil chemotaxis leukocyte chemotaxis chemokine-mediated signaling pathway cellular response to lipopolysaccharide uc003hhg.1 uc003hhg.2 uc003hhg.3 
ENST00000226574.9 NFKB1 ENST00000226574.9 nuclear factor kappa B subunit 1, transcript variant 1 (from RefSeq NM_003998.4) A8K5Y5 B3KVE8 ENST00000226574.1 ENST00000226574.2 ENST00000226574.3 ENST00000226574.4 ENST00000226574.5 ENST00000226574.6 ENST00000226574.7 ENST00000226574.8 NFKB1_HUMAN NM_003998 P19838 Q68D84 Q86V43 Q8N4X7 Q9NZC0 uc011cep.1 uc011cep.2 uc011cep.3 This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappa-B (NFKB) protein complex. NFKB is a transcription regulator that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NFKB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFKB has been associated with a number of inflammatory diseases while persistent inhibition of NFKB leads to inappropriate immune cell development or delayed cell growth. Alternative splicing results in multiple transcript variants encoding different isoforms, at least one of which is proteolytically processed. [provided by RefSeq, Feb 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC051765.1, M55643.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226574.9/ ENSP00000226574.4 RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain- containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I- kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. [Nuclear factor NF-kappa-B p105 subunit]: P105 is the precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 subunit) of the nuclear factor NF-kappa-B (PubMed:1423592). Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105 (PubMed:1423592). [Nuclear factor NF-kappa-B p50 subunit]: Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65- p50 complex to form a transcription factor (PubMed:1740106, PubMed:7830764). Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions (PubMed:1740106, PubMed:7830764). Component of the NF-kappa-B p65-p50 complex (PubMed:1740106, PubMed:7830764). Homodimer; component of the NF-kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50 complex (PubMed:1423592). Component of the NF-kappa-B p50-c-Rel complex (PubMed:15102766, PubMed:8152812). Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (PubMed:10469655). Also interacts with MAP3K8 (PubMed:9950430, PubMed:15485931). NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity (PubMed:11094166). Interacts with TSC22D3; this interaction prevents nuclear translocation and DNA-binding (PubMed:11468175, PubMed:12393603). Interacts with SPAG9 and UNC5CL (PubMed:14769797, PubMed:14743216). NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50 (PubMed:13679070). NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (PubMed:15169888). Interacts with GSK3B; the interaction prevents processing of p105 to p50 (PubMed:12871932). NFKB1/p50 interacts with NFKBIE (PubMed:9315679). NFKB1/p50 interacts with NFKBIZ (By similarity). Nuclear factor NF- kappa-B p50 subunit interacts with NFKBID (By similarity). Directly interacts with MEN1 (PubMed:11526476). Interacts with HIF1AN (PubMed:17003112). Interacts with FEM1A; interaction is direct (By similarity). P19838; Q92887: ABCC2; NbExp=3; IntAct=EBI-300010, EBI-3916193; P19838; O15111: CHUK; NbExp=3; IntAct=EBI-300010, EBI-81249; P19838; P35606: COPB2; NbExp=5; IntAct=EBI-300010, EBI-1056534; P19838; P35222: CTNNB1; NbExp=3; IntAct=EBI-300010, EBI-491549; P19838; Q13547: HDAC1; NbExp=5; IntAct=EBI-300010, EBI-301834; P19838; Q9NWT6: HIF1AN; NbExp=7; IntAct=EBI-300010, EBI-745632; P19838; O14920: IKBKB; NbExp=3; IntAct=EBI-300010, EBI-81266; P19838; P41279: MAP3K8; NbExp=14; IntAct=EBI-300010, EBI-354900; P19838; P19838: NFKB1; NbExp=7; IntAct=EBI-300010, EBI-300010; P19838; Q00653: NFKB2; NbExp=8; IntAct=EBI-300010, EBI-307326; P19838; P25963: NFKBIA; NbExp=8; IntAct=EBI-300010, EBI-307386; P19838; Q15653: NFKBIB; NbExp=3; IntAct=EBI-300010, EBI-352889; P19838; P46531: NOTCH1; NbExp=2; IntAct=EBI-300010, EBI-636374; P19838; Q14690: PDCD11; NbExp=2; IntAct=EBI-300010, EBI-300028; P19838; Q8IZL8: PELP1; NbExp=2; IntAct=EBI-300010, EBI-716449; P19838; Q8IV08: PLD3; NbExp=2; IntAct=EBI-300010, EBI-2689908; P19838; Q04206: RELA; NbExp=14; IntAct=EBI-300010, EBI-73886; P19838; Q01201: RELB; NbExp=5; IntAct=EBI-300010, EBI-357837; P19838; P23396: RPS3; NbExp=4; IntAct=EBI-300010, EBI-351193; P19838; Q15025: TNIP1; NbExp=5; IntAct=EBI-300010, EBI-357849; P19838; Q8NFZ5: TNIP2; NbExp=7; IntAct=EBI-300010, EBI-359372; P19838; P10226: UL42; Xeno; NbExp=4; IntAct=EBI-300010, EBI-1029310; P19838-1; Q8NFZ5: TNIP2; NbExp=8; IntAct=EBI-1452239, EBI-359372; P19838-2; P42858: HTT; NbExp=3; IntAct=EBI-1452242, EBI-466029; PRO_0000030311; P03372: ESR1; NbExp=3; IntAct=EBI-697771, EBI-78473; PRO_0000030311; O00255: MEN1; NbExp=2; IntAct=EBI-697771, EBI-592789; PRO_0000030311; O00255-2: MEN1; NbExp=4; IntAct=EBI-697771, EBI-9869387; PRO_0000030311; Q04206: RELA; NbExp=7; IntAct=EBI-697771, EBI-73886; PRO_0000030311; P10226: UL42; Xeno; NbExp=2; IntAct=EBI-697771, EBI-1029310; [Nuclear factor NF-kappa-B p105 subunit]: Cytoplasm [Nuclear factor NF-kappa-B p50 subunit]: Nucleus Cytoplasm Note=Association with NFKBIA inhibitor (I-kappa-B), promotes its retention in the cytoplasm in an inactive form (PubMed:9865693). Translocates into the nucleus following NFKBIA degradation (PubMed:9865693). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P19838-1; Sequence=Displayed; Name=2; IsoId=P19838-2; Sequence=VSP_021025; Name=3; IsoId=P19838-3; Sequence=VSP_042869, VSP_042870; By phorbol ester and TNF. The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation. Glycine-rich region (GRR) is a critical element in the generation of p50 (Nuclear factor NF-kappa-B p50 subunit) by acting as a proteasomal 'stop signal', which leads to limited proteasomal degradation of the C-terminus, while generating p50. Generation of the NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) transcription factor takes place both cotranslationally and post-translationally via non-mutually exclusive mechanisms (PubMed:8628291, PubMed:9529257, PubMed:10970863, PubMed:25860612). A cotranslational processing allows the production of both p50 and p105 (Nuclear factor NF-kappa-B p105 subunit) from a single NFKB1 mRNA (PubMed:8628291, PubMed:9529257, PubMed:10970863). While translation occurs, the particular unfolded structure after the GRR repeat region acts as a substrate for the proteasome, promoting degradation of the C- terminus (PubMed:9529257, PubMed:10970863). The GRR acts as a proteasomal 'stop signal', protecting the region upstream of the GRR from degradation and promoting generation of p50 (PubMed:9529257, PubMed:10970863). It is unclear if limited proteasome degradation during cotranslational processing depends on ubiquitination (PubMed:9529257, PubMed:10970863). NF-kappa-B p50 is also generated post-translationally following ubiquitination by the KPC complex, leading to limited processing by the proteasome downstream of the GRR region, thereby generating p50 (PubMed:25860612). [Nuclear factor NF-kappa-B p105 subunit]: Phosphorylation at the C-terminus by IKBKB/IKKB acts as a signal for ubiquitination and promotes either complete degradation or processing to generate the NF- kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (PubMed:8626394, PubMed:10835356, PubMed:11297557, PubMed:11158290, PubMed:12482991, PubMed:14673179, PubMed:25860612). Phosphorylation at Ser-903 and Ser- 907 primes p105 for proteolytic processing in response to TNF-alpha stimulation (PubMed:12871932). Phosphorylation at Ser-923, Ser-927 and Ser-932 are required for BTRC/BTRCP-mediated ubiquitination and proteolysis (PubMed:10835356, PubMed:11297557, PubMed:11158290, PubMed:12482991, PubMed:14673179). Phosphorylation at Ser-927 is also required for ubiquitination by the KPC complex and limited processing to generate NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (PubMed:25860612). [Nuclear factor NF-kappa-B p105 subunit]: Polyubiquitinated at multiple Lys residues in the C-terminus (PubMed:11158290, PubMed:14673179, PubMed:25860612). Polyubiquitinated by the SCF(FBXW11) and SCF(BTRC) complexes following phosphorylation at Ser-923, Ser-927 and Ser-932, leading to its complete degradation (PubMed:11158290). In contrast, polyubiquitination by the KPC complex following phosphorylation at Ser-927 leads to limited proteosomal processing and generation of the active NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (PubMed:25860612). S-nitrosylation of Cys-61 affects DNA binding. The covalent modification of cysteine by 15-deoxy-Delta12,14- prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation. Immunodeficiency, common variable, 12, with autoimmunity (CVID12) [MIM:616576]: A primary immunodeficiency characterized by hypogammaglobulinemia and recurrent bacterial infections. About half of patients develop autoimmune features, including cytopenia, as well as generalized inflammation and lymphoproliferation manifest as lymphadenopathy or hepatosplenomegaly. Note=The disease is caused by variants affecting the gene represented in this entry. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/323/NFKB1"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/nfkb1/"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin transcription regulatory region sequence-specific DNA binding RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding RNA polymerase II transcription coactivator binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding negative regulation of cytokine production stimulatory C-type lectin receptor signaling pathway DNA binding chromatin binding transcription factor activity, sequence-specific DNA binding protein binding extracellular region nucleus nucleoplasm cytoplasm mitochondrion cytosol regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter transcription from RNA polymerase II promoter apoptotic process inflammatory response signal transduction I-kappaB kinase/NF-kappaB signaling transcription factor binding negative regulation of gene expression positive regulation of macrophage derived foam cell differentiation positive regulation of lipid storage negative regulation of calcidiol 1-monooxygenase activity negative regulation of vitamin D biosynthetic process enzyme binding membrane protein intracellular domain proteolysis negative regulation of cellular protein metabolic process negative regulation of cholesterol transport positive regulation of type I interferon production I-kappaB/NF-kappaB complex response to cytokine secretory granule lumen specific granule lumen response to muscle stretch NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway identical protein binding protein homodimerization activity actinin binding negative regulation of apoptotic process neutrophil degranulation sequence-specific DNA binding transcription regulatory region DNA binding negative regulation of interleukin-12 biosynthetic process negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity negative regulation of inflammatory response T cell receptor signaling pathway positive regulation of NF-kappaB transcription factor activity stress-activated MAPK cascade interleukin-1-mediated signaling pathway cellular response to lipopolysaccharide cellular response to mechanical stimulus cellular response to nicotine cellular response to interleukin-1 cellular response to interleukin-6 cellular response to tumor necrosis factor cellular response to dsRNA positive regulation of canonical Wnt signaling pathway positive regulation of hyaluronan biosynthetic process cellular response to angiotensin positive regulation of miRNA metabolic process uc011cep.1 uc011cep.2 uc011cep.3 
ENST00000226725.11 KLHL2 ENST00000226725.11 kelch like family member 2, transcript variant 1 (from RefSeq NM_007246.4) A6NCM7 B2RD18 B4DFH7 ENST00000226725.1 ENST00000226725.10 ENST00000226725.2 ENST00000226725.3 ENST00000226725.4 ENST00000226725.5 ENST00000226725.6 ENST00000226725.7 ENST00000226725.8 ENST00000226725.9 F5H6M3 KLHL2 KLHL2_HUMAN NM_007246 O95198 Q8N484 Q8TBH5 uc003irb.1 uc003irb.2 uc003irb.3 uc003irb.4 uc003irb.5 Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, WNK1, WNK3 and WNK4, leading most often to their proteasomal degradation (PubMed:23838290). The BCR(KLHL2) complex catalyzes ubiquitination and degradation of NPTXR (By similarity). Responsible for degradative ubiquitination of the WNK kinases WNK1, WNK3 and WNK4 (PubMed:23838290). Plays a role in the reorganization of the actin cytoskeleton (PubMed:10397770). Promotes growth of cell projections in oligodendrocyte precursors (PubMed:15715669). Protein modification; protein ubiquitination. Component of the BCR(KLHL2) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL2 and RBX1 (PubMed:23838290). Binds actin (PubMed:10397770). Interacts with KLHL12 (PubMed:15383316). Interacts (via N-terminus) with FYN (via SH3 domain) (PubMed:15715669). O95198; P50895: BCAM; NbExp=6; IntAct=EBI-746999, EBI-10212133; O95198; Q13895: BYSL; NbExp=3; IntAct=EBI-746999, EBI-358049; O95198; Q86WV7: CCDC43; NbExp=5; IntAct=EBI-746999, EBI-10260148; O95198; Q96MW1: CCDC43; NbExp=3; IntAct=EBI-746999, EBI-9247198; O95198; Q16543: CDC37; NbExp=3; IntAct=EBI-746999, EBI-295634; O95198; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-746999, EBI-12155483; O95198; P49760: CLK2; NbExp=6; IntAct=EBI-746999, EBI-750020; O95198; Q13618: CUL3; NbExp=7; IntAct=EBI-746999, EBI-456129; O95198; Q9HCG8: CWC22; NbExp=3; IntAct=EBI-746999, EBI-373289; O95198; Q14241: ELOA; NbExp=3; IntAct=EBI-746999, EBI-742350; O95198; Q14145: KEAP1; NbExp=5; IntAct=EBI-746999, EBI-751001; O95198; Q53G59: KLHL12; NbExp=8; IntAct=EBI-746999, EBI-740929; O95198; O95198: KLHL2; NbExp=5; IntAct=EBI-746999, EBI-746999; O95198; Q9UH77: KLHL3; NbExp=3; IntAct=EBI-746999, EBI-8524663; O95198; P55081: MFAP1; NbExp=3; IntAct=EBI-746999, EBI-1048159; O95198; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-746999, EBI-3911716; O95198; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746999, EBI-741158; O95198; Q6TGC4: PADI6; NbExp=3; IntAct=EBI-746999, EBI-10892722; O95198; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-746999, EBI-14066006; O95198; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-746999, EBI-5452779; O95198; O00560: SDCBP; NbExp=3; IntAct=EBI-746999, EBI-727004; O95198; Q96EY4: TMA16; NbExp=7; IntAct=EBI-746999, EBI-1045338; O95198; O14787: TNPO2; NbExp=4; IntAct=EBI-746999, EBI-431907; O95198; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-746999, EBI-9867283; O95198; O95881: TXNDC12; NbExp=4; IntAct=EBI-746999, EBI-2564581; O95198; Q5TZN3: UBE2C; NbExp=3; IntAct=EBI-746999, EBI-10247554; O95198; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-746999, EBI-10180829; O95198; Q8NC26: ZNF114; NbExp=8; IntAct=EBI-746999, EBI-10265237; Cytoplasm, cytoskeleton Cell projection, ruffle Cell projection Cell projection, lamellipodium Cytoplasm, cytosol Note=A proportion colocalizes with the actin cytoskeleton (PubMed:10397770). When over-expressed, colocalizes with NPTXR in perinuclear aggresomes (By similarity). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O95198-1; Sequence=Displayed; Name=2; IsoId=O95198-2; Sequence=VSP_042837; Name=3; IsoId=O95198-3; Sequence=VSP_047004; Ubiquitous. Detected throughout the brain. ruffle actin binding protein binding cytoplasm cytosol cytoskeleton actin cytoskeleton protein ubiquitination lamellipodium Cul3-RING ubiquitin ligase complex identical protein binding cell projection post-translational protein modification uc003irb.1 uc003irb.2 uc003irb.3 uc003irb.4 uc003irb.5 
ENST00000226730.5 IL2 ENST00000226730.5 interleukin 2 (from RefSeq NM_000586.4) ENST00000226730.1 ENST00000226730.2 ENST00000226730.3 ENST00000226730.4 IL2 NM_000586 Q0GK43 Q0GK43_HUMAN hCG_38828 uc003ier.1 uc003ier.2 uc003ier.3 uc003ier.4 uc003ier.5 The protein encoded by this gene is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: S82692.1, BC070338.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226730.5/ ENSP00000226730.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cytokine produced by activated CD4-positive helper T-cells and to a lesser extend activated CD8-positive T-cells and natural killer (NK) cells that plays pivotal roles in the immune response and tolerance. Binds to a receptor complex composed of either the high- affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122 and IL2RG/CD132) or the low-affinity dimeric IL-2R (IL2RB and IL2RG). Interaction with the receptor leads to oligomerization and conformation changes in the IL-2R subunits resulting in downstream signaling starting with phosphorylation of JAK1 and JAK3. In turn, JAK1 and JAK3 phosphorylate the receptor to form a docking site leading to the phosphorylation of several substrates including STAT5. This process leads to activation of several pathways including STAT, phosphoinositide-3-kinase/PI3K and mitogen-activated protein kinase/MAPK pathways. Functions as a T-cell growth factor and can increase NK-cell cytolytic activity as well. Promotes strong proliferation of activated B-cells and subsequently immunoglobulin production. Plays a pivotal role in regulating the adaptive immune system by controlling the survival and proliferation of regulatory T-cells, which are required for the maintenance of immune tolerance. Moreover, participates in the differentiation and homeostasis of effector T-cell subsets, including Th1, Th2, Th17 as well as memory CD8-positive T-cells. Secreted Belongs to the IL-2 family. negative regulation of protein phosphorylation positive regulation of protein phosphorylation adaptive immune response immune system process cytokine activity interleukin-2 receptor binding extracellular region extracellular space cell immune response G-protein coupled receptor signaling pathway positive regulation of cytosolic calcium ion concentration protein kinase C-activating G-protein coupled receptor signaling pathway growth factor activity carbohydrate binding kappa-type opioid receptor binding positive regulation of interferon-gamma production positive regulation of T cell proliferation positive regulation of activated T cell proliferation positive regulation of tyrosine phosphorylation of STAT protein glycosphingolipid binding response to ethanol positive regulation of T cell differentiation positive regulation of regulatory T cell differentiation negative regulation of heart contraction positive regulation of transcription from RNA polymerase II promoter regulation of T cell homeostatic proliferation positive regulation of isotype switching to IgG isotypes negative regulation of lymphocyte proliferation negative regulation of inflammatory response positive regulation of immunoglobulin secretion positive regulation of dendritic spine development extrinsic apoptotic signaling pathway in absence of ligand negative regulation of T-helper 17 cell differentiation uc003ier.1 uc003ier.2 uc003ier.3 uc003ier.4 uc003ier.5 
ENST00000226760.5 WFS1 ENST00000226760.5 wolframin ER transmembrane glycoprotein, transcript variant 1 (from RefSeq NM_006005.3) B2R797 D3DVT1 ENST00000226760.1 ENST00000226760.2 ENST00000226760.3 ENST00000226760.4 NM_006005 O76024 Q8N6I3 Q9UNW6 WFS1_HUMAN uc003gix.1 uc003gix.2 uc003gix.3 This gene encodes a transmembrane protein, which is located primarily in the endoplasmic reticulum and ubiquitously expressed with highest levels in brain, pancreas, heart, and insulinoma beta-cell lines. Mutations in this gene are associated with Wolfram syndrome, also called DIDMOAD (Diabetes Insipidus, Diabetes Mellitus, Optic Atrophy, and Deafness), an autosomal recessive disorder. The disease affects the brain and central nervous system. Mutations in this gene can also cause autosomal dominant deafness 6 (DFNA6), also known as DFNA14 or DFNA38. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Mar 2009]. Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store (PubMed:16989814). Negatively regulates the ER stress response and positively regulates the stability of V-ATPase subunits ATP6V1A and ATP1B1 by preventing their degradation through an unknown proteasome-independent mechanism (PubMed:23035048). Interacts with ATP6V1A. O76024; Q9H172: ABCG4; NbExp=3; IntAct=EBI-720609, EBI-8584118; O76024; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-720609, EBI-10173507; O76024; P20933: AGA; NbExp=3; IntAct=EBI-720609, EBI-1223922; O76024; Q9UIJ7: AK3; NbExp=3; IntAct=EBI-720609, EBI-3916527; O76024; P14550: AKR1A1; NbExp=3; IntAct=EBI-720609, EBI-372388; O76024; P02768-3: ALB; NbExp=3; IntAct=EBI-720609, EBI-25830928; O76024; Q9BS18: ANAPC13; NbExp=3; IntAct=EBI-720609, EBI-2555953; O76024; Q6ZTN6-2: ANKRD13D; NbExp=3; IntAct=EBI-720609, EBI-25840993; O76024; Q8N8A2-2: ANKRD44; NbExp=3; IntAct=EBI-720609, EBI-21636328; O76024; Q92688: ANP32B; NbExp=3; IntAct=EBI-720609, EBI-762428; O76024; P08758: ANXA5; NbExp=3; IntAct=EBI-720609, EBI-296601; O76024; P13928: ANXA8; NbExp=3; IntAct=EBI-720609, EBI-2556915; O76024; D3DTF8: APLN; NbExp=3; IntAct=EBI-720609, EBI-22002556; O76024; P05067: APP; NbExp=3; IntAct=EBI-720609, EBI-77613; O76024; Q13520: AQP6; NbExp=3; IntAct=EBI-720609, EBI-13059134; O76024; O94778: AQP8; NbExp=3; IntAct=EBI-720609, EBI-19124986; O76024; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-720609, EBI-2875816; O76024; Q86TN1: ARNT2; NbExp=3; IntAct=EBI-720609, EBI-25844820; O76024; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-720609, EBI-14199987; O76024; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-720609, EBI-10254793; O76024; Q96FT7-2: ASIC4; NbExp=3; IntAct=EBI-720609, EBI-25898949; O76024; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-720609, EBI-9089489; O76024; P05026: ATP1B1; NbExp=6; IntAct=EBI-720609, EBI-714630; O76024; P16615: ATP2A2; NbExp=3; IntAct=EBI-720609, EBI-358933; O76024; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-720609, EBI-2891281; O76024; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-720609, EBI-4290814; O76024; O95817: BAG3; NbExp=3; IntAct=EBI-720609, EBI-747185; O76024; P46379-2: BAG6; NbExp=3; IntAct=EBI-720609, EBI-10988864; O76024; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-720609, EBI-9092016; O76024; Q8IXM2: BAP18; NbExp=3; IntAct=EBI-720609, EBI-4280811; O76024; Q16520: BATF; NbExp=3; IntAct=EBI-720609, EBI-749503; O76024; Q8WY36-3: BBX; NbExp=3; IntAct=EBI-720609, EBI-22013474; O76024; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-720609, EBI-747430; O76024; Q14457: BECN1; NbExp=3; IntAct=EBI-720609, EBI-949378; O76024; Q96LC9: BMF; NbExp=3; IntAct=EBI-720609, EBI-3919268; O76024; Q9GZL8: BPESC1; NbExp=3; IntAct=EBI-720609, EBI-25861458; O76024; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-720609, EBI-741210; O76024; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-720609, EBI-10693038; O76024; Q8WZ55: BSND; NbExp=3; IntAct=EBI-720609, EBI-7996695; O76024; Q9Y297: BTRC; NbExp=3; IntAct=EBI-720609, EBI-307461; O76024; Q9H0W9-4: C11orf54; NbExp=3; IntAct=EBI-720609, EBI-25849710; O76024; Q13901: C1D; NbExp=3; IntAct=EBI-720609, EBI-3844053; O76024; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-720609, EBI-747505; O76024; Q14C60: C21orf29; NbExp=3; IntAct=EBI-720609, EBI-22013264; O76024; Q6P5X5-2: C22orf39; NbExp=3; IntAct=EBI-720609, EBI-10692329; O76024; Q9BVC5: C2orf49; NbExp=3; IntAct=EBI-720609, EBI-5458641; O76024; Q9BRJ6: C7orf50; NbExp=3; IntAct=EBI-720609, EBI-751612; O76024; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-720609, EBI-751596; O76024; Q96NX5: CAMK1G; NbExp=3; IntAct=EBI-720609, EBI-3920838; O76024; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-720609, EBI-25850646; O76024; P29466-3: CASP1; NbExp=3; IntAct=EBI-720609, EBI-12248206; O76024; Q8N163: CCAR2; NbExp=3; IntAct=EBI-720609, EBI-355410; O76024; Q6ZP82: CCDC141; NbExp=3; IntAct=EBI-720609, EBI-928795; O76024; Q96LX7-5: CCDC17; NbExp=3; IntAct=EBI-720609, EBI-12165781; O76024; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-720609, EBI-10181422; O76024; Q9Y3X0: CCDC9; NbExp=3; IntAct=EBI-720609, EBI-2557532; O76024; O96020: CCNE2; NbExp=3; IntAct=EBI-720609, EBI-375033; O76024; P78371: CCT2; NbExp=3; IntAct=EBI-720609, EBI-357407; O76024; P11912: CD79A; NbExp=3; IntAct=EBI-720609, EBI-7797864; O76024; Q9BWT1: CDCA7; NbExp=3; IntAct=EBI-720609, EBI-7054803; O76024; Q5VV42: CDKAL1; NbExp=3; IntAct=EBI-720609, EBI-10194801; O76024; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-720609, EBI-11953200; O76024; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-720609, EBI-743375; O76024; O14646-2: CHD1; NbExp=3; IntAct=EBI-720609, EBI-10961487; O76024; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-720609, EBI-744045; O76024; Q99967: CITED2; NbExp=3; IntAct=EBI-720609, EBI-937732; O76024; P12532: CKMT1B; NbExp=3; IntAct=EBI-720609, EBI-1050662; O76024; Q9Y240: CLEC11A; NbExp=3; IntAct=EBI-720609, EBI-3957044; O76024; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-720609, EBI-11749983; O76024; Q14677: CLINT1; NbExp=3; IntAct=EBI-720609, EBI-1171113; O76024; Q96DZ5: CLIP3; NbExp=3; IntAct=EBI-720609, EBI-12823145; O76024; Q16740: CLPP; NbExp=3; IntAct=EBI-720609, EBI-1056029; O76024; Q9BQ75: CMSS1; NbExp=3; IntAct=EBI-720609, EBI-395649; O76024; Q9BT09: CNPY3; NbExp=3; IntAct=EBI-720609, EBI-2835965; O76024; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-720609, EBI-25836090; O76024; O43405-2: COCH; NbExp=3; IntAct=EBI-720609, EBI-25896722; O76024; P21964: COMT; NbExp=3; IntAct=EBI-720609, EBI-372265; O76024; P61201: COPS2; NbExp=3; IntAct=EBI-720609, EBI-1050386; O76024; Q9P021: CRIPT; NbExp=3; IntAct=EBI-720609, EBI-946968; O76024; P01040: CSTA; NbExp=3; IntAct=EBI-720609, EBI-724303; O76024; Q8TB03: CXorf38; NbExp=3; IntAct=EBI-720609, EBI-12024320; O76024; P00167: CYB5A; NbExp=3; IntAct=EBI-720609, EBI-1047284; O76024; Q7L576: CYFIP1; NbExp=3; IntAct=EBI-720609, EBI-1048143; O76024; Q5D0E6-2: DALRD3; NbExp=3; IntAct=EBI-720609, EBI-9090939; O76024; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-720609, EBI-25842815; O76024; Q9H816: DCLRE1B; NbExp=3; IntAct=EBI-720609, EBI-3508943; O76024; O00148: DDX39A; NbExp=3; IntAct=EBI-720609, EBI-348253; O76024; P78524: DENND2B; NbExp=3; IntAct=EBI-720609, EBI-962633; O76024; Q68D51-2: DENND2C; NbExp=3; IntAct=EBI-720609, EBI-13075846; O76024; Q96F81: DISP1; NbExp=3; IntAct=EBI-720609, EBI-10230179; O76024; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-720609, EBI-25842538; O76024; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-720609, EBI-12019838; O76024; Q5VZB9: DMRTA1; NbExp=3; IntAct=EBI-720609, EBI-3939812; O76024; Q9NNZ3: DNAJC4; NbExp=3; IntAct=EBI-720609, EBI-4397791; O76024; P49184: DNASE1L1; NbExp=3; IntAct=EBI-720609, EBI-20894690; O76024; Q9Y6K1: DNMT3A; NbExp=3; IntAct=EBI-720609, EBI-923653; O76024; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-720609, EBI-10694655; O76024; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-720609, EBI-25847826; O76024; O14531: DPYSL4; NbExp=3; IntAct=EBI-720609, EBI-719542; O76024; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-720609, EBI-724653; O76024; Q9BY84: DUSP16; NbExp=3; IntAct=EBI-720609, EBI-3443956; O76024; Q92997: DVL3; NbExp=3; IntAct=EBI-720609, EBI-739789; O76024; P63172: DYNLT1; NbExp=3; IntAct=EBI-720609, EBI-1176455; O76024; Q9H1Z8: ECRG4; NbExp=3; IntAct=EBI-720609, EBI-12208839; O76024; Q3B7T1: EDRF1; NbExp=3; IntAct=EBI-720609, EBI-2870947; O76024; O00303: EIF3F; NbExp=3; IntAct=EBI-720609, EBI-711990; O76024; O60841: EIF5B; NbExp=3; IntAct=EBI-720609, EBI-928530; O76024; I6L9I8: EPN3; NbExp=3; IntAct=EBI-720609, EBI-12866582; O76024; Q8TE68-3: EPS8L1; NbExp=3; IntAct=EBI-720609, EBI-21574901; O76024; Q9H6S3: EPS8L2; NbExp=3; IntAct=EBI-720609, EBI-3940939; O76024; Q2NKX8: ERCC6L; NbExp=3; IntAct=EBI-720609, EBI-1042535; O76024; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-720609, EBI-12260294; O76024; P03372: ESR1; NbExp=3; IntAct=EBI-720609, EBI-78473; O76024; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-720609, EBI-10213520; O76024; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-720609, EBI-6448852; O76024; Q01844-4: EWSR1; NbExp=3; IntAct=EBI-720609, EBI-25896785; O76024; O00471: EXOC5; NbExp=3; IntAct=EBI-720609, EBI-949824; O76024; Q99504: EYA3; NbExp=3; IntAct=EBI-720609, EBI-9089567; O76024; O15540: FABP7; NbExp=3; IntAct=EBI-720609, EBI-10697159; O76024; Q6P587-2: FAHD1; NbExp=3; IntAct=EBI-720609, EBI-12902289; O76024; Q6SJ93: FAM111B; NbExp=3; IntAct=EBI-720609, EBI-6309082; O76024; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-720609, EBI-3893327; O76024; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-720609, EBI-25835236; O76024; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-720609, EBI-11793142; O76024; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-720609, EBI-18304435; O76024; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-720609, EBI-10247271; O76024; Q5HYJ3-3: FAM76B; NbExp=3; IntAct=EBI-720609, EBI-11956087; O76024; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-720609, EBI-5461838; O76024; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-720609, EBI-8468186; O76024; O15287: FANCG; NbExp=3; IntAct=EBI-720609, EBI-81610; O76024; Q8TC84: FANK1; NbExp=3; IntAct=EBI-720609, EBI-21975404; O76024; Q53R41: FASTKD1; NbExp=3; IntAct=EBI-720609, EBI-3957005; O76024; Q8NFZ0: FBH1; NbExp=3; IntAct=EBI-720609, EBI-724767; O76024; Q9UBX5: FBLN5; NbExp=3; IntAct=EBI-720609, EBI-947897; O76024; Q9UKT5: FBXO4; NbExp=3; IntAct=EBI-720609, EBI-960409; O76024; Q6P3S6: FBXO42; NbExp=3; IntAct=EBI-720609, EBI-2506081; O76024; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-720609, EBI-396453; O76024; P15407: FOSL1; NbExp=3; IntAct=EBI-720609, EBI-744510; O76024; P02792: FTL; NbExp=3; IntAct=EBI-720609, EBI-713279; O76024; Q7L622: G2E3; NbExp=3; IntAct=EBI-720609, EBI-751757; O76024; P35575: G6PC1; NbExp=3; IntAct=EBI-720609, EBI-3906612; O76024; Q8NCL4: GALNT6; NbExp=3; IntAct=EBI-720609, EBI-3907241; O76024; P15976-2: GATA1; NbExp=3; IntAct=EBI-720609, EBI-9090198; O76024; P23769-2: GATA2; NbExp=3; IntAct=EBI-720609, EBI-21856389; O76024; P14136: GFAP; NbExp=3; IntAct=EBI-720609, EBI-744302; O76024; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-720609, EBI-8799578; O76024; P10075: GLI4; NbExp=3; IntAct=EBI-720609, EBI-14061927; O76024; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-720609, EBI-11975289; O76024; Q9HBQ8: GOLGA2P5; NbExp=3; IntAct=EBI-720609, EBI-22000587; O76024; O95872: GPANK1; NbExp=3; IntAct=EBI-720609, EBI-751540; O76024; Q8IYG2: GPC3; NbExp=3; IntAct=EBI-720609, EBI-25896879; O76024; Q7Z602: GPR141; NbExp=3; IntAct=EBI-720609, EBI-21649723; O76024; P0CG08: GPR89B; NbExp=3; IntAct=EBI-720609, EBI-11905631; O76024; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-720609, EBI-347538; O76024; Q8IY40: GRIK2; NbExp=3; IntAct=EBI-720609, EBI-25832107; O76024; O75409: H2AP; NbExp=3; IntAct=EBI-720609, EBI-6447217; O76024; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-720609, EBI-2868501; O76024; P68431: H3C12; NbExp=3; IntAct=EBI-720609, EBI-79722; O76024; A8K0U2: hCG_2001421; NbExp=3; IntAct=EBI-720609, EBI-25843825; O76024; A0A024R1L7: hCG_41307; NbExp=3; IntAct=EBI-720609, EBI-25849938; O76024; P08631-2: HCK; NbExp=3; IntAct=EBI-720609, EBI-9834454; O76024; Q03014: HHEX; NbExp=3; IntAct=EBI-720609, EBI-747421; O76024; P52790: HK3; NbExp=3; IntAct=EBI-720609, EBI-2965780; O76024; O75330-3: HMMR; NbExp=3; IntAct=EBI-720609, EBI-12098658; O76024; O14979: HNRNPDL; NbExp=3; IntAct=EBI-720609, EBI-299727; O76024; Q96EW2-2: HSPBAP1; NbExp=3; IntAct=EBI-720609, EBI-25835621; O76024; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-720609, EBI-9091197; O76024; P22692: IGFBP4; NbExp=3; IntAct=EBI-720609, EBI-2831948; O76024; Q14005-2: IL16; NbExp=3; IntAct=EBI-720609, EBI-17178971; O76024; O95256: IL18RAP; NbExp=4; IntAct=EBI-720609, EBI-21018056; O76024; Q96RQ9: IL4I1; NbExp=3; IntAct=EBI-720609, EBI-20831744; O76024; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-720609, EBI-743980; O76024; Q9UNL4: ING4; NbExp=3; IntAct=EBI-720609, EBI-2866661; O76024; Q8WYH8-2: ING5; NbExp=3; IntAct=EBI-720609, EBI-21602071; O76024; Q8IXL9: IQCF2; NbExp=3; IntAct=EBI-720609, EBI-10238842; O76024; Q8NA54: IQUB; NbExp=3; IntAct=EBI-720609, EBI-10220600; O76024; Q9Y6F6-3: IRAG1; NbExp=3; IntAct=EBI-720609, EBI-25840037; O76024; Q86U28: ISCA2; NbExp=3; IntAct=EBI-720609, EBI-10258659; O76024; P0C870: JMJD7; NbExp=3; IntAct=EBI-720609, EBI-9090173; O76024; Q9NVX7-2: KBTBD4; NbExp=3; IntAct=EBI-720609, EBI-25871195; O76024; Q9Y691: KCNMB2; NbExp=3; IntAct=EBI-720609, EBI-7932244; O76024; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-720609, EBI-742916; O76024; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-720609, EBI-12382297; O76024; Q06136: KDSR; NbExp=3; IntAct=EBI-720609, EBI-3909166; O76024; Q14145: KEAP1; NbExp=3; IntAct=EBI-720609, EBI-751001; O76024; A0A384DVV8: KIAA0040; NbExp=3; IntAct=EBI-720609, EBI-20764875; O76024; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-720609, EBI-739493; O76024; Q12756: KIF1A; NbExp=3; IntAct=EBI-720609, EBI-2679809; O76024; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-720609, EBI-2796400; O76024; P57682: KLF3; NbExp=3; IntAct=EBI-720609, EBI-8472267; O76024; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-720609, EBI-714379; O76024; P08727: KRT19; NbExp=3; IntAct=EBI-720609, EBI-742756; O76024; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-720609, EBI-8473062; O76024; Q14525: KRT33B; NbExp=3; IntAct=EBI-720609, EBI-1049638; O76024; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-720609, EBI-10241252; O76024; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-720609, EBI-10241353; O76024; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-720609, EBI-10261141; O76024; Q14847-2: LASP1; NbExp=3; IntAct=EBI-720609, EBI-9088686; O76024; O95447: LCA5L; NbExp=3; IntAct=EBI-720609, EBI-8473670; O76024; P04180: LCAT; NbExp=3; IntAct=EBI-720609, EBI-9104464; O76024; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-720609, EBI-10245913; O76024; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-720609, EBI-10246607; O76024; Q96PV6: LENG8; NbExp=3; IntAct=EBI-720609, EBI-739546; O76024; O00214: LGALS8; NbExp=3; IntAct=EBI-720609, EBI-740058; O76024; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-720609, EBI-10258746; O76024; Q68G74: LHX8; NbExp=3; IntAct=EBI-720609, EBI-8474075; O76024; Q8N448: LNX2; NbExp=3; IntAct=EBI-720609, EBI-2340947; O76024; A2RU56: LOC401296; NbExp=3; IntAct=EBI-720609, EBI-9088215; O76024; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-720609, EBI-749562; O76024; Q14693: LPIN1; NbExp=3; IntAct=EBI-720609, EBI-5278370; O76024; Q6Q4G3-4: LVRN; NbExp=3; IntAct=EBI-720609, EBI-25862057; O76024; Q9H063: MAF1; NbExp=3; IntAct=EBI-720609, EBI-720354; O76024; Q96M61: MAGEB18; NbExp=3; IntAct=EBI-720609, EBI-741835; O76024; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-720609, EBI-12056869; O76024; P52564: MAP2K6; NbExp=3; IntAct=EBI-720609, EBI-448135; O76024; P61244-4: MAX; NbExp=3; IntAct=EBI-720609, EBI-25848049; O76024; O95243-2: MBD4; NbExp=3; IntAct=EBI-720609, EBI-6448717; O76024; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-720609, EBI-10182361; O76024; O15068-4: MCF2L; NbExp=3; IntAct=EBI-720609, EBI-21375623; O76024; Q03112-9: MECOM; NbExp=3; IntAct=EBI-720609, EBI-23820194; O76024; P51608: MECP2; NbExp=3; IntAct=EBI-720609, EBI-1189067; O76024; Q15528-2: MED22; NbExp=3; IntAct=EBI-720609, EBI-12954271; O76024; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-720609, EBI-8487781; O76024; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-720609, EBI-1104552; O76024; Q15049: MLC1; NbExp=3; IntAct=EBI-720609, EBI-8475277; O76024; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-720609, EBI-25835557; O76024; Q86VF5-3: MOGAT3; NbExp=3; IntAct=EBI-720609, EBI-25840143; O76024; Q8N594: MPND; NbExp=3; IntAct=EBI-720609, EBI-2512452; O76024; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-720609, EBI-995714; O76024; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-720609, EBI-748896; O76024; Q9Y2R5: MRPS17; NbExp=3; IntAct=EBI-720609, EBI-1046443; O76024; O43196-4: MSH5; NbExp=3; IntAct=EBI-720609, EBI-25860238; O76024; Q8N5Y2: MSL3; NbExp=3; IntAct=EBI-720609, EBI-2560796; O76024; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-720609, EBI-10699187; O76024; Q96A32: MYL11; NbExp=3; IntAct=EBI-720609, EBI-1390771; O76024; Q9H1R3: MYLK2; NbExp=3; IntAct=EBI-720609, EBI-356910; O76024; Q9Y3Q0: NAALAD2; NbExp=3; IntAct=EBI-720609, EBI-2863682; O76024; Q969V3: NCLN; NbExp=3; IntAct=EBI-720609, EBI-1056979; O76024; Q99608: NDN; NbExp=3; IntAct=EBI-720609, EBI-718177; O76024; Q9P032: NDUFAF4; NbExp=3; IntAct=EBI-720609, EBI-2606839; O76024; P28331-5: NDUFS1; NbExp=3; IntAct=EBI-720609, EBI-25876328; O76024; I6L9F6: NEFL; NbExp=3; IntAct=EBI-720609, EBI-10178578; O76024; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-720609, EBI-718372; O76024; Q96AM0: NLRP1; NbExp=3; IntAct=EBI-720609, EBI-25860999; O76024; Q6IAD4: NOTCH1; NbExp=3; IntAct=EBI-720609, EBI-25860267; O76024; O15130-2: NPFF; NbExp=3; IntAct=EBI-720609, EBI-25840002; O76024; Q14995: NR1D2; NbExp=3; IntAct=EBI-720609, EBI-6144053; O76024; Q6X4W1-6: NSMF; NbExp=3; IntAct=EBI-720609, EBI-25842707; O76024; P36639-4: NUDT1; NbExp=3; IntAct=EBI-720609, EBI-25834643; O76024; Q9NZJ9: NUDT4; NbExp=3; IntAct=EBI-720609, EBI-4280066; O76024; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-720609, EBI-1210753; O76024; O15381-5: NVL; NbExp=3; IntAct=EBI-720609, EBI-18577082; O76024; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-720609, EBI-9090919; O76024; O43482: OIP5; NbExp=3; IntAct=EBI-720609, EBI-536879; O76024; Q96CV9-2: OPTN; NbExp=3; IntAct=EBI-720609, EBI-9091423; O76024; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-720609, EBI-1058491; O76024; Q9BWI9: OTUB2; NbExp=3; IntAct=EBI-720609, EBI-10300896; O76024; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-720609, EBI-25830200; O76024; Q15077: P2RY6; NbExp=3; IntAct=EBI-720609, EBI-10235794; O76024; Q9H361: PABPC3; NbExp=3; IntAct=EBI-720609, EBI-1055272; O76024; Q9P286: PAK5; NbExp=3; IntAct=EBI-720609, EBI-741896; O76024; O75781-2: PALM; NbExp=3; IntAct=EBI-720609, EBI-16399860; O76024; Q9NP74: PALMD; NbExp=3; IntAct=EBI-720609, EBI-2811699; O76024; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-720609, EBI-2513978; O76024; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-720609, EBI-11022007; O76024; Q9Y5G3-2: PCDHGB1; NbExp=3; IntAct=EBI-720609, EBI-21584477; O76024; P22061-2: PCMT1; NbExp=3; IntAct=EBI-720609, EBI-12386584; O76024; Q9BRX2: PELO; NbExp=3; IntAct=EBI-720609, EBI-1043580; O76024; O15534: PER1; NbExp=3; IntAct=EBI-720609, EBI-2557276; O76024; Q96FX8: PERP; NbExp=3; IntAct=EBI-720609, EBI-17183069; O76024; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-720609, EBI-12339509; O76024; Q7RTV0: PHF5A; NbExp=3; IntAct=EBI-720609, EBI-2555365; O76024; A2BDE7: PHLDA1; NbExp=3; IntAct=EBI-720609, EBI-14084211; O76024; O75925: PIAS1; NbExp=3; IntAct=EBI-720609, EBI-629434; O76024; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-720609, EBI-9090282; O76024; Q9BZM1: PLA2G12A; NbExp=3; IntAct=EBI-720609, EBI-3916751; O76024; Q9UF11-2: PLEKHB1; NbExp=3; IntAct=EBI-720609, EBI-12832742; O76024; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-720609, EBI-21503705; O76024; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-720609, EBI-12891828; O76024; Q99541: PLIN2; NbExp=3; IntAct=EBI-720609, EBI-2115275; O76024; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-720609, EBI-18063495; O76024; P06746: POLB; NbExp=3; IntAct=EBI-720609, EBI-713836; O76024; Q9H1D9: POLR3F; NbExp=3; IntAct=EBI-720609, EBI-710067; O76024; P09565: PP9974; NbExp=3; IntAct=EBI-720609, EBI-10196507; O76024; Q8NI37: PPTC7; NbExp=3; IntAct=EBI-720609, EBI-9089276; O76024; P54646: PRKAA2; NbExp=3; IntAct=EBI-720609, EBI-1383852; O76024; P60891: PRPS1; NbExp=3; IntAct=EBI-720609, EBI-749195; O76024; P11908: PRPS2; NbExp=3; IntAct=EBI-720609, EBI-4290895; O76024; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-720609, EBI-743880; O76024; P25788-2: PSMA3; NbExp=3; IntAct=EBI-720609, EBI-348394; O76024; P20618: PSMB1; NbExp=3; IntAct=EBI-720609, EBI-372273; O76024; P28062-2: PSMB8; NbExp=3; IntAct=EBI-720609, EBI-372312; O76024; P62333: PSMC6; NbExp=3; IntAct=EBI-720609, EBI-357669; O76024; Q16401: PSMD5; NbExp=3; IntAct=EBI-720609, EBI-752143; O76024; Q8TBK9: PTMA; NbExp=3; IntAct=EBI-720609, EBI-1056327; O76024; Q14671: PUM1; NbExp=3; IntAct=EBI-720609, EBI-948453; O76024; Q7Z7K5: PXN; NbExp=3; IntAct=EBI-720609, EBI-25841978; O76024; P47897: QARS1; NbExp=3; IntAct=EBI-720609, EBI-347462; O76024; Q15907: RAB11B; NbExp=3; IntAct=EBI-720609, EBI-722234; O76024; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-720609, EBI-746228; O76024; Q7Z6E9-3: RBBP6; NbExp=3; IntAct=EBI-720609, EBI-11743772; O76024; Q96PK6: RBM14; NbExp=3; IntAct=EBI-720609, EBI-954272; O76024; Q8NDT2-2: RBM15B; NbExp=3; IntAct=EBI-720609, EBI-10269922; O76024; Q96I25: RBM17; NbExp=3; IntAct=EBI-720609, EBI-740272; O76024; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-720609, EBI-1504830; O76024; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-720609, EBI-17589229; O76024; Q8TCX5: RHPN1; NbExp=3; IntAct=EBI-720609, EBI-746325; O76024; Q9H871: RMND5A; NbExp=3; IntAct=EBI-720609, EBI-2797992; O76024; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-720609, EBI-714023; O76024; Q9NTX7-2: RNF146; NbExp=3; IntAct=EBI-720609, EBI-11750630; O76024; Q8IYW5: RNF168; NbExp=3; IntAct=EBI-720609, EBI-914207; O76024; Q96D59: RNF183; NbExp=3; IntAct=EBI-720609, EBI-743938; O76024; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-720609, EBI-751555; O76024; Q9H0F5-2: RNF38; NbExp=3; IntAct=EBI-720609, EBI-25866807; O76024; P13489: RNH1; NbExp=3; IntAct=EBI-720609, EBI-1237106; O76024; P39023: RPL3; NbExp=3; IntAct=EBI-720609, EBI-1056348; O76024; P62244: RPS15A; NbExp=3; IntAct=EBI-720609, EBI-347895; O76024; P62979: RPS27A; NbExp=3; IntAct=EBI-720609, EBI-357375; O76024; P08865: RPSA; NbExp=3; IntAct=EBI-720609, EBI-354112; O76024; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-720609, EBI-10248967; O76024; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-720609, EBI-8636004; O76024; Q9Y2B1: RXYLT1; NbExp=3; IntAct=EBI-720609, EBI-3914763; O76024; P25815: S100P; NbExp=3; IntAct=EBI-720609, EBI-743700; O76024; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-720609, EBI-11528848; O76024; Q7Z3H4: SAMD7; NbExp=3; IntAct=EBI-720609, EBI-12148649; O76024; P82979: SARNP; NbExp=3; IntAct=EBI-720609, EBI-347495; O76024; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-720609, EBI-4403649; O76024; P34741: SDC2; NbExp=3; IntAct=EBI-720609, EBI-1172957; O76024; O00560: SDCBP; NbExp=3; IntAct=EBI-720609, EBI-727004; O76024; P16581: SELE; NbExp=3; IntAct=EBI-720609, EBI-8007671; O76024; Q9C0C4: SEMA4C; NbExp=3; IntAct=EBI-720609, EBI-10303490; O76024; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-720609, EBI-9089805; O76024; Q9H4L4: SENP3; NbExp=3; IntAct=EBI-720609, EBI-2880236; O76024; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-720609, EBI-745901; O76024; Q13530: SERINC3; NbExp=3; IntAct=EBI-720609, EBI-1045571; O76024; O14796-2: SH2D1B; NbExp=3; IntAct=EBI-720609, EBI-25899828; O76024; Q96B97: SH3KBP1; NbExp=3; IntAct=EBI-720609, EBI-346595; O76024; Q9NUL5-3: SHFL; NbExp=3; IntAct=EBI-720609, EBI-22000547; O76024; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-720609, EBI-2560428; O76024; O60902-3: SHOX2; NbExp=3; IntAct=EBI-720609, EBI-9092164; O76024; Q8N1H7: SIX6OS1; NbExp=3; IntAct=EBI-720609, EBI-12182077; O76024; P12757: SKIL; NbExp=3; IntAct=EBI-720609, EBI-2902468; O76024; Q13183: SLC13A2; NbExp=3; IntAct=EBI-720609, EBI-17460043; O76024; O15403: SLC16A6; NbExp=3; IntAct=EBI-720609, EBI-11041701; O76024; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-720609, EBI-12832276; O76024; Q86UG4-2: SLCO6A1; NbExp=3; IntAct=EBI-720609, EBI-21657139; O76024; O94933: SLITRK3; NbExp=3; IntAct=EBI-720609, EBI-20855537; O76024; P53814-5: SMTN; NbExp=3; IntAct=EBI-720609, EBI-11100581; O76024; Q2TAY7: SMU1; NbExp=3; IntAct=EBI-720609, EBI-298027; O76024; Q9HCE7-2: SMURF1; NbExp=3; IntAct=EBI-720609, EBI-9845742; O76024; Q92966: SNAPC3; NbExp=3; IntAct=EBI-720609, EBI-1760638; O76024; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-720609, EBI-11959123; O76024; A0A024R4B0: SPATA3; NbExp=3; IntAct=EBI-720609, EBI-14123856; O76024; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-720609, EBI-8635958; O76024; P20155: SPINK2; NbExp=3; IntAct=EBI-720609, EBI-10200479; O76024; Q8TCT8: SPPL2A; NbExp=3; IntAct=EBI-720609, EBI-750784; O76024; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-720609, EBI-7082156; O76024; Q9C004: SPRY4; NbExp=3; IntAct=EBI-720609, EBI-354861; O76024; Q8NEQ6: SRARP; NbExp=3; IntAct=EBI-720609, EBI-17858294; O76024; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-720609, EBI-18616594; O76024; O75886: STAM2; NbExp=3; IntAct=EBI-720609, EBI-373258; O76024; Q9UJZ1: STOML2; NbExp=3; IntAct=EBI-720609, EBI-1044428; O76024; A1L378: STRC; NbExp=3; IntAct=EBI-720609, EBI-22013242; O76024; P46977: STT3A; NbExp=3; IntAct=EBI-720609, EBI-719212; O76024; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-720609, EBI-357085; O76024; Q08AL9: STXBP4; NbExp=3; IntAct=EBI-720609, EBI-10318905; O76024; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-720609, EBI-723091; O76024; A1L190: SYCE3; NbExp=3; IntAct=EBI-720609, EBI-10283466; O76024; Q9H7C4: SYNC; NbExp=3; IntAct=EBI-720609, EBI-11285923; O76024; Q17RD7-3: SYT16; NbExp=3; IntAct=EBI-720609, EBI-25861603; O76024; Q9BQG1: SYT3; NbExp=3; IntAct=EBI-720609, EBI-17284568; O76024; Q8TDW5-2: SYTL5; NbExp=3; IntAct=EBI-720609, EBI-12243980; O76024; Q86TJ2-3: TADA2B; NbExp=3; IntAct=EBI-720609, EBI-18173581; O76024; Q8WUA7-2: TBC1D22A; NbExp=3; IntAct=EBI-720609, EBI-21575846; O76024; P62380: TBPL1; NbExp=3; IntAct=EBI-720609, EBI-716225; O76024; Q96EI5: TCEAL4; NbExp=3; IntAct=EBI-720609, EBI-2511291; O76024; Q8IYN2: TCEAL8; NbExp=3; IntAct=EBI-720609, EBI-2116184; O76024; Q9BQ70: TCF25; NbExp=3; IntAct=EBI-720609, EBI-745182; O76024; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-720609, EBI-3923210; O76024; Q13569: TDG; NbExp=3; IntAct=EBI-720609, EBI-348333; O76024; P28347-2: TEAD1; NbExp=3; IntAct=EBI-720609, EBI-12151837; O76024; Q96A09: TENT5B; NbExp=3; IntAct=EBI-720609, EBI-752030; O76024; P54274: TERF1; NbExp=2; IntAct=EBI-720609, EBI-710997; O76024; Q8NA77: TEX19; NbExp=3; IntAct=EBI-720609, EBI-13323487; O76024; P21980-2: TGM2; NbExp=3; IntAct=EBI-720609, EBI-25842075; O76024; Q9BTF0: THUMPD2; NbExp=3; IntAct=EBI-720609, EBI-15105991; O76024; O60830: TIMM17B; NbExp=3; IntAct=EBI-720609, EBI-2372529; O76024; O60220: TIMM8A; NbExp=3; IntAct=EBI-720609, EBI-1049822; O76024; Q9BXR5: TLR10; NbExp=3; IntAct=EBI-720609, EBI-16825459; O76024; A0AVI4-2: TMEM129; NbExp=3; IntAct=EBI-720609, EBI-25871541; O76024; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-720609, EBI-25830583; O76024; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-720609, EBI-10242677; O76024; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-720609, EBI-9089156; O76024; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-720609, EBI-25831574; O76024; P19429: TNNI3; NbExp=3; IntAct=EBI-720609, EBI-704146; O76024; P36406: TRIM23; NbExp=3; IntAct=EBI-720609, EBI-740098; O76024; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-720609, EBI-17716262; O76024; Q9BVS5: TRMT61B; NbExp=3; IntAct=EBI-720609, EBI-3197877; O76024; Q96Q11-3: TRNT1; NbExp=3; IntAct=EBI-720609, EBI-25861172; O76024; Q86WV8: TSC1; NbExp=3; IntAct=EBI-720609, EBI-12806590; O76024; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-720609, EBI-739485; O76024; A0A024RCB9: TSSC4; NbExp=3; IntAct=EBI-720609, EBI-25860845; O76024; Q99614: TTC1; NbExp=3; IntAct=EBI-720609, EBI-742074; O76024; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-720609, EBI-9090990; O76024; Q9BUF5: TUBB6; NbExp=3; IntAct=EBI-720609, EBI-356735; O76024; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-720609, EBI-10964469; O76024; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-720609, EBI-11988865; O76024; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-720609, EBI-9088812; O76024; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-720609, EBI-749370; O76024; Q8NBM4-4: UBAC2; NbExp=3; IntAct=EBI-720609, EBI-25840976; O76024; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-720609, EBI-348496; O76024; Q8N2K1: UBE2J2; NbExp=3; IntAct=EBI-720609, EBI-2340110; O76024; P61086: UBE2K; NbExp=3; IntAct=EBI-720609, EBI-473850; O76024; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-720609, EBI-11530712; O76024; O75604-3: USP2; NbExp=3; IntAct=EBI-720609, EBI-10696113; O76024; Q96B65: USP25; NbExp=3; IntAct=EBI-720609, EBI-25876491; O76024; A2RRA6: USP35; NbExp=3; IntAct=EBI-720609, EBI-22013216; O76024; P45880: VDAC2; NbExp=3; IntAct=EBI-720609, EBI-354022; O76024; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-720609, EBI-2850578; O76024; P58304: VSX2; NbExp=3; IntAct=EBI-720609, EBI-6427899; O76024; Q9BQA1: WDR77; NbExp=3; IntAct=EBI-720609, EBI-1237307; O76024; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-720609, EBI-7705033; O76024; Q15007-2: WTAP; NbExp=3; IntAct=EBI-720609, EBI-25840023; O76024; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-720609, EBI-12040603; O76024; O00308: WWP2; NbExp=6; IntAct=EBI-720609, EBI-743923; O76024; P12956: XRCC6; NbExp=3; IntAct=EBI-720609, EBI-353208; O76024; O95070: YIF1A; NbExp=3; IntAct=EBI-720609, EBI-2799703; O76024; P25490: YY1; NbExp=3; IntAct=EBI-720609, EBI-765538; O76024; O43167-2: ZBTB24; NbExp=3; IntAct=EBI-720609, EBI-25842419; O76024; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-720609, EBI-14104088; O76024; Q8TBF4: ZCRB1; NbExp=3; IntAct=EBI-720609, EBI-11124401; O76024; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-720609, EBI-524753; O76024; Q5W0Z9-4: ZDHHC20; NbExp=3; IntAct=EBI-720609, EBI-25840130; O76024; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-720609, EBI-711679; O76024; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-720609, EBI-2602314; O76024; Q15973: ZNF124; NbExp=3; IntAct=EBI-720609, EBI-2555767; O76024; P52744: ZNF138; NbExp=3; IntAct=EBI-720609, EBI-10746567; O76024; Q9UJW8-4: ZNF180; NbExp=3; IntAct=EBI-720609, EBI-12055755; O76024; Q9UK10: ZNF225; NbExp=3; IntAct=EBI-720609, EBI-21856539; O76024; Q16600: ZNF239; NbExp=3; IntAct=EBI-720609, EBI-8787052; O76024; Q9NR11-2: ZNF302; NbExp=3; IntAct=EBI-720609, EBI-12988373; O76024; Q8N895: ZNF366; NbExp=3; IntAct=EBI-720609, EBI-2813661; O76024; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-720609, EBI-8489702; O76024; Q8IYI8: ZNF440; NbExp=3; IntAct=EBI-720609, EBI-726439; O76024; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-720609, EBI-12010736; O76024; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-720609, EBI-25831733; O76024; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-720609, EBI-10486136; O76024; Q96C55: ZNF524; NbExp=3; IntAct=EBI-720609, EBI-10283126; O76024; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-720609, EBI-8490788; O76024; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-720609, EBI-10172590; O76024; Q96I27-2: ZNF625; NbExp=3; IntAct=EBI-720609, EBI-12038525; O76024; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-720609, EBI-12939666; O76024; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-720609, EBI-745276; O76024; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-720609, EBI-11090299; O76024; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-720609, EBI-25845217; O76024; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-720609, EBI-10251462; O76024; Q3KP31: ZNF791; NbExp=3; IntAct=EBI-720609, EBI-2849119; O76024; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-720609, EBI-18036029; O76024; Q16670: ZSCAN26; NbExp=3; IntAct=EBI-720609, EBI-3920053; O76024; O15535: ZSCAN9; NbExp=3; IntAct=EBI-720609, EBI-751531; O76024; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-720609, EBI-1538838; O76024; A0A384ME25; NbExp=3; IntAct=EBI-720609, EBI-10211777; O76024; Q7L8T7; NbExp=3; IntAct=EBI-720609, EBI-25831943; O76024; Q7Z783; NbExp=3; IntAct=EBI-720609, EBI-9088990; O76024; Q86V28; NbExp=3; IntAct=EBI-720609, EBI-10259496; O76024; Q9BQ29; NbExp=3; IntAct=EBI-720609, EBI-22013570; Endoplasmic reticulum membrane ; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle Note=Co-localizes with ATP6V1A in the secretory granules in neuroblastoma cell lines. Highly expressed in heart followed by brain, placenta, lung and pancreas. Weakly expressed in liver, kidney and skeletal muscle. Also expressed in islet and beta-cell insulinoma cell line. Arg-456-His, Arg-611-His and Ile-720-Val polymorphisms are in tight linkage disequilibrium with one another and associated with type 1 diabetes in Japanese. Wolfram syndrome 1 (WFS1) [MIM:222300]: A rare disorder characterized by juvenile-onset insulin-dependent diabetes mellitus with optic atrophy. Other manifestations include diabetes insipidus, sensorineural deafness, dementia, psychiatric illnesses. te=The disease is caused by variants affecting the gene represented in this entry. Deafness, autosomal dominant, 6 (DFNA6) [MIM:600965]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA6 is a low-frequency hearing loss in which frequencies of 2000 Hz and below are predominantly affected. Many patients have tinnitus, but there are otherwise no associated features such as vertigo. Because high-frequency hearing is generally preserved, patients retain excellent understanding of speech, although presbycusis or noise exposure may cause high-frequency loss later in life. DFNA6 worsens over time without progressing to profound deafness. te=The disease is caused by variants affecting the gene represented in this entry. Wolfram-like syndrome autosomal dominant (WFSL) [MIM:614296]: A disease characterized by the clinical triad of congenital progressive hearing impairment, diabetes mellitus, and optic atrophy. The hearing impairment, which is usually diagnosed in the first decade of life, is relatively constant and alters mainly low- and middle-frequency ranges. te=The disease is caused by variants affecting the gene represented in this entry. Cataract 41 (CTRCT41) [MIM:116400]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. Note=The disease is caused by variants affecting the gene represented in this entry. negative regulation of transcription from RNA polymerase II promoter kidney development renal water homeostasis protein binding calmodulin binding endoplasmic reticulum endoplasmic reticulum lumen endoplasmic reticulum membrane ER overload response visual perception sensory perception of sound membrane integral component of membrane protein maturation by protein folding integral component of endoplasmic reticulum membrane integral component of synaptic vesicle membrane dendrite ER-associated ubiquitin-dependent protein catabolic process endoplasmic reticulum unfolded protein response pancreas development positive regulation of protein ubiquitination ubiquitin protein ligase binding endoplasmic reticulum calcium ion homeostasis activating transcription factor binding response to endoplasmic reticulum stress IRE1-mediated unfolded protein response olfactory behavior glucose homeostasis negative regulation of programmed cell death negative regulation of sequence-specific DNA binding transcription factor activity negative regulation of neuron apoptotic process post-translational protein modification cellular protein metabolic process positive regulation of growth calcium-dependent protein binding protein stabilization neurological system process ATPase binding positive regulation of protein metabolic process positive regulation of calcium ion transport calcium ion homeostasis proteasome binding negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway negative regulation of ATF6-mediated unfolded protein response negative regulation of type B pancreatic cell apoptotic process uc003gix.1 uc003gix.2 uc003gix.3 
ENST00000226796.7 GAR1 ENST00000226796.7 GAR1 ribonucleoprotein, transcript variant 1 (from RefSeq NM_018983.4) ENST00000226796.1 ENST00000226796.2 ENST00000226796.3 ENST00000226796.4 ENST00000226796.5 ENST00000226796.6 GAR1_HUMAN NM_018983 NOLA1 Q5MJQ2 Q9NY12 uc003hzt.1 uc003hzt.2 uc003hzt.3 uc003hzt.4 uc003hzt.5 This gene is a member of the H/ACA snoRNPs (small nucleolar ribonucleoproteins) gene family. snoRNPs are involved in various aspects of rRNA processing and modification and have been classified into two families: C/D and H/ACA. The H/ACA snoRNPs also include the DKC1, NOLA2 and NOLA3 proteins. These four H/ACA snoRNP proteins localize to the dense fibrillar components of nucleoli and to coiled (Cajal) bodies in the nucleus. Both 18S rRNA production and rRNA pseudouridylation are impaired if any one of the four proteins is depleted. These four H/ACA snoRNP proteins are also components of the telomerase complex. The encoded protein of this gene contains two glycine- and arginine-rich domains and is related to Saccharomyces cerevisiae Gar1p. Two splice variants have been found for this gene. [provided by RefSeq, Jul 2008]. Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit (PubMed:11509230, PubMed:12244096). The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1 (PubMed:11509230, PubMed:12244096). The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate (PubMed:11509230, PubMed:12244096). The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs (PubMed:11509230, PubMed:12244096). Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2 (PubMed:11509230, PubMed:12244096). Associates with NOLC1/NOPP140 (PubMed:11509230, PubMed:12244096). H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4 (PubMed:11509230, PubMed:12244096). This is mediated by interaction between GAR1 and SMN1 or SMN2 (PubMed:11509230, PubMed:12244096). The SMN complex may be required for correct assembly of the H/ACA snoRNP complex (PubMed:11509230, PubMed:12244096). Component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC) (PubMed:19179534, PubMed:20351177, PubMed:29695869). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1 (PubMed:19179534). Nucleus, nucleolus. Nucleus, Cajal body. Note=Also localized to Cajal bodies (coiled bodies). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NY12-1; Sequence=Displayed; Name=2; IsoId=Q9NY12-2; Sequence=VSP_014594; Interaction with SMN1 requires at least one of the RGG-box regions. Belongs to the GAR1 family. snoRNA guided rRNA pseudouridine synthesis nuclear chromosome, telomeric region pseudouridine synthesis fibrillar center RNA binding protein binding nucleus nucleoplasm telomerase holoenzyme complex nucleolus rRNA processing telomere maintenance via telomerase Cajal body rRNA pseudouridine synthesis box H/ACA snoRNP complex box H/ACA snoRNA binding ribosome biogenesis telomerase RNA binding box H/ACA scaRNP complex box H/ACA telomerase RNP complex uc003hzt.1 uc003hzt.2 uc003hzt.3 uc003hzt.4 uc003hzt.5 
ENST00000226798.9 FRG1 ENST00000226798.9 FSHD region gene 1 (from RefSeq NM_004477.3) A8K775 ENST00000226798.1 ENST00000226798.2 ENST00000226798.3 ENST00000226798.4 ENST00000226798.5 ENST00000226798.6 ENST00000226798.7 ENST00000226798.8 FRG1 FRG1_HUMAN NM_004477 Q14331 uc003izs.1 uc003izs.2 uc003izs.3 uc003izs.4 uc003izs.5 This gene maps to a location 100 kb centromeric of the repeat units on chromosome 4q35 which are deleted in facioscapulohumeral muscular dystrophy (FSHD). It is evolutionarily conserved and has related sequences on multiple human chromosomes but DNA sequence analysis did not reveal any homology to known genes. In vivo studies demonstrate the encoded protein is localized to the nucleolus. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC053997.1, AK291890.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226798.9/ ENSP00000226798.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Binds to mRNA in a sequence-independent manner. May play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. May be involved in mRNA transport. May be involved in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. Homodimer and homotetramer in solution. Identified in the spliceosome C complex. Interacts with KMT5B (via C-terminus). Interacts (via N-terminus) with KPNA2 and NXF1/TAP. Interacts with F-actin with a stoichiometry of 2:1. Interacts with GARIN3, SMN1 and PABPN1 (PubMed:17103222). Q14331; Q9HCG8: CWC22; NbExp=2; IntAct=EBI-2515248, EBI-373289; Q14331; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-2515248, EBI-371922; Q14331; Q14749: GNMT; NbExp=3; IntAct=EBI-2515248, EBI-744239; Q14331; Q6A162: KRT40; NbExp=3; IntAct=EBI-2515248, EBI-10171697; Q14331; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2515248, EBI-741037; Nucleus, Cajal body cleus, nucleolus toplasm toplasm, myofibril, sarcomere, Z line Note=Localization changes during myogenesis from mainly cytoplasmic in undifferentiated myoblasts, to strongly nucleolar in early myotubes and back to cytoplasmic 5 days post-differentiation (PubMed:20970242). Localized at the Z-line in the sarcomere of matured myotubes 8 days post-differentiation (PubMed:20970242). Expressed in adult muscle, lymphocytes, fetal brain, muscle, and placenta. Also expressed in the smooth muscle of arteries and veins, the sweat glands and the epidermis. Facioscapulohumeral muscular dystrophy 1 (FSHD1) [MIM:158900]: A degenerative muscle disease characterized by slowly progressive weakness of the muscles of the face, upper-arm, and shoulder girdle. The onset of symptoms usually occurs in the first or second decade of life. Affected individuals usually present with impairment of upper extremity elevation. This tends to be followed by facial weakness, primarily involving the orbicularis oris and orbicularis oculi muscles. Note=The gene represented in this entry may be involved in disease pathogenesis. Overexpression of human FRG1 in mice leads to development of facioscapulohumeral muscular dystrophy (FSHD1)-like symptoms such as kyphosis, progressive muscle dystrophy and skeletal muscle atrophy (PubMed:16341202). It also causes aberrant pre-mRNA splicing of TNNT3 and MTMR1, affects the localization and activity of KMT5B, and leads to increased levels of EID3, resulting in inhibited muscle differentiation (PubMed:23720823). These results suggest that FSHD1 results from inappropriate overexpression of FRG1 which leads to abnormal alternative splicing of specific pre-mRNAs. Belongs to the FRG1 family. Was originally thought to be located in nuclear speckles based on overexpression of the protein (PubMed:15060122). However, the endogenous protein was later shown not be expressed in nuclear speckles (PubMed:21699900). mRNA splicing, via spliceosome RNA binding actin binding protein binding nucleus spliceosomal complex nucleolus cytoplasm rRNA processing mRNA processing muscle organ development RNA splicing Cajal body Z disc ribosome biogenesis actin filament binding striated muscle dense body catalytic step 2 spliceosome uc003izs.1 uc003izs.2 uc003izs.3 uc003izs.4 uc003izs.5 
ENST00000226951.11 CLNK ENST00000226951.11 cytokine dependent hematopoietic cell linker (from RefSeq NM_052964.4) CLNK_HUMAN ENST00000226951.1 ENST00000226951.10 ENST00000226951.2 ENST00000226951.3 ENST00000226951.4 ENST00000226951.5 ENST00000226951.6 ENST00000226951.7 ENST00000226951.8 ENST00000226951.9 MIST NM_052964 Q05C27 Q7Z7G1 Q9P2U9 uc003gmo.1 uc003gmo.2 uc003gmo.3 uc003gmo.4 uc003gmo.5 uc003gmo.6 MIST is a member of the SLP76 family of adaptors (see LCP2, MIM 601603; BLNK, MIM 604515). MIST plays a role in the regulation of immunoreceptor signaling, including PLC-gamma (PLCG1; MIM 172420)-mediated B cell antigen receptor (BCR) signaling and FC-epsilon R1 (see FCER1A, MIM 147140)-mediated mast cell degranulation (Cao et al., 1999 [PubMed 10562326]; Goitsuka et al., 2000, 2001 [PubMed 10744659] [PubMed 11463797]).[supplied by OMIM, Mar 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: AK093001.1, AB110420.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA2152719 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000226951.11/ ENSP00000226951.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## An adapter protein which plays a role in the regulation of immunoreceptor signaling, including PLC-gamma-mediated B-cell antigen receptor (BCR) signaling and FC-epsilon R1-mediated mast cell degranulation (By similarity). Together with FGR, it acts as a negative regulator of natural killer cell-activating receptors and inhibits interferon-gamma production (By similarity). Acts as a positive regulator of both T-cell receptor and natural killer T (NKT) cell receptor signaling in CD4-positive NKT cells (By similarity). Together with MAP4K1, it enhances CD3-triggered activation of T-cells and subsequent IL2 production (By similarity). May be involved in tumor necrosis factor induced cell death by promoting reactive oxidative species generation, and MLKL oligomerization, ultimately leading to necrosis (By similarity). Involved in phosphorylation of LAT (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity). When phosphorylated, interacts with PLCG1, PLCG2, GRB2, VAV and LAT (By similarity). Interacts with LBR and AGO2 (PubMed:26009488). Interacts with FGR (By similarity). Part of a complex consisting of CLNK, SKAP1 and FYB1 (By similarity). Interacts (via SH2 domain) with FYB1; this interaction allows SKAP1 and FYB1 to promote tyrosine phosphorylation of CLNK by LYN (By similarity). Interacts (via SH2 domain) with MAP4K1 (By similarity). Q7Z7G1; P00533: EGFR; NbExp=2; IntAct=EBI-7878194, EBI-297353; Q7Z7G1; P04626: ERBB2; NbExp=2; IntAct=EBI-7878194, EBI-641062; Cytoplasm Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q7Z7G1-1; Sequence=Displayed; Name=2; IsoId=Q7Z7G1-2; Sequence=VSP_030330, VSP_030332, VSP_030333; Name=3; IsoId=Q7Z7G1-3; Sequence=VSP_030331; The N-terminal proline-rich region interacts with the SH3 domain of PLCG1. The SH2 domain is important for restoration of BCR-induced calcium response and JNK2 activation in BLNK-deficient DT40 cells expressing LAT. Tyrosine-phosphorylated upon BCR cross-linking. Tyrosine phosphorylation at both Tyr-69 and Tyr-96 are required for BCR-induced calcium response and are essential to restore PLCG2-mediated signaling in BLNK-deficient DT40 cells, but this phosphorylation is dispensable in cells expressing LAT. Interacts with the SH2 domain of PLCG1 via phosphorylated Tyr-96 (By similarity). Tyrosine phosphorylation is increased when complexed with SKAP1 and FYB1 (By similarity). positive regulation of natural killer cell cytokine production SH3/SH2 adaptor activity protein binding cytoplasm immune response transmembrane receptor protein tyrosine kinase signaling pathway positive regulation of signal transduction regulation of cell death negative regulation of natural killer cell activation intracellular signal transduction uc003gmo.1 uc003gmo.2 uc003gmo.3 uc003gmo.4 uc003gmo.5 uc003gmo.6 
ENST00000227135.7 SPA17 ENST00000227135.7 sperm autoantigenic protein 17 (from RefSeq NM_017425.4) B2R4F2 ENST00000227135.1 ENST00000227135.2 ENST00000227135.3 ENST00000227135.4 ENST00000227135.5 ENST00000227135.6 NM_017425 Q15506 Q9BXF7 SP17 SP17_HUMAN uc001qap.1 uc001qap.2 uc001qap.3 uc001qap.4 uc001qap.5 This gene encodes a protein present at the cell surface. The N-terminus has sequence similarity to human cAMP-dependent protein kinase A (PKA) type II alpha regulatory subunit (RIIa) while the C-terminus has an IQ calmodulin-binding motif. The central portion of the protein has carbohydrate binding motifs and likely functions in cell-cell adhesion. The protein was initially characterized by its involvement in the binding of sperm to the zona pellucida of the oocyte. Recent studies indicate that it is also involved in additional cell-cell adhesion functions such as immune cell migration and metastasis. A retrotransposed pseudogene is present on chromosome 10q22.[provided by RefSeq, Jan 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803613.223840.1, SRR1803617.128145.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates (By similarity). Homodimer (By similarity). May interact with ROPN1. Q15506; P35609: ACTN2; NbExp=3; IntAct=EBI-1377865, EBI-77797; Q15506; O43687-2: AKAP7; NbExp=6; IntAct=EBI-1377865, EBI-10185182; Q15506; P14649: MYL6B; NbExp=12; IntAct=EBI-1377865, EBI-358570; Q15506; Q9HAT0: ROPN1; NbExp=9; IntAct=EBI-1377865, EBI-1378139; Q15506; Q96C74: ROPN1L; NbExp=4; IntAct=EBI-1377865, EBI-9033237; Membrane ; Peripheral membrane protein Testis and sperm specific. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42360/SPA17"; epithelial cilium movement protein binding calmodulin binding extracellular region cytoplasm cilium spermatogenesis single fertilization binding of sperm to zona pellucida external side of plasma membrane membrane motile cilium sperm fibrous sheath sperm principal piece uc001qap.1 uc001qap.2 uc001qap.3 uc001qap.4 uc001qap.5 
ENST00000227155.9 CD82 ENST00000227155.9 CD82 molecule, transcript variant 1 (from RefSeq NM_002231.4) CD82_HUMAN D3DQN6 E9PC70 ENST00000227155.1 ENST00000227155.2 ENST00000227155.3 ENST00000227155.4 ENST00000227155.5 ENST00000227155.6 ENST00000227155.7 ENST00000227155.8 KAI1 NM_002231 P27701 Q7Z2D4 Q7Z5N2 SAR2 ST6 TSPAN27 uc001myc.1 uc001myc.2 uc001myc.3 uc001myc.4 uc001myc.5 This metastasis suppressor gene product is a membrane glycoprotein that is a member of the transmembrane 4 superfamily. Expression of this gene has been shown to be downregulated in tumor progression of human cancers and can be activated by p53 through a consensus binding sequence in the promoter. Its expression and that of p53 are strongly correlated, and the loss of expression of these two proteins is associated with poor survival for prostate cancer patients. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway. Interacts directly with IGSF8. P27701; O15552: FFAR2; NbExp=3; IntAct=EBI-682379, EBI-2833872; P27701; P26715: KLRC1; NbExp=3; IntAct=EBI-682379, EBI-9018187; P27701; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-682379, EBI-741850; P27701; P01033: TIMP1; NbExp=11; IntAct=EBI-682379, EBI-712536; P27701; Q8TAA9: VANGL1; NbExp=6; IntAct=EBI-682379, EBI-682393; Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P27701-1; Sequence=Displayed; Name=2; IsoId=P27701-2; Sequence=VSP_045656; Lymphoid specific. Belongs to the tetraspanin (TM4SF) family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41045/CD82"; protein binding plasma membrane integral component of plasma membrane membrane integral component of membrane extracellular exosome uc001myc.1 uc001myc.2 uc001myc.3 uc001myc.4 uc001myc.5 
ENST00000227266.10 CTSC ENST00000227266.10 cathepsin C, transcript variant 1 (from RefSeq NM_001814.6) A8K7V2 B5MDD5 CATC_HUMAN CPPI ENST00000227266.1 ENST00000227266.2 ENST00000227266.3 ENST00000227266.4 ENST00000227266.5 ENST00000227266.6 ENST00000227266.7 ENST00000227266.8 ENST00000227266.9 NM_001814 P53634 Q2HIY8 Q53G93 Q71E75 Q71E76 Q7M4N9 Q7Z3G7 Q7Z5U7 Q8WY99 Q8WYA7 Q8WYA8 uc001pck.1 uc001pck.2 uc001pck.3 uc001pck.4 uc001pck.5 uc001pck.6 This gene encodes a member of the peptidase C1 family and lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in cells of the immune system. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate heavy and light chains that form a disulfide-linked dimer. A portion of the propeptide acts as an intramolecular chaperone for the folding and stabilization of the mature enzyme. This enzyme requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. [provided by RefSeq, Nov 2015]. Thiol protease (PubMed:1586157). Has dipeptidylpeptidase activity (PubMed:1586157). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:1586157). Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate (PubMed:1586157). Can act as both an exopeptidase and endopeptidase (PubMed:1586157). Activates serine proteases such as elastase, cathepsin G and granzymes A and B (PubMed:8428921). Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.; EC=3.4.14.1; Evidence=; Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence=; Note=Binds 1 Cl(-) ion per heavy chain. ; Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N- ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators. pH dependence: High activity at pH 4.5-6.8. ; Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains. P53634; O76096: CST7; NbExp=2; IntAct=EBI-1047323, EBI-2807448; P53634; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1047323, EBI-10976677; P53634; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1047323, EBI-5235340; Lysosome Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P53634-1; Sequence=Displayed; Name=2; IsoId=P53634-2; Sequence=VSP_039123, VSP_039124; Name=3; IsoId=P53634-3; Sequence=VSP_043232, VSP_043233; Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas. Up-regulated in lymphocytes by IL2/interleukin-2. N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes. In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond. Papillon-Lefevre syndrome (PLS) [MIM:245000]: An autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees. te=The disease is caused by variants affecting the gene represented in this entry. Haim-Munk syndrome (HMS) [MIM:245010]: An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis. Note=The disease is caused by variants affecting the gene represented in this entry. Periodontititis, aggressive, 1 (AP1) [MIM:170650]: A disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the peptidase C1 family. Sequence=CAD97897.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=CTSCbase; Note=CTSC mutation db; URL="http://structure.bmc.lu.se/idbase/CTSCbase/"; Golgi membrane T cell mediated cytotoxicity cysteine-type endopeptidase activity serine-type endopeptidase activity protein binding extracellular region extracellular space nucleoplasm cytoplasm lysosome endoplasmic reticulum endoplasmic reticulum lumen Golgi apparatus centrosome proteolysis ER to Golgi vesicle-mediated transport apoptotic process immune response aging peptidase activity cysteine-type peptidase activity response to organic substance membrane peptidase activator activity involved in apoptotic process hydrolase activity phosphatase binding ER to Golgi transport vesicle chloride ion binding negative regulation of myelination endoplasmic reticulum-Golgi intermediate compartment membrane azurophil granule lumen identical protein binding intracellular membrane-bounded organelle neutrophil degranulation protein self-association COPII vesicle coating chaperone binding proteolysis involved in cellular protein catabolic process extracellular exosome positive regulation of proteolysis involved in cellular protein catabolic process positive regulation of microglial cell activation positive regulation of apoptotic signaling pathway uc001pck.1 uc001pck.2 uc001pck.3 uc001pck.4 uc001pck.5 uc001pck.6 
ENST00000227322.8 ZPR1 ENST00000227322.8 ZPR1 zinc finger, transcript variant 1 (from RefSeq NM_003904.5) ENST00000227322.1 ENST00000227322.2 ENST00000227322.3 ENST00000227322.4 ENST00000227322.5 ENST00000227322.6 ENST00000227322.7 NM_003904 O75312 Q2TAA0 ZNF259 ZPR1_HUMAN uc001ppp.1 uc001ppp.2 uc001ppp.3 uc001ppp.4 uc001ppp.5 The protein encoded by this gene is found in the cytoplasm of quiescent cells but translocates to the nucleolus in proliferating cells. The encoded protein interacts with survival motor neuron protein (SMN1) to enhance pre-mRNA splicing and to induce neuronal differentiation and axonal growth. Defects in this gene or the SMN1 gene can cause spinal muscular atrophy. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015]. Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. It is involved in the positive regulation of cell cycle progression (PubMed:29851065). Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death. Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Interacts (via C-terminal region) with SMN1 (via C- terminal region); the interaction occurs after treatment with serum. Interacts with elongation factor 1-alpha EEF1A1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner. Interacts (via zinc fingers) with EGFR (via C-terminal cytoplasmic kinase domain); the interaction is negatively regulated in response to epidermal growth factor (EGF) stimulation and the EGFR kinase activity. May also bind to the PDGFR receptor. Nucleus. Nucleus, nucleolus. Nucleus, gem. Nucleus, Cajal body. Cytoplasm, perinuclear region. Cytoplasm. Cell projection, axon Cell projection, growth cone Note=Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle- dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. Expressed in fibroblast; weakly expressed in fibroblast of spinal muscular atrophy (SMA) patients. Growth restriction, hypoplastic kidneys, alopecia, and distinctive facies (GKAF) [MIM:619321]: An autosomal recessive disorder characterized by pre- and postnatal growth restriction with microcephaly, distinctive craniofacial features, congenital alopecia, hypoplastic kidneys with renal insufficiency, global developmental delay, severe congenital sensorineural hearing loss, hydrocephalus, genital hypoplasia, and early mortality. Note=The disease may be caused by variants affecting the gene represented in this entry. Belongs to the ZPR1 family. microtubule cytoskeleton organization inner cell mass cell proliferation trophectodermal cell proliferation protein binding nucleus nucleoplasm nucleolus cytoplasm mRNA processing signal transduction zinc ion binding RNA splicing positive regulation of gene expression Cajal body spinal cord development cell differentiation axon growth cone Cajal body organization receptor tyrosine kinase binding translation initiation factor binding regulation of myelination positive regulation of RNA splicing DNA endoreduplication positive regulation of protein import into nucleus cell projection neuronal cell body perikaryon positive regulation of growth metal ion binding perinuclear region of cytoplasm axon development cellular response to epidermal growth factor stimulus positive regulation of transcription involved in G1/S transition of mitotic cell cycle Gemini of coiled bodies apoptotic process involved in development pre-mRNA catabolic process negative regulation of motor neuron apoptotic process uc001ppp.1 uc001ppp.2 uc001ppp.3 uc001ppp.4 uc001ppp.5 
ENST00000227348.9 CRTAM ENST00000227348.9 cytotoxic and regulatory T cell molecule, transcript variant 1 (from RefSeq NM_019604.4) CRTAM CRTAM_HUMAN ENST00000227348.1 ENST00000227348.2 ENST00000227348.3 ENST00000227348.4 ENST00000227348.5 ENST00000227348.6 ENST00000227348.7 ENST00000227348.8 NM_019604 O95727 Q59EI1 Q6IRX2 uc001pyj.1 uc001pyj.2 uc001pyj.3 uc001pyj.4 uc001pyj.5 The CRTAM gene is upregulated in CD4 (see MIM 186940)-positive and CD8 (see CD8A; MIM 186910)-positive T cells and encodes a type I transmembrane protein with V and C1-like Ig domains (Yeh et al., 2008 [PubMed 18329370]).[supplied by OMIM, Feb 2009]. Mediates heterophilic cell-cell adhesion which regulates the activation, differentiation and tissue retention of various T-cell subsets (By similarity). Interaction with CADM1 promotes natural killer (NK) cell cytotoxicity and IFNG/interferon-gamma secretion by CD8+ T- cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM1 in vivo (PubMed:15811952). Regulates CD8+ T-cell proliferation in response to T-cell receptor (TCR) activation (By similarity). Appears to be dispensable for CD8+ T-cell-mediated cytotoxicity (By similarity). Interaction with SCRIB promotes the late phase of cellular polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG, IL17 and IL22 production (By similarity). By interacting with CADM1 on CD8+ dendritic cells, regulates the retention of activated CD8+ T-cells within the draining lymph node (By similarity). Required for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells (By similarity). Interaction with CADM1 promotes the adhesion to gut- associated CD103+ dendritic cells, which may facilitate the expression of gut-homing and adhesion molecules on T-cells and the conversion of CD4+ T-cells into CD4+ CD8+ T-cells (By similarity). Monomer (PubMed:23583034). May form homodimer (via Ig-like V- type domain) (PubMed:23583034, PubMed:23871486). Interacts (via Ig-like V-type domain) with CADM1 (via Ig-like V-type domain); the interaction competes with CRTAM homodimerization and CADM1 homodimerization (PubMed:15781451, PubMed:15811952, PubMed:23871486). Interacts (via PDZ-binding motif) with SCRIB (via PDZ domain 3); the interaction promotes CRTAM and SCRIB polarization in a subset of CD4+ T-cells (By similarity). O95727-1; Q9BY67: CADM1; NbExp=4; IntAct=EBI-16044697, EBI-5652260; O95727-1; O95727-1: CRTAM; NbExp=5; IntAct=EBI-16044697, EBI-16044697; Cell membrane ; Single-pass type I membrane protein Note=In a subset of CD4+ T-cells, colocalizes with SCRIB at the immunological synapse during the late phase of T-cell activation. Event=Alternative splicing; Named isoforms=2; Name=1 ; IsoId=O95727-1; Sequence=Displayed; Name=2; IsoId=O95727-2; Sequence=VSP_052471, VSP_052472; In the immune system, expression is restricted to activated class-I MHC-restricted cells, including NKT and CD8 T-cells (PubMed:10811014, PubMed:15811952, PubMed:16300832). Strongly expressed in spleen, thymus, small intestine, peripheral blood leukocyte, and in Purkinje neurons in cerebellum. Expressed at much lower levels in testis, ovary, colon, lung and lymphoid tissues (PubMed:16300832). The extracellular domain is required for the regulation of IFNG and IL22 production, but is dispensable for late T-cell polarization. Belongs to the nectin family. Sequence=BAD93067.1; Type=Erroneous initiation; Evidence=; adaptive immune response detection of tumor cell immune system process positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target receptor binding protein binding plasma membrane cell recognition membrane integral component of membrane identical protein binding positive regulation of natural killer cell mediated cytotoxicity positive regulation of cytokine secretion regulation of immune response detection of stimulus T cell mediated cytotoxicity activated T cell proliferation uc001pyj.1 uc001pyj.2 uc001pyj.3 uc001pyj.4 uc001pyj.5 
ENST00000227349.7 JHY ENST00000227349.7 junctional cadherin complex regulator, transcript variant 1 (from RefSeq NM_024806.4) A8K6G0 C11orf63 ENST00000227349.1 ENST00000227349.2 ENST00000227349.3 ENST00000227349.4 ENST00000227349.5 ENST00000227349.6 JHY JHY_HUMAN NM_024806 Q6NUN7 Q96GB5 Q9H5D6 uc001pym.1 uc001pym.2 uc001pym.3 uc001pym.4 uc001pym.5 uc001pym.6 Required for the normal development of cilia in brain ependymal cells lining the ventricular surfaces. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6NUN7-1; Sequence=Displayed; Name=2; IsoId=Q6NUN7-2; Sequence=VSP_023915, VSP_023916; Sequence=AAH09820.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=BAB15691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; brain development cell projection organization ciliary basal body organization cerebrospinal fluid secretion axoneme assembly uc001pym.1 uc001pym.2 uc001pym.3 uc001pym.4 uc001pym.5 uc001pym.6 
ENST00000227451.4 DTX4 ENST00000227451.4 deltex E3 ubiquitin ligase 4, transcript variant 1 (from RefSeq NM_015177.2) DTX4_HUMAN ENST00000227451.1 ENST00000227451.2 ENST00000227451.3 KIAA0937 NM_015177 Q0VF38 Q9Y2E6 RNF155 uc001nns.1 uc001nns.2 uc001nns.3 uc001nns.4 Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations (By similarity). Functions as a ubiquitin ligase protein in vivo, mediating 'Lys48'-linked polyubiquitination and promoting degradation of TBK1, targeting to TBK1 requires interaction with NLRP4. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence=; Protein modification; protein ubiquitination. Interacts with NLRP4. Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y2E6-1; Sequence=Displayed; Name=2; IsoId=Q9Y2E6-2; Sequence=VSP_023784; The WWE domains are thought to mediate some protein-protein interaction, and are frequently found in ubiquitin ligases. Belongs to the Deltex family. Sequence=BAA76781.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; ubiquitin-protein transferase activity cytoplasm cytosol Notch signaling pathway zinc ion binding protein ubiquitination transferase activity regulation of type I interferon production metal ion binding uc001nns.1 uc001nns.2 uc001nns.3 uc001nns.4 
ENST00000227471.7 UNC93B1 ENST00000227471.7 unc-93 homolog B1, TLR signaling regulator (from RefSeq NM_030930.4) ENST00000227471.1 ENST00000227471.2 ENST00000227471.3 ENST00000227471.4 ENST00000227471.5 ENST00000227471.6 NM_030930 O95764 Q569H6 Q710D4 Q9H1C4 UN93B_HUMAN UNC93 UNC93B UNC93B1 uc031xth.1 uc031xth.2 This gene encodes a protein that is involved in innate and adaptive immune response by regulating toll-like receptor signaling. The encoded protein traffics nucleotide sensing toll-like receptors to the endolysosome from the endoplasmic reticulum. Deficiency of the encoded protein has been associated with herpes simplex encephalitis. [provided by RefSeq, Feb 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1053743.1, SRR3476690.884834.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000227471.7/ ENSP00000227471.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Plays an important role in innate and adaptive immunity by regulating nucleotide-sensing Toll-like receptor (TLR) signaling. Required for the transport of a subset of TLRs (including TLR3, TLR7 and TLR9) from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. May play a role in autoreactive B-cells removal. Interacts with TLR3, TLR5, TLR7, and TLR9 (probably via transmembrane domain). Q9H1C4; Q8NFU1: BEST2; NbExp=3; IntAct=EBI-4401271, EBI-19947314; Q9H1C4; Q8WV48: CCDC107; NbExp=3; IntAct=EBI-4401271, EBI-947033; Q9H1C4; P11912: CD79A; NbExp=3; IntAct=EBI-4401271, EBI-7797864; Q9H1C4; O95471: CLDN7; NbExp=3; IntAct=EBI-4401271, EBI-740744; Q9H1C4; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-4401271, EBI-6942903; Q9H1C4; P55060: CSE1L; NbExp=2; IntAct=EBI-4401271, EBI-286709; Q9H1C4; Q15125: EBP; NbExp=3; IntAct=EBI-4401271, EBI-3915253; Q9H1C4; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-4401271, EBI-781551; Q9H1C4; Q969F0: FATE1; NbExp=3; IntAct=EBI-4401271, EBI-743099; Q9H1C4; O14843: FFAR3; NbExp=3; IntAct=EBI-4401271, EBI-17762181; Q9H1C4; Q96P66: GPR101; NbExp=3; IntAct=EBI-4401271, EBI-17935713; Q9H1C4; O60883: GPR37L1; NbExp=3; IntAct=EBI-4401271, EBI-2927498; Q9H1C4; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-4401271, EBI-13067820; Q9H1C4; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-4401271, EBI-2867874; Q9H1C4; P26715: KLRC1; NbExp=3; IntAct=EBI-4401271, EBI-9018187; Q9H1C4; Q14974: KPNB1; NbExp=2; IntAct=EBI-4401271, EBI-286758; Q9H1C4; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-4401271, EBI-10173166; Q9H1C4; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-4401271, EBI-17490413; Q9H1C4; Q9H400: LIME1; NbExp=3; IntAct=EBI-4401271, EBI-2830566; Q9H1C4; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-4401271, EBI-11956541; Q9H1C4; Q9H902: REEP1; NbExp=3; IntAct=EBI-4401271, EBI-1644241; Q9H1C4; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-4401271, EBI-17295964; Q9H1C4; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-4401271, EBI-17280858; Q9H1C4; Q9H7V2: SYNDIG1; NbExp=3; IntAct=EBI-4401271, EBI-726331; Q9H1C4; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-4401271, EBI-13351685; Q9H1C4; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-4401271, EBI-10982110; Q9H1C4; P0DTD8: 7b; Xeno; NbExp=2; IntAct=EBI-4401271, EBI-25475914; Endoplasmic reticulum membrane ; Multi-pass membrane protein Endosome Lysosome Cytoplasmic vesicle, phagosome Note=Relocalizes from endoplasmic reticulum to endosome and lysosome upon cell-stimulation with CpG dinucleotides (By similarity). Colocalizes with LAMP5 in large endosomal intracellular vesicles. Expressed in plasmocytoid dendritic cells (at protein level). Highly expressed in antigen-presenting cells. Expressed in heart, and at lower level in kidney. Expressed at low level in other tissues. Up-regulated by TLRs agonists. N-glycosylated. Encephalopathy, acute, infection-induced, 1, herpes-specific (IIAE1) [MIM:610551]: A rare complication of human herpesvirus 1 (HHV- 1) infection, occurring in only a small minority of HHV-1 infected individuals. It is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mutations in UNC93B1 resulting in autosomal recessive UNC93B1 deficiency predispose otherwise healthy individuals to isolated herpes simplex encephalitis due to impaired IFNs production. UNC93B1 deficiency, however, does not compromise immunity to most pathogens, unlike most known primary immunodeficiencies. Belongs to the unc-93 family. Sequence=AAD15416.1; Type=Erroneous gene model prediction; Evidence=; Name=UNC93B1base; Note=UNC93B1 mutation db; URL="http://structure.bmc.lu.se/idbase/UNC93B1base/"; Golgi membrane toll-like receptor signaling pathway adaptive immune response immune system process protein binding lysosome endosome endoplasmic reticulum endoplasmic reticulum membrane intracellular protein transport membrane integral component of membrane cytoplasmic vesicle early phagosome toll-like receptor 3 signaling pathway toll-like receptor 7 signaling pathway toll-like receptor 9 signaling pathway Toll-like receptor binding innate immune response phagocytic vesicle defense response to virus uc031xth.1 uc031xth.2 
ENST00000227474.8 PUS3 ENST00000227474.8 pseudouridine synthase 3, transcript variant 1 (from RefSeq NM_031307.4) B2RAM0 ENST00000227474.1 ENST00000227474.2 ENST00000227474.3 ENST00000227474.4 ENST00000227474.5 ENST00000227474.6 ENST00000227474.7 FKSG32 NM_031307 PUS3_HUMAN Q96D17 Q96J23 Q96NB4 Q9BZE2 uc001qcy.1 uc001qcy.2 uc001qcy.3 uc001qcy.4 The protein encoded by this gene catalyzes the formation of tRNA pseudouridine from tRNA uridine at position 39 in the anticodon stem and loop of transfer RNAs. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2012]. Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs. Reaction=uridine(38/39) in tRNA = pseudouridine(38/39) in tRNA; Xref=Rhea:RHEA:42564, Rhea:RHEA-COMP:10117, Rhea:RHEA-COMP:10118, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.45; Evidence=; Nucleus Neurodevelopmental disorder with microcephaly and gray sclerae (NEDMIGS) [MIM:617051]: An autosomal recessive disorder characterized by global developmental delay, hypotonia, profoundly impaired intellectual development with poor or absent language, mild microcephaly, abnormal visual fixation, and seizures in most patients. Affected individuals also have gray sclerae. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the tRNA pseudouridine synthase TruA family. pseudouridine synthesis RNA binding nucleus cytoplasm cytosol tRNA modification tRNA processing RNA modification pseudouridine synthase activity isomerase activity tRNA pseudouridine synthesis mRNA pseudouridine synthesis uc001qcy.1 uc001qcy.2 uc001qcy.3 uc001qcy.4 
ENST00000227507.3 CCND1 ENST00000227507.3 cyclin D1 (from RefSeq NM_053056.3) CCND1 ENST00000227507.1 ENST00000227507.2 NM_053056 Q6FI00 Q6FI00_HUMAN hCG_2016647 uc001opa.1 uc001opa.2 uc001opa.3 uc001opa.4 uc001opa.5 The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance throughout the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activity is required for cell cycle G1/S transition. This protein has been shown to interact with tumor suppressor protein Rb and the expression of this gene is regulated positively by Rb. Mutations, amplification and overexpression of this gene, which alters cell cycle progression, are observed frequently in a variety of human cancers. [provided by RefSeq, Dec 2019]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC023620.2, X59798.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000227507.3/ ENSP00000227507.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cytoplasm Nucleus membrane Belongs to the cyclin family. Cyclin D subfamily. regulation of cyclin-dependent protein serine/threonine kinase activity G1/S transition of mitotic cell cycle negative regulation of transcription from RNA polymerase II promoter cyclin-dependent protein kinase holoenzyme complex re-entry into mitotic cell cycle liver development protein kinase activity nucleus nucleoplasm cytoplasm bicellular tight junction protein phosphorylation lactation positive regulation of cell proliferation response to organic substance response to iron ion response to X-ray response to organonitrogen compound response to organic cyclic compound Wnt signaling pathway kinase activity cyclin-dependent protein serine/threonine kinase regulator activity protein kinase binding negative regulation of epithelial cell differentiation endoplasmic reticulum unfolded protein response animal organ regeneration response to magnesium ion response to estradiol response to vitamin E Leydig cell differentiation mammary gland epithelial cell proliferation positive regulation of mammary gland epithelial cell proliferation response to drug response to estrogen macromolecular complex binding fat cell differentiation response to ethanol response to steroid hormone positive regulation of epithelial cell proliferation response to glucocorticoid response to corticosterone response to calcium ion regulation of cell cycle mammary gland alveolus development cellular response to organic substance liver regeneration regulation of G1/S transition of mitotic cell cycle uc001opa.1 uc001opa.2 uc001opa.3 uc001opa.4 uc001opa.5 
ENST00000227520.10 CCDC86 ENST00000227520.10 coiled-coil domain containing 86 (from RefSeq NM_024098.4) B4DY99 CCD86_HUMAN CYCLON ENST00000227520.1 ENST00000227520.2 ENST00000227520.3 ENST00000227520.4 ENST00000227520.5 ENST00000227520.6 ENST00000227520.7 ENST00000227520.8 ENST00000227520.9 NM_024098 Q9H6F5 uc001nqa.1 uc001nqa.2 uc001nqa.3 uc001nqa.4 (Microbial infection) Interacts with hepatitis C virus (HCV) protein NS5A. Q9H6F5; PRO_0000037576 [P27958]; Xeno; NbExp=3; IntAct=EBI-721289, EBI-8753518; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H6F5-1; Sequence=Displayed; Name=2; IsoId=Q9H6F5-2; Sequence=VSP_056905; Citrullinated by PADI4. RNA binding protein binding nucleus nucleolus viral process uc001nqa.1 uc001nqa.2 uc001nqa.3 uc001nqa.4 
ENST00000227524.9 PRPF19 ENST00000227524.9 pre-mRNA processing factor 19 (from RefSeq NM_014502.5) ENST00000227524.1 ENST00000227524.2 ENST00000227524.3 ENST00000227524.4 ENST00000227524.5 ENST00000227524.6 ENST00000227524.7 ENST00000227524.8 NMP200 NM_014502 PRP19 PRP19_HUMAN PRPF19 Q9UMS4 SNEV uc001nqf.1 uc001nqf.2 uc001nqf.3 uc001nqf.4 uc001nqf.5 PSO4 is the human homolog of yeast Pso4, a gene essential for cell survival and DNA repair (Beck et al., 2008 [PubMed 18263876]).[supplied by OMIM, Sep 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1095229.1, SRR3476690.922188.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000227524.9/ ENSP00000227524.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:28076346, PubMed:29360106, PubMed:29301961, PubMed:30705154). Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri- snRNP spliceosomal complex (PubMed:20595234). Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries (PubMed:21536736). The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair (PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'- linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response (PubMed:24332808). May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA (PubMed:18263876). As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process (PubMed:16223718). In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:11435423). May play a role in the biogenesis of lipid droplets (By similarity). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence=; Protein modification; protein ubiquitination. Homotetramer. Component of activated, catalytic and post- catalytic spliceosomes (PubMed:28502770, PubMed:28076346, PubMed:29360106, PubMed:29301961, PubMed:30705154). Component of the Prp19 complex/PRP19C/Nineteen complex/NTC and related complexes described as PRP19-CDC5L splicing complex and PSO4 complex. A homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is direct within this core complex. At least three less stably associated proteins CTNNBL1, CWC15 and HSPA8 are found in the Prp19 complex. The Prp19 complex associates with the spliceosome during its assembly and remodeling recruiting additional proteins. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts with CWC22 and EIF4A3 in an RNA- independent manner. Interacts with RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it interacts with the replication protein A complex (RPA). Interacts with SETMAR; required for SETMAR recruitment to site of DNA damage. Interacts with U2AF2; the interaction is direct and recruits the Prp19 complex to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with PSMC5 (By similarity). Interacts with KNSTRN (PubMed:24718257). Interacts (via N- terminus) with CDC5L (By similarity). Interacts with KHDC4 (PubMed:19641227). Interacts with USB1 (PubMed:23022480). Q9UMS4; O75934: BCAS2; NbExp=7; IntAct=EBI-395746, EBI-1050106; Q9UMS4; O60508: CDC40; NbExp=3; IntAct=EBI-395746, EBI-2557812; Q9UMS4; Q99459: CDC5L; NbExp=11; IntAct=EBI-395746, EBI-374880; Q9UMS4; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-395746, EBI-538479; Q9UMS4; P98175: RBM10; NbExp=2; IntAct=EBI-395746, EBI-721525; Q9UMS4; P52756: RBM5; NbExp=8; IntAct=EBI-395746, EBI-714003; Nucleus cleus, nucleoplasm Cytoplasm, cytoskeleton, spindle Cytoplasm Lipid droplet Note=Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin. Recruited on damaged DNA at sites of double-strand break. Ubiquitous. Weakly expressed in senescent cells of different tissue origins. Highly expressed in tumor cell lines. By gamma irradiation and chemical mutagens but not by UV irradiation. The 7 WD repeats are necessary and sufficient to support interaction with the RPA complex. Belongs to the WD repeat PRP19 family. protein polyubiquitination spliceosomal tri-snRNP complex assembly spliceosomal complex assembly generation of catalytic spliceosome for first transesterification step mRNA splicing, via spliceosome Prp19 complex inner cell mass cell proliferation ubiquitin-protein transferase activity protein binding nucleus nucleoplasm spliceosomal complex cytoplasm lipid particle spindle cytoskeleton DNA repair transcription-coupled nucleotide-excision repair double-strand break repair via nonhomologous end joining mRNA processing cellular response to DNA damage stimulus RNA splicing lipid biosynthetic process proteasomal protein catabolic process membrane protein ubiquitination nuclear speck transferase activity ubiquitin-ubiquitin ligase activity cellular protein localization site of double-strand break identical protein binding positive regulation of neuron differentiation positive regulation of mRNA splicing, via spliceosome positive regulation of astrocyte differentiation ubiquitin protein ligase activity protein K63-linked ubiquitination U2-type catalytic step 1 spliceosome U2-type catalytic step 2 spliceosome catalytic step 2 spliceosome signal transduction involved in DNA damage checkpoint DNA replication factor A complex uc001nqf.1 uc001nqf.2 uc001nqf.3 uc001nqf.4 uc001nqf.5 
ENST00000227525.8 TMEM109 ENST00000227525.8 transmembrane protein 109 (from RefSeq NM_024092.3) ENST00000227525.1 ENST00000227525.2 ENST00000227525.3 ENST00000227525.4 ENST00000227525.5 ENST00000227525.6 ENST00000227525.7 NM_024092 Q9BVC6 TM109_HUMAN TMEM109 uc001nqg.1 uc001nqg.2 uc001nqg.3 uc001nqg.4 uc001nqg.5 Functions as a voltage-gated monoatomic cation channel permeable to both potassium and calcium (By similarity). Plays a role in the cellular response to DNA damage (PubMed:23542032). Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence=; Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence=; Homooligomer (By similarity). Interacts with CRYAB; in the cellular response to DNA damage (PubMed:23542032). Q9BVC6; P41181: AQP2; NbExp=3; IntAct=EBI-1057733, EBI-12701138; Q9BVC6; O43315: AQP9; NbExp=3; IntAct=EBI-1057733, EBI-17444777; Q9BVC6; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1057733, EBI-781551; Q9BVC6; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-1057733, EBI-712073; Q9BVC6; Q8TED1: GPX8; NbExp=3; IntAct=EBI-1057733, EBI-11721746; Q9BVC6; O14880: MGST3; NbExp=3; IntAct=EBI-1057733, EBI-724754; Q9BVC6; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-1057733, EBI-3923617; Q9BVC6; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-1057733, EBI-716063; Q9BVC6; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-1057733, EBI-12055631; Q9BVC6; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-1057733, EBI-3920694; Q9BVC6; Q05940: SLC18A2; NbExp=3; IntAct=EBI-1057733, EBI-18036244; Q9BVC6; O43278-2: SPINT1; NbExp=3; IntAct=EBI-1057733, EBI-12078338; Q9BVC6; P27105: STOM; NbExp=3; IntAct=EBI-1057733, EBI-1211440; Q9BVC6; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-1057733, EBI-18178701; Q9BVC6; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-1057733, EBI-11742770; Nucleus outer membrane ; Multi-pass membrane protein Endoplasmic reticulum membrane ; Multi-pass membrane protein Sarcoplasmic reticulum membrane ; Multi-pass membrane protein molecular_function voltage-gated ion channel activity nucleus nuclear outer membrane endoplasmic reticulum endoplasmic reticulum membrane ion transport membrane integral component of membrane sarcoplasmic reticulum sarcoplasmic reticulum membrane ion transmembrane transport regulation of ion transmembrane transport intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator negative regulation of cell death extracellular exosome cellular response to gamma radiation uc001nqg.1 uc001nqg.2 uc001nqg.3 uc001nqg.4 uc001nqg.5 
ENST00000227618.9 ANAPC15 ENST00000227618.9 anaphase promoting complex subunit 15, transcript variant 47 (from RefSeq NR_171685.1) APC15_HUMAN C11orf51 ENST00000227618.1 ENST00000227618.2 ENST00000227618.3 ENST00000227618.4 ENST00000227618.5 ENST00000227618.6 ENST00000227618.7 ENST00000227618.8 G3V1Q3 HSPC020 NR_171685 P60006 Q9CXK2 Q9Y269 uc001orw.1 uc001orw.2 uc001orw.3 uc001orw.4 uc001orw.5 Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. In the complex, plays a role in the release of the mitotic checkpoint complex (MCC) from the APC/C: not required for APC/C activity itself, but promotes the turnover of CDC20 and MCC on the APC/C, thereby participating in the responsiveness of the spindle assembly checkpoint. Also required for degradation of CDC20. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. P60006; Q96LK0: CEP19; NbExp=3; IntAct=EBI-8787535, EBI-741885; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P60006-1; Sequence=Displayed; Name=2; IsoId=P60006-2; Sequence=VSP_055048; Belongs to the APC15 family. Sequence=EAW74842.1; Type=Erroneous gene model prediction; Evidence=; intracellular nucleoplasm anaphase-promoting complex cytosol ubiquitin-dependent protein catabolic process cell cycle anaphase-promoting complex-dependent catabolic process cell division regulation of mitotic cell cycle spindle assembly checkpoint regulation of mitotic cell cycle phase transition uc001orw.1 uc001orw.2 uc001orw.3 uc001orw.4 uc001orw.5 
ENST00000227638.8 PANX1 ENST00000227638.8 pannexin 1 (from RefSeq NM_015368.4) ENST00000227638.1 ENST00000227638.2 ENST00000227638.3 ENST00000227638.4 ENST00000227638.5 ENST00000227638.6 ENST00000227638.7 MRS1 NM_015368 O75968 PANX1 PANX1_HUMAN Q543A0 Q6UW26 Q96AM9 Q96L77 Q96RD7 Q96RS5 UNQ2529/PRO6028 uc001per.1 uc001per.2 uc001per.3 uc001per.4 uc001per.5 The protein encoded by this gene belongs to the innexin family. Innexin family members are the structural components of gap junctions. This protein and pannexin 2 are abundantly expressed in central nerve system (CNS) and are coexpressed in various neuronal populations. Studies in Xenopus oocytes suggest that this protein alone and in combination with pannexin 2 may form cell type-specific gap junctions with distinct properties. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803617.81357.1, SRR1660809.236064.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000227638.8/ ENSP00000227638.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Structural component of the gap junctions and the hemichannels involved in the ATP release and nucleotide permeation (PubMed:16908669, PubMed:20829356, PubMed:30918116). May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (PubMed:16908669). Plays a critical role in oogenesis (PubMed:30918116). Homohexamer. Forms homomeric or PANX1/PANX2-heteromeric intercellular channels on coexpression in paired Xenopus oocytes (By similarity). Q96RD7; P02652: APOA2; NbExp=3; IntAct=EBI-7037612, EBI-1171525; Q96RD7; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-7037612, EBI-4290634; Q96RD7; P41181: AQP2; NbExp=3; IntAct=EBI-7037612, EBI-12701138; Q96RD7; Q92843: BCL2L2; NbExp=3; IntAct=EBI-7037612, EBI-707714; Q96RD7; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-7037612, EBI-11579371; Q96RD7; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-7037612, EBI-12142299; Q96RD7; P37268: FDFT1; NbExp=3; IntAct=EBI-7037612, EBI-714550; Q96RD7; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-7037612, EBI-10314552; Q96RD7; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-7037612, EBI-12195227; Q96RD7; P01375: TNF; NbExp=3; IntAct=EBI-7037612, EBI-359977; Q96RD7; O95183: VAMP5; NbExp=3; IntAct=EBI-7037612, EBI-10191195; Q96RD7; Q14508: WFDC2; NbExp=3; IntAct=EBI-7037612, EBI-723529; Q96RD7-1; Q96RD7-1: PANX1; NbExp=4; IntAct=EBI-25747443, EBI-25747443; Cell membrane ; Multi-pass membrane protein Cell junction, gap junction doplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96RD7-1; Sequence=Displayed; Name=2; IsoId=Q96RD7-2; Sequence=VSP_011476; Widely expressed (PubMed:30918116). Highest expression is observed in oocytes and brain (PubMed:30918116). Detected at very low levels in sperm cells (PubMed:30918116). S-nitrosylation inhibits channel currents and ATP release. N-glycosylation may play a role in cell surface targeting (By similarity). Exists in three glycosylation states: non-glycosylated (GLY0), high-mannose glycosylated (GLY1), and fully mature glycosylated (GLY2) (PubMed:30918116). Oocyte/zygote/embryo maturation arrest 7 (OZEMA7) [MIM:618550]: An autosomal dominant infertility disorder due to oocyte degeneration and death, which may occur before or after fertilization. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the pannexin family. Name=Wikipedia; Note=Pannexin entry; URL="https://en.wikipedia.org/wiki/Pannexin"; protease binding response to ischemia actin binding receptor binding gap junction channel activity calcium channel activity endoplasmic reticulum endoplasmic reticulum membrane plasma membrane gap junction ion transport cation transport calcium ion transport cell-cell signaling channel activity membrane integral component of membrane wide pore channel activity leak channel activity cell junction bleb macromolecular complex response to ATP protein hexamerization ion channel binding protein heterodimerization activity positive regulation of cytokine secretion positive regulation of interleukin-1 secretion positive regulation of interleukin-1 alpha secretion positive regulation of interleukin-1 beta secretion actin filament binding gap junction hemi-channel activity transmembrane transport calcium ion transmembrane transport scaffold protein binding uc001per.1 uc001per.2 uc001per.3 uc001per.4 uc001per.5 
ENST00000227665.9 APOA5 ENST00000227665.9 apolipoprotein A5, transcript variant 3 (from RefSeq NM_001371904.1) APOA5_HUMAN B0YIV9 ENST00000227665.1 ENST00000227665.2 ENST00000227665.3 ENST00000227665.4 ENST00000227665.5 ENST00000227665.6 ENST00000227665.7 ENST00000227665.8 NM_001371904 Q3MIK6 Q6Q788 Q6UWK9 Q9UBJ3 RAP3 UNQ411/PRO773 uc058hqs.1 uc058hqs.2 The protein encoded by this gene is an apolipoprotein that plays an important role in regulating the plasma triglyceride levels, a major risk factor for coronary artery disease. It is a component of high density lipoprotein and is highly similar to a rat protein that is upregulated in response to liver injury. Mutations in this gene have been associated with hypertriglyceridemia and hyperlipoproteinemia type 5. This gene is located proximal to the apolipoprotein gene cluster on chromosome 11q23. Alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Oct 2009]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189664.114462.1, DRR138515.775853.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000227665.9/ ENSP00000227665.4 RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Minor apolipoprotein mainly associated with HDL and to a lesser extent with VLDL. May also be associated with chylomicrons. Important determinant of plasma triglyceride (TG) levels by both being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis and an inhibitor of the hepatic VLDL-TG production rate (without affecting the VLDL-apoB production rate) (By similarity). Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux of cholesterol from macrophages. Binds heparin (PubMed:17326667). Interacts with GPIHBP1 (PubMed:17997385). Interacts with SORL1; this interaction leads to APOA5 internalization and sorting either to lysosomes and degradation, or to the trans-Golgi network (PubMed:17326667, PubMed:18603531). Q6Q788; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-3936819, EBI-2876502; Q6Q788; O95393: BMP10; NbExp=3; IntAct=EBI-3936819, EBI-3922513; Q6Q788; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-3936819, EBI-7247651; Q6Q788; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-3936819, EBI-11522780; Q6Q788; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-3936819, EBI-1054315; Q6Q788; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-3936819, EBI-10269566; Q6Q788; Q9HB07: MYG1; NbExp=3; IntAct=EBI-3936819, EBI-709754; Q6Q788; Q9BQE4: SELENOS; NbExp=3; IntAct=EBI-3936819, EBI-398970; Q6Q788; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-3936819, EBI-10171534; Q6Q788; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-3936819, EBI-741829; Q6Q788; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-3936819, EBI-721293; Q6Q788; P49638: TTPA; NbExp=3; IntAct=EBI-3936819, EBI-10210710; Q6Q788; O95070: YIF1A; NbExp=3; IntAct=EBI-3936819, EBI-2799703; Secreted Early endosome Late endosome Golgi apparatus, trans-Golgi network Note=In the presence of SORL1, internalized to early endosomes, sorted in a retrograde fashion to late endosomes, from which a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network. Liver and plasma. Up-regulated by PPARA agonists, which are used clinically to lower serum TG (such as fibrates). Phosphorylated by FAM20C in the extracellular medium. Three common alleles are known: allele APOA5*1, APOA5*2 and APOA5*3. The APOA5*2 haplotype, which consists of 3 non-coding SNPs, is present in approximately 16% of Caucasians and is associated with increased plasma triglyceride concentrations. APOA5*3 haplotype is defined by the rare Ser-19-Trp substitution. Together, the APOA5*2 and APOA5*3 haplotypes are found in 25 to 50% of African Americans, Hispanics, and Caucasians. Hypertriglyceridemia 1 (HYTG1) [MIM:145750]: A common inherited disorder in which the concentration of very low density lipoprotein (VLDL) is elevated in the plasma. This leads to increased risk of heart disease, obesity, and pancreatitis. Inheritance is autosomal dominant. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Hyperlipoproteinemia 5 (HLPP5) [MIM:144650]: Characterized by increased amounts of chylomicrons and very low density lipoprotein (VLDL) and decreased low density lipoprotein (LDL) and high density lipoprotein (HDL) in the plasma after a fast. Numerous conditions cause this phenotype, including insulin-dependent diabetes mellitus, contraceptive steroids, alcohol abuse, and glycogen storage disease type 1A (GSD1A). Note=The disease is caused by variants affecting the gene represented in this entry. Induced in early phase of liver regeneration. Belongs to the apolipoprotein A1/A4/E family. It is uncertain whether Met-1 or Met-4 is the initiator. Sequence=AAF25661.1; Type=Erroneous initiation; Evidence=; Sequence=AAF25662.1; Type=Erroneous initiation; Evidence=; Sequence=AAQ89109.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence=; phospholipid binding extracellular region extracellular space endosome early endosome late endosome endoplasmic reticulum lumen Golgi apparatus triglyceride metabolic process cholesterol biosynthetic process lipid transport enzyme activator activity heparin binding lipid binding positive regulation of cholesterol esterification positive regulation of triglyceride catabolic process positive regulation of very-low-density lipoprotein particle remodeling cholesterol binding regulation of lipid metabolic process triglyceride catabolic process enzyme binding regulation of intestinal cholesterol absorption phosphatidylcholine binding cholesterol efflux phospholipid efflux very-low-density lipoprotein particle high-density lipoprotein particle triglyceride-rich lipoprotein particle remodeling very-low-density lipoprotein particle remodeling high-density lipoprotein particle assembly lipase binding lipoprotein metabolic process tissue regeneration chylomicron cholesterol homeostasis post-translational protein modification cellular protein metabolic process positive regulation of fatty acid biosynthetic process phosphatidylcholine metabolic process positive regulation of receptor-mediated endocytosis low-density lipoprotein particle receptor binding positive regulation of lipid catabolic process positive regulation of lipoprotein lipase activity acylglycerol homeostasis phosphatidylcholine-sterol O-acyltransferase activator activity lipase activator activity lipoprotein lipase activator activity lipoprotein particle receptor binding triglyceride homeostasis low-density lipoprotein particle uc058hqs.1 uc058hqs.2 
ENST00000227667.8 APOC3 ENST00000227667.8 apolipoprotein C3 (from RefSeq NM_000040.3) APOC3_HUMAN ENST00000227667.1 ENST00000227667.2 ENST00000227667.3 ENST00000227667.4 ENST00000227667.5 ENST00000227667.6 ENST00000227667.7 NM_000040 P02656 Q08E83 Q6Q786 uc001ppt.1 uc001ppt.2 uc001ppt.3 This gene encodes a protein component of triglyceride (TG)-rich lipoproteins (TRLs) including very low density lipoproteins (VLDL), high density lipoproteins (HDL) and chylomicrons. The encoded protein plays a role in role in the metabolism of these TRLs through multiple modes. This protein has been shown to promote the secretion of VLDL1, inhibit lipoprotein lipase enzyme activity, and delay catabolism of TRL remnants. Mutations in this gene are associated with low plasma triglyceride levels and reduced risk of ischemic cardiovascular disease, and hyperalphalipoproteinemia, which is characterized by elevated levels of high density lipoprotein (HDL) and HDL cholesterol in human patients. This gene and other related genes comprise an apolipoprotein gene cluster on chromosome 11. [provided by RefSeq, Sep 2017]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC027977.1, X01388.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000227667.8/ ENSP00000227667.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma (PubMed:18201179, PubMed:22510806). Plays a multifaceted role in triglyceride homeostasis (PubMed:18201179, PubMed:22510806). Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride- rich lipoproteins (TRLs) (PubMed:18201179, PubMed:22510806). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors (PubMed:18201179, PubMed:22510806). Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners (PubMed:18408013). P02656; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1220113, EBI-781551; P02656; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-1220113, EBI-18304435; P02656; Q8TED1: GPX8; NbExp=3; IntAct=EBI-1220113, EBI-11721746; Secreted Liver. The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan. Hyperalphalipoproteinemia 2 (HALP2) [MIM:614028]: A condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the apolipoprotein C3 family. retinoid metabolic process phospholipid binding extracellular region extracellular space early endosome lipid metabolic process triglyceride metabolic process lipid transport G-protein coupled receptor signaling pathway lipid binding negative regulation of triglyceride catabolic process negative regulation of very-low-density lipoprotein particle remodeling negative regulation of very-low-density lipoprotein particle clearance negative regulation of high-density lipoprotein particle clearance negative regulation of low-density lipoprotein particle clearance cholesterol binding lipid catabolic process triglyceride catabolic process enzyme regulator activity regulation of Cdc42 protein signal transduction cholesterol efflux phospholipid efflux very-low-density lipoprotein particle intermediate-density lipoprotein particle spherical high-density lipoprotein particle chylomicron remodeling high-density lipoprotein particle remodeling chylomicron assembly very-low-density lipoprotein particle assembly chylomicron remnant clearance lipoprotein metabolic process chylomicron cholesterol homeostasis reverse cholesterol transport negative regulation of fatty acid biosynthetic process negative regulation of lipid metabolic process negative regulation of receptor-mediated endocytosis negative regulation of lipid catabolic process negative regulation of lipoprotein lipase activity lipase inhibitor activity negative regulation of cholesterol import extracellular exosome triglyceride homeostasis high-density lipoprotein particle receptor binding uc001ppt.1 uc001ppt.2 uc001ppt.3 
ENST00000227752.8 IL10RA ENST00000227752.8 interleukin 10 receptor subunit alpha, transcript variant 1 (from RefSeq NM_001558.4) A8K6I0 B0YJ27 ENST00000227752.1 ENST00000227752.2 ENST00000227752.3 ENST00000227752.4 ENST00000227752.5 ENST00000227752.6 ENST00000227752.7 I10R1_HUMAN IL10R NM_001558 Q13651 uc001prv.1 uc001prv.2 uc001prv.3 uc001prv.4 uc001prv.5 uc001prv.6 The protein encoded by this gene is a receptor for interleukin 10. This protein is structurally related to interferon receptors. It has been shown to mediate the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. This receptor is reported to promote survival of progenitor myeloid cells through the insulin receptor substrate-2/PI 3-kinase/AKT pathway. Activation of this receptor leads to tyrosine phosphorylation of JAK1 and TYK2 kinases. Two transcript variants, one protein-coding and the other not protein-coding, have been found for this gene. [provided by RefSeq, Jan 2009]. Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well (PubMed:16982608). In turn, the heterotetrameric assembly complex, composed of two subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB respectively (PubMed:12133952). These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3. Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus and activates the expression of anti-inflammatory genes. In addition, IL10RA-mediated activation of STAT3 inhibits starvation-induced autophagy (PubMed:26962683). Interacts with IL10 (PubMed:16982608, PubMed:15837194). Interacts with IL10RB (PubMed:16982608). Interacts (via its cytoplasmic domain) with JAK1 (via N-terminus) (PubMed:12133952). Interacts with BTRC; this interaction leads to IL10RA ubiquitination and subsequent degradation (PubMed:22087322). Interacts with STAT3 (By similarity). (Microbial infection) Interacts with human cytomegalovirus protein IL10. (Microbial infection) Interacts with Epstein-Barr virus protein IL10. Q13651; P27449: ATP6V0C; NbExp=3; IntAct=EBI-1031656, EBI-721179; Q13651; Q9Y297: BTRC; NbExp=6; IntAct=EBI-1031656, EBI-307461; Q13651; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-1031656, EBI-12062109; Q13651; Q8IX05: CD302; NbExp=3; IntAct=EBI-1031656, EBI-14259393; Q13651; O95674: CDS2; NbExp=3; IntAct=EBI-1031656, EBI-3913685; Q13651; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-1031656, EBI-7247651; Q13651; P02724: GYPA; NbExp=3; IntAct=EBI-1031656, EBI-702665; Q13651; B0YJ81: HACD1; NbExp=3; IntAct=EBI-1031656, EBI-12051643; Q13651; Q6Y1H2: HACD2; NbExp=3; IntAct=EBI-1031656, EBI-530257; Q13651; P22301: IL10; NbExp=9; IntAct=EBI-1031656, EBI-1031632; Q13651; P21145: MAL; NbExp=3; IntAct=EBI-1031656, EBI-3932027; Q13651; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-1031656, EBI-9550165; Q13651; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-1031656, EBI-11721828; Q13651; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-1031656, EBI-8636004; Q13651; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-1031656, EBI-9679163; Q13651; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-1031656, EBI-8644112; Q13651; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-1031656, EBI-10314552; Q13651; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-1031656, EBI-3907610; Q13651; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-1031656, EBI-5235586; Q13651; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-1031656, EBI-8640191; Q13651; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-1031656, EBI-10315004; Q13651; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-1031656, EBI-2852148; Q13651; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-1031656, EBI-2820477; Q13651; O95183: VAMP5; NbExp=3; IntAct=EBI-1031656, EBI-10191195; Q13651; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-1031656, EBI-751210; Q13651; P03180: BCRF1; Xeno; NbExp=4; IntAct=EBI-1031656, EBI-1042167; Q13651; P03495: NS; Xeno; NbExp=2; IntAct=EBI-1031656, EBI-2548993; Q13651; P17150: UL111A; Xeno; NbExp=2; IntAct=EBI-1031656, EBI-1033736; Cell membrane ingle-pass type I membrane protein. Cytoplasm Primarily expressed in hematopoetic cells including B-cells, T-cells, NK cells, monocytes and macrophages. Not expressed in non-hematopoetic cells such as fibroblasts or endothelial cells. Phosphorylated. Phosphorylation of the cytoplasmic tail induced STAT3 activation. Ubiquitinated by BTRC; ubiquitination leads to endocytosis and subsequent degradation of IL10RA. Inflammatory bowel disease 28, autosomal recessive (IBD28) [MIM:613148]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the type II cytokine receptor family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/il10ra/"; cytokine receptor activity interleukin-10 receptor activity protein binding cytoplasm plasma membrane negative regulation of autophagy membrane integral component of membrane cytokine-mediated signaling pathway interleukin-10 binding response to lipopolysaccharide signaling receptor activity positive regulation of JAK-STAT cascade regulation of synapse organization ubiquitin-dependent endocytosis uc001prv.1 uc001prv.2 uc001prv.3 uc001prv.4 uc001prv.5 uc001prv.6 
ENST00000227756.5 GALNT18 ENST00000227756.5 polypeptide N-acetylgalactosaminyltransferase 18, transcript variant 1 (from RefSeq NM_198516.3) ENST00000227756.1 ENST00000227756.2 ENST00000227756.3 ENST00000227756.4 GALNTL4 GLT18_HUMAN NM_198516 O95903 Q6P9A2 Q8NDY9 uc001mjo.1 uc001mjo.2 uc001mjo.3 uc001mjo.4 Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine (GalNAc) residue from UDP-GalNAc to a serine or threonine residue on the protein receptor. Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O- [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23957; Evidence=; Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3- O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Protein modification; protein glycosylation. Golgi apparatus membrane ; Single- pass type II membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6P9A2-1; Sequence=Displayed; Name=2; IsoId=Q6P9A2-2; Sequence=VSP_011234, VSP_011235; There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Sequence=AAD20062.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Golgi membrane polypeptide N-acetylgalactosaminyltransferase activity cellular_component Golgi apparatus protein glycosylation protein O-linked glycosylation membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups carbohydrate binding metal ion binding uc001mjo.1 uc001mjo.2 uc001mjo.3 uc001mjo.4 
ENST00000227758.7 BIRC2 ENST00000227758.7 baculoviral IAP repeat containing 2, transcript variant 1 (from RefSeq NM_001166.5) API1 B4E026 BIRC2_HUMAN ENST00000227758.1 ENST00000227758.2 ENST00000227758.3 ENST00000227758.4 ENST00000227758.5 ENST00000227758.6 MIHB NM_001166 Q13490 Q16516 Q4TTG0 RNF48 uc001pgy.1 uc001pgy.2 uc001pgy.3 uc001pgy.4 uc001pgy.5 uc001pgy.6 The protein encoded by this gene is a member of a family of proteins that inhibits apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. This encoded protein inhibits apoptosis induced by serum deprivation and menadione, a potent inducer of free radicals. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]. Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non- canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase- independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence= The CARD domain inhibits the activation of E3 ubiquitin ligase activity by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. The CARD domain-mediated autoinhibition of the E3 ubiquitin-protein ligase activity suppresses cell proliferation and migration. USP19 regulates the stability of BIRC2/c-IAP1 by preventing its ubiquitination. Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2; the interaction is required for IKBKE ubiquitination. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19. HSP90AB1 (PubMed:25486457). Interacts with UBXN1 (PubMed:25681446). Interacts with GSK3B (PubMed:18846110). Interacts with several death receptors, inclusing FAS, TNFRSF10A and TNFRSF10B (PubMed:18846110). Recruited to TNFRSF10B in the absence of receptor stimulation. When TNFRSF10B is stimulated, further recruited to the receptor and cleaved by caspases. Proteolytic fragments remain associated with TNFRSF10B (PubMed:18846110). Q13490; Q13490: BIRC2; NbExp=4; IntAct=EBI-514538, EBI-514538; Q13490; Q96CA5: BIRC7; NbExp=6; IntAct=EBI-514538, EBI-517623; Q13490; P51451: BLK; NbExp=3; IntAct=EBI-514538, EBI-2105445; Q13490; P51813: BMX; NbExp=3; IntAct=EBI-514538, EBI-696657; Q13490; Q9Y3E2: BOLA1; NbExp=7; IntAct=EBI-514538, EBI-1049556; Q13490; A0A087WZT3: BOLA2-SMG1P6; NbExp=3; IntAct=EBI-514538, EBI-12006120; Q13490; P55210: CASP7; NbExp=2; IntAct=EBI-514538, EBI-523958; Q13490; P55211: CASP9; NbExp=12; IntAct=EBI-514538, EBI-516799; Q13490; Q9NR28: DIABLO; NbExp=5; IntAct=EBI-514538, EBI-517508; Q13490; Q96CJ1: EAF2; NbExp=3; IntAct=EBI-514538, EBI-1245604; Q13490; Q9NQT4: EXOSC5; NbExp=6; IntAct=EBI-514538, EBI-371876; Q13490; Q96CN9: GCC1; NbExp=6; IntAct=EBI-514538, EBI-746252; Q13490; P14136: GFAP; NbExp=3; IntAct=EBI-514538, EBI-744302; Q13490; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-514538, EBI-1055254; Q13490; O60341: KDM1A; NbExp=3; IntAct=EBI-514538, EBI-710124; Q13490; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-514538, EBI-739832; Q13490; P08949: NMB; NbExp=3; IntAct=EBI-514538, EBI-7964376; Q13490; P08949-2: NMB; NbExp=6; IntAct=EBI-514538, EBI-12302085; Q13490; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-514538, EBI-741158; Q13490; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-514538, EBI-398874; Q13490; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-514538, EBI-1058491; Q13490; Q8N3J5: PPM1K; NbExp=6; IntAct=EBI-514538, EBI-3923368; Q13490; P63000: RAC1; NbExp=2; IntAct=EBI-514538, EBI-413628; Q13490; P40937: RFC5; NbExp=3; IntAct=EBI-514538, EBI-712376; Q13490; Q13546: RIPK1; NbExp=5; IntAct=EBI-514538, EBI-358507; Q13490; O43353: RIPK2; NbExp=3; IntAct=EBI-514538, EBI-358522; Q13490; Q9Y572: RIPK3; NbExp=3; IntAct=EBI-514538, EBI-298250; Q13490; P57078: RIPK4; NbExp=3; IntAct=EBI-514538, EBI-4422308; Q13490; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-514538, EBI-11984663; Q13490; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-514538, EBI-11974855; Q13490; Q9NP84: TNFRSF12A; NbExp=2; IntAct=EBI-514538, EBI-2851995; Q13490; Q13077: TRAF1; NbExp=5; IntAct=EBI-514538, EBI-359224; Q13490; Q12933: TRAF2; NbExp=17; IntAct=EBI-514538, EBI-355744; Q13490; Q9BZW7: TSGA10; NbExp=4; IntAct=EBI-514538, EBI-744794; Q13490-1; Q13490-1: BIRC2; NbExp=4; IntAct=EBI-16127374, EBI-16127374; Cytoplasm. Nucleus. Note=Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13490-1; Sequence=Displayed; Name=2; IsoId=Q13490-2; Sequence=VSP_045314; Present in many fetal and adult tissues. Mainly expressed in adult skeletal muscle, thymus, testis, ovary, and pancreas, low or absent in brain and peripheral blood leukocytes. The BIR domains mediate nuclear localization. The CARD domain is necessary to stabilize the protein and inhibit the activation of E3 ubiquitin-protein ligase activity of BIRC2/c-IAP1 by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. Auto-ubiquitinated and degraded by the proteasome in apoptotic cells. Upon stimulation of death receptors, including TNFRSF10B, recruited to receptors and cleaved by caspases. Proteolytic fragments remain associated with the receptors. This cleavage presumably inactivates the protein. Belongs to the IAP family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/birc2/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/795/BIRC2"; protein polyubiquitination response to hypoxia XY body placenta development MyD88-independent toll-like receptor signaling pathway transcription coactivator activity ubiquitin-protein transferase activity protein binding nucleus cytoplasm cytosol apoptotic process cell surface receptor signaling pathway I-kappaB kinase/NF-kappaB signaling zinc ion binding cytoplasmic side of plasma membrane response to organonitrogen compound regulation of tumor necrosis factor-mediated signaling pathway response to organic cyclic compound protein deubiquitination transferase activity positive regulation of protein ubiquitination macromolecular complex tumor necrosis factor-mediated signaling pathway regulation of toll-like receptor signaling pathway CD40 receptor complex TRIF-dependent toll-like receptor signaling pathway NIK/NF-kappaB signaling regulation of RIG-I signaling pathway regulation of cell proliferation identical protein binding regulation of apoptotic process cysteine-type endopeptidase inhibitor activity involved in apoptotic process negative regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling ubiquitin binding negative regulation of cysteine-type endopeptidase activity involved in apoptotic process proteasome-mediated ubiquitin-dependent protein catabolic process regulation of innate immune response membrane raft response to ethanol regulation of cell differentiation metal ion binding protein N-terminus binding regulation of inflammatory response chaperone binding protein heterooligomerization response to cAMP regulation of cell cycle regulation of necroptotic process negative regulation of necroptotic process ubiquitin protein ligase activity necroptotic process regulation of nucleotide-binding oligomerization domain containing signaling pathway cellular response to tumor necrosis factor FBXO family protein binding regulation of NIK/NF-kappaB signaling negative regulation of ripoptosome assembly involved in necroptotic process positive regulation of protein K63-linked ubiquitination positive regulation of protein K48-linked ubiquitination positive regulation of protein monoubiquitination positive regulation of protein polyubiquitination positive regulation of nucleic acid-templated transcription inhibition of cysteine-type endopeptidase activity involved in apoptotic process regulation of cysteine-type endopeptidase activity regulation of reactive oxygen species metabolic process uc001pgy.1 uc001pgy.2 uc001pgy.3 uc001pgy.4 uc001pgy.5 uc001pgy.6 
ENST00000227868.9 PDHX ENST00000227868.9 pyruvate dehydrogenase complex component X, transcript variant 1 (from RefSeq NM_003477.3) B4DW62 D3DR11 E9PB14 E9PBP7 ENST00000227868.1 ENST00000227868.2 ENST00000227868.3 ENST00000227868.4 ENST00000227868.5 ENST00000227868.6 ENST00000227868.7 ENST00000227868.8 NM_003477 O00330 O60221 ODPX_HUMAN PDX1 Q96FV8 Q99783 uc001mvt.1 uc001mvt.2 uc001mvt.3 uc001mvt.4 uc001mvt.5 The pyruvate dehydrogenase (PDH) complex is located in the mitochondrial matrix and catalyzes the conversion of pyruvate to acetyl coenzyme A. The PDH complex thereby links glycolysis to Krebs cycle. The PDH complex contains three catalytic subunits, E1, E2, and E3, two regulatory subunits, E1 kinase and E1 phosphatase, and a non-catalytic subunit, E3 binding protein (E3BP). This gene encodes the E3 binding protein subunit; also known as component X of the pyruvate dehydrogenase complex. This protein tethers E3 dimers to the E2 core of the PDH complex. Defects in this gene are a cause of pyruvate dehydrogenase deficiency which results in neurological dysfunction and lactic acidosis in infancy and early childhood. This protein is also a minor antigen for antimitochondrial antibodies. These autoantibodies are present in nearly 95% of patients with the autoimmune liver disease primary biliary cirrhosis (PBC). In PBC, activated T lymphocytes attack and destroy epithelial cells in the bile duct where this protein is abnormally distributed and overexpressed. PBC eventually leads to cirrhosis and liver failure. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Oct 2009]. Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules (PubMed:14638692, PubMed:20361979). This core binds multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (PubMed:14638692). Interacts with SIRT4 (PubMed:25525879). Interacts with DLD (PubMed:20385101, PubMed:16263718, PubMed:16442803, PubMed:20160912, PubMed:20361979). O00330; Q6RW13: AGTRAP; NbExp=5; IntAct=EBI-751566, EBI-741181; O00330; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-751566, EBI-7062247; O00330; P09622: DLD; NbExp=7; IntAct=EBI-751566, EBI-353366; O00330; Q9Y6E7: SIRT4; NbExp=4; IntAct=EBI-751566, EBI-2606540; Mitochondrion matrix. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O00330-1; Sequence=Displayed; Name=2; IsoId=O00330-2; Sequence=VSP_045271; Name=3; IsoId=O00330-3; Sequence=VSP_053817; Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity. Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:245349]: A metabolic disorder characterized by decreased activity of the pyruvate dehydrogenase complex without observable reduction in the activities of enzymes E1, E2, or E3. Clinical features include hypotonia and psychomotor retardation. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the 2-oxoacid dehydrogenase family. protein binding mitochondrion mitochondrial matrix pyruvate metabolic process transferase activity, transferring acyl groups pyruvate dehydrogenase complex mitochondrial acetyl-CoA biosynthetic process from pyruvate pyruvate dehydrogenase (NAD+) activity uc001mvt.1 uc001mvt.2 uc001mvt.3 uc001mvt.4 uc001mvt.5 
ENST00000227880.8 SLC15A3 ENST00000227880.8 solute carrier family 15 member 3, transcript variant 1 (from RefSeq NM_016582.3) ENST00000227880.1 ENST00000227880.2 ENST00000227880.3 ENST00000227880.4 ENST00000227880.5 ENST00000227880.6 ENST00000227880.7 NM_016582 OCTP PHT2 PTR3 Q8IY34 Q9P2X9 S15A3_HUMAN SLC15A3 uc001nqn.1 uc001nqn.2 uc001nqn.3 uc001nqn.4 Proton-coupled amino-acid transporter that transports free histidine and certain di- and tripeptides, and is involved in innate immune response (By similarity). Also able to transport carnosine (PubMed:31073693, PubMed:31254495). Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand (By similarity). Reaction=glycylglycylglycine(out) + n H(+)(out) = glycylglycylglycine(in) + n H(+)(in); Xref=Rhea:RHEA:76391, ChEBI:CHEBI:15378, ChEBI:CHEBI:195214; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76392; Evidence=; Reaction=carnosine(out) + n H(+)(out) = carnosine(in) + n H(+)(in); Xref=Rhea:RHEA:76383, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76384; Evidence=; Reaction=n H(+)(out) + L-histidine(out) = n H(+)(in) + L-histidine(in); Xref=Rhea:RHEA:76379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57595; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76380; Evidence=; Reaction=n H(+)(out) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(out) = n H(+)(in) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(in); Xref=Rhea:RHEA:76371, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76372; Evidence=; Kinetic parameters: KM=428 uM for glycyl-sarcosine ; KM=66.9 uM for L-histidine ; KM=5350 uM for valacyclovir ; Vmax=1860 pmol/min/mg enzyme toward L-histidine ; Vmax=73.6 pmol/min/mg enzyme glycyl-sarcosine ; Vmax=63.7 pmol/min/mg enzyme valacyclovir ; pH dependence: Optimum pH is 5.5. ; Q8IY34; P49639: HOXA1; NbExp=3; IntAct=EBI-12179023, EBI-740785; Q8IY34; P59991: KRTAP12-2; NbExp=4; IntAct=EBI-12179023, EBI-10176379; Q8IY34; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-12179023, EBI-12196745; Q8IY34; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-12179023, EBI-3958099; Q8IY34; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-12179023, EBI-11958364; Q8IY34; Q99750: MDFI; NbExp=3; IntAct=EBI-12179023, EBI-724076; Q8IY34; Q9HC29: NOD2; NbExp=2; IntAct=EBI-12179023, EBI-7445625; Q8IY34; Q8N697: SLC15A4; NbExp=2; IntAct=EBI-12179023, EBI-4319594; Lysosome membrane ; Multi-pass membrane protein Endosome membrane ; Multi-pass membrane protein Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. protein binding lysosome lysosomal membrane ion transport protein transport symporter activity peptide:proton symporter activity peptide transport membrane integral component of membrane transmembrane transporter activity oligopeptide transmembrane transport oligopeptide transmembrane transporter activity intracellular membrane-bounded organelle transmembrane transport hydrogen ion transmembrane transport peptide transmembrane transporter activity uc001nqn.1 uc001nqn.2 uc001nqn.3 uc001nqn.4 
ENST00000227918.3 SCGB2A2 ENST00000227918.3 secretoglobin family 2A member 2 (from RefSeq NM_002411.4) A1A522 ENST00000227918.1 ENST00000227918.2 MGB1 NM_002411 Q13296 Q86WH8 SG2A2_HUMAN UGB2 uc001ntc.1 uc001ntc.2 uc001ntc.3 uc001ntc.4 uc001ntc.5 uc001ntc.6 Q13296; P50552: VASP; NbExp=3; IntAct=EBI-9058786, EBI-748201; Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13296-1; Sequence=Displayed; Name=2; IsoId=Q13296-2; Sequence=VSP_009122; Mammary gland specific. Over-expressed in breast cancer. Belongs to the secretoglobin family. Lipophilin subfamily. molecular_function protein binding cellular_component extracellular region extracellular space biological_process androgen receptor signaling pathway uc001ntc.1 uc001ntc.2 uc001ntc.3 uc001ntc.4 uc001ntc.5 uc001ntc.6 
ENST00000228027.12 DGAT2 ENST00000228027.12 diacylglycerol O-acyltransferase 2, transcript variant 1 (from RefSeq NM_032564.5) A6ND76 DGAT2 DGAT2_HUMAN ENST00000228027.1 ENST00000228027.10 ENST00000228027.11 ENST00000228027.2 ENST00000228027.3 ENST00000228027.4 ENST00000228027.5 ENST00000228027.6 ENST00000228027.7 ENST00000228027.8 ENST00000228027.9 HMFN1045 NM_032564 Q5U810 Q68CL3 Q68DJ0 Q8NDB7 Q96BS0 Q96PD7 Q9BYE5 UNQ738/PRO1433 uc001oxa.1 uc001oxa.2 uc001oxa.3 uc001oxa.4 uc001oxa.5 This gene encodes one of two enzymes which catalyzes the final reaction in the synthesis of triglycerides in which diacylglycerol is covalently bound to long chain fatty acyl-CoAs. The encoded protein catalyzes this reaction at low concentrations of magnesium chloride while the other enzyme has high activity at high concentrations of magnesium chloride. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011]. Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides (PubMed:27184406). Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1- monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705). Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; Evidence=; Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di- (9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73990; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; Evidence=; Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O- (9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:197429; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di- (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915, ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75342; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916; Evidence=; Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2- di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75583; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75735; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75824; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440; Evidence=; Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1- hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:73990, ChEBI:CHEBI:75466; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072; Evidence=; Inhibited by niacin. Glycerolipid metabolism; triacylglycerol biosynthesis. Forms multimeric complexes consisting of several DGAT2 subunits (By similarity). Interacts with SLC27A1 and this interaction is enhanced in the presence of ZFYVE1 (PubMed:30970241). Endoplasmic reticulum membrane ; Multi-pass membrane protein Lipid droplet Cytoplasm, perinuclear region Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96PD7-1; Sequence=Displayed; Name=2; IsoId=Q96PD7-2; Sequence=VSP_020356; Predominantly expressed in liver and white adipose tissue. Expressed at lower level in mammary gland, testis and peripheral blood leukocytes. Expressed in sebaceous glands of normal skin but decreased psoriatic skin. Belongs to the diacylglycerol acyltransferase family. Sequence=BAD38635.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=CAD38961.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; 2-acylglycerol O-acyltransferase activity diacylglycerol O-acyltransferase activity cytoplasm mitochondrion endoplasmic reticulum endoplasmic reticulum membrane lipid particle glycerol metabolic process lipid metabolic process positive regulation of triglyceride biosynthetic process membrane integral component of membrane transferase activity transferase activity, transferring acyl groups transferase activity, transferring acyl groups other than amino-acyl groups triglyceride biosynthetic process lipid storage integral component of endoplasmic reticulum membrane low-density lipoprotein particle clearance long-chain fatty-acyl-CoA metabolic process cellular triglyceride homeostasis acylglycerol acyl-chain remodeling retinol metabolic process cholesterol homeostasis protein homodimerization activity intracellular membrane-bounded organelle positive regulation of gluconeogenesis negative regulation of fatty acid oxidation diacylglycerol metabolic process perinuclear region of cytoplasm retinol O-fatty-acyltransferase activity regulation of lipoprotein metabolic process fatty acid homeostasis fat pad development cellular response to oleic acid regulation of cholesterol metabolic process regulation of plasma lipoprotein particle levels perinuclear endoplasmic reticulum membrane uc001oxa.1 uc001oxa.2 uc001oxa.3 uc001oxa.4 uc001oxa.5 
ENST00000228136.9 C11orf58 ENST00000228136.9 chromosome 11 open reading frame 58 (from RefSeq NM_014267.6) B2RD28 ENST00000228136.1 ENST00000228136.2 ENST00000228136.3 ENST00000228136.4 ENST00000228136.5 ENST00000228136.6 ENST00000228136.7 ENST00000228136.8 NM_014267 O00193 SMAP SMAP_HUMAN uc001mmk.1 uc001mmk.2 uc001mmk.3 uc001mmk.4 Belongs to the SMAP family. molecular_function cellular_component biological_process uc001mmk.1 uc001mmk.2 uc001mmk.3 uc001mmk.4 
ENST00000228251.9 YBX3 ENST00000228251.9 Y-box binding protein 3, transcript variant 1 (from RefSeq NM_003651.5) B2RBW6 CSDA DBPA ENST00000228251.1 ENST00000228251.2 ENST00000228251.3 ENST00000228251.4 ENST00000228251.5 ENST00000228251.6 ENST00000228251.7 ENST00000228251.8 NM_003651 P16989 Q14121 Q969N6 Q96B76 YBOX3_HUMAN uc001qyt.1 uc001qyt.2 uc001qyt.3 uc001qyt.4 uc001qyt.5 Binds to the GM-CSF promoter. Seems to act as a repressor. Binds also to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). Found in a mRNP complex with YBX2 (By similarity). Interacts with RRP1B (PubMed:19710015). P16989; P62136: PPP1CA; NbExp=3; IntAct=EBI-358193, EBI-357253; Cytoplasm. Nucleus. Event=Alternative splicing; Named isoforms=3; Comment=Additional isoforms seem to exist.; Name=1; IsoId=P16989-1; Sequence=Displayed; Name=2; IsoId=P16989-2; Sequence=VSP_001135; Name=3; IsoId=P16989-3; Sequence=VSP_001136; Highly expressed in skeletal muscle and heart. Sequence=AAA35749.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding in utero embryonic development nucleic acid binding DNA binding double-stranded DNA binding transcription factor activity, sequence-specific DNA binding transcription corepressor activity RNA binding mRNA 3'-UTR binding protein binding nucleus cytoplasm cytosol bicellular tight junction spermatogenesis male gonad development response to cold fertilization Rho GTPase binding negative regulation of apoptotic process positive regulation of organ growth perinuclear region of cytoplasm negative regulation of skeletal muscle tissue development negative regulation of necroptotic process 3'-UTR-mediated mRNA stabilization cellular response to tumor necrosis factor cellular hyperosmotic response negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress polysome binding positive regulation of cytoplasmic translation uc001qyt.1 uc001qyt.2 uc001qyt.3 uc001qyt.4 uc001qyt.5 
ENST00000228347.9 POLR3B ENST00000228347.9 RNA polymerase III subunit B, transcript variant 1 (from RefSeq NM_018082.6) A8K6H0 B3KV73 ENST00000228347.1 ENST00000228347.2 ENST00000228347.3 ENST00000228347.4 ENST00000228347.5 ENST00000228347.6 ENST00000228347.7 ENST00000228347.8 F5H1E6 NM_018082 POLR3B Q9NW08 Q9NW59 RPC2_HUMAN uc001tlp.1 uc001tlp.2 uc001tlp.3 uc001tlp.4 This gene encodes the second largest subunit of RNA polymerase III, the polymerase responsible for synthesizing transfer and small ribosomal RNAs in eukaryotes. The largest subunit and the encoded protein form the catalytic center of RNA polymerase III. Mutations in this gene are a cause of hypomyelinating leukodystrophy. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Dec 2011]. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci (PubMed:20413673, PubMed:33558766). Pol III-mediated transcription proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol III is recruited to DNA promoters type I, II or III with the help of general transcription factors and other specific initiation factors. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (PubMed:20413673, PubMed:33335104, PubMed:33674783, PubMed:34675218, PubMed:33558764, PubMed:33558766). Forms Pol III active center together with the largest subunit POLR3A/RPC1. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from POLR3A/RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the DNA-RNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR3A/RPC1 most likely contributing a Mg(2+)- coordinating DxDGD motif, and POLR3B/RPC2 providing lysine residues involved in catalysis. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphoester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate (PubMed:19609254, PubMed:33335104, PubMed:33674783, PubMed:34675218, PubMed:33558764, PubMed:20413673). Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through the RIG-I pathway. Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence= Component of the RNA polymerase III complex consisting of 17 subunits: a ten-subunit horseshoe-shaped catalytic core composed of POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10, POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and CRCP/RPC9, protruding from the core and functioning primarily in transcription initiation; and additional subunits homologous to general transcription factors of the RNA polymerase II machinery, POLR3C/RPC3- POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both transcription initiation and termination. Nucleus toplasm, cytosol Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NW08-1; Sequence=Displayed; Name=2; IsoId=Q9NW08-2; Sequence=VSP_045286; Leukodystrophy, hypomyelinating, 8, with or without oligodontia and/or hypogonadotropic hypogonadism (HLD8) [MIM:614381]: An autosomal recessive neurodegenerative disorder characterized by early childhood onset of cerebellar ataxia and mild intellectual disabilities associated with diffuse hypomyelination apparent on brain MRI. Variable features include oligodontia and/or hypogonadotropic hypogonadism. te=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, demyelinating, 1I (CMT1I) [MIM:619742]: An autosomal dominant demyelinating form of Charcot- Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot- Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. CMT1I is characterized predominantly by delayed motor development in the first years of life associated with gait abnormalities, sensory ataxia, hyporeflexia, and distal sensory impairment due to a sensorimotor peripheral neuropathy that mainly affects the lower limbs. The disorder is progressive, and some may have upper limb involvement. A subset of patients has central nervous system involvement that manifests as global developmental delay with impaired intellectual development and speech difficulties. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the RNA polymerase beta chain family. Sequence=BAA91527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAA91581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; immune system process DNA binding DNA-directed 5'-3' RNA polymerase activity nucleus nucleoplasm DNA-directed RNA polymerase III complex cytosol transcription, DNA-templated transcription from RNA polymerase III promoter transferase activity nucleotidyltransferase activity positive regulation of type I interferon production ribonucleoside binding positive regulation of interferon-beta production innate immune response positive regulation of innate immune response metal ion binding defense response to virus RNA polymerase III activity uc001tlp.1 uc001tlp.2 uc001tlp.3 uc001tlp.4 
ENST00000228425.11 PPFIBP1 ENST00000228425.11 PPFIA binding protein 1, transcript variant 1 (from RefSeq NM_003622.4) ENST00000228425.1 ENST00000228425.10 ENST00000228425.2 ENST00000228425.3 ENST00000228425.4 ENST00000228425.5 ENST00000228425.6 ENST00000228425.7 ENST00000228425.8 ENST00000228425.9 KIAA1230 LIPB1_HUMAN NM_003622 O75336 Q86W92 Q86X70 Q9NY03 Q9ULJ0 uc001rib.1 uc001rib.2 uc001rib.3 uc001rib.4 The protein encoded by this gene is a member of the LAR protein-tyrosine phosphatase-interacting protein (liprin) family. Liprins interact with members of LAR family of transmembrane protein tyrosine phosphatases, which are known to be important for axon guidance and mammary gland development. It has been proposed that liprins are multivalent proteins that form complex structures and act as scaffolds for the recruitment and anchoring of LAR family of tyrosine phosphatases. This protein was found to interact with S100A4, a calcium-binding protein related to tumor invasiveness and metastasis. In vitro experiment demonstrated that the interaction inhibited the phosphorylation of this protein by protein kinase C and protein kinase CK2. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]. May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A. Forms homodimers and heterodimers. Interacts with S100A4 in a calcium-dependent mode. Q86W92; P40425: PBX2; NbExp=3; IntAct=EBI-1045582, EBI-348489; Q86W92; P31947: SFN; NbExp=4; IntAct=EBI-1045582, EBI-476295; Q86W92; P62258: YWHAE; NbExp=4; IntAct=EBI-1045582, EBI-356498; Q86W92; P63104: YWHAZ; NbExp=3; IntAct=EBI-1045582, EBI-347088; Q86W92; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-1045582, EBI-25492395; Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q86W92-1; Sequence=Displayed; Name=2; IsoId=Q86W92-2; Sequence=VSP_009397, VSP_009398, VSP_009399, VSP_009400; Name=3; IsoId=Q86W92-3; Sequence=VSP_009394; Name=4; IsoId=Q86W92-4; Sequence=VSP_009397; Name=5; Synonyms=L2; IsoId=Q86W92-5; Sequence=VSP_009395, VSP_009396; Widely expressed. Absent in liver. The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type beta/beta. The C-terminal, non-coiled coil regions mediate heterodimerization type beta/alpha and interaction with S100A4. Neurodevelopmental disorder with seizures, microcephaly, and brain abnormalities (NEDSMBA) [MIM:620024]: An autosomal recessive disorder characterized by global developmental delay, severe to profound intellectual disability, progressive microcephaly, refractory early-onset epilepsy, white matter abnormalities, and periventricular calcifications. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 5]: Due to intron retention. Belongs to the liprin family. Liprin-beta subfamily. Sequence=AAH46159.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAA86544.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; cytosol plasma membrane focal adhesion cell adhesion cadherin binding uc001rib.1 uc001rib.2 uc001rib.3 uc001rib.4 
ENST00000228434.7 CD69 ENST00000228434.7 CD69 molecule (from RefSeq NM_001781.2) CD69 ENST00000228434.1 ENST00000228434.2 ENST00000228434.3 ENST00000228434.4 ENST00000228434.5 ENST00000228434.6 NM_001781 Q53ZX0 Q53ZX0_HUMAN hCG_38142 uc001qwk.1 uc001qwk.2 uc001qwk.3 This gene encodes a member of the calcium dependent lectin superfamily of type II transmembrane receptors. Expression of the encoded protein is induced upon activation of T lymphocytes, and may play a role in proliferation. Furthermore, the protein may act to transmit signals in natural killer cells and platelets. [provided by RefSeq, Aug 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC007037.1, Z22576.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228434.7/ ENSP00000228434.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## calcium ion binding external side of plasma membrane cell surface membrane integral component of membrane carbohydrate binding cellular response to drug uc001qwk.1 uc001qwk.2 uc001qwk.3 
ENST00000228437.10 PRDM4 ENST00000228437.10 PR/SET domain 4 (from RefSeq NM_012406.4) ENST00000228437.1 ENST00000228437.2 ENST00000228437.3 ENST00000228437.4 ENST00000228437.5 ENST00000228437.6 ENST00000228437.7 ENST00000228437.8 ENST00000228437.9 NM_012406 PFM1 PRDM4_HUMAN Q9UFA6 Q9UKN5 uc001tmp.1 uc001tmp.2 uc001tmp.3 uc001tmp.4 uc001tmp.5 The protein encoded by this gene is a transcription factor of the PR-domain protein family. It contains a PR-domain and multiple zinc finger motifs. Transcription factors of the PR-domain family are known to be involved in cell differentiation and tumorigenesis. An elevated expression level of this gene has been observed in PC12 cells treated with nerve growth factor, beta polypeptide (NGF). This gene is located in a chromosomal region that is thought to contain tumor suppressor genes. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.39635.1, SRR1660807.82133.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228437.10/ ENSP00000228437.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## May function as a transcription factor involved in cell differentiation. Q9UKN5; Q8WYA6: CTNNBL1; NbExp=3; IntAct=EBI-2803427, EBI-748128; Q9UKN5; Q8IXL7: MSRB3; NbExp=3; IntAct=EBI-2803427, EBI-8634060; Q9UKN5; P62166: NCS1; NbExp=3; IntAct=EBI-2803427, EBI-746987; Nucleus Expressed in many tissues. Highly expressed in ovary, testis, pancreas, brain, heart and prostate. Belongs to the class V-like SAM-binding methyltransferase superfamily. RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus cytoplasm transcription from RNA polymerase II promoter methyltransferase activity transferase activity chromatin DNA binding methylation histone methyltransferase complex sequence-specific DNA binding histone H4-R3 methylation positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter metal ion binding histone methyltransferase binding uc001tmp.1 uc001tmp.2 uc001tmp.3 uc001tmp.4 uc001tmp.5 
ENST00000228438.3 CLEC2B ENST00000228438.3 C-type lectin domain family 2 member B (from RefSeq NM_005127.3) AICL B2R9U1 CLC2B_HUMAN CLECSF2 ENST00000228438.1 ENST00000228438.2 IFNRG1 NM_005127 Q8IZE9 Q92478 Q9BS74 Q9UQB4 uc001qwn.1 uc001qwn.2 uc001qwn.3 uc001qwn.4 uc001qwn.5 This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions, such as cell adhesion, cell-cell signalling, glycoprotein turnover, and roles in inflammation and immune response. The encoded type 2 transmembrane protein may function as a cell activation antigen. An alternative splice variant has been described but its full-length sequence has not been determined. This gene is closely linked to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.267603.1, SRR1803615.357743.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Q92478; P01023: A2M; NbExp=3; IntAct=EBI-13350535, EBI-640741; Q92478; Q92478: CLEC2B; NbExp=2; IntAct=EBI-13350535, EBI-13350535; Q92478; P50570-2: DNM2; NbExp=3; IntAct=EBI-13350535, EBI-10968534; Q92478; P42858: HTT; NbExp=9; IntAct=EBI-13350535, EBI-466029; Q92478; O14656-2: TOR1A; NbExp=3; IntAct=EBI-13350535, EBI-25847109; Membrane ; Single-pass type II membrane protein Expressed preferentially in lymphoid tissues, and in most hematopoietic cell types. Name=Functional Glycomics Gateway - Glycan Binding; Note=CD69 homolog; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_236"; plasma membrane integral component of plasma membrane membrane integral component of membrane carbohydrate binding identical protein binding regulation of immune response uc001qwn.1 uc001qwn.2 uc001qwn.3 uc001qwn.4 uc001qwn.5 
ENST00000228476.8 DAO ENST00000228476.8 D-amino acid oxidase, transcript variant 2 (from RefSeq NM_001917.5) B2R7I5 DAMOX ENST00000228476.1 ENST00000228476.2 ENST00000228476.3 ENST00000228476.4 ENST00000228476.5 ENST00000228476.6 ENST00000228476.7 NM_001917 OXDA_HUMAN P14920 Q16758 Q8N6R2 uc001tnr.1 uc001tnr.2 uc001tnr.3 uc001tnr.4 uc001tnr.5 uc001tnr.6 This gene encodes the peroxisomal enzyme D-amino acid oxidase. The enzyme is a flavoprotein which uses flavin adenine dinucleotide (FAD) as its prosthetic group. Its substrates include a wide variety of D-amino acids, but it is inactive on the naturally occurring L-amino acids. Its biological function is not known; it may act as a detoxifying agent which removes D-amino acids that accumulate during aging. In mice, it degrades D-serine, a co-agonist of the NMDA receptor. This gene may play a role in the pathophysiology of schizophrenia. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.254102.1, SRR3476690.493112.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1970526, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228476.8/ ENSP00000228476.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids. Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence=; Name=FAD; Xref=ChEBI:CHEBI:57692; Kinetic parameters: KM=3.6 mM for D-serine KM=1.7 mM for D-proline KM=1.1 mM for D-tyrosine KM=1.5 mM for D-DOPA KM=1.2 mM for D-phenylalanine KM=0.9 mM for D-alanine Homodimer (PubMed:17088322, PubMed:18455394). Interacts with DAOA (PubMed:12364586). P14920; O43741: PRKAB2; NbExp=6; IntAct=EBI-3908043, EBI-1053424; Peroxisome. Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry. Belongs to the DAMOX/DASOX family. D-amino-acid oxidase activity protein binding peroxisome peroxisomal membrane peroxisomal matrix cytosol proline catabolic process protein targeting to peroxisome oxidoreductase activity cellular nitrogen compound metabolic process D-serine catabolic process dopamine biosynthetic process D-amino acid metabolic process protein dimerization activity cofactor binding oxidation-reduction process D-alanine catabolic process D-serine metabolic process FAD binding mitochondrial outer membrane uc001tnr.1 uc001tnr.2 uc001tnr.3 uc001tnr.4 uc001tnr.5 uc001tnr.6 
ENST00000228495.11 KCTD10 ENST00000228495.11 potassium channel tetramerization domain containing 10, transcript variant 5 (from RefSeq NR_133898.2) BACD3_HUMAN ENST00000228495.1 ENST00000228495.10 ENST00000228495.2 ENST00000228495.3 ENST00000228495.4 ENST00000228495.5 ENST00000228495.6 ENST00000228495.7 ENST00000228495.8 ENST00000228495.9 MSTP028 NR_133898 Q53HN2 Q59FV1 Q6PL47 Q96SU0 Q9H3F6 ULR061 uc001toi.1 uc001toi.2 uc001toi.3 The protein encoded by this gene binds proliferating cell nuclear antigen (PCNA) and may be involved in DNA synthesis and cell proliferation. In addition, the encoded protein may be a tumor suppressor. Several protein-coding and non-protein coding transcript variants have been found for this gene. [provided by RefSeq, Dec 2015]. Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome (By similarity). Protein modification; protein ubiquitination. Homotetramer; forms a two-fold symmetric tetramer in solution (PubMed:28963344). Interacts with CUL3; interaction is direct and forms a 5:5 heterodecamer (PubMed:28963344). Component of the BCR(BACURD3) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD10/BACURD3 and RBX1 (By similarity). Interacts with DNA polymerase delta subunit 2/POLD2 (By similarity). Interacts with PCNA (PubMed:19125419). Q9H3F6; Q13618: CUL3; NbExp=7; IntAct=EBI-2505886, EBI-456129; Q9H3F6; Q92997: DVL3; NbExp=3; IntAct=EBI-2505886, EBI-739789; Q9H3F6; Q9H3F6: KCTD10; NbExp=3; IntAct=EBI-2505886, EBI-2505886; Q9H3F6; Q8WZ19: KCTD13; NbExp=4; IntAct=EBI-2505886, EBI-742916; Q9H3F6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2505886, EBI-741158; Q9H3F6; Q15560: TCEA2; NbExp=3; IntAct=EBI-2505886, EBI-710310; Q9H3F6; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-2505886, EBI-11523345; Q9H3F6; Q13829: TNFAIP1; NbExp=6; IntAct=EBI-2505886, EBI-2505861; Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9H3F6-1; Sequence=Displayed; Name=2; IsoId=Q9H3F6-2; Sequence=VSP_019980; Name=3; IsoId=Q9H3F6-3; Sequence=VSP_019978, VSP_019979; Belongs to the BACURD family. Sequence=BAB55188.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAD92595.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Notch binding protein binding nucleus nucleoplasm cytosol ubiquitin-dependent protein catabolic process protein ubiquitination GTP-Rho binding Cul3-RING ubiquitin ligase complex negative regulation of Rho protein signal transduction proteasome-mediated ubiquitin-dependent protein catabolic process protein homooligomerization ubiquitin-protein transferase activity uc001toi.1 uc001toi.2 uc001toi.3 
ENST00000228506.8 MLEC ENST00000228506.8 malectin, transcript variant 1 (from RefSeq NM_014730.4) ENST00000228506.1 ENST00000228506.2 ENST00000228506.3 ENST00000228506.4 ENST00000228506.5 ENST00000228506.6 ENST00000228506.7 KIAA0152 MLEC MLEC_HUMAN NM_014730 Q14165 uc001tyy.1 uc001tyy.2 uc001tyy.3 This gene encodes the carbohydrate-binding protein malectin which is a Type I membrane-anchored endoplasmic reticulum protein. This protein has an affinity for Glc2Man9GlcNAc2 (G2M9) N-glycans and is involved in regulating glycosylation in the endoplasmic reticulum. This protein has also been shown to interact with ribophorin I and may be involved in the directing the degradation of misfolded proteins. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jan 2015]. Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N- glycosylation (By similarity). Interacts with the oligosaccharyltransferase (OST) complex. Q14165; P04843: RPN1; NbExp=2; IntAct=EBI-1046466, EBI-355963; Endoplasmic reticulum membrane ; Single-pass type I membrane protein Belongs to the malectin family. Sequence=BAA09773.2; Type=Erroneous initiation; Evidence=; endoplasmic reticulum endoplasmic reticulum membrane plasma membrane carbohydrate metabolic process protein folding membrane integral component of membrane enzyme binding carbohydrate binding specific granule membrane neutrophil degranulation uc001tyy.1 uc001tyy.2 uc001tyy.3 
ENST00000228510.8 MVK ENST00000228510.8 mevalonate kinase, transcript variant 10 (from RefSeq NR_182760.1) ENST00000228510.1 ENST00000228510.2 ENST00000228510.3 ENST00000228510.4 ENST00000228510.5 ENST00000228510.6 ENST00000228510.7 KIME_HUMAN MVK NR_182760 Q03426 uc009zvk.1 uc009zvk.2 uc009zvk.3 uc009zvk.4 uc009zvk.5 Catalyzes the phosphorylation of mevalonate to mevalonate 5- phosphate, a key step in isoprenoid and cholesterol biosynthesis (PubMed:9325256, PubMed:18302342, PubMed:9392419, PubMed:11278915). Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+); Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.1.36; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Farnesyl pyrophosphate and geranyl pyrophosphate inhibit mevalonate kinase activity by binding competitively at the ATP- binding sites. Kinetic parameters: KM=74 uM for ATP ; KM=178 uM for ATP ; KM=12.2 uM for adenosine 5-O-[S-(acetamidoproxyl)-3-thiotriphosphate] ; KM=24 uM for (R)-mevalonate ; KM=40 uM for (R)-mevalonate ; Vmax=37 umol/min/mg enzyme with (R)-mevalonate as substrate ; Vmax=28 umol/min/mg enzyme with (R)-mevalonate as substrate ; Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3. Homodimer. Q03426; Q03426: MVK; NbExp=12; IntAct=EBI-740630, EBI-740630; Q03426; Q9NUX5: POT1; NbExp=2; IntAct=EBI-740630, EBI-752420; Q03426; Q8WVD5: RNF141; NbExp=3; IntAct=EBI-740630, EBI-4308142; Cytoplasm Peroxisome Mevalonic aciduria (MEVA) [MIM:610377]: Accumulation of mevalonic acid which causes a variety of symptoms such as psychomotor retardation, dysmorphic features, cataracts, hepatosplenomegaly, lymphadenopathy, anemia, hypotonia, myopathy, and ataxia. te=The disease is caused by variants affecting the gene represented in this entry. Hyperimmunoglobulinemia D and periodic fever syndrome (HIDS) [MIM:260920]: Autosomal recessive disease characterized by recurrent episodes of unexplained high fever associated with skin rash, diarrhea, adenopathy (swollen, tender lymph nodes), arthralgias and/or arthritis. Concentration of IgD, and often IgA, are above normal. te=The disease is caused by variants affecting the gene represented in this entry. Porokeratosis 3, multiple types (POROK3) [MIM:175900]: A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the GHMP kinase family. Mevalonate kinase subfamily. Sequence=CAA53059.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=INFEVERS; Note=Repertory of FMF and hereditary autoinflammatory disorders mutations; URL="https://infevers.umai-montpellier.fr/web/search.php?n=3"; nucleotide binding magnesium ion binding mevalonate kinase activity protein binding ATP binding cytoplasm peroxisome cytosol lipid metabolic process steroid biosynthetic process cholesterol biosynthetic process steroid metabolic process cholesterol metabolic process isoprenoid biosynthetic process sterol biosynthetic process kinase activity phosphorylation transferase activity isopentenyl diphosphate biosynthetic process, mevalonate pathway identical protein binding regulation of cholesterol biosynthetic process metal ion binding negative regulation of inflammatory response uc009zvk.1 uc009zvk.2 uc009zvk.3 uc009zvk.4 uc009zvk.5 
ENST00000228515.6 CSRNP2 ENST00000228515.6 cysteine and serine rich nuclear protein 2, transcript variant 2 (from RefSeq NR_045072.2) C12orf22 CSRN2_HUMAN ENST00000228515.1 ENST00000228515.2 ENST00000228515.3 ENST00000228515.4 ENST00000228515.5 FAM130A1 NR_045072 Q9H175 TAIP12 uc001rxu.1 uc001rxu.2 uc001rxu.3 uc001rxu.4 The protein encoded by this gene belongs to the CSRNP family of nuclear proteins that share conserved regions, including cysteine- and serine- rich regions, a basic domain, a transcriptional activation domain, and bind the sequence 'AGAGTG', thus have the hallmark of transcription factors. Studies in mice suggest that these genes may have redundant functions. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Aug 2011]. Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity (By similarity). May play a role in apoptosis. Q9H175; P62136: PPP1CA; NbExp=10; IntAct=EBI-5235958, EBI-357253; Q9H175; P62140: PPP1CB; NbExp=7; IntAct=EBI-5235958, EBI-352350; Q9H175; P36873: PPP1CC; NbExp=7; IntAct=EBI-5235958, EBI-356283; Nucleus Belongs to the AXUD1 family. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus apoptotic process negative regulation of phosphatase activity phosphatase binding sequence-specific DNA binding positive regulation of transcription from RNA polymerase II promoter uc001rxu.1 uc001rxu.2 uc001rxu.3 uc001rxu.4 
ENST00000228534.6 IL23A ENST00000228534.6 interleukin 23 subunit alpha (from RefSeq NM_016584.3) ENST00000228534.1 ENST00000228534.2 ENST00000228534.3 ENST00000228534.4 ENST00000228534.5 IL23A_HUMAN NM_016584 Q6NZ80 Q6NZ82 Q9H2A5 Q9NPF7 SGRF UNQ2498/PRO5798 uc001sla.1 uc001sla.2 uc001sla.3 uc001sla.4 uc001sla.5 This gene encodes a subunit of the heterodimeric cytokine interleukin 23 (IL23). IL23 is composed of this protein and the p40 subunit of interleukin 12 (IL12B). The receptor of IL23 is formed by the beta 1 subunit of IL12 (IL12RB1) and an IL23 specific subunit, IL23R. Both IL23 and IL12 can activate the transcription activator STAT4, and stimulate the production of interferon-gamma (IFNG). In contrast to IL12, which acts mainly on naive CD4(+) T cells, IL23 preferentially acts on memory CD4(+) T cells. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY359083.1, SRR1163658.347730.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228534.6/ ENSP00000228534.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Associates with IL12B to form the pro-inflammatory cytokine IL-23 that plays different roles in innate and adaptive immunity (PubMed:11114383). Released by antigen-presenting cells such as dendritic cells or macrophages, binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R to activate JAK2 and TYK2 which then phosphorylate the receptor to form a docking site leading to the phosphorylation of STAT3 and STAT4 (PubMed:32474165, PubMed:29287995, PubMed:33606986). This process leads to activation of several pathways including p38 MAPK or NF-kappa-B and promotes the production of pro- inflammatory cytokines such as interleukin-17A/IL17A (PubMed:12023369). In turn, participates in the early and effective intracellular bacterial clearance (PubMed:32474165). Promotes the expansion and survival of T-helper 17 cells, a CD4-positive helper T-cell subset that produces IL-17, as well as other IL-17-producing cells (PubMed:17676044). Heterodimer with IL12B; disulfide-linked (PubMed:11114383, PubMed:18680750). The heterodimer is known as interleukin IL-23 (PubMed:11114383, PubMed:18680750). Interacts with IL23R; this interaction enables recruitment of IL12RB1 (PubMed:29287995, PubMed:33606986). Q9NPF7; P29460: IL12B; NbExp=6; IntAct=EBI-2481154, EBI-1029614; Q9NPF7; Q5VWK5: IL23R; NbExp=2; IntAct=EBI-2481154, EBI-10248005; Q9NPF7; P40855: PEX19; NbExp=6; IntAct=EBI-2481154, EBI-594747; Secreted Note=Secreted upon association with IL12B. Secreted by activated dendritic and phagocytic cells and keratinocytes. Also expressed by dermal Langerhans cells (at protein level). Expressed by newborns dendritic cells. Up-regulated by a wide array of pathogens and pathogen- products together with self-signals for danger or injury. Up-regulated in psoriatic dermal tissues, in dendritic cells of multiple sclerosis patients and in tumors. Belongs to the IL-6 superfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44517/IL23A"; positive regulation of T cell mediated cytotoxicity positive regulation of defense response to virus by host immune system process positive regulation of T-helper 1 type immune response cytokine activity protein binding extracellular region extracellular space endoplasmic reticulum lumen inflammatory response immune response positive regulation of activation of Janus kinase activity cytokine-mediated signaling pathway negative regulation of interleukin-10 production positive regulation of granulocyte macrophage colony-stimulating factor production positive regulation of interferon-gamma production positive regulation of interleukin-10 production positive regulation of interleukin-12 production positive regulation of interleukin-17 production positive regulation of tumor necrosis factor production positive regulation of natural killer cell activation positive regulation of natural killer cell proliferation positive regulation of tissue remodeling interleukin-23-mediated signaling pathway T cell proliferation positive regulation of T cell proliferation positive regulation of activated T cell proliferation regulation of tyrosine phosphorylation of STAT protein positive regulation of tyrosine phosphorylation of STAT protein positive regulation of memory T cell differentiation innate immune response interleukin-23 receptor binding positive regulation of osteoclast differentiation positive regulation of transcription from RNA polymerase II promoter tissue remodeling positive regulation of inflammatory response defense response to Gram-negative bacterium positive regulation of NK T cell activation positive regulation of NK T cell proliferation defense response to virus interleukin-23 complex positive regulation of neutrophil chemotaxis positive regulation of NIK/NF-kappaB signaling positive regulation of T-helper 17 type immune response positive regulation of T-helper 17 cell lineage commitment uc001sla.1 uc001sla.2 uc001sla.3 uc001sla.4 uc001sla.5 
ENST00000228567.7 SYT10 ENST00000228567.7 synaptotagmin 10 (from RefSeq NM_198992.4) ENST00000228567.1 ENST00000228567.2 ENST00000228567.3 ENST00000228567.4 ENST00000228567.5 ENST00000228567.6 NM_198992 Q495U2 Q6XYQ8 SYT10_HUMAN uc001rll.1 uc001rll.2 Ca(2+) sensor specifically required for the Ca(2+)-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb. Exocytosis of IGF1 is required for sensory perception of smell. Not involved in Ca(2+)-dependent synaptic vesicle exocytosis (By similarity). Acts through Ca(2+) and phospholipid binding to the C2 domain: Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. ; Homodimer; disulfide-linked via the cysteine motif. Can also form heterodimers with SYT3, SYT6, SYT7 and SYT9. Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass membrane protein Note=Localizes to neuronal vesicles containing IGF1 that are not enriched at synapses. Does not colocalize with synaptic vesicles or with the Golgi apparatus. Expressed only in pancreas, lung and kidney. The cysteine motif mediates homo- or heterodimer formation via formation of disulfide bonds. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. Belongs to the synaptotagmin family. SNARE binding phosphatidylserine binding calcium ion binding calcium-dependent phospholipid binding phosphatidylinositol-4,5-bisphosphate binding plasma membrane exocytosis chemical synaptic transmission sensory perception of smell regulation of dopamine secretion membrane integral component of membrane vesicle-mediated transport calcium ion regulated exocytosis regulation of calcium ion-dependent exocytosis syntaxin binding clathrin binding transport vesicle membrane cytoplasmic vesicle identical protein binding protein homodimerization activity positive regulation of calcium ion-dependent exocytosis metal ion binding protein heterodimerization activity exocytic vesicle cellular response to calcium ion presynapse synaptic vesicle exocytosis uc001rll.1 uc001rll.2 
ENST00000228606.9 CYP27B1 ENST00000228606.9 cytochrome P450 family 27 subfamily B member 1 (from RefSeq NM_000785.4) B2RC61 CP27B_HUMAN CYP1ALPHA CYP27B ENST00000228606.1 ENST00000228606.2 ENST00000228606.3 ENST00000228606.4 ENST00000228606.5 ENST00000228606.6 ENST00000228606.7 ENST00000228606.8 NM_000785 O15528 Q548T3 uc001spz.1 uc001spz.2 uc001spz.3 This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The protein encoded by this gene localizes to the inner mitochondrial membrane where it hydroxylates 25-hydroxyvitamin D3 at the 1alpha position. This reaction synthesizes 1alpha,25-dihydroxyvitamin D3, the active form of vitamin D3, which binds to the vitamin D receptor and regulates calcium metabolism. Thus this enzyme regulates the level of biologically active vitamin D and plays an important role in calcium homeostasis. Mutations in this gene can result in vitamin D-dependent rickets type I. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB005038.1, AF020192.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1970526, SAMEA2145774 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000228606.9/ ENSP00000228606.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## A cytochrome P450 monooxygenase involved in vitamin D metabolism and in calcium and phosphorus homeostasis. Catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1alpha- position to form the hormonally active form of vitamin D3, 1alpha,25- dihydroxyvitamin D3/calcitriol that acts via the vitamin D receptor (VDR) (PubMed:10518789, PubMed:9486994, PubMed:22862690, PubMed:10566658, PubMed:12050193). Has 1alpha-hydroxylase activity on vitamin D intermediates of the CYP24A1-mediated inactivation pathway (PubMed:10518789, PubMed:22862690). Converts 24R,25-dihydroxyvitamin D3/secalciferol to 1-alpha,24,25-trihydroxyvitamin D3, an active ligand of VDR. Also active on 25-hydroxyvitamin D2 (PubMed:10518789). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin (PubMed:22862690). Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitriol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:20573, Rhea:RHEA- COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:17933, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.18; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20574; Evidence=; Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = calcitetrol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49064, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799; EC=1.14.15.18; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49065; Evidence=; Reaction=25-hydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,25-dihydroxy-24-oxocalciol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49068, Rhea:RHEA-COMP:9998, Rhea:RHEA- COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47805, ChEBI:CHEBI:47812; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49069; Evidence=; Reaction=25-hydroxyvitamin D2 + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 1alpha,25-dihydroxyvitamin D2 + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49048, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:86319, ChEBI:CHEBI:86320; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49049; Evidence=; Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Activated by cardiolipin and dioleoyl phosphatidylethanolamine (DOPE), phospholipids found in the inner mitochondrial membrane. Inhibited by high substrate concentration. Kinetic parameters: KM=2.7 uM for 25-hydroxyvitamin D3 ; KM=1.1 uM for 24,25-dihydroxyvitamin D3 ; KM=0.9 uM for 25-hydroxyvitamin D3 ; Vmax=3.9 pmol/min/mg enzyme toward 25-hydroxyvitamin D3 ; Vmax=3.2 pmol/min/mg enzyme toward 24,25-dihydroxyvitamin D3 ; Vmax=1.3 nmol/min/mg enzyme toward 25-hydroxyvitamin D3 ; Hormone biosynthesis; vitamin D biosynthesis. Mitochondrion membrane. Kidney. Rickets vitamin D-dependent 1A (VDDR1A) [MIM:264700]: A disorder caused by a selective deficiency of the active form of vitamin D (1,25-dihydroxyvitamin D3) and resulting in defective bone mineralization and clinical features of rickets. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the cytochrome P450 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cyp27b1/"; monooxygenase activity calcidiol 1-monooxygenase activity iron ion binding cytoplasm mitochondrion mitochondrial outer membrane vitamin metabolic process calcium ion transport negative regulation of cell proliferation negative regulation of calcidiol 1-monooxygenase activity positive regulation of vitamin D 24-hydroxylase activity membrane oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen heme binding bone mineralization negative regulation of cell growth regulation of bone mineralization mitochondrial membrane response to lipopolysaccharide response to vitamin D response to interferon-gamma calcitriol biosynthetic process from calciol vitamin D metabolic process vitamin D catabolic process response to estrogen positive regulation of keratinocyte differentiation decidualization metal ion binding calcium ion homeostasis oxidation-reduction process G1 to G0 transition positive regulation of vitamin D receptor signaling pathway uc001spz.1 uc001spz.2 uc001spz.3 
ENST00000228641.4 MYF6 ENST00000228641.4 myogenic factor 6 (from RefSeq NM_002469.3) B2R898 BHLHC4 ENST00000228641.1 ENST00000228641.2 ENST00000228641.3 MRF4 MYF6_HUMAN NM_002469 P23409 Q53X80 Q6FHI9 uc001szf.1 uc001szf.2 uc001szf.3 uc001szf.4 The protein encoded by this gene is a probable basic helix-loop-helix (bHLH) DNA binding protein involved in muscle differentiation. The encoded protein likely acts as a heterodimer with another bHLH protein. Defects in this gene are a cause of autosomal dominant centronuclear myopathy (ADCNM). [provided by RefSeq, May 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: ERR279860.4145.1, ERR279848.597.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158800, SAMEA2162946 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228641.4/ ENSP00000228641.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein. Efficient DNA binding requires dimerization with another bHLH protein. Interacts with CSRP3. Nucleus. Skeletal muscle. nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding somitogenesis DNA binding transcription factor activity, sequence-specific DNA binding nucleus nucleoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development muscle organ development skeletal muscle tissue development cell differentiation skeletal muscle cell differentiation muscle cell fate commitment skeletal muscle tissue regeneration positive regulation of myoblast differentiation negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity protein dimerization activity positive regulation of skeletal muscle fiber development positive regulation of muscle cell differentiation muscle tissue morphogenesis RNA polymerase II transcription factor complex positive regulation of myoblast fusion E-box binding uc001szf.1 uc001szf.2 uc001szf.3 uc001szf.4 
ENST00000228644.4 MYF5 ENST00000228644.4 myogenic factor 5 (from RefSeq NM_005593.3) BHLHC2 ENST00000228644.1 ENST00000228644.2 ENST00000228644.3 MYF5_HUMAN NM_005593 P13349 Q6ISR9 uc001szg.1 uc001szg.2 uc001szg.3 uc001szg.4 Transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation (PubMed:29887215). Together with MYOG and MYOD1, co-occupies muscle- specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein. Efficient DNA binding requires dimerization with another bHLH protein. P13349; X5D778: ANKRD11; NbExp=3; IntAct=EBI-17491620, EBI-17183751; P13349; P29972: AQP1; NbExp=3; IntAct=EBI-17491620, EBI-745213; P13349; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-17491620, EBI-725606; P13349; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-17491620, EBI-10961312; P13349; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-17491620, EBI-741528; P13349; Q9H0I2: ENKD1; NbExp=5; IntAct=EBI-17491620, EBI-744099; P13349; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-17491620, EBI-11986315; P13349; Q6QHK4: FIGLA; NbExp=3; IntAct=EBI-17491620, EBI-11976617; P13349; P41134: ID1; NbExp=5; IntAct=EBI-17491620, EBI-1215527; P13349; Q02535: ID3; NbExp=3; IntAct=EBI-17491620, EBI-1387094; P13349; P16144-2: ITGB4; NbExp=3; IntAct=EBI-17491620, EBI-11051601; P13349; A6NI15: MSGN1; NbExp=3; IntAct=EBI-17491620, EBI-11991020; P13349; Q02577: NHLH2; NbExp=3; IntAct=EBI-17491620, EBI-5378683; P13349; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-17491620, EBI-10694433; P13349; Q13526: PIN1; NbExp=3; IntAct=EBI-17491620, EBI-714158; P13349; P13631: RARG; NbExp=3; IntAct=EBI-17491620, EBI-2568901; P13349; Q7RTU7: SCX; NbExp=3; IntAct=EBI-17491620, EBI-17492262; P13349; Q96ES7: SGF29; NbExp=5; IntAct=EBI-17491620, EBI-743117; P13349; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-17491620, EBI-12004298; P13349; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-17491620, EBI-11955057; P13349; Q08117-2: TLE5; NbExp=3; IntAct=EBI-17491620, EBI-11741437; P13349; P15622-3: ZNF250; NbExp=3; IntAct=EBI-17491620, EBI-10177272; P13349; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-17491620, EBI-740727; P13349; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-17491620, EBI-14069183; P13349; Q96SQ5: ZNF587; NbExp=5; IntAct=EBI-17491620, EBI-6427977; P13349; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-17491620, EBI-5667516; Nucleus Ophthalmoplegia, external, with rib and vertebral anomalies (EORVA) [MIM:618155]: An autosomal recessive disorder characterized by congenital nonprogressive external ophthalmoplegia, ptosis, scoliosis, torticollis, and vertebral and rib anomalies. Note=The disease is caused by variants affecting the gene represented in this entry. nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding cartilage condensation ossification somitogenesis regulation of cell-matrix adhesion DNA binding protein binding nucleus nucleoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development muscle organ development skeletal muscle tissue development cell differentiation extracellular matrix organization skeletal muscle cell differentiation muscle cell fate commitment camera-type eye development sequence-specific DNA binding positive regulation of myoblast differentiation positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity protein dimerization activity muscle organ morphogenesis embryonic skeletal system morphogenesis positive regulation of skeletal muscle fiber development positive regulation of muscle cell differentiation muscle tissue morphogenesis RNA polymerase II transcription factor complex positive regulation of myoblast fusion E-box binding uc001szg.1 uc001szg.2 uc001szg.3 uc001szg.4 
ENST00000228682.7 GLI1 ENST00000228682.7 GLI family zinc finger 1, transcript variant 1 (from RefSeq NM_005269.3) D0EUY3 E9PQQ9 ENST00000228682.1 ENST00000228682.2 ENST00000228682.3 ENST00000228682.4 ENST00000228682.5 ENST00000228682.6 F5H6H8 GLI GLI1_HUMAN NM_005269 P08151 Q8TDN9 uc001snx.1 uc001snx.2 uc001snx.3 uc001snx.4 uc001snx.5 This gene encodes a member of the Kruppel family of zinc finger proteins. The encoded transcription factor is activated by the sonic hedgehog signal transduction cascade and regulates stem cell proliferation. The activity and nuclear localization of this protein is negatively regulated by p53 in an inhibitory loop. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2009]. Acts as a transcriptional activator (PubMed:19706761, PubMed:10806483, PubMed:19878745, PubMed:24076122, PubMed:24311597, PubMed:24217340). Binds to the DNA consensus sequence 5'-GACCACCCA-3' (PubMed:2105456, PubMed:8378770, PubMed:24217340). Regulates the transcription of specific genes during normal development (PubMed:19706761). Plays a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling (PubMed:19706761, PubMed:28973407). Plays a role in cell proliferation and differentiation via its role in SHH signaling (PubMed:11238441, PubMed:28973407). [Isoform 2]: Acts as a transcriptional activator, but activates a different set of genes than isoform 1. Activates expression of CD24, unlike isoform 1. Mediates SHH signaling. Promotes cancer cell migration. Interacts with KIF7 (By similarity). Interacts with STK36 (PubMed:10806483). Interacts with ZIC1; the interaction enhances transcription activation (PubMed:11238441). Interacts with SUFU; this inhibits transcriptional activation by GLI1 (PubMed:10806483, PubMed:24311597, PubMed:24217340, PubMed:28965847). P08151; P29972: AQP1; NbExp=3; IntAct=EBI-308084, EBI-745213; P08151; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-308084, EBI-744545; P08151; P53673: CRYBA4; NbExp=3; IntAct=EBI-308084, EBI-7519711; P08151; Q96CN9: GCC1; NbExp=3; IntAct=EBI-308084, EBI-746252; P08151; Q96J02: ITCH; NbExp=4; IntAct=EBI-308084, EBI-1564678; P08151; Q13526: PIN1; NbExp=3; IntAct=EBI-308084, EBI-714158; P08151; P54646: PRKAA2; NbExp=3; IntAct=EBI-308084, EBI-1383852; P08151; P23443: RPS6KB1; NbExp=4; IntAct=EBI-308084, EBI-1775921; P08151; P23443-2: RPS6KB1; NbExp=2; IntAct=EBI-308084, EBI-6093204; P08151; Q9UMX1: SUFU; NbExp=27; IntAct=EBI-308084, EBI-740595; P08151; Q9UMX1-1: SUFU; NbExp=2; IntAct=EBI-308084, EBI-740615; P08151; Q9UMX1-2: SUFU; NbExp=4; IntAct=EBI-308084, EBI-740621; P08151; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-308084, EBI-5235829; P08151; P40337-1: VHL; NbExp=2; IntAct=EBI-308084, EBI-3504450; P08151; P40337-3: VHL; NbExp=2; IntAct=EBI-308084, EBI-301270; P08151; Q9QZS3-2: Numb; Xeno; NbExp=4; IntAct=EBI-308084, EBI-3896014; P08151; P46684: Zic1; Xeno; NbExp=2; IntAct=EBI-308084, EBI-308006; P08151-1; P41743: PRKCI; NbExp=3; IntAct=EBI-16038799, EBI-286199; Cytoplasm cleus te=Tethered in the cytoplasm by binding to SUFU (PubMed:10806483). Activation and translocation to the nucleus is promoted by interaction with STK36 (PubMed:10806483). Phosphorylation by ULK3 may promote nuclear localization (PubMed:19878745). Translocation to the nucleus is promoted by interaction with ZIC1 (PubMed:11238441). [Isoform 2]: Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P08151-1; Sequence=Displayed; Name=2; Synonyms=tGLI1; IsoId=P08151-2; Sequence=VSP_042215; Name=3; IsoId=P08151-3; Sequence=VSP_054829; Detected in testis (at protein level) (PubMed:2105456). Testis, myometrium and fallopian tube. Also expressed in the brain with highest expression in the cerebellum, optic nerve and olfactory tract (PubMed:19878745). Isoform 1 is detected in brain, spleen, pancreas, liver, kidney and placenta; isoform 2 is not detectable in these tissues (PubMed:19706761). Isoform 1 and isoform 2 are amplified in glioblastoma cells. Phosphorylated in vitro by ULK3. Acetylation at Lys-518 down-regulates transcriptional activity. Deacetylated by HDAC1. Ubiquitinated by the CRL2(FEM1B) complex, suppressing GLI1 transcriptional activator activity. Polydactyly, postaxial, A8 (PAPA8) [MIM:618123]: A form of postaxial polydactyly, a condition characterized by the occurrence of supernumerary digits in the upper and/or lower extremities. In postaxial polydactyly type A, the extra digit is well-formed and articulates with the fifth or a sixth metacarpal/metatarsal. PAPA8 is an autosomal recessive condition characterized by the presence of postaxial extra digits (hexadactyly) on the hands and/or the feet. Note=The disease is caused by variants affecting the gene represented in this entry. Polydactyly, preaxial 1 (PPD1) [MIM:174400]: A form of polydactyly, a condition defined by the occurrence of supernumerary digits in the upper and/or lower extremities. Preaxial or radial polydactyly refers to the presence of extra digits on the radial side of the hand. PPD1 is an autosomal recessive form characterized by duplication of the distal phalanx of the thumb. Note=The disease may be caused by variants affecting the gene represented in this entry. [Isoform 2]: Undetectable in normal cells but highly expressed in cancer cells. Belongs to the GLI C2H2-type zinc-finger protein family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/310/GLI"; RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding osteoblast differentiation nucleic acid binding DNA binding chromatin binding protein binding nucleus nucleoplasm cytoplasm cytosol cilium axoneme smoothened signaling pathway multicellular organism development spermatogenesis ventral midline development microtubule binding positive regulation of cell proliferation regulation of smoothened signaling pathway response to wounding epidermal cell differentiation dorsal/ventral pattern formation proximal/distal pattern formation cerebellar cortex morphogenesis smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation pituitary gland development cell differentiation lung development positive regulation of cell migration prostate gland development sequence-specific DNA binding transcription regulatory region DNA binding regulation of osteoblast differentiation positive regulation of DNA replication positive regulation of smoothened signaling pathway positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter metal ion binding digestive tract morphogenesis notochord regression positive regulation of cardiac muscle cell proliferation canonical Wnt signaling pathway negative regulation of canonical Wnt signaling pathway liver regeneration ciliary tip ciliary base positive regulation of cell cycle G1/S phase transition regulation of hepatocyte proliferation uc001snx.1 uc001snx.2 uc001snx.3 uc001snx.4 uc001snx.5 
ENST00000228705.7 PPM1H ENST00000228705.7 protein phosphatase, Mg2+/Mn2+ dependent 1H (from RefSeq NM_020700.2) ARHCL1 B1Q2A9 B2RXG4 ENST00000228705.1 ENST00000228705.2 ENST00000228705.3 ENST00000228705.4 ENST00000228705.5 ENST00000228705.6 KIAA1157 NM_020700 PPM1H_HUMAN Q6PI86 Q9ULR3 URCC2 uc001srk.1 uc001srk.2 uc001srk.3 uc001srk.4 uc001srk.5 uc001srk.6 Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation. Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Q9ULR3; Q9ULR3: PPM1H; NbExp=3; IntAct=EBI-8796752, EBI-8796752; Q9ULR3; P61026: RAB10; NbExp=4; IntAct=EBI-8796752, EBI-726075; Nucleus Cytoplasm May act as a suppressor of trastuzumab resistance. Belongs to the PP2C family. A report observed N-glycosylation at Asn-354 (PubMed:19139490). However, as the protein is not predicted to localize in an extracellular compartment of the cell, additional evidence is required to confirm this result. catalytic activity phosphoprotein phosphatase activity protein serine/threonine phosphatase activity magnesium-dependent protein serine/threonine phosphatase activity [pyruvate dehydrogenase (lipoamide)] phosphatase activity nucleus nucleoplasm cytoplasm mitochondrion protein dephosphorylation hydrolase activity synapse glutamatergic synapse positive regulation of pyruvate dehydrogenase activity uc001srk.1 uc001srk.2 uc001srk.3 uc001srk.4 uc001srk.5 uc001srk.6 
ENST00000228740.7 LTA4H ENST00000228740.7 leukotriene A4 hydrolase, transcript variant 10 (from RefSeq NR_182266.1) B4DNQ9 ENST00000228740.1 ENST00000228740.2 ENST00000228740.3 ENST00000228740.4 ENST00000228740.5 ENST00000228740.6 F8VV40 LKHA4_HUMAN LTA4 NR_182266 P09960 Q6IAT6 Q9UCT7 uc001ten.1 uc001ten.2 uc001ten.3 uc001ten.4 Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4) (PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, PubMed:1975494, PubMed:2244921). Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides (PubMed:20813919, PubMed:18804029). In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL) (PubMed:20813919, PubMed:24591641). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti- inflammatory and pro-resolving actions (PubMed:21206090). Reaction=H2O + leukotriene A4 = leukotriene B4; Xref=Rhea:RHEA:22324, ChEBI:CHEBI:15377, ChEBI:CHEBI:57461, ChEBI:CHEBI:57463; EC=3.3.2.6; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22325; Evidence=; Reaction=(5S,6S)-epoxy-(18R)-hydroxy-(7E,9E,11Z,14Z,16E)- eicosapentaenoate + H2O = resolvin E1; Xref=Rhea:RHEA:50272, ChEBI:CHEBI:15377, ChEBI:CHEBI:91000, ChEBI:CHEBI:132219; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50273; Evidence=; Reaction=(5S,6S)-epoxy-(18S)-hydroxy-(7E,9E,11Z,14Z,16E)- eicosapentaenoate + H2O = 18S-resolvin E1; Xref=Rhea:RHEA:51988, ChEBI:CHEBI:15377, ChEBI:CHEBI:134661, ChEBI:CHEBI:136057; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51989; Evidence=; Reaction=Release of the N-terminal residue from a tripeptide.; EC=3.4.11.4; Evidence= Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence= Note=Binds 1 zinc ion per subunit. Inhibited by bestatin (PubMed:11175901). The epoxide hydrolase activity is restrained by suicide inactivation that involves binding of LTA4 to Tyr-379 (PubMed:7667299). 4-(4- benzylphenyl)thiazol-2-amine (ARM1) selectively inhibits the epoxide hydrolase activity (PubMed:24591641). Kinetic parameters: KM=1.29 mM for Pro-Gly-Pro ; Lipid metabolism; leukotriene B4 biosynthesis. Monomer. P09960; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-721089, EBI-717399; Cytoplasm Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=L-LTA4; IsoId=P09960-1; Sequence=Displayed; Name=2; Synonyms=S-LTA4; IsoId=P09960-2; Sequence=VSP_041108, VSP_041109; Name=3; IsoId=P09960-3; Sequence=VSP_041107, VSP_041108, VSP_041109; Name=4; IsoId=P09960-4; Sequence=VSP_041107; Isoform 1 and isoform 2 are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts. Phosphorylation at Ser-416 inhibits leukotriene-A4 hydrolase activity. Belongs to the peptidase M1 family. RNA binding aminopeptidase activity epoxide hydrolase activity leukotriene-A4 hydrolase activity protein binding extracellular region nucleus nucleoplasm cytoplasm cytosol proteolysis leukotriene metabolic process peptidase activity metallopeptidase activity zinc ion binding hydrolase activity leukotriene biosynthetic process long-chain fatty acid biosynthetic process peptide catabolic process neutrophil degranulation cellular lipid metabolic process cellular protein metabolic process metal ion binding metalloaminopeptidase activity extracellular exosome tertiary granule lumen ficolin-1-rich granule lumen uc001ten.1 uc001ten.2 uc001ten.3 uc001ten.4 
ENST00000228741.8 ELK3 ENST00000228741.8 ETS transcription factor ELK3, transcript variant 12 (from RefSeq NR_182215.1) B2R6S6 ELK3_HUMAN ENST00000228741.1 ENST00000228741.2 ENST00000228741.3 ENST00000228741.4 ENST00000228741.5 ENST00000228741.6 ENST00000228741.7 NET NR_182215 P41970 Q6FG57 Q6GU29 Q9UD17 SAP2 uc001teo.1 uc001teo.2 uc001teo.3 May be a negative regulator of transcription, but can activate transcription when coexpressed with Ras, Src or Mos. Forms a ternary complex with the serum response factor and the ETS and SRF motifs of the Fos serum response element. Interacts with CTBP1. P41970; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-1758534, EBI-953896; P41970; P46108: CRK; NbExp=4; IntAct=EBI-1758534, EBI-886; P41970; Q13449: LSAMP; NbExp=3; IntAct=EBI-1758534, EBI-4314821; P41970; P16333: NCK1; NbExp=3; IntAct=EBI-1758534, EBI-389883; P41970; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-1758534, EBI-2811583; P41970; Q99471: PFDN5; NbExp=3; IntAct=EBI-1758534, EBI-357275; P41970; P27986: PIK3R1; NbExp=2; IntAct=EBI-1758534, EBI-79464; P41970; Q02446: SP4; NbExp=3; IntAct=EBI-1758534, EBI-10198587; Nucleus. Belongs to the ETS family. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding angiogenesis DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm mitochondrion regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter signal transduction cell differentiation purine-rich negative regulatory element binding wound healing sequence-specific DNA binding negative regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter uc001teo.1 uc001teo.2 uc001teo.3 
ENST00000228799.7 ITFG2 ENST00000228799.7 integrin alpha FG-GAP repeat containing 2, transcript variant 1 (from RefSeq NM_018463.4) A8K4Z5 D3DUQ2 ENST00000228799.1 ENST00000228799.2 ENST00000228799.3 ENST00000228799.4 ENST00000228799.5 ENST00000228799.6 ITFG2 ITFG2_HUMAN NM_018463 Q6PKU5 Q969R8 Q96SX6 uc001qlb.1 uc001qlb.2 uc001qlb.3 uc001qlb.4 As part of the KICSTOR complex functions in the amino acid- sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose. Part of the KICSTOR complex composed of KPTN, ITFG2, KICS2 and SZT2. SZT2 probably serves as a link between the other three proteins in the KICSTOR complex and may mediate the direct interaction with the GATOR complex via GATOR1. The KICSTOR complex interacts directly with the GATOR1 complex and most probably indirectly with the GATOR2 complex in an amino acid-independent manner. Lysosome membrane Note=Localization to lysosomes is amino acid-independent. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q969R8-1; Sequence=Displayed; Name=2; IsoId=Q969R8-2; Sequence=VSP_055985, VSP_055986; germinal center B cell differentiation nucleoplasm lysosome lysosomal membrane cytosol membrane cellular response to amino acid starvation cellular response to glucose starvation negative regulation of TORC1 signaling uc001qlb.1 uc001qlb.2 uc001qlb.3 uc001qlb.4 
ENST00000228811.8 PRR4 ENST00000228811.8 proline rich 4, transcript variant 2 (from RefSeq NM_007244.3) A8KA69 ENST00000228811.1 ENST00000228811.2 ENST00000228811.3 ENST00000228811.4 ENST00000228811.5 ENST00000228811.6 ENST00000228811.7 F5H0D7 LPRP NM_007244 PROL4 PROL4_HUMAN Q16378 Q8NFB3 uc001qyz.1 uc001qyz.2 uc001qyz.3 uc001qyz.4 uc001qyz.5 This gene encodes a member of the proline-rich protein family that lacks a conserved repetitive domain. This protein may play a role in protective functions in the eye. Alternative splicing result in multiple transcript variants. Read-through transcription also exists between this gene and the upstream PRH1 (proline-rich protein HaeIII subfamily 1) gene. [provided by RefSeq, Feb 2011]. Q16378; O43681: GET3; NbExp=3; IntAct=EBI-738624, EBI-2515857; Q16378; O43561-2: LAT; NbExp=3; IntAct=EBI-738624, EBI-8070286; Q16378; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-738624, EBI-740987; Q16378; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-738624, EBI-744081; Q16378; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-738624, EBI-741480; Q16378; Q9UHD9: UBQLN2; NbExp=6; IntAct=EBI-738624, EBI-947187; Secreted. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q16378-1; Sequence=Displayed; Name=2; IsoId=Q16378-2; Sequence=VSP_044635; Abundantly expressed in lacrimal gland where it is found in the acinar cells but not in the intralobular ducts. Also found in the submandibular gland, the parotid and sublingual glands. retina homeostasis extracellular region extracellular space visual perception uc001qyz.1 uc001qyz.2 uc001qyz.3 uc001qyz.4 uc001qyz.5 
ENST00000228820.9 PARP11 ENST00000228820.9 poly(ADP-ribose) polymerase family member 11, transcript variant 4 (from RefSeq NR_104461.2) B4DRQ0 C12orf6 ENST00000228820.1 ENST00000228820.2 ENST00000228820.3 ENST00000228820.4 ENST00000228820.5 ENST00000228820.6 ENST00000228820.7 ENST00000228820.8 F8WBZ7 NR_104461 PAR11_HUMAN PARP11 Q68DS1 Q8N5Y9 Q9NR21 uc001qml.1 uc001qml.2 uc001qml.3 uc001qml.4 uc001qml.5 Mono-ADP-ribosyltransferase that mediates mono-ADP- ribosylation of target proteins (PubMed:25043379, PubMed:25673562). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (By similarity). Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L- aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA- COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; Evidence=; Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP- D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA- COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540, ChEBI:CHEBI:140607; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56613; Evidence=; Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L- glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA- COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; Evidence=; Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L- lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA- COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:142515; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58221; Evidence=; Q9NR21-1; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-17644640, EBI-2340258; Q9NR21-1; Q969Y2: GTPBP3; NbExp=7; IntAct=EBI-17644640, EBI-740290; Q9NR21-1; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-17644640, EBI-10961706; Q9NR21-1; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-17644640, EBI-12039345; Q9NR21-1; Q969G2: LHX4; NbExp=3; IntAct=EBI-17644640, EBI-2865388; Q9NR21-5; P07550: ADRB2; NbExp=3; IntAct=EBI-17159452, EBI-491169; Q9NR21-5; P28329-3: CHAT; NbExp=3; IntAct=EBI-17159452, EBI-25837549; Q9NR21-5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-17159452, EBI-10976677; Q9NR21-5; P22607: FGFR3; NbExp=3; IntAct=EBI-17159452, EBI-348399; Q9NR21-5; Q14957: GRIN2C; NbExp=3; IntAct=EBI-17159452, EBI-8285963; Q9NR21-5; P28799: GRN; NbExp=3; IntAct=EBI-17159452, EBI-747754; Q9NR21-5; P06396: GSN; NbExp=3; IntAct=EBI-17159452, EBI-351506; Q9NR21-5; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-17159452, EBI-1055254; Q9NR21-5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-17159452, EBI-10975473; Q9NR21-5; O60260-5: PRKN; NbExp=3; IntAct=EBI-17159452, EBI-21251460; Q9NR21-5; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-17159452, EBI-396669; Q9NR21-5; P37840: SNCA; NbExp=3; IntAct=EBI-17159452, EBI-985879; Q9NR21-5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-17159452, EBI-5235340; Q9NR21-5; Q13148: TARDBP; NbExp=3; IntAct=EBI-17159452, EBI-372899; Q9NR21-5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-17159452, EBI-12806590; Q9NR21-5; Q9Y649; NbExp=3; IntAct=EBI-17159452, EBI-25900580; Nucleus, nuclear pore complex Note=Colocalizes with NUP153 at nuclear pores. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9NR21-4; Sequence=Displayed; Name=2; IsoId=Q9NR21-2; Sequence=VSP_059435, VSP_059437; Name=3; IsoId=Q9NR21-1; Sequence=VSP_059436; Name=4; IsoId=Q9NR21-5; Sequence=VSP_059438, VSP_059439; Auto-mono-ADP-ribosylated. [Isoform 4]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the ARTD/PARP family. Sequence=AAH17569.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH31073.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; NAD+ ADP-ribosyltransferase activity nucleus nuclear envelope nuclear pore nuclear envelope organization spermatogenesis protein transport transferase activity transferase activity, transferring glycosyl groups cell differentiation mRNA transport protein auto-ADP-ribosylation protein ADP-ribosylase activity uc001qml.1 uc001qml.2 uc001qml.3 uc001qml.4 uc001qml.5 
ENST00000228825.12 ARPC3 ENST00000228825.12 actin related protein 2/3 complex subunit 3, transcript variant 2 (from RefSeq NM_001287222.2) ARC21 ARPC3_HUMAN ENST00000228825.1 ENST00000228825.10 ENST00000228825.11 ENST00000228825.2 ENST00000228825.3 ENST00000228825.4 ENST00000228825.5 ENST00000228825.6 ENST00000228825.7 ENST00000228825.8 ENST00000228825.9 NM_001287222 O00554 O15145 uc001tqq.1 uc001tqq.2 uc001tqq.3 uc001tqq.4 uc001tqq.5 uc001tqq.6 This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been conserved through evolution and is implicated in the control of actin polymerization in cells. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Dec 2013]. Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. O15145; P59998: ARPC4; NbExp=4; IntAct=EBI-351829, EBI-351872; O15145; P46092: CCR10; NbExp=3; IntAct=EBI-351829, EBI-348022; O15145; Q68J44: DUSP29; NbExp=3; IntAct=EBI-351829, EBI-1054321; O15145; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-351829, EBI-8468186; O15145; Q08379: GOLGA2; NbExp=6; IntAct=EBI-351829, EBI-618309; O15145; O43365: HOXA3; NbExp=6; IntAct=EBI-351829, EBI-8643838; O15145; O95835-2: LATS1; NbExp=3; IntAct=EBI-351829, EBI-17978514; O15145; P48552: NRIP1; NbExp=3; IntAct=EBI-351829, EBI-746484; O15145; P14859-6: POU2F1; NbExp=3; IntAct=EBI-351829, EBI-11526590; O15145; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-351829, EBI-11322432; O15145; Q86VR2: RETREG3; NbExp=5; IntAct=EBI-351829, EBI-10192441; O15145; Q9NX95-5: SYBU; NbExp=3; IntAct=EBI-351829, EBI-12816095; O15145; A2RTX5: TARS3; NbExp=3; IntAct=EBI-351829, EBI-1056629; O15145; O00401: WASL; NbExp=6; IntAct=EBI-351829, EBI-957615; O15145; Q9H609: ZNF576; NbExp=3; IntAct=EBI-351829, EBI-3921014; O15145; P0DTC9: N; Xeno; NbExp=5; IntAct=EBI-351829, EBI-25475856; Cytoplasm, cytoskeleton Cell projection Nucleus Belongs to the ARPC3 family. actin binding structural constituent of cytoskeleton protein binding nucleus cytoplasm cytosol cytoskeleton Arp2/3 protein complex focal adhesion actin cytoskeleton membrane lamellipodium regulation of actin filament polymerization cell leading edge filamentous actin Arp2/3 complex-mediated actin nucleation site of double-strand break Fc-gamma receptor signaling pathway involved in phagocytosis cell projection ephrin receptor signaling pathway membrane organization extracellular exosome actin polymerization-dependent cell motility cellular response to nerve growth factor stimulus actin filament binding uc001tqq.1 uc001tqq.2 uc001tqq.3 uc001tqq.4 uc001tqq.5 uc001tqq.6 
ENST00000228827.8 GPN3 ENST00000228827.8 GPN-loop GTPase 3, transcript variant 1 (from RefSeq NM_016301.4) AD-009 ATPBD1C B2RC54 D4YWV1 ENST00000228827.1 ENST00000228827.2 ENST00000228827.3 ENST00000228827.4 ENST00000228827.5 ENST00000228827.6 ENST00000228827.7 F5H759 GPN3 GPN3_HUMAN NM_016301 Q53FS3 Q6UVZ6 Q7Z3D3 Q8NEI2 Q96HK9 Q9UHW5 UNQ1876/PRO4319 uc001tqr.1 uc001tqr.2 uc001tqr.3 uc001tqr.4 uc001tqr.5 Small GTPase required for proper localization of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. Heterodimer with GPN1 (PubMed:21768307). Binds to RNA polymerase II (RNAPII) (PubMed:20864038, PubMed:21768307). Interacts directly with subunits RPB4 and RPB7 and the CTD of RPB1 (PubMed:21768307). Q9UHW5; Q9HCN4: GPN1; NbExp=3; IntAct=EBI-395491, EBI-745137; Q9UHW5; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-395491, EBI-6115579; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9UHW5-1; Sequence=Displayed; Name=2; IsoId=Q9UHW5-2; Sequence=VSP_028125; Name=3; IsoId=Q9UHW5-3; Sequence=VSP_047327; Belongs to the GPN-loop GTPase family. Sequence=CAD97937.1; Type=Erroneous initiation; Evidence=; nucleotide binding GTPase activity protein binding GTP binding hydrolase activity macromolecular complex uc001tqr.1 uc001tqr.2 uc001tqr.3 uc001tqr.4 uc001tqr.5 
ENST00000228837.3 FGF6 ENST00000228837.3 fibroblast growth factor 6 (from RefSeq NM_020996.3) ENST00000228837.1 ENST00000228837.2 FGF6_HUMAN HST2 HSTF2 NM_020996 P10767 Q0VAE1 uc001qmr.1 uc001qmr.2 uc001qmr.3 The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This gene displayed oncogenic transforming activity when transfected into mammalian cells. The mouse homolog of this gene exhibits a restricted expression profile predominantly in the myogenic lineage, which suggested a role in muscle regeneration or differentiation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X63454.1, BC121097.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158800, SAMN03465413 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. Interacts with FGFR1, FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. P10767; P61601: NCALD; NbExp=3; IntAct=EBI-11479013, EBI-749635; Secreted, extracellular space. Leukemia cell lines with platelet/ megakaryocytic differentiation potential. Belongs to the heparin-binding growth factors family. Sequence=CAA40359.1; Type=Erroneous initiation; Evidence=; Sequence=CAA40360.1; Type=Erroneous initiation; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fgf6/"; MAPK cascade cartilage condensation angiogenesis extracellular region extracellular space multicellular organism development growth factor activity positive regulation of cell proliferation fibroblast growth factor receptor signaling pathway cell differentiation sarcolemma myoblast differentiation positive regulation of cell division positive regulation of protein kinase B signaling uc001qmr.1 uc001qmr.2 uc001qmr.3 
ENST00000228841.15 MYL2 ENST00000228841.15 myosin light chain 2, transcript variant 1 (from RefSeq NM_000432.4) ENST00000228841.1 ENST00000228841.10 ENST00000228841.11 ENST00000228841.12 ENST00000228841.13 ENST00000228841.14 ENST00000228841.2 ENST00000228841.3 ENST00000228841.4 ENST00000228841.5 ENST00000228841.6 ENST00000228841.7 ENST00000228841.8 ENST00000228841.9 MYL2 NM_000432 Q6IB42 Q6IB42_HUMAN hCG_40212 uc001try.1 uc001try.2 uc001try.3 uc001try.4 uc001try.5 uc001try.6 uc001try.7 Thus gene encodes the regulatory light chain associated with cardiac myosin beta (or slow) heavy chain. Ca+ triggers the phosphorylation of regulatory light chain that in turn triggers contraction. Mutations in this gene are associated with mid-left ventricular chamber type hypertrophic cardiomyopathy. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC031008.1, BU193625.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228841.15/ ENSP00000228841.8 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cytoplasm, myofibril, sarcomere, A band heart morphogenesis calcium ion binding heart development post-embryonic development myofibril muscle cell fate specification muscle fiber development cardiac myofibril assembly heart contraction cardiac muscle contraction positive regulation of the force of heart contraction uc001try.1 uc001try.2 uc001try.3 uc001try.4 uc001try.5 uc001try.6 uc001try.7 
ENST00000228850.6 AKAP3 ENST00000228850.6 A-kinase anchoring protein 3, transcript variant 1 (from RefSeq NM_001278309.2) ENST00000228850.1 ENST00000228850.2 ENST00000228850.3 ENST00000228850.4 ENST00000228850.5 HEL159 NM_001278309 V9HWD4 V9HWD4_HUMAN uc001qnb.1 uc001qnb.2 uc001qnb.3 uc001qnb.4 uc001qnb.5 uc001qnb.6 uc001qnb.7 This gene encodes a member of A-kinase anchoring proteins (AKAPs), a family of functionally related proteins that target protein kinase A to discrete locations within the cell. The encoded protein is reported to participate in protein-protein interactions with the R-subunit of the protein kinase A as well as sperm-associated proteins. This protein is expressed in spermatozoa and localized to the acrosomal region of the sperm head as well as the length of the principal piece. It may function as a regulator of motility, capacitation, and the acrosome reaction. [provided by RefSeq, May 2013]. Belongs to the AKAP110 family. acrosomal vesicle blastocyst hatching transmembrane receptor protein serine/threonine kinase signaling pathway protein localization motile cilium sperm fibrous sheath protein kinase A binding sperm principal piece uc001qnb.1 uc001qnb.2 uc001qnb.3 uc001qnb.4 uc001qnb.5 uc001qnb.6 uc001qnb.7 
ENST00000228865.3 CREBL2 ENST00000228865.3 cAMP responsive element binding protein like 2 (from RefSeq NM_001310.4) B5BUM5 CRBL2_HUMAN ENST00000228865.1 ENST00000228865.2 NM_001310 O60519 uc001rap.1 uc001rap.2 uc001rap.3 uc001rap.4 cAMP response element (CRE)-binding protein-like-2 (CREBL2) was identified in a search to find genes in a commonly deleted region on chromosome 12p13 flanked by ETV6 and CDKN1B genes, frequently associated with hematopoietic malignancies, as well as breast, non-small-cell lung and ovarian cancers. CREBL2 shares a 41% identity with CRE-binding protein (CREB) over a 48-base long region which encodes the bZip domain of CREB. The bZip domain consists of about 30 amino acids rich in basic residues involved in DNA binding, followed by a leucine zipper motif involved in protein dimerization. This suggests that CREBL2 encodes a protein with DNA binding capabilities. The occurance of CREBL2 deletion in malignancy suggests that CREBL2 may act as a tumor suppressor gene. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: BC106052.1, AF039081.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228865.3/ ENSP00000228865.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle. Identification in a chromosomal region frequently deleted in various cancers suggests that it might act as a tumor suppressor. Interacts with CREB1; regulates CREB1 phosphorylation, stability and transcriptional activity. O60519; Q8IUR6: CREBRF; NbExp=5; IntAct=EBI-2872455, EBI-1042699; O60519; P35638: DDIT3; NbExp=3; IntAct=EBI-2872455, EBI-742651; O60519; Q16236: NFE2L2; NbExp=5; IntAct=EBI-2872455, EBI-2007911; O60519; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-2872455, EBI-2692890; O60519; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2872455, EBI-10180829; Nucleus Phosphorylated by AMPK. Belongs to the bZIP family. ATF subfamily. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus transcription, DNA-templated regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter cell cycle signal transduction cell differentiation positive regulation of peptidyl-serine phosphorylation positive regulation of fat cell differentiation positive regulation of transcription, DNA-templated positive regulation of glucose import positive regulation of lipid biosynthetic process protein stabilization uc001rap.1 uc001rap.2 uc001rap.3 uc001rap.4 
ENST00000228872.9 CDKN1B ENST00000228872.9 cyclin dependent kinase inhibitor 1B (from RefSeq NM_004064.5) CDKN1B ENST00000228872.1 ENST00000228872.2 ENST00000228872.3 ENST00000228872.4 ENST00000228872.5 ENST00000228872.6 ENST00000228872.7 ENST00000228872.8 NM_004064 Q6I9V6 Q6I9V6_HUMAN hCG_27692 uc001rat.1 uc001rat.2 uc001rat.3 uc001rat.4 This gene encodes a cyclin-dependent kinase inhibitor, which shares a limited similarity with CDK inhibitor CDKN1A/p21. The encoded protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and thus controls the cell cycle progression at G1. The degradation of this protein, which is triggered by its CDK dependent phosphorylation and subsequent ubiquitination by SCF complexes, is required for the cellular transition from quiescence to the proliferative state. Mutations in this gene are associated with multiple endocrine neoplasia type IV (MEN4). [provided by RefSeq, Apr 2014]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC001971.1, AY004255.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228872.9/ ENSP00000228872.4 RefSeq Select criteria :: based on single protein-coding transcript regulatory uORF :: PMID: 12837699 ##RefSeq-Attributes-END## Cytoplasm Endosome Nucleus Belongs to the CDI family. G1/S transition of mitotic cell cycle response to hypoxia placenta development cyclin-dependent protein serine/threonine kinase inhibitor activity nucleus cytoplasm cytosol potassium ion transport cell cycle arrest regulation of exit from mitosis Notch signaling pathway heart development sensory perception of sound cell death positive regulation of cell proliferation negative regulation of cell proliferation response to glucose response to organic cyclic compound kinase activity phosphorylation cyclin binding Hsp70 protein binding positive regulation of microtubule polymerization response to estradiol macromolecular complex regulation of cell proliferation response to drug negative regulation of apoptotic process response to amino acid intracellular membrane-bounded organelle response to peptide hormone macromolecular complex binding negative regulation of cyclin-dependent protein serine/threonine kinase activity positive regulation of cyclin-dependent protein serine/threonine kinase activity response to cadmium ion inner ear development negative regulation of epithelial cell proliferation chaperone binding negative regulation of cellular component movement negative regulation of epithelial cell proliferation involved in prostate gland development cellular response to antibiotic cellular response to organic cyclic compound mitotic cell cycle arrest regulation of lens fiber cell differentiation negative regulation of cardiac muscle tissue regeneration uc001rat.1 uc001rat.2 uc001rat.3 uc001rat.4 
ENST00000228887.6 GPRC5D ENST00000228887.6 G protein-coupled receptor class C group 5 member D (from RefSeq NM_018654.2) ENST00000228887.1 ENST00000228887.2 ENST00000228887.3 ENST00000228887.4 ENST00000228887.5 GPC5D_HUMAN NM_018654 Q3KNV3 Q7Z5J9 Q8TDS6 Q9NZD1 uc010shp.1 uc010shp.2 uc010shp.3 The protein encoded by this gene is a member of the G protein-coupled receptor family; however, the specific function of this gene has not yet been determined. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: BC069341.1, AF209923.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2144120 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, longest protein ##RefSeq-Attributes-END## Q9NZD1; O95236-2: APOL3; NbExp=3; IntAct=EBI-13067820, EBI-11976321; Q9NZD1; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-13067820, EBI-8648738; Q9NZD1; P13236: CCL4; NbExp=3; IntAct=EBI-13067820, EBI-2873970; Q9NZD1; P54849: EMP1; NbExp=3; IntAct=EBI-13067820, EBI-4319440; Q9NZD1; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-13067820, EBI-10976398; Q9NZD1; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-13067820, EBI-12175685; Q9NZD1; P02724: GYPA; NbExp=3; IntAct=EBI-13067820, EBI-702665; Q9NZD1; Q01628: IFITM3; NbExp=3; IntAct=EBI-13067820, EBI-7932862; Q9NZD1; P24593: IGFBP5; NbExp=3; IntAct=EBI-13067820, EBI-720480; Q9NZD1; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-13067820, EBI-2820517; Q9NZD1; Q8N386: LRRC25; NbExp=3; IntAct=EBI-13067820, EBI-11304917; Q9NZD1; Q9H2W1: MS4A6A; NbExp=3; IntAct=EBI-13067820, EBI-1266965; Q9NZD1; Q8N912: NRAC; NbExp=3; IntAct=EBI-13067820, EBI-12051377; Q9NZD1; Q99650: OSMR; NbExp=3; IntAct=EBI-13067820, EBI-2804080; Q9NZD1; Q01453: PMP22; NbExp=3; IntAct=EBI-13067820, EBI-2845982; Q9NZD1; Q7Z6L0: PRRT2; NbExp=3; IntAct=EBI-13067820, EBI-722696; Q9NZD1; P15151: PVR; NbExp=3; IntAct=EBI-13067820, EBI-3919694; Q9NZD1; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-13067820, EBI-8644112; Q9NZD1; Q6ZP29-3: SLC66A1; NbExp=3; IntAct=EBI-13067820, EBI-12889586; Q9NZD1; Q9H7V2: SYNDIG1; NbExp=3; IntAct=EBI-13067820, EBI-726331; Q9NZD1; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-13067820, EBI-10171534; Q9NZD1; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-13067820, EBI-741829; Q9NZD1; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-13067820, EBI-12876824; Q9NZD1; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-13067820, EBI-8649725; Q9NZD1; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-13067820, EBI-11988865; Q9NZD1; Q9GZX9: TWSG1; NbExp=3; IntAct=EBI-13067820, EBI-10304067; Q9NZD1; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-13067820, EBI-4401271; Q9NZD1; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-13067820, EBI-7850136; Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NZD1-1; Sequence=Displayed; Name=2; IsoId=Q9NZD1-2; Sequence=VSP_010006, VSP_010007; Name=3; IsoId=Q9NZD1-3; Sequence=VSP_010008; Widely expressed in the peripheral system. Expression pattern is high in pancreas, medium in kidney, small intestine, spleen and testis, low in lung, colon, leukocyte, prostate and thymus and not detectable in brain, heart, liver, placenta, skeletal muscle and ovary. Belongs to the G-protein coupled receptor 3 family. G-protein coupled receptor activity plasma membrane signal transduction G-protein coupled receptor signaling pathway membrane integral component of membrane protein kinase activator activity activation of protein kinase activity intracellular membrane-bounded organelle receptor complex extracellular exosome uc010shp.1 uc010shp.2 uc010shp.3 
ENST00000228916.7 SCNN1A ENST00000228916.7 sodium channel epithelial 1 subunit alpha, transcript variant 1 (from RefSeq NM_001038.6) A5X2U9 B4E2Q5 C5HTZ0 ENST00000228916.1 ENST00000228916.2 ENST00000228916.3 ENST00000228916.4 ENST00000228916.5 ENST00000228916.6 NM_001038 O43271 P37088 Q6GSQ6 Q9UM64 SCNN1 SCNNA_HUMAN uc001qnx.1 uc001qnx.2 uc001qnx.3 uc001qnx.4 uc001qnx.5 Nonvoltage-gated, amiloride-sensitive, sodium channels control fluid and electrolyte transport across epithelia in many organs. These channels are heteromeric complexes consisting of 3 subunits: alpha, beta, and gamma. This gene encodes the alpha subunit, and mutations in this gene have been associated with pseudohypoaldosteronism type 1 (PHA1), a rare salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Apr 2009]. Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and eccrine sweat glands. Also plays a role in taste perception. Activated by WNK1, WNK2, WNK3 and WNK4. Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in some organisms and can replace the alpha/SCNN1A subunit to form an alternative channel with specific properties (By similarity). Interacts with NEDD4 (via WW domains) (PubMed:11244092, PubMed:11696533, PubMed:12167593, PubMed:23665454). Interacts with NEDD4L (via WW domains) (PubMed:11244092, PubMed:11696533). Interacts with WWP1 (via WW domains) (PubMed:9169421). Interacts with WWP2 (via WW domains) (PubMed:12167593, PubMed:9169421). Interacts with the full-length immature form of PCSK9 (pro-PCSK9) (PubMed:22493497). P37088; P46934: NEDD4; NbExp=3; IntAct=EBI-7845444, EBI-726944; P37088; P51170: SCNN1G; NbExp=3; IntAct=EBI-7845444, EBI-2547354; Apical cell membrane ; Multi-pass membrane protein Cell projection, cilium Cytoplasmic granule Cytoplasm Cytoplasmic vesicle, secretory vesicle, acrosome Cell projection, cilium, flagellum Note=In the oviduct and bronchus, located on cilia in multi-ciliated cells. In endometrial non-ciliated epithelial cells, restricted to apical surfaces. In epidermis, located nearly uniformly in the cytoplasm in a granular distribution (PubMed:28130590). In sebaceous glands, observed only in the cytoplasmic space in between the lipid vesicles (PubMed:28130590). In eccrine sweat glands, mainly located at the apical surface of the cells facing the lumen (PubMed:28130590). In skin, in arrector pili muscle cells and in adipocytes, located in the cytoplasm and colocalized with actin fibers (PubMed:28130590). In spermatogonia, spermatocytes and round spermatids, located in the cytoplasm (By similarity). Prior to spermiation, location shifts from the cytoplasm to the spermatid tail (By similarity). In spermatozoa, localizes at the acrosome and the central region of the sperm flagellum (By similarity). Event=Alternative splicing; Named isoforms=6; Name=1; Synonyms=Alpha ENAC1; IsoId=P37088-1; Sequence=Displayed; Name=2; Synonyms=Alpha ENAC2; IsoId=P37088-2; Sequence=VSP_007719; Name=3; Synonyms=Alpha ENACx; IsoId=P37088-3; Sequence=VSP_007720, VSP_007721; Name=4; Synonyms=Alpha ENAC-19; IsoId=P37088-4; Sequence=VSP_007722; Name=5; Synonyms=Alpha ENAC+22; IsoId=P37088-5; Sequence=VSP_007723; Name=6; IsoId=P37088-6; Sequence=VSP_043667; Expressed in the female reproductive tract, from the fimbrial end of the fallopian tube to the endometrium (at protein level) (PubMed:22207244). Expressed in kidney (at protein level). In the respiratory tract, expressed in the bronchial epithelium (at protein level). Highly expressed in lung. Detected at intermediate levels in pancreas and liver, and at low levels in heart and placenta (PubMed:22207244). in skin, expressed in keratinocytes, melanocytes and Merkel cells of the epidermal sub-layers, stratum basale, stratum spinosum and stratum granulosum (at protein level) (PubMed:28130590). Expressed in the outer root sheath of the hair follicles (at protein level) (PubMed:28130590). Detected in both peripheral and central cells of the sebaceous gland (at protein level) (PubMed:28130590). Expressed by eccrine sweat glands (at protein level) (PubMed:28130590). In skin, also expressed by arrector pili muscle cells and intradermal adipocytes (PubMed:28130590). Isoform 1 and isoform 2 predominate in all tissues. Expression of isoform 3, isoform 4 and isoform 5 is very low or not detectable, except in lung and heart (PubMed:9575806). By aldosterone. Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation. ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma subunit inhibitory tracts, respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects ENaC against proteolytic activation. N-glycosylated. Pseudohypoaldosteronism 1B1, autosomal recessive (PHA1B1) [MIM:264350]: A form of pseudohypoaldosteronism type 1, a rare salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. The disorder affects multiple organs, and is characterized by an often fulminant presentation in the neonatal period with dehydration, hyponatremia, hyperkalemia, metabolic acidosis, failure to thrive and weight loss. te=The disease is caused by variants affecting the gene represented in this entry. The degree of channel function impairment differentially affects the renin-aldosterone system and urinary Na/K ratios, resulting in distinct genotype-phenotype relationships in PHA1 patients. Loss-of- function mutations are associated with a severe clinical course and age-dependent hyperactivation of the renin-aldosterone system. This feature is not observed in patients with missense mutations that reduce but do not eliminate channel function. Markedly reduced channel activity results in impaired linear growth and delayed puberty (PubMed:18634878). Bronchiectasis with or without elevated sweat chloride 2 (BESC2) [MIM:613021]: A debilitating respiratory disease characterized by chronic, abnormal dilatation of the bronchi and other cystic fibrosis-like symptoms in the absence of known causes of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary dyskinesia, common variable immunodeficiency, foreign body obstruction). Clinical features include sub-normal lung function, sinopulmonary infections, chronic productive cough, excessive sputum production, and elevated sweat chloride in some cases. Note=The disease is caused by variants affecting the gene represented in this entry. Liddle syndrome 3 (LIDLS3) [MIM:618126]: A form of Liddle syndrome, an autosomal dominant disorder characterized by early onset of hypertension, hypokalemic alkalosis, and suppression of plasma renin activity and aldosterone secretion. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 3]: Does not give rise to amiloride-sensitive ion current. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. [Isoform 4]: Amiloride-sensitive ion current is nearly abolished. [Isoform 5]: Does not give rise to amiloride-sensitive ion current. Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1A subfamily. Sequence=AAH06526.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; acrosomal vesicle sodium channel activity protein binding cytoplasm plasma membrane integral component of plasma membrane cilium ion transport sodium ion transport ligand-gated sodium channel activity membrane integral component of membrane apical plasma membrane cytoplasmic vesicle motile cilium ion transmembrane transport sodium channel complex sodium ion transmembrane transport cell projection WW domain binding multicellular organismal water homeostasis response to stimulus sensory perception of taste sodium ion homeostasis ciliary membrane extracellular exosome sperm principal piece uc001qnx.1 uc001qnx.2 uc001qnx.3 uc001qnx.4 uc001qnx.5 
ENST00000228918.9 LTBR ENST00000228918.9 lymphotoxin beta receptor, transcript variant 16 (from RefSeq NR_182273.1) B7Z1D2 D12S370 D3DUR2 ENST00000228918.1 ENST00000228918.2 ENST00000228918.3 ENST00000228918.4 ENST00000228918.5 ENST00000228918.6 ENST00000228918.7 ENST00000228918.8 F5GXE7 NR_182273 P36941 TNFCR TNFR3 TNFRSF3 TNR3_HUMAN uc001qny.1 uc001qny.2 uc001qny.3 uc001qny.4 Receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3 and TRAF5. May play a role in the development of lymphoid organs. Self-associates. Associates with TRAF3, TRAF4 and TRAF5. (Microbial infection) Interacts with HCV core protein. P36941; Q08426: EHHADH; NbExp=3; IntAct=EBI-3509981, EBI-2339219; P36941; P36941: LTBR; NbExp=2; IntAct=EBI-3509981, EBI-3509981; P36941; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-3509981, EBI-712367; P36941; O43557: TNFSF14; NbExp=3; IntAct=EBI-3509981, EBI-524131; P36941; Q13114: TRAF3; NbExp=2; IntAct=EBI-3509981, EBI-357631; P36941; Q15326: ZMYND11; NbExp=5; IntAct=EBI-3509981, EBI-2623509; P36941; PRO_0000037666 [P29846]; Xeno; NbExp=5; IntAct=EBI-3509981, EBI-8847394; Membrane; Single-pass type I membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P36941-1; Sequence=Displayed; Name=2; IsoId=P36941-2; Sequence=VSP_047533; protein binding Golgi apparatus plasma membrane apoptotic process immune response signal transduction membrane integral component of membrane viral process ubiquitin protein ligase binding tumor necrosis factor-mediated signaling pathway identical protein binding myeloid dendritic cell differentiation positive regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of JNK cascade hematopoietic or lymphoid organ development cellular response to mechanical stimulus positive regulation of extrinsic apoptotic signaling pathway uc001qny.1 uc001qny.2 uc001qny.3 uc001qny.4 
ENST00000228922.12 OGFOD2 ENST00000228922.12 2-oxoglutarate and iron dependent oxygenase domain containing 2, transcript variant 1 (from RefSeq NM_001304833.2) B3KT24 ENST00000228922.1 ENST00000228922.10 ENST00000228922.11 ENST00000228922.2 ENST00000228922.3 ENST00000228922.4 ENST00000228922.5 ENST00000228922.6 ENST00000228922.7 ENST00000228922.8 ENST00000228922.9 NM_001304833 OGFD2_HUMAN Q4KN13 Q6N023 Q6N063 Q9H8K6 uc001uea.1 uc001uea.2 uc001uea.3 Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence=; Q6N063-2; P55212: CASP6; NbExp=3; IntAct=EBI-22006224, EBI-718729; Q6N063-2; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-22006224, EBI-745535; Q6N063-2; O00291: HIP1; NbExp=3; IntAct=EBI-22006224, EBI-473886; Q6N063-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-22006224, EBI-21591415; Q6N063-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-22006224, EBI-5280197; Q6N063-2; P62826: RAN; NbExp=3; IntAct=EBI-22006224, EBI-286642; Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q6N063-1; Sequence=Displayed; Name=2; IsoId=Q6N063-2; Sequence=VSP_025856, VSP_025857; Name=3; IsoId=Q6N063-3; Sequence=VSP_025858, VSP_025859; Name=4; IsoId=Q6N063-4; Sequence=VSP_025855; Belongs to the OGFOD2 family. Sequence=CAE45849.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence=; Sequence=CAE45849.1; Type=Frameshift; Evidence=; iron ion binding oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen L-ascorbic acid binding metal ion binding dioxygenase activity oxidation-reduction process uc001uea.1 uc001uea.2 uc001uea.3 
ENST00000228928.12 OAS3 ENST00000228928.12 2'-5'-oligoadenylate synthetase 3, transcript variant 1 (from RefSeq NM_006187.4) ENST00000228928.1 ENST00000228928.10 ENST00000228928.11 ENST00000228928.2 ENST00000228928.3 ENST00000228928.4 ENST00000228928.5 ENST00000228928.6 ENST00000228928.7 ENST00000228928.8 ENST00000228928.9 NM_006187 OAS3_HUMAN P/OKcl.4 Q2HJ14 Q9H3P5 Q9Y6K5 uc001tug.1 uc001tug.2 uc001tug.3 uc001tug.4 uc001tug.5 This gene encodes an enzyme included in the 2', 5' oligoadenylate synthase family. This enzyme is induced by interferons and catalyzes the 2', 5' oligomers of adenosine in order to bind and activate RNase L. This enzyme family plays a significant role in the inhibition of cellular protein synthesis and viral infection resistance. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB044545.1, AF063613.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228928.12/ ENSP00000228928.7 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV). Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')- adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Produced as a latent enzyme which is activated by dsRNA generated during the course of viral infection (Probable). Strongly activated by long dsRNAs at least 50 nucleotides in length (PubMed:25775560). ssRNA does not activate the enzyme (PubMed:25775560). Monomer. Q9Y6K5; Q7L2E3: DHX30; NbExp=2; IntAct=EBI-6115729, EBI-1211456; Q9Y6K5; P56537: EIF6; NbExp=2; IntAct=EBI-6115729, EBI-372243; Q9Y6K5; Q8IY81: FTSJ3; NbExp=2; IntAct=EBI-6115729, EBI-744088; Q9Y6K5; Q12894: IFRD2; NbExp=2; IntAct=EBI-6115729, EBI-2512448; Q9Y6K5; Q7Z434: MAVS; NbExp=2; IntAct=EBI-6115729, EBI-995373; Cytoplasm. Nucleus. Present at high level in placenta trophoblast. By type I interferon (IFN) and viruses. OAS domain 3 is catalytically active. OAS domain 1 has no catalytic activity but is essential for recognition of long dsRNAs. Belongs to the 2-5A synthase family. Sequence=AAD28543.1; Type=Frameshift; Evidence=; nucleotide binding 2'-5'-oligoadenylate synthetase activity immune system process RNA binding double-stranded RNA binding protein binding ATP binding extracellular space nucleus nucleoplasm cytoplasm cytosol plasma membrane nucleobase-containing compound metabolic process immune response response to virus transferase activity nucleotidyltransferase activity intracellular membrane-bounded organelle negative regulation of viral genome replication innate immune response metal ion binding defense response to virus interferon-gamma-mediated signaling pathway type I interferon signaling pathway regulation of ribonuclease activity uc001tug.1 uc001tug.2 uc001tug.3 uc001tug.4 uc001tug.5 
ENST00000228936.6 ART4 ENST00000228936.6 ADP-ribosyltransferase 4 (inactive) (Dombrock blood group), transcript variant 1 (from RefSeq NM_021071.4) DO DOK1 ENST00000228936.1 ENST00000228936.2 ENST00000228936.3 ENST00000228936.4 ENST00000228936.5 NAR4_HUMAN NM_021071 Q93070 Q9BZ50 Q9BZ51 Q9HB06 uc001rcl.1 uc001rcl.2 uc001rcl.3 uc001rcl.4 This gene encodes a protein that contains a mono-ADP-ribosylation (ART) motif. It is a member of the ADP-ribosyltransferase gene family but enzymatic activity has not been demonstrated experimentally. Antigens of the Dombrock blood group system are located on the gene product, which is glycosylphosphatidylinosotol-anchored to the erythrocyte membrane. Allelic variants, some of which lead to adverse transfusion reactions, are known. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK291662.1, AY829434.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA2142363 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000228936.6/ ENSP00000228936.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D- ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; EC=2.4.2.31; Cell membrane; Lipid-anchor, GPI-anchor. Expressed in spleen and T-cells. Variations in the ART4 gene are the basis of the Dombrock blood group system (Do). ART4 carries two antithetical antigens (Do(a) and Do(b)) and 3 high-incidence antigens, Gregory (Gy(a)), Holley (Hy), and Joseph (Jo(a)). Do(a) and Do(b) differ by a single variation at position 265, with Asn-265 corresponding to Do(a) and Asp-265 (shown in this entry) to Do(b). Belongs to the Arg-specific ADP-ribosyltransferase family. Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation database; URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=dombrock"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/do/"; NAD+ ADP-ribosyltransferase activity NAD(P)+-protein-arginine ADP-ribosyltransferase activity extracellular region plasma membrane protein ADP-ribosylation arginine metabolic process membrane transferase activity transferase activity, transferring glycosyl groups peptidyl-arginine ADP-ribosylation anchored component of membrane uc001rcl.1 uc001rcl.2 uc001rcl.3 uc001rcl.4 
ENST00000228945.9 ARHGDIB ENST00000228945.9 Rho GDP dissociation inhibitor beta, transcript variant 3 (from RefSeq NM_001321421.2) B5BU79 ENST00000228945.1 ENST00000228945.2 ENST00000228945.3 ENST00000228945.4 ENST00000228945.5 ENST00000228945.6 ENST00000228945.7 ENST00000228945.8 GDIA2 GDID4 GDIR2_HUMAN NM_001321421 P52566 RAP1GN1 uc001rcq.1 uc001rcq.2 uc001rcq.3 Members of the Rho (or ARH) protein family (see MIM 165390) and other Ras-related small GTP-binding proteins (see MIM 179520) are involved in diverse cellular events, including cell signaling, proliferation, cytoskeletal organization, and secretion. The GTP-binding proteins are active only in the GTP-bound state. At least 3 classes of proteins tightly regulate cycling between the GTP-bound and GDP-bound states: GTPase-activating proteins (GAPs), guanine nucleotide-releasing factors (GRFs), and GDP-dissociation inhibitors (GDIs). The GDIs, including ARHGDIB, decrease the rate of GDP dissociation from Ras-like GTPases (summary by Scherle et al., 1993 [PubMed 8356058]).[supplied by OMIM, Dec 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DRR138524.471636.1, SRR1163658.204622.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them (PubMed:8356058, PubMed:7512369). Regulates reorganization of the actin cytoskeleton mediated by Rho family members (PubMed:8262133). Interacts with RHOA (PubMed:20400958). Interacts with RAC1 (PubMed:7512369). Interacts with RAC2 (PubMed:10655614). Interacts with CDC42 (PubMed:7512369). P52566; P01100: FOS; NbExp=3; IntAct=EBI-2806617, EBI-852851; P52566; P62993: GRB2; NbExp=3; IntAct=EBI-2806617, EBI-401755; P52566; P31930: UQCRC1; NbExp=3; IntAct=EBI-2806617, EBI-1052596; Cytoplasm, cytosol Detected in bone marrow, thymus and spleen. Belongs to the Rho GDI family. GTPase activity Rho GDP-dissociation inhibitor activity GTPase activator activity protein binding cytoplasm cytosol cytoskeleton negative regulation of cell adhesion Rho protein signal transduction multicellular organism development membrane cytoplasmic vesicle regulation of Rho protein signal transduction positive regulation of GTPase activity Rac GTPase binding regulation of catalytic activity regulation of small GTPase mediated signal transduction extracellular exosome cellular response to redox state negative regulation of trophoblast cell migration regulation of actin cytoskeleton reorganization uc001rcq.1 uc001rcq.2 uc001rcq.3 
ENST00000229030.5 FZD10 ENST00000229030.5 frizzled class receptor 10 (from RefSeq NM_007197.4) ENST00000229030.1 ENST00000229030.2 ENST00000229030.3 ENST00000229030.4 FZD10_HUMAN NM_007197 Q9ULW2 uc001uii.1 uc001uii.2 uc001uii.3 uc001uii.4 uc001uii.5 This gene is a member of the frizzled gene family. Members of this family encode 7-transmembrane domain proteins that are receptors for the Wingless type MMTV integration site family of signaling proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway. Using array analysis, expression of this intronless gene is significantly up-regulated in two cases of primary colon cancer. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript is intronless :: BC070037.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor for Wnt proteins. Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). Interacts with WNT7B (By similarity). Interacts with MYOC (PubMed:19188438). Q9ULW2; O95273: CCNDBP1; NbExp=3; IntAct=EBI-8803802, EBI-748961; Q9ULW2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-8803802, EBI-3867333; Q9ULW2; Q9Y5L2: HILPDA; NbExp=2; IntAct=EBI-8803802, EBI-8803836; Q9ULW2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-8803802, EBI-11959885; Q9ULW2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8803802, EBI-10171774; Q9ULW2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-8803802, EBI-22310682; Q9ULW2; P07237: P4HB; NbExp=3; IntAct=EBI-8803802, EBI-395883; Cell membrane ; Multi-pass membrane protein Highest levels in the placenta and fetal kidney, followed by fetal lung and brain. In adult brain, abundantly expressed in the cerebellum, followed by cerebral cortex, medulla and spinal cord; very low levels in total brain, frontal lobe, temporal lobe and putamen. Weak expression detected in adult brain, heart, lung, skeletal muscle, pancreas, spleen and prostate. Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. The FZ domain is involved in binding with Wnt ligands. Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. Belongs to the G-protein coupled receptor Fz/Smo family. transmembrane signaling receptor activity G-protein coupled receptor activity protein binding nucleoplasm cytoplasm plasma membrane integral component of plasma membrane signal transduction cell surface receptor signaling pathway G-protein coupled receptor signaling pathway multicellular organism development cell surface membrane integral component of membrane Wnt signaling pathway Wnt-protein binding neuron differentiation regulation of actin cytoskeleton organization negative regulation of GTPase activity non-canonical Wnt signaling pathway non-canonical Wnt signaling pathway via JNK cascade Wnt-activated receptor activity positive regulation of JUN kinase activity positive regulation of GTPase activity canonical Wnt signaling pathway cellular response to retinoic acid uc001uii.1 uc001uii.2 uc001uii.3 uc001uii.4 uc001uii.5 
ENST00000229134.5 IL26 ENST00000229134.5 interleukin 26 (from RefSeq NM_018402.2) AK155 ENST00000229134.1 ENST00000229134.2 ENST00000229134.3 ENST00000229134.4 IL26_HUMAN NM_018402 Q9NPH9 uc001stx.1 uc001stx.2 uc001stx.3 This gene was identified by its overexpression specifically in herpesvirus samimiri-transformed T cells. The encoded protein is a member of the IL10 family of cytokines. It is a secreted protein and may function as a homodimer. This protein is thought to contribute to the transformed phenotype of T cells after infection by herpesvirus samimiri. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AJ251549.1, CF271979.2 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA2142586 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229134.5/ ENSP00000229134.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May play a role in local mechanisms of mucosal immunity and seems to have a pro-inflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin. Homodimer. Secreted Expressed in HVS transformed T-cells but not other T-cell lines or primary stimulated T-cells. Expressed in colonic T- cells including Th17 inflammatory T-cells; the expression is significantly increased in serum of patients with Crohn's disease (at protein level). By Herpesvirus saimiri infection. Belongs to the IL-10 family. Name=Wikipedia; Note=Interleukin-26 entry; URL="https://en.wikipedia.org/wiki/Interleukin_26"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/il26/"; cytokine activity extracellular region extracellular space cytosol cell-cell signaling cytokine-mediated signaling pathway positive regulation of stress-activated MAPK cascade positive regulation of transcription from RNA polymerase II promoter positive regulation of JAK-STAT cascade negative regulation of epithelial cell proliferation positive regulation of cytokine secretion positive regulation of protein kinase B signaling positive regulation of ERK1 and ERK2 cascade uc001stx.1 uc001stx.2 uc001stx.3 
ENST00000229135.4 IFNG ENST00000229135.4 interferon gamma (from RefSeq NM_000619.3) B5BU88 ENST00000229135.1 ENST00000229135.2 ENST00000229135.3 IFNG_HUMAN NM_000619 P01579 Q53ZV4 uc001stw.1 uc001stw.2 uc001stw.3 This gene encodes a soluble cytokine that is a member of the type II interferon class. The encoded protein is secreted by cells of both the innate and adaptive immune systems. The active protein is a homodimer that binds to the interferon gamma receptor which triggers a cellular response to viral and microbial infections. Mutations in this gene are associated with an increased susceptibility to viral, bacterial and parasitic infections and to several autoimmune diseases. [provided by RefSeq, Dec 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC070256.1, SRR1163655.241293.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2154529 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229135.4/ ENSP00000229135.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:16914093, PubMed:8666937). Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation (PubMed:8349687). Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription (PubMed:16914093). Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits (PubMed:8666937). In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading (PubMed:8163024). Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference (PubMed:11112687). Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (PubMed:7729559). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity). Homodimer (PubMed:1902591). Interacts with IFNGR1 (via extracellular domain); this interaction promotes IFNGR1 dimerization (PubMed:8349687). P01579; P15260: IFNGR1; NbExp=3; IntAct=EBI-1030767, EBI-1030755; P01579; Q66793: C4R; Xeno; NbExp=2; IntAct=EBI-1030767, EBI-15683787; Secreted. Released primarily from activated T lymphocytes. By cytokines, most notably interleukin IL-12, secreted by professional antigen-presenting cells such as monocytes/macrophages and dendritic cells. Proteolytic processing produces C-terminal heterogeneity, with proteins ending alternatively at Gly-150, Met-157 or Gly-161. Aplastic anemia (AA) [MIM:609135]: A form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. It is characterized by peripheral pancytopenia and marrow hypoplasia. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry. Immunodeficiency 69 (IMD69) [MIM:618963]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. IMD69 is an autosomal recessive disorder manifesting with fever, hepatosplenomegaly, leukocytosis, and thrombocytosis during the acute infection. Note=The disease is caused by variants affecting the gene represented in this entry. Available under the name Actimmune (Genentech). Used for reducing the frequency and severity of serious infections associated with chronic granulomatous disease (CGD). Belongs to the type II (or gamma) interferon family. Name=Wikipedia; Note=Interferon gamma entry; URL="https://en.wikipedia.org/wiki/Interferon_gamma"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ifng/"; negative regulation of transcription from RNA polymerase II promoter microglial cell activation positive regulation of protein phosphorylation adaptive immune response cytokine activity interferon-gamma receptor binding protein binding extracellular region extracellular space apoptotic process immune response humoral immune response cell cycle arrest cell surface receptor signaling pathway JAK-STAT cascade positive regulation of cell proliferation response to virus positive regulation of autophagy positive regulation of gene expression negative regulation of gene expression positive regulation of epithelial cell migration regulation of protein ADP-ribosylation positive regulation of receptor biosynthetic process negative regulation of epithelial cell differentiation positive regulation of protein complex assembly negative regulation of interleukin-17 production positive regulation of interleukin-12 production positive regulation of interleukin-23 production positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response positive regulation of peptidyl-serine phosphorylation of STAT protein positive regulation of smooth muscle cell apoptotic process interleukin-12-mediated signaling pathway regulation of growth positive regulation of protein import into nucleus positive regulation of tyrosine phosphorylation of STAT protein positive regulation of tumor necrosis factor biosynthetic process positive regulation of chemokine biosynthetic process positive regulation of MHC class II biosynthetic process positive regulation of nitric oxide biosynthetic process regulation of regulatory T cell differentiation positive regulation of osteoclast differentiation positive regulation of glycolytic process negative regulation of transcription, DNA-templated astrocyte activation negative regulation of smooth muscle cell proliferation positive regulation of interleukin-1 beta biosynthetic process positive regulation of phagocytosis positive regulation of neurogenesis regulation of insulin secretion positive regulation of membrane protein ectodomain proteolysis positive regulation of nitrogen compound metabolic process defense response to virus positive regulation of killing of cells of other organism positive regulation of nitric-oxide synthase biosynthetic process interferon-gamma-mediated signaling pathway regulation of interferon-gamma-mediated signaling pathway positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity positive regulation of fructose 1,6-bisphosphate metabolic process positive regulation of vitamin D biosynthetic process positive regulation of calcidiol 1-monooxygenase activity positive regulation of protein serine/threonine kinase activity positive regulation of protein deacetylation extrinsic apoptotic signaling pathway negative regulation of beta-amyloid clearance positive regulation of neuron death positive regulation of cellular respiration positive regulation of beta-amyloid formation negative regulation of tau-protein kinase activity positive regulation of protein localization to plasma membrane positive regulation of exosomal secretion positive regulation of ferrous iron import across plasma membrane positive regulation of tumor necrosis factor secretion positive regulation of NMDA glutamate receptor activity positive regulation of core promoter binding positive regulation of tumor necrosis factor (ligand) superfamily member 11 production uc001stw.1 uc001stw.2 uc001stw.3 
ENST00000229179.9 NUP107 ENST00000229179.9 nucleoporin 107, transcript variant 1 (from RefSeq NM_020401.4) B4DZ67 ENST00000229179.1 ENST00000229179.2 ENST00000229179.3 ENST00000229179.4 ENST00000229179.5 ENST00000229179.6 ENST00000229179.7 ENST00000229179.8 NM_020401 NU107_HUMAN P57740 Q6PJE1 uc001suf.1 uc001suf.2 uc001suf.3 uc001suf.4 uc001suf.5 This gene encodes a member of the nucleoporin family. The protein is localized to the nuclear rim and is an essential component of the nuclear pore complex (NPC). All molecules entering or leaving the nucleus either diffuse through or are actively transported by the NPC. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008]. Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:12552102, PubMed:15229283, PubMed:30179222). Required for the assembly of peripheral proteins into the NPC (PubMed:15229283, PubMed:12552102). May anchor NUP62 to the NPC (PubMed:15229283). Involved in nephrogenesis (PubMed:30179222). Part of the nuclear pore complex (NPC) (PubMed:11564755, PubMed:12802065, PubMed:15229283, PubMed:26411495). Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96; this complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus (PubMed:11564755, PubMed:11684705, PubMed:26411495, PubMed:30179222). Does not interact with TPR (PubMed:12802065). Interacts with ZNF106 (By similarity). P57740; Q8WUM0: NUP133; NbExp=14; IntAct=EBI-295687, EBI-295695; Nucleus membrane cleus, nuclear pore complex romosome, centromere, kinetochore Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755). Dissociates from the dissasembled NPC structure late during prophase of mitosis (PubMed:11564755). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P57740-1; Sequence=Displayed; Name=2; IsoId=P57740-2; Sequence=VSP_054263; Name=3; IsoId=P57740-3; Sequence=VSP_054262, VSP_054264; Ubiquitously expressed in fetal and adult tissues. Nephrotic syndrome 11 (NPHS11) [MIM:616730]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS11 is an autosomal recessive, steroid-resistant and progressive form with onset in the first decade of life. te=The disease is caused by variants affecting the gene represented in this entry. Ovarian dysgenesis 6 (ODG6) [MIM:618078]: A form of ovarian dysgenesis, a disorder characterized by lack of spontaneous pubertal development, primary amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism as a result of streak gonads. ODG6 is an autosomal recessive condition. Note=The disease may be caused by variants affecting the gene represented in this entry. Galloway-Mowat syndrome 7 (GAMOS7) [MIM:618348]: A form of Galloway-Mowat syndrome, a severe renal-neurological disease characterized by early-onset nephrotic syndrome associated with microcephaly, central nervous system abnormalities, developmental delays, and a propensity for seizures. Brain anomalies include gyration defects ranging from lissencephaly to pachygyria and polymicrogyria, and cerebellar hypoplasia. Most patients show facial dysmorphism characterized by a small, narrow forehead, large/floppy ears, deep-set eyes, hypertelorism and micrognathia. Additional variable features are visual impairment and arachnodactyly. Most patients die in early childhood. GAMOS7 inheritance is autosomal recessive. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the nucleoporin Nup84/Nup107 family. chromosome, centromeric region kinetochore condensed chromosome kinetochore posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery protein binding nucleus nuclear envelope nuclear pore chromosome cytosol regulation of glycolytic process mRNA export from nucleus tRNA export from nucleus protein import into nucleus female gonad development protein transport membrane viral process protein sumoylation structural constituent of nuclear pore viral transcription nuclear pore outer ring nuclear membrane nuclear periphery host cell mRNA transport nuclear pore complex assembly regulation of gene silencing by miRNA nephron development intracellular transport of virus regulation of cellular response to heat uc001suf.1 uc001suf.2 uc001suf.3 uc001suf.4 uc001suf.5 
ENST00000229195.8 CNOT2 ENST00000229195.8 CCR4-NOT transcription complex subunit 2, transcript variant 2 (from RefSeq NM_014515.7) CDC36 CNOT2_HUMAN ENST00000229195.1 ENST00000229195.2 ENST00000229195.3 ENST00000229195.4 ENST00000229195.5 ENST00000229195.6 ENST00000229195.7 HSPC131 MSTP046 NM_014515 NOT2 Q9H3E0 Q9NSX5 Q9NWR6 Q9NZN8 Q9P028 uc001svv.1 uc001svv.2 uc001svv.3 uc001svv.4 uc001svv.5 This gene encodes a subunit of the multi-component CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and degradation and is also thought to be involved in mRNA splicing, transport and localization. The encoded protein interacts with histone deacetylases and functions as a repressor of polymerase II transcription. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, Dec 2010]. Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4- NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specifically involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of embryonic stem (ES) cell identity. Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. In the complex interacts directly with CNOT3. Interacts with NCOR1, NCOR2. HDAC3 and GPS2. Q9NZN8; Q96C12: ARMC5; NbExp=3; IntAct=EBI-743033, EBI-6425121; Q9NZN8; P41182: BCL6; NbExp=3; IntAct=EBI-743033, EBI-765407; Q9NZN8; Q9HBH7: BEX1; NbExp=3; IntAct=EBI-743033, EBI-7162175; Q9NZN8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-743033, EBI-10175300; Q9NZN8; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-743033, EBI-718615; Q9NZN8; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-743033, EBI-12155483; Q9NZN8; A5YKK6: CNOT1; NbExp=5; IntAct=EBI-743033, EBI-1222758; Q9NZN8; O75175: CNOT3; NbExp=10; IntAct=EBI-743033, EBI-743073; Q9NZN8; Q96LI5: CNOT6L; NbExp=2; IntAct=EBI-743033, EBI-1046635; Q9NZN8; Q9UFF9: CNOT8; NbExp=3; IntAct=EBI-743033, EBI-742299; Q9NZN8; P33240: CSTF2; NbExp=3; IntAct=EBI-743033, EBI-711360; Q9NZN8; F2Z2M7: GALNT10; NbExp=3; IntAct=EBI-743033, EBI-23893155; Q9NZN8; Q8N6F7: GCSAM; NbExp=3; IntAct=EBI-743033, EBI-10267082; Q9NZN8; Q13098-7: GPS1; NbExp=3; IntAct=EBI-743033, EBI-10983983; Q9NZN8; O75031: HSF2BP; NbExp=3; IntAct=EBI-743033, EBI-7116203; Q9NZN8; Q9H019: MTFR1L; NbExp=3; IntAct=EBI-743033, EBI-2824497; Q9NZN8; P0CG20: PRR35; NbExp=3; IntAct=EBI-743033, EBI-11986293; Q9NZN8; P28070: PSMB4; NbExp=3; IntAct=EBI-743033, EBI-603350; Q9NZN8; P63244: RACK1; NbExp=3; IntAct=EBI-743033, EBI-296739; Q9NZN8; Q13207: TBX2; NbExp=3; IntAct=EBI-743033, EBI-2853051; Q9NZN8; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-743033, EBI-8644516; Q9NZN8; Q9HCJ0: TNRC6C; NbExp=4; IntAct=EBI-743033, EBI-6507625; Q9NZN8; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-743033, EBI-10237226; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q9NZN8-1; Sequence=Displayed; Name=2; IsoId=Q9NZN8-2; Sequence=VSP_009912; Name=3; IsoId=Q9NZN8-3; Sequence=VSP_009913; Name=4; IsoId=Q9NZN8-4; Sequence=VSP_009915, VSP_009916; Name=5; IsoId=Q9NZN8-5; Sequence=VSP_009914; Ubiquitous. Highly expressed in brain, heart, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocytes. Expressed in embryonic stem (ES) cells. Intellectual developmental disorder with nasal speech, dysmorphic facies, and variable skeletal anomalies (IDNADFS) [MIM:618608]: An autosomal dominant disorder characterized by delayed development, speech delay with nasal speech, and characteristic facial features including upslanted palpebral fissures, anteverted nares, a thin upper lip, and micrognathia. Some patients may have skeletal anomalies, such as brachydactyly, toe syndactyly and flat feet. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 3]: May be due to an intron retention. [Isoform 4]: May be due to an intron retention. Belongs to the CNOT2/3/5 family. Sequence=AAF29095.1; Type=Frameshift; Evidence=; Sequence=AAQ13426.1; Type=Frameshift; Evidence=; negative regulation of transcription from RNA polymerase II promoter nuclear-transcribed mRNA poly(A) tail shortening P-body RNA polymerase II transcription corepressor binding trophectodermal cell differentiation transcription cofactor activity protein binding nucleus cytoplasm cytosol plasma membrane regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter regulation of translation DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest multicellular organism development positive regulation of cytoplasmic mRNA processing body assembly membrane negative regulation of translation CCR4-NOT complex CCR4-NOT core complex gene silencing by RNA negative regulation of intracellular estrogen receptor signaling pathway RNA phosphodiester bond hydrolysis, exonucleolytic regulation of stem cell population maintenance poly(A)-specific ribonuclease activity uc001svv.1 uc001svv.2 uc001svv.3 uc001svv.4 uc001svv.5 
ENST00000229214.9 KRR1 ENST00000229214.9 KRR1 small subunit processome component homolog (from RefSeq NM_007043.7) A0FIK6 A0JLP0 B2R989 E7EUQ0 ENST00000229214.1 ENST00000229214.2 ENST00000229214.3 ENST00000229214.4 ENST00000229214.5 ENST00000229214.6 ENST00000229214.7 ENST00000229214.8 HRB2 KRR1 KRR1_HUMAN NM_007043 Q13601 Q8NEA8 Q8TC37 Q96AT5 uc001sxt.1 uc001sxt.2 uc001sxt.3 uc001sxt.4 uc001sxt.5 Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre- rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre- ribosomal RNA by the RNA exosome. Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. (Microbial infection) Directly interacts with HIV-1 protein VPR. Also identified in a complex with NR3C1 and HIV-1 protein VPR. Q13601; P62263: RPS14; NbExp=4; IntAct=EBI-744525, EBI-352783; Q13601; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-744525, EBI-539478; Q13601; Q9H171: ZBP1; NbExp=3; IntAct=EBI-744525, EBI-6264672; Nucleus, nucleolus Nucleus Cytoplasm Note=(Microbial infection) Translocates from cytoplasm to nucleus after exposure to HIV-1 virus or HIV-1 protein VPR or induction by hydrocortisone and dexamethasone in the absence of HIV-1 protein VPR. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13601-1; Sequence=Displayed; Name=2; IsoId=Q13601-2; Sequence=VSP_042223; Belongs to the KRR1 family. Sequence=AAB00557.1; Type=Frameshift; Evidence=; Sequence=AAH05225.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; nucleic acid binding RNA binding protein binding nucleus nucleoplasm nucleolus cytoplasm rRNA processing membrane small-subunit processome ribosome biogenesis intercellular bridge uc001sxt.1 uc001sxt.2 uc001sxt.3 uc001sxt.4 uc001sxt.5 
ENST00000229238.5 MRPL51 ENST00000229238.5 mitochondrial ribosomal protein L51 (from RefSeq NM_016497.4) CDA09 ENST00000229238.1 ENST00000229238.2 ENST00000229238.3 ENST00000229238.4 HSPC241 MRP64 NM_016497 Q4U2R6 Q96Q57 Q9BQ36 Q9P0N7 RM51_HUMAN uc001qom.1 uc001qom.2 uc001qom.3 uc001qom.4 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein. Pseudogenes corresponding to this gene are found on chromosomes 4p and 21q. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.458397.1, SRR1660805.184931.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000229238.5/ ENSP00000229238.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the mitochondrial large ribosomal subunit (mt- LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins (PubMed:25278503, PubMed:25838379). Interacts with OXA1L (By similarity). Mitochondrion Belongs to the mitochondrion-specific ribosomal protein mL51 family. structural constituent of ribosome protein binding mitochondrion mitochondrial inner membrane mitochondrial ribosome mitochondrial large ribosomal subunit ribosome translation mitochondrial translation mitochondrial translational elongation mitochondrial translational termination uc001qom.1 uc001qom.2 uc001qom.3 uc001qom.4 
ENST00000229239.10 GAPDH ENST00000229239.10 glyceraldehyde-3-phosphate dehydrogenase, transcript variant 6 (from RefSeq NR_152150.2) ENST00000229239.1 ENST00000229239.2 ENST00000229239.3 ENST00000229239.4 ENST00000229239.5 ENST00000229239.6 ENST00000229239.7 ENST00000229239.8 ENST00000229239.9 HEL-S-162eP NR_152150 V9HVZ4 V9HVZ4_HUMAN uc001qop.1 uc001qop.2 uc001qop.3 uc001qop.4 uc001qop.5 This gene encodes a member of the glyceraldehyde-3-phosphate dehydrogenase protein family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. The product of this gene catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The encoded protein has additionally been identified to have uracil DNA glycosylase activity in the nucleus. Also, this protein contains a peptide that has antimicrobial activity against E. coli, P. aeruginosa, and C. albicans. Studies of a similar protein in mouse have assigned a variety of additional functions including nitrosylation of nuclear proteins, the regulation of mRNA stability, and acting as a transferrin receptor on the cell surface of macrophage. Many pseudogenes similar to this locus are present in the human genome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2014]. Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3- phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence= Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L- cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089, Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950, ChEBI:CHEBI:149494; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; Evidence=; Carbohydrate degradation; glycolysis; pyruvate from D- glyceraldehyde 3-phosphate: step 1/5. Homotetramer. Cytoplasm, cytoskeleton Cytoplasm, cytosol Nucleus Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. nucleotide binding glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity cytosol plasma membrane glucose metabolic process glycolytic process oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor nuclear membrane intracellular membrane-bounded organelle NADP binding NAD binding oxidation-reduction process uc001qop.1 uc001qop.2 uc001qop.3 uc001qop.4 uc001qop.5 
ENST00000229243.7 ACRBP ENST00000229243.7 acrosin binding protein (from RefSeq NM_032489.3) ACRBP ACRBP_HUMAN ENST00000229243.1 ENST00000229243.2 ENST00000229243.3 ENST00000229243.4 ENST00000229243.5 ENST00000229243.6 NM_032489 Q8NEB7 Q9BY87 uc001qpu.1 uc001qpu.2 uc001qpu.3 The protein encoded by this gene is similar to proacrosin binding protein sp32 precursor found in mouse, guinea pig, and pig. This protein is located in the sperm acrosome and is thought to function as a binding protein to proacrosin for packaging and condensation of the acrosin zymogen in the acrosomal matrix. This protein is a member of the cancer/testis family of antigens and it is found to be immunogenic. In normal tissues, this mRNA is expressed only in testis, whereas it is detected in a range of different tumor types such as bladder, breast, lung, liver, and colon. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR5189667.225875.1, SRR5189667.186649.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229243.7/ ENSP00000229243.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## [Acrosin-binding protein, mature form]: Acrosomal protein that maintains proacrosin (pro-ACR) as an enzymatically inactive zymogen in the acrosome. Involved also in the acrosome formation. [Acrosin-binding protein, mature form]: Binds proacrosin (pro- ACR). Does not bind the mature form of ACR. Secreted Cytoplasmic vesicle, secretory vesicle, acrosome Expression restricted to testis in normal tissue. Expressed in a wide spectrum of cancers, including bladder, breast, liver, lung and colon cancers. Phosphorylated on Tyr residues in capacitated sperm. The N-terminus is blocked. Synthesized as a 60-kDa precursor, the 32-kDa mature form is post- translationally produced by the removal of the N-terminal half of the precursor during sperm maturation in the testis and/or epididymis. acrosomal vesicle acrosome assembly acrosomal membrane molecular_function extracellular region nucleus spermatid development biological_process fertilization cytoplasmic vesicle uc001qpu.1 uc001qpu.2 uc001qpu.3 
ENST00000229264.8 GNB3 ENST00000229264.8 G protein subunit beta 3, transcript variant 1 (from RefSeq NM_002075.4) ENST00000229264.1 ENST00000229264.2 ENST00000229264.3 ENST00000229264.4 ENST00000229264.5 ENST00000229264.6 ENST00000229264.7 GBB3_HUMAN NM_002075 P16520 Q96B71 Q9BQC0 uc001qrd.1 uc001qrd.2 uc001qrd.3 uc001qrd.4 Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit which belongs to the WD repeat G protein beta family. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. A single-nucleotide polymorphism (C825T) in this gene is associated with essential hypertension and obesity. This polymorphism is also associated with the occurrence of the splice variant GNB3-s, which appears to have increased activity. GNB3-s is an example of alternative splicing caused by a nucleotide change outside of the splice donor and acceptor sites. Alternative splicing results in multiple transcript variants. Additional alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known. [provided by RefSeq, Jul 2014]. Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. G proteins are composed of 3 units, alpha, beta and gamma. Interacts with RASD2. P16520; P32302: CXCR5; NbExp=3; IntAct=EBI-2880663, EBI-2835269; P16520-2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-17871073, EBI-7062247; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P16520-1; Sequence=Displayed; Name=2; IsoId=P16520-2; Sequence=VSP_055233; Night blindness, congenital stationary, 1H (CSNB1H) [MIM:617024]: A form of congenital stationary night blindness, a non- progressive retinal disorder characterized by impaired night vision or in dim light, with good vision only on bright days. CSNB1H patients present with childhood-onset night blindness and middle age-onset photophobia, but have near-normal vision and do not exhibit nystagmus or high myopia. CSNB1H inheritance is autosomal recessive. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the WD repeat G protein beta family. GTPase activity protein binding cytosol plasma membrane protein folding cell volume homeostasis signal transduction G-protein coupled receptor signaling pathway regulation of blood pressure regulation of gene expression regulation of glucose metabolic process dendrite spectrin binding regulation of hormone metabolic process neuron projection cell body regulation of fat cell differentiation GTPase binding extracellular exosome regulation of cholesterol metabolic process regulation of triglyceride metabolic process regulation of phospholipid metabolic process regulation of feeding behavior regulation of locomotion involved in locomotory behavior uc001qrd.1 uc001qrd.2 uc001qrd.3 uc001qrd.4 
ENST00000229266.8 CHPT1 ENST00000229266.8 choline phosphotransferase 1 (from RefSeq NM_020244.3) B3KQM2 CHPT1 CHPT1_HUMAN CPT1 ENST00000229266.1 ENST00000229266.2 ENST00000229266.3 ENST00000229266.4 ENST00000229266.5 ENST00000229266.6 ENST00000229266.7 MSTP022 NM_020244 Q7Z7H0 Q7Z7H1 Q7Z7H2 Q8IWQ4 Q8IWQ5 Q8WUD6 Q8WYI4 Q9NRQ6 Q9NRQ7 Q9Y6M6 uc001tin.1 uc001tin.2 uc001tin.3 uc001tin.4 uc001tin.5 Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producing a PC. It thereby plays a central role in the formation and maintenance of vesicular membranes. Reaction=a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn- glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940; Evidence=; Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + CDP-choline = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn- glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54344, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:74965, ChEBI:CHEBI:75728; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54345; Evidence=; Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-choline = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54244, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:73001, ChEBI:CHEBI:75466; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245; Evidence=; Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- glycerol + CDP-choline = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z- docosahexaenoyl)-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54332, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:74963, ChEBI:CHEBI:82949; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333; Evidence=; Reaction=1,2-dioctanoyl-sn-glycerol + CDP-choline = 1,2-dioctanoyl-sn- glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54232, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:76979, ChEBI:CHEBI:78228; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54233; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2. Q8WUD6; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-11337856, EBI-12947623; Golgi apparatus membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Alpha; IsoId=Q8WUD6-1; Sequence=Displayed; Name=2; Synonyms=Beta; IsoId=Q8WUD6-2; Sequence=VSP_025989, VSP_025990; Highly expressed in testis, colon, small intestine, heart, prostate and spleen. Also detected in kidney, skeletal muscle, pancreas, leukocytes, ovary and thymus. Weakly expressed in the brain, placenta and lung. Overexpressed in cancerous breast epithelial cell lines. Belongs to the CDP-alcohol phosphatidyltransferase class-I family. Sequence=AAD44019.1; Type=Frameshift; Evidence=; Sequence=AAL39005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Golgi membrane regulation of cell growth diacylglycerol cholinephosphotransferase activity endoplasmic reticulum membrane Golgi apparatus lipid metabolic process phosphatidylcholine biosynthetic process CDP-choline pathway platelet activating factor biosynthetic process phospholipid biosynthetic process membrane integral component of membrane transferase activity phosphotransferase activity, for other substituted phosphate groups diacylglycerol binding intracellular membrane-bounded organelle metal ion binding uc001tin.1 uc001tin.2 uc001tin.3 uc001tin.4 uc001tin.5 
ENST00000229268.13 USP5 ENST00000229268.13 ubiquitin specific peptidase 5, transcript variant 12 (from RefSeq NR_168455.1) D3DUS7 D3DUS8 ENST00000229268.1 ENST00000229268.10 ENST00000229268.11 ENST00000229268.12 ENST00000229268.2 ENST00000229268.3 ENST00000229268.4 ENST00000229268.5 ENST00000229268.6 ENST00000229268.7 ENST00000229268.8 ENST00000229268.9 ISOT NR_168455 P45974 Q96J22 UBP5_HUMAN uc001qri.1 uc001qri.2 uc001qri.3 uc001qri.4 uc001qri.5 uc001qri.6 Ubiquitin (see MIM 191339)-dependent proteolysis is a complex pathway of protein metabolism implicated in such diverse cellular functions as maintenance of chromatin structure, receptor function, and degradation of abnormal proteins. A late step of the process involves disassembly of the polyubiquitin chains on degraded proteins into ubiquitin monomers. USP5 disassembles branched polyubiquitin chains by a sequential exo mechanism, starting at the proximal end of the chain (Wilkinson et al., 1995 [PubMed 7578059]).[supplied by OMIM, Mar 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys- 48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Interacts with TRIML1. P45974; Q15038: DAZAP2; NbExp=3; IntAct=EBI-741277, EBI-724310; P45974; P54727: RAD23B; NbExp=2; IntAct=EBI-741277, EBI-954531; P45974; O75528: TADA3; NbExp=2; IntAct=EBI-741277, EBI-473249; P45974; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-741277, EBI-9675724; P45974-2; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-12072186, EBI-723313; P45974-2; Q8N0X7: SPART; NbExp=3; IntAct=EBI-12072186, EBI-2643803; P45974-2; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-12072186, EBI-11528917; P45974-2; O14773: TPP1; NbExp=3; IntAct=EBI-12072186, EBI-2800203; P45974-2; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-12072186, EBI-2340370; P45974-2; P0CG47: UBB; NbExp=3; IntAct=EBI-12072186, EBI-413034; Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=P45974-1; Sequence=Displayed; Name=Short; IsoId=P45974-2; Sequence=VSP_005259; The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition. The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer. Belongs to the peptidase C19 family. cysteine-type endopeptidase activity thiol-dependent ubiquitin-specific protease activity protein binding lysosome cytosol proteolysis ubiquitin-dependent protein catabolic process peptidase activity cysteine-type peptidase activity zinc ion binding protein ubiquitination protein deubiquitination hydrolase activity positive regulation of proteasomal ubiquitin-dependent protein catabolic process thiol-dependent ubiquitinyl hydrolase activity ubiquitin binding metal ion binding protein K48-linked deubiquitination uc001qri.1 uc001qri.2 uc001qri.3 uc001qri.4 uc001qri.5 uc001qri.6 
ENST00000229277.6 ENO2 ENST00000229277.6 enolase 2 (from RefSeq NM_001975.3) ENO2 ENST00000229277.1 ENST00000229277.2 ENST00000229277.3 ENST00000229277.4 ENST00000229277.5 HEL-S-279 NM_001975 Q6FHV6 Q6FHV6_HUMAN hCG_25937 uc001qru.1 uc001qru.2 This gene encodes one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in mature neurons and cells of neuronal origin. A switch from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803613.161086.1, SRR3476690.1104951.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229277.6/ ENSP00000229277.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Carbohydrate degradation; glycolysis; pyruvate from D- glyceraldehyde 3-phosphate: step 4/5. Belongs to the enolase family. phosphopyruvate hydratase complex magnesium ion binding photoreceptor inner segment phosphopyruvate hydratase activity protein binding cytoplasm cytosol plasma membrane glycolytic process neuronal cell body perikaryon uc001qru.1 uc001qru.2 
ENST00000229281.6 C12orf57 ENST00000229281.6 chromosome 12 open reading frame 57, transcript variant 1 (from RefSeq NM_138425.4) B2R4Q6 C10 C10_HUMAN ENST00000229281.1 ENST00000229281.2 ENST00000229281.3 ENST00000229281.4 ENST00000229281.5 NM_138425 Q99622 uc001qrz.1 uc001qrz.2 uc001qrz.3 uc001qrz.4 uc001qrz.5 This gene is ubiquitously expressed in human tissues. It is required for development of the human corpus callosum. Mutations in this gene are associated with Temtamy syndrome (TEMTYS). Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Sep 2014]. In brain, may be required for corpus callosum development. Q99622; Q8NFD2: ANKK1; NbExp=3; IntAct=EBI-2808472, EBI-13280688; Q99622; P51460: INSL3; NbExp=3; IntAct=EBI-2808472, EBI-12919766; Cytoplasm Ubiquitously expressed, with higher expression in lung and fetal brain. Temtamy syndrome (TEMTYS) [MIM:218340]: An autosomal recessive syndrome characterized by intellectual disability, variable craniofacial dysmorphism, ocular coloboma, seizures, and brain abnormalities, including abnormalities of the corpus callosum and thalamus. te=The disease is caused by variants affecting the gene represented in this entry. A variant resulting in a GUG start codon may be able to produce some protein because of a consensus Kozak sequence, although less efficiently than the wild type. This would explain the phenotypic variability observed. Belongs to the UPF0456 family. molecular_function cytoplasm post-embryonic development regulation of skeletal muscle contraction nuclear speck corpus callosum morphogenesis third ventricle development psychomotor behavior camera-type eye morphogenesis cognition uc001qrz.1 uc001qrz.2 uc001qrz.3 uc001qrz.4 uc001qrz.5 
ENST00000229304.5 APOBEC1 ENST00000229304.5 apolipoprotein B mRNA editing enzyme catalytic subunit 1, transcript variant 3 (from RefSeq NM_005889.4) ABEC1_HUMAN APOBEC1 ENST00000229304.1 ENST00000229304.2 ENST00000229304.3 ENST00000229304.4 NM_005889 P41238 Q9UE64 Q9UM71 uc001qtb.1 uc001qtb.2 uc001qtb.3 uc001qtb.4 uc001qtb.5 This gene encodes a member of the cytidine deaminase enzyme family. The encoded protein forms a multiple-protein editing holoenzyme with APOBEC1 complementation factor (ACF) and APOBEC1 stimulating protein (ASP). This holoenzyme is involved in the editing of C-to-U nucleotide bases in apolipoprotein B and neurofibromatosis-1 mRNAs. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2015]. Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs (PubMed:30844405). Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the apolipoprotein B mRNA (PubMed:24916387). Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA (PubMed:11727199). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (By similarity). Reaction=a cytidine in mRNA + H(+) + H2O = a uridine in mRNA + NH4(+); Xref=Rhea:RHEA:74355, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:15145, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:65315, ChEBI:CHEBI:82748; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74356; Evidence=; Reaction=cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) + uridine(6666) in apoB mRNA; Xref=Rhea:RHEA:21772, Rhea:RHEA- COMP:13888, Rhea:RHEA-COMP:13889, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:65315, ChEBI:CHEBI:82748; EC=3.5.4.36; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21773; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 Zn(2+) ion per subunit. ; Homodimer (PubMed:8078915). Interacts with A1CF; form an mRNA editing complex (PubMed:30844405). Interacts with RBM47; form an mRNA editing complex (PubMed:24916387, PubMed:30844405). Found in a complex with CELF2/CUGBP2 and A1CF. Interacts with HNRPAB (PubMed:8999813). Interacts with SYNCRIP (PubMed:11352648). P41238; Q00534: CDK6; NbExp=3; IntAct=EBI-12819523, EBI-295663; P41238; P52597: HNRNPF; NbExp=3; IntAct=EBI-12819523, EBI-352986; P41238; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-12819523, EBI-7060731; P41238; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-12819523, EBI-1048945; P41238; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-12819523, EBI-12111050; P41238; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12819523, EBI-11962084; P41238; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-12819523, EBI-17490746; P41238; Q9NUQ7: UFSP2; NbExp=3; IntAct=EBI-12819523, EBI-11153325; Cytoplasm Nucleus Expressed exclusively in the small intestine. Belongs to the cytidine and deoxycytidylate deaminase family. RNA binding mRNA binding catalytic activity cytidine deaminase activity cytosine deaminase activity protein binding nucleus nucleoplasm cytoplasm RNA processing mRNA processing lipid metabolic process triglyceride metabolic process response to osmotic stress enzyme activator activity zinc ion binding cytidine deamination response to zinc ion response to gamma radiation cytidine to uridine editing mRNA modification hydrolase activity protein domain specific binding cellular response to insulin stimulus mRNA 3'-UTR AU-rich region binding regulation of cell proliferation lipoprotein metabolic process lipoprotein biosynthetic process response to drug lipoprotein transport ribonucleoprotein complex binding positive regulation of catalytic activity response to ethanol metal ion binding mRNA stabilization response to calcium ion defense response to virus DNA cytosine deamination DNA demethylation negative regulation of triglyceride metabolic process negative regulation of methylation-dependent chromatin silencing positive regulation of mRNA modification uc001qtb.1 uc001qtb.2 uc001qtb.3 uc001qtb.4 uc001qtb.5 
ENST00000229307.9 NANOG ENST00000229307.9 Nanog homeobox, transcript variant 1 (from RefSeq NM_024865.4) D3DUU4 ENST00000229307.1 ENST00000229307.2 ENST00000229307.3 ENST00000229307.4 ENST00000229307.5 ENST00000229307.6 ENST00000229307.7 ENST00000229307.8 NANOG_HUMAN NM_024865 Q2TTG0 Q6JZS5 Q9H9S0 uc009zfy.1 uc009zfy.2 uc009zfy.3 The protein encoded by this gene is a DNA binding homeobox transcription factor involved in embryonic stem (ES) cell proliferation, renewal, and pluripotency. The encoded protein can block ES cell differentiation and can also autorepress its own expression in differentiating cells. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2015]. Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]- 3'. Binds to the POU5F1/OCT4 promoter (PubMed:25825768). Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation. Interacts with SMAD1 (By similarity). Interacts with SALL4 (By similarity). Interacts with ZNF281/ZFP281 (By similarity). Interacts with PCGF1 (PubMed:26687479). Interacts with ESRRB; reciprocally modulates their transcriptional activities (By similarity). Interacts with NSD2 (By similarity). Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H9S0-1; Sequence=Displayed; Name=2; Synonyms=Nanog-delta 48; IsoId=Q9H9S0-2; Sequence=VSP_021688; Expressed in testicular carcinoma and derived germ cell tumors (at protein level). Expressed in fetal gonads, ovary and testis. Also expressed in ovary teratocarcinoma cell line and testicular embryonic carcinoma. Not expressed in many somatic organs and oocytes. Expressed in embryonic stem (ES) and carcinoma (EC) cells. Expressed in inner cell mass (ICM) of the blastocyst and gonocytes between 14 and 19 weeks of gestation (at protein level). Not expressed in oocytes, unfertilized oocytes, 2-16 cell embryos and early morula (at protein level). Expressed in embryonic stem cells (ES). Expression decreases with ES differentiation. Exists an other tandem duplicated non-processed pseudogene (NANOGP1) and 10 other NANOG-related nucleotide sequences located on different chromosomes, all of which are processed pseudogenes lacking introns (NANOGP2 to NANOGP11); except NANOGP8 which is a retrogene. Belongs to the Nanog homeobox family. Name=Wikipedia; Note=Nanog entry; URL="https://en.wikipedia.org/wiki/Nanog"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/46540/NANOG"; nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding endodermal cell fate specification DNA binding transcription factor activity, sequence-specific DNA binding transcription corepressor activity protein binding nucleus nucleoplasm nucleolus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development regulation of gene expression cytokine-mediated signaling pathway stem cell population maintenance cell differentiation somatic stem cell population maintenance sequence-specific DNA binding transcription regulatory region DNA binding regulation of cell differentiation positive regulation of transcription from RNA polymerase II promoter negative regulation of nucleic acid-templated transcription positive regulation of stem cell proliferation uc009zfy.1 uc009zfy.2 uc009zfy.3 
ENST00000229314.10 GOLT1B ENST00000229314.10 golgi transport 1B (from RefSeq NM_016072.5) B2R4R4 CGI-141 ENST00000229314.1 ENST00000229314.2 ENST00000229314.3 ENST00000229314.4 ENST00000229314.5 ENST00000229314.6 ENST00000229314.7 ENST00000229314.8 ENST00000229314.9 GCT2 GOT1A GOT1B_HUMAN HDCMA39P NM_016072 Q54A40 Q6I9W6 Q9P1R9 Q9Y3E0 UNQ432/PRO793 uc001rez.1 uc001rez.2 uc001rez.3 uc001rez.4 May be involved in fusion of ER-derived transport vesicles with the Golgi complex. Q9Y3E0; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-4402607, EBI-6942903; Q9Y3E0; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-4402607, EBI-13345167; Q9Y3E0; Q9BT40: INPP5K; NbExp=3; IntAct=EBI-4402607, EBI-749162; Q9Y3E0; P15941-11: MUC1; NbExp=3; IntAct=EBI-4402607, EBI-17263240; Q9Y3E0; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-4402607, EBI-3920694; Q9Y3E0; O00560: SDCBP; NbExp=3; IntAct=EBI-4402607, EBI-727004; Q9Y3E0; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-4402607, EBI-6503765; Q9Y3E0; Q6UWV7: SHISAL2A; NbExp=3; IntAct=EBI-4402607, EBI-18396772; Q9Y3E0; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-4402607, EBI-18159983; Q9Y3E0; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-4402607, EBI-742688; Golgi apparatus membrane ; Multi-pass membrane protein Widely expressed. Tends to be up-regulated in seminomas compared to normal testis. Belongs to the GOT1 family. Sequence=AAF65181.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Golgi membrane endoplasmic reticulum Golgi apparatus protein transport membrane integral component of membrane vesicle-mediated transport macromolecular complex positive regulation of I-kappaB kinase/NF-kappaB signaling uc001rez.1 uc001rez.2 uc001rez.3 uc001rez.4 
ENST00000229328.10 PRKAB1 ENST00000229328.10 protein kinase AMP-activated non-catalytic subunit beta 1 (from RefSeq NM_006253.5) AAKB1_HUMAN AMPK ENST00000229328.1 ENST00000229328.2 ENST00000229328.3 ENST00000229328.4 ENST00000229328.5 ENST00000229328.6 ENST00000229328.7 ENST00000229328.8 ENST00000229328.9 NM_006253 Q9UBV0 Q9UE20 Q9UEX2 Q9Y478 Q9Y6V8 uc001txg.1 uc001txg.2 uc001txg.3 uc001txg.4 uc001txg.5 The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC017671.1, AF022116.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229328.10/ ENSP00000229328.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C- terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3). AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2. Q9Y478; P62993: GRB2; NbExp=2; IntAct=EBI-719769, EBI-401755; Q9Y478; Q13131: PRKAA1; NbExp=9; IntAct=EBI-719769, EBI-1181405; Q9Y478; P54646: PRKAA2; NbExp=8; IntAct=EBI-719769, EBI-1383852; Q9Y478; P54619: PRKAG1; NbExp=12; IntAct=EBI-719769, EBI-1181439; Q9Y478; O75385: ULK1; NbExp=3; IntAct=EBI-719769, EBI-908831; Q9Y478; O70302: Cidea; Xeno; NbExp=4; IntAct=EBI-719769, EBI-7927848; The glycogen-binding domain may target AMPK to glycogen so that other factors like glycogen-bound debranching enzyme or protein phosphatases can directly affect AMPK activity. Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Belongs to the 5'-AMP-activated protein kinase beta subunit family. Sequence=AAB71326.1; Type=Erroneous gene model prediction; Evidence=; Sequence=AAC98897.1; Type=Frameshift; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44100/PRKAB1"; protein kinase activity AMP-activated protein kinase activity protein binding nucleus nucleoplasm cytoplasm cytosol protein phosphorylation lipid metabolic process fatty acid metabolic process fatty acid biosynthetic process cell cycle arrest signal transduction positive regulation of gene expression macroautophagy regulation of macroautophagy protein kinase binding nucleotide-activated protein kinase complex macromolecular complex nail development regulation of catalytic activity protein heterooligomerization regulation of signal transduction by p53 class mediator uc001txg.1 uc001txg.2 uc001txg.3 uc001txg.4 uc001txg.5 
ENST00000229329.7 CMAS ENST00000229329.7 cytidine monophosphate N-acetylneuraminic acid synthetase, transcript variant 1 (from RefSeq NM_018686.6) ENST00000229329.1 ENST00000229329.2 ENST00000229329.3 ENST00000229329.4 ENST00000229329.5 ENST00000229329.6 NEUA_HUMAN NM_018686 Q8NFW8 Q96AX5 Q9NQZ0 uc001rfm.1 uc001rfm.2 uc001rfm.3 uc001rfm.4 uc001rfm.5 uc001rfm.6 This gene encodes an enzyme that converts N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc). This process is important in the formation of sialylated glycoprotein and glycolipids. This modification plays a role in cell-cell communications and immune responses. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]. Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D- glycero-D-galacto-nononic acid (KDN). Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate + diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43; Evidence=; Amino-sugar metabolism; N-acetylneuraminate metabolism. Homotetramer; the active enzyme is formed by a dimer of dimers. Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8NFW8-1; Sequence=Displayed; Name=2; IsoId=Q8NFW8-2; Sequence=VSP_012764; Ubiquitously expressed. Expressed in pancreas, kidney, liver, skeletal muscle, lung, placenta, brain, heart, colon, PBL, small intestine, ovary, testis, prostate, thymus and spleen. The BC2 (basic cluster 2) motif is necessary and sufficient for the nuclear localization and contains the catalytic active site. The localization in the nucleus is however not required for the enzyme activity (By similarity). Belongs to the CMP-NeuNAc synthase family. nucleus nucleoplasm N-acetylneuraminate metabolic process N-acylneuraminate cytidylyltransferase activity membrane transferase activity nucleotidyltransferase activity uc001rfm.1 uc001rfm.2 uc001rfm.3 uc001rfm.4 uc001rfm.5 uc001rfm.6 
ENST00000229330.9 HCFC2 ENST00000229330.9 host cell factor C2 (from RefSeq NM_013320.3) B2R8Q5 C0H5X3 ENST00000229330.1 ENST00000229330.2 ENST00000229330.3 ENST00000229330.4 ENST00000229330.5 ENST00000229330.6 ENST00000229330.7 ENST00000229330.8 HCFC2_HUMAN NM_013320 Q9Y5Z7 uc001tkj.1 uc001tkj.2 uc001tkj.3 uc001tkj.4 uc001tkj.5 uc001tkj.6 This gene encodes one of two proteins which interact with VP16, a herpes simplex virus protein that initiates virus infection. Both the encoded protein and the original Herpes host cell factor interact with VP16 through a beta-propeller domain. The original Herpes host cell factor, however, is effective at initiating viral infection while the encoded protein is not. Transcripts of varying length due to alternative polyadenylation signals have been described. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.206310.1, SRR1660803.229480.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229330.9/ ENSP00000229330.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Binds KMT2A/MLL1. Component of the MLL1/MLL complex, at least composed of KMT2A/MLL1, ASH2L, RBBP5, DPY30, WDR5, MEN1, HCFC1 and HCFC2 (PubMed:15199122). Interacts with TASOR (By similarity). Q9Y5Z7; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-592728, EBI-744342; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y5Z7-1; Sequence=Displayed; Name=2; IsoId=Q9Y5Z7-2; Sequence=VSP_057024, VSP_057025; Highly expressed in testis. Detected at lower levels in spleen, thymus, prostate, ovary, small intestine and colon. negative regulation of transcription from RNA polymerase II promoter transcription coactivator activity protein binding nucleus nucleoplasm cytoplasm cytosol plasma membrane regulation of transcription from RNA polymerase II promoter viral process MLL1 complex positive regulation of nucleic acid-templated transcription uc001tkj.1 uc001tkj.2 uc001tkj.3 uc001tkj.4 uc001tkj.5 uc001tkj.6 
ENST00000229332.12 CLEC4A ENST00000229332.12 C-type lectin domain family 4 member A, transcript variant 1 (from RefSeq NM_016184.4) CLC4A_HUMAN CLEC4A CLECSF6 DCIR ENST00000229332.1 ENST00000229332.10 ENST00000229332.11 ENST00000229332.2 ENST00000229332.3 ENST00000229332.4 ENST00000229332.5 ENST00000229332.6 ENST00000229332.7 ENST00000229332.8 ENST00000229332.9 HDCGC13P LLIR NM_016184 Q17R69 Q8WXW9 Q9H2Z9 Q9NS33 Q9UI34 Q9UMR7 uc001qtz.1 uc001qtz.2 This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions, such as cell adhesion, cell-cell signalling, glycoprotein turnover, and roles in inflammation and immune response. The encoded type 2 transmembrane protein may play a role in inflammatory and immune response. Multiple transcript variants encoding distinct isoforms have been identified for this gene. This gene is closely linked to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. [provided by RefSeq, Jul 2008]. C-type lectin receptor that binds carbohydrates mannose and fucose but also weakly interacts with N-acetylglucosamine (GlcNAc) in a Ca(2+)-dependent manner (PubMed:27015765). Involved in regulating immune reactivity (PubMed:18258799, PubMed:10438934). Once triggered by antigen, it is internalized by clathrin-dependent endocytosis and delivers its antigenic cargo into the antigen presentation pathway resulting in cross-priming of CD8(+) T cells. This cross-presentation and cross-priming are enhanced by TLR7 and TLR8 agonists with increased expansion of the CD8(+) T cells, high production of IFNG and TNF with reduced levels of IL4, IL5 and IL13 (PubMed:18258799, PubMed:20530286). In plasmacytoid dendritic cells, inhibits TLR9-mediated IFNA and TNF production (PubMed:18258799). May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation (PubMed:10438934). (Microbial infection) Involved in the interaction between HIV-1 virus and dendritic cells. Enhances HIV-1 binding/entry and virus infection. Requires ITIM motif-associated signal transduction pathway involving phosphatases PTPN6 and PTPN11, SYK, Src kinases and MAP kinases. May interact with PTPN6 via its ITIM motif. Cell membrane ; Single-pass type II membrane protein ; Extracellular side Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9UMR7-1; Sequence=Displayed; Name=2; IsoId=Q9UMR7-2; Sequence=VSP_012844; Name=3; Synonyms=llirV1; IsoId=Q9UMR7-3; Sequence=VSP_041348; Name=4; Synonyms=llirV2; IsoId=Q9UMR7-4; Sequence=VSP_012842; Expressed preferentially in hematopoietic tissues. Expressed in all circulating Ag-presenting cells such as dendritic cells, myeloid cells, monocytes, macrophages, B-cells and epidermal Langerhans cells (at protein level). Expressed in peripheral blood leukocytes, neutrophils, moderate quantities in spleen, lymph node, and bone marrow, and at very low levels in thymus. TNF alpha, IL-1 alpha, and LPS, down-regulated expression at the surface of neutrophils (at protein level) (PubMed:11994513). Expression is decreased in dendritic cells by signals inducing their maturation (e.g. CD40 ligand, TLR9 ligands, LPS, and TNF alpha) (PubMed:10438934, PubMed:18258799). Isoform 2: mRNA expression is up- regulated by agonists of neutrophils CSF2/GM-CSF, IL3/interleukin-3, IL4/interleukin-4 and IL13/interleukin-13 (PubMed:11994513). Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases (PubMed:20530286). Involved in the interaction between HIV-1 virus and dendritic cells. Enhances HIV-1 binding/entry and virus infection. Requires ITIM motif-associated signal transduction pathway involving phosphatases PTPN6 and PTPN11, SYK, Src kinases and MAP kinases (PubMed:20530286). ITIM motif-associated signal transduction pathway involving phosphatases PTPN6 and PTPN11, SYK, Src kinases and MAP kinases is required for HIV-1 binding/entry and virus infection (PubMed:20530286). Sequence=AAL56016.1; Type=Frameshift; Evidence=; Name=Functional Glycomics Gateway - Glycan Binding; Note=DCIR; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00137"; negative regulation of cytokine production stimulatory C-type lectin receptor signaling pathway adaptive immune response immune system process plasmacytoid dendritic cell antigen processing and presentation transmembrane signaling receptor activity calcium ion binding mannose binding plasma membrane integral component of plasma membrane cell adhesion cell surface receptor signaling pathway membrane integral component of membrane carbohydrate binding negative regulation of tumor necrosis factor production CD8-positive, alpha-beta T cell activation antigen processing and presentation of exogenous peptide antigen via MHC class I innate immune response metal ion binding uc001qtz.1 uc001qtz.2 
ENST00000229335.11 AICDA ENST00000229335.11 activation induced cytidine deaminase, transcript variant 1 (from RefSeq NM_020661.4) AICDA_HUMAN AID ENST00000229335.1 ENST00000229335.10 ENST00000229335.2 ENST00000229335.3 ENST00000229335.4 ENST00000229335.5 ENST00000229335.6 ENST00000229335.7 ENST00000229335.8 ENST00000229335.9 NM_020661 Q6QJ81 Q8NFC1 Q9GZX7 uc001qur.1 uc001qur.2 uc001qur.3 uc001qur.4 This gene encodes a RNA-editing deaminase that is a member of the cytidine deaminase family. AICDA is specifically expressed and active in germinal center-like B cells. In the germinal center, AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination of immunoglobulin genes. An epigenetic role in neoplastic transformation and lymphoma progression has been experimentally ascribed to AICDA using mouse models. Defects in this gene are the cause of autosomal recessive hyper-IgM immunodeficiency syndrome type 2 (HIGM2). [provided by RefSeq, Jul 2020]. Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses (PubMed:18722174, PubMed:21385873, PubMed:21518874, PubMed:27716525). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (PubMed:21496894). Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'- deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948, Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452, ChEBI:CHEBI:133902; EC=3.5.4.38; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Interacts with CTNNBL1; the interaction is important for the immunoglobulin switch activity of AICDA (PubMed:18722174, PubMed:21385873, PubMed:32484799). Interacts (via its NLS) with KPNA1. Interacts with PKA/PRKACA and PRKAR1A/PKR1 (PubMed:16387847). Interacts with TRIM28 and NCL (By similarity). Interacts with SUPT6H (PubMed:21518874). Interacts with RNF126 (PubMed:23277564). Directly interacts with MCM3AP; this interaction may favor AICDA recruitment to immunoglobulin variable region genes, hence promoting somatic hypermutations (PubMed:20507984). Q9GZX7; Q9GZX7: AICDA; NbExp=2; IntAct=EBI-3834328, EBI-3834328; Q9GZX7; P31689: DNAJA1; NbExp=6; IntAct=EBI-3834328, EBI-347834; Q9GZX7; O60884: DNAJA2; NbExp=3; IntAct=EBI-3834328, EBI-352957; Q9GZX7; P24522: GADD45A; NbExp=5; IntAct=EBI-3834328, EBI-448167; Q9GZX7; P11142: HSPA8; NbExp=2; IntAct=EBI-3834328, EBI-351896; Q9GZX7; P52294: KPNA1; NbExp=2; IntAct=EBI-3834328, EBI-358383; Q9GZX7; O00505: KPNA3; NbExp=2; IntAct=EBI-3834328, EBI-358297; Q9GZX7; O15131: KPNA5; NbExp=2; IntAct=EBI-3834328, EBI-540602; Q9GZX7; P17612: PRKACA; NbExp=3; IntAct=EBI-3834328, EBI-476586; Q9GZX7; P10644: PRKAR1A; NbExp=5; IntAct=EBI-3834328, EBI-476431; Q9GZX7; Q13569: TDG; NbExp=5; IntAct=EBI-3834328, EBI-348333; Q9GZX7; Q784Z8: C; Xeno; NbExp=2; IntAct=EBI-3834328, EBI-11666471; Nucleus toplasm, cytosol Note=Predominantly cytosolic (PubMed:21385873). In the presence of MCM3AP/GANP, relocalizes to the nucleus (By similarity). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9GZX7-1; Sequence=Displayed; Name=2; IsoId=Q9GZX7-2; Sequence=VSP_047803; Strongly expressed in lymph nodes and tonsils. Negatively regulated by microRNA-155 (miR-155). Ser-38 is the major site whereas Thr-27 is the minor site of phosphorylation. Phosphorylation regulates its class-switch recombination activity. Probably monoubiquitinated on several residues by RNF126. Immunodeficiency with hyper-IgM 2 (HIGM2) [MIM:605258]: A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the cytidine and deoxycytidylate deaminase family. Name=AICDAbase; Note=AICDA mutation db; URL="http://structure.bmc.lu.se/idbase/AICDAbase/"; P-body RNA binding catalytic activity cytidine deaminase activity protein binding nucleus cytoplasm mRNA processing zinc ion binding cytidine deamination negative regulation of transposition somatic diversification of immunoglobulins somatic hypermutation of immunoglobulin genes cytidine to uridine editing hydrolase activity B cell differentiation ubiquitin protein ligase binding macromolecular complex regulation of nuclear cell cycle DNA replication defense response to bacterium identical protein binding isotype switching negative regulation of single stranded viral RNA replication via double stranded DNA intermediate metal ion binding deoxycytidine deaminase activity defense response to virus DNA cytosine deamination cellular response to lipopolysaccharide DNA demethylation negative regulation of methylation-dependent chromatin silencing uc001qur.1 uc001qur.2 uc001qur.3 uc001qur.4 
ENST00000229340.10 RAB35 ENST00000229340.10 RAB35, member RAS oncogene family, transcript variant 1 (from RefSeq NM_006861.7) B2R6E0 B4E390 ENST00000229340.1 ENST00000229340.2 ENST00000229340.3 ENST00000229340.4 ENST00000229340.5 ENST00000229340.6 ENST00000229340.7 ENST00000229340.8 ENST00000229340.9 NM_006861 Q15286 RAB1C RAB35_HUMAN RAY uc001txm.1 uc001txm.2 uc001txm.3 The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP) (PubMed:20154091). That Rab is activated by the guanine exchange factors DENND1A, DENND1B and DENND1C (PubMed:20154091). Interacts with DENND1A and DENND1B; in a nucleotide-dependent manner (PubMed:20154091, PubMed:22065758). Interacts with DENND1C; weak interaction which is nucleotide-independent (PubMed:20154091). Interacts (GTP-bound form) with ACAP2 and MICALL1; the interaction is direct and probably recruits ACAP2 and MICALL1 to membranes (PubMed:21951725). Interacts with EHD1; the interaction is indirect through MICALL1 and probably recruits EHD1 to membranes (By similarity). Interacts with GDI1, GDI2, CHM and CHML; phosphorylation at Thr-72 disrupts these interactions (PubMed:29125462). Q15286; P50570-2: DNM2; NbExp=3; IntAct=EBI-722275, EBI-10968534; Q15286; P42858: HTT; NbExp=3; IntAct=EBI-722275, EBI-466029; Q15286; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-722275, EBI-1055254; Q15286; Q8N3F8: MICALL1; NbExp=2; IntAct=EBI-722275, EBI-1056885; Cell membrane ipid-anchor ; Cytoplasmic side Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Endosome Melanosome Note=Present on sorting endosomes and recycling endosome tubules (PubMed:16950109). Tends to be enriched in PIP2-positive cell membrane domains (PubMed:16950109). During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis (PubMed:16950109). Identified in stage I to stage IV melanosomes (PubMed:17081065). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q15286-1; Sequence=Displayed; Name=2; IsoId=Q15286-2; Sequence=VSP_042918; AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB35 constitutively active. Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and GTP- bound forms can be phosphocholinated. Phosphocholination inhibits the GEF activity of DENND1A. Belongs to the small GTPase superfamily. Rab family. nucleotide binding mitotic cytokinesis GTPase activity protein binding GTP binding phosphatidylinositol-4,5-bisphosphate binding endosome cytosol plasma membrane clathrin-coated pit intracellular protein transport protein localization endosome membrane protein transport membrane endosomal transport GDP binding antigen processing and presentation clathrin-coated vesicle clathrin-coated vesicle membrane neuron projection development cell projection membrane cytoplasmic vesicle endocytic recycling Rab protein signal transduction protein localization to endosome melanosome intercellular bridge clathrin-coated endocytic vesicle plasma membrane to endosome transport recycling endosome membrane extracellular exosome anchored component of synaptic vesicle membrane cellular response to nerve growth factor stimulus uc001txm.1 uc001txm.2 uc001txm.3 
ENST00000229379.3 COX6A1 ENST00000229379.3 cytochrome c oxidase subunit 6A1 (from RefSeq NM_004373.4) B2R500 COX6AL CX6A1_HUMAN ENST00000229379.1 ENST00000229379.2 NM_004373 O43714 P12074 Q32Q37 uc001tyf.1 uc001tyf.2 uc001tyf.3 Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in the electron transfer and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes polypeptide 1 (liver isoform) of subunit VIa, and polypeptide 1 is found in all non-muscle tissues. Polypeptide 2 (heart/muscle isoform) of subunit VIa is encoded by a different gene, and is present only in striated muscles. These two polypeptides share 66% amino acid sequence identity. It has been reported that there may be several pseudogenes on chromosomes 1, 6, 7q21, 7q31-32 and 12. However, only one pseudogene (COX6A1P) on chromosome 1p31.1 has been documented. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AV716665.1, SRR1163657.341458.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000229379.3/ ENSP00000229379.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Energy metabolism; oxidative phosphorylation. Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 14 subunits. The complex is composed of a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or COX4I2), COX5A, COX5B, COX6A1 (or COX6A2), COX6B1 (or COX6B2), COX6C, COX7A2 (or COX7A1), COX7B, COX7C, COX8A and NDUFA4, which are encoded in the nuclear genome (PubMed:30030519). The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in different assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:28844695). P12074; P42858: HTT; NbExp=4; IntAct=EBI-2115950, EBI-466029; P12074; Q9BS40: LXN; NbExp=3; IntAct=EBI-2115950, EBI-1044504; Mitochondrion inner membrane ; Single-pass membrane protein Charcot-Marie-Tooth disease, recessive intermediate D (CMTRID) [MIM:616039]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie- Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the cytochrome c oxidase subunit 6A family. Sequence=CAA33392.1; Type=Frameshift; Evidence=; cytochrome-c oxidase activity mitochondrion mitochondrial inner membrane mitochondrial respiratory chain complex IV generation of precursor metabolites and energy mitochondrial electron transport, cytochrome c to oxygen aerobic respiration membrane enzyme regulator activity regulation of catalytic activity hydrogen ion transmembrane transport uc001tyf.1 uc001tyf.2 uc001tyf.3 
ENST00000229390.8 SRSF9 ENST00000229390.8 serine and arginine rich splicing factor 9 (from RefSeq NM_003769.3) ENST00000229390.1 ENST00000229390.2 ENST00000229390.3 ENST00000229390.4 ENST00000229390.5 ENST00000229390.6 ENST00000229390.7 NM_003769 Q13242 Q52LD1 SFRS9 SRP30C SRSF9_HUMAN uc001tyi.1 uc001tyi.2 uc001tyi.3 uc001tyi.4 uc001tyi.5 The protein encoded by this gene is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Each of these factors contains an RNA recognition motif (RRM) for binding RNA and an RS domain for binding other proteins. The RS domain is rich in serine and arginine residues and facilitates interaction between different SR splicing factors. In addition to being critical for mRNA splicing, the SR proteins have also been shown to be involved in mRNA export from the nucleus and in translation. Two pseudogenes, one on chromosome 15 and the other on chromosome 21, have been found for this gene. [provided by RefSeq, Sep 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.125813.1, SRR1163655.38947.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2142680 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229390.8/ ENSP00000229390.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. Interacts with KHDRBS3 (By similarity). Interacts with HABP4 (PubMed:19523114). Interacts with NOL3/ARC/NOP30 (PubMed:10196175). Interacts with NSEP1/YB-1/YB1 (PubMed:12604611). Interacts with SAFB/SAFB1 (PubMed:9671816, PubMed:11694584). Interacts with SRSF6/SFRS6 (PubMed:15695522). Interacts with TRA2B/SFRS10 (PubMed:11875052, PubMed:15695522). Interacts with C1QBP (PubMed:10022843). May also interact with DUSP11/PIR1(PubMed:11694584). Q13242; Q5JVS0: HABP4; NbExp=2; IntAct=EBI-2949710, EBI-523625; Q13242; P38159: RBMX; NbExp=3; IntAct=EBI-2949710, EBI-743526; Q13242; Q15287: RNPS1; NbExp=3; IntAct=EBI-2949710, EBI-395959; Q13242; P62995: TRA2B; NbExp=3; IntAct=EBI-2949710, EBI-725485; Nucleus te=Cellular stresses such as heat shock may induce localization to discrete nuclear bodies termed SAM68 nuclear bodies (SNBs), HAP bodies, or stress bodies. Numerous splicing factors including SRSF1/SFRS1/SF2, SRSF7/SFRS7, SAFB and KHDRBS1/SAM68 accumulate at these structures, which may participate in the post- transcriptional regulation of mRNAs in stressed cells. Expressed at high levels in the heart, kidney, pancreas and placenta, and at lower levels in the brain, liver, lung and skeletal muscle. Extensively phosphorylated on serine residues in the RS domain. Belongs to the splicing factor SR family. regulation of alternative mRNA splicing, via spliceosome mRNA splicing, via spliceosome nucleic acid binding RNA binding protein binding nucleus nucleoplasm nucleolus mRNA splice site selection mRNA processing RNA export from nucleus mRNA export from nucleus RNA splicing response to toxic substance nuclear speck protein domain specific binding mRNA 3'-end processing response to alkaloid mRNA cis splicing, via spliceosome negative regulation of mRNA splicing, via spliceosome uc001tyi.1 uc001tyi.2 uc001tyi.3 uc001tyi.4 uc001tyi.5 
ENST00000229395.8 FGFR1OP2 ENST00000229395.8 FGFR1 oncogene partner 2, transcript variant 1 (from RefSeq NM_015633.3) ENST00000229395.1 ENST00000229395.2 ENST00000229395.3 ENST00000229395.4 ENST00000229395.5 ENST00000229395.6 ENST00000229395.7 FGOP2_HUMAN HSPC123 NM_015633 Q6R955 Q8N5L7 Q9NVK5 Q9P034 Q9UFK8 uc001rhm.1 uc001rhm.2 uc001rhm.3 uc001rhm.4 uc001rhm.5 May be involved in wound healing pathway. Q9NVK5; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-1104764, EBI-2514791; Q9NVK5-3; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-12377025, EBI-7353612; Q9NVK5-3; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-12377025, EBI-14104088; Cytoplasm Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NVK5-1; Sequence=Displayed; Name=2; IsoId=Q9NVK5-2; Sequence=VSP_027538; Name=3; IsoId=Q9NVK5-3; Sequence=VSP_027539, VSP_027540; Expressed in bone marrow, spleen and thymus. Note=A chromosomal aberration involving FGFR1OP2 may be a cause of stem cell myeloproliferative disorder (MPD). Insertion ins(12;8)(p11;p11p22) with FGFR1. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein FGFR1OP2-FGFR1 may exhibit constitutive kinase activity and be responsible for the transforming activity. Belongs to the SIKE family. Sequence=AAF29087.1; Type=Frameshift; Evidence=; Sequence=CAB56012.1; Type=Frameshift; Evidence=; protein binding cytoplasm cytosol response to wounding wound healing protein homodimerization activity uc001rhm.1 uc001rhm.2 uc001rhm.3 uc001rhm.4 uc001rhm.5 
ENST00000229402.4 KLRB1 ENST00000229402.4 killer cell lectin like receptor B1 (from RefSeq NM_002258.3) CLEC5B ENST00000229402.1 ENST00000229402.2 ENST00000229402.3 KLRB1_HUMAN NKRP1A NM_002258 Q12918 Q24K24 uc010sgt.1 uc010sgt.2 uc010sgt.3 uc010sgt.4 Natural killer (NK) cells are lymphocytes that mediate cytotoxicity and secrete cytokines after immune stimulation. Several genes of the C-type lectin superfamily, including the rodent NKRP1 family of glycoproteins, are expressed by NK cells and may be involved in the regulation of NK cell function. The KLRB1 protein contains an extracellular domain with several motifs characteristic of C-type lectins, a transmembrane domain, and a cytoplasmic domain. The KLRB1 protein is classified as a type II membrane protein because it has an external C terminus. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC027885.1, AK292022.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229402.4/ ENSP00000229402.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays an inhibitory role on natural killer (NK) cells cytotoxicity. Activation results in specific acid sphingomyelinase/SMPD1 stimulation with subsequent marked elevation of intracellular ceramide. Activation also leads to AKT1/PKB and RPS6KA1/RSK1 kinases stimulation as well as markedly enhanced T-cell proliferation induced by anti-CD3. Acts as a lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal epitope as well as to the N- acetyllactosamine epitope. Binds also to CLEC2D/LLT1 as a ligand and inhibits NK cell-mediated cytotoxicity as well as interferon-gamma secretion in target cells. Homodimer; disulfide-linked. Interacts with acid sphingomyelinase/SMPD1. Q12918; Q9UHP7-1: CLEC2D; NbExp=2; IntAct=EBI-2805465, EBI-13640978; Membrane ; Single-pass type II membrane protein Expressed in a subset of NK cells predominantly in intestinal epithelium and liver. Detected in peripheral blood T-cells and preferentially in adult T-cells with a memory antigenic phenotype. By IL12/interleukin-12 in NK cells. N-glycosylated. Contains sialic acid residues. Name=Functional Glycomics Gateway - Glycan Binding; Note=NKRP1; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_248"; transmembrane signaling receptor activity protein binding plasma membrane cell surface receptor signaling pathway membrane integral component of membrane carbohydrate binding regulation of immune response uc010sgt.1 uc010sgt.2 uc010sgt.3 uc010sgt.4 
ENST00000229465.10 LINC03033 ENST00000229465.10 LINC03033 (from geneSymbol) AK026100 ENST00000229465.1 ENST00000229465.2 ENST00000229465.3 ENST00000229465.4 ENST00000229465.5 ENST00000229465.6 ENST00000229465.7 ENST00000229465.8 ENST00000229465.9 uc059cgh.1 uc059cgh.1 
ENST00000229554.10 RSPH4A ENST00000229554.10 radial spoke head component 4A, transcript variant 1 (from RefSeq NM_001010892.3) B4DSI1 ENST00000229554.1 ENST00000229554.2 ENST00000229554.3 ENST00000229554.4 ENST00000229554.5 ENST00000229554.6 ENST00000229554.7 ENST00000229554.8 ENST00000229554.9 NM_001010892 Q3KP24 Q5TD94 Q5TD95 RSH4A_HUMAN RSHL3 uc003pxe.1 uc003pxe.2 uc003pxe.3 uc003pxe.4 This gene encodes a protein that appears to be a component the radial spoke head, as determined by homology to similar proteins in the biflagellate alga Chlamydomonas reinhardtii and other ciliates. Radial spokes, which are regularly spaced along cilia, sperm, and flagella axonemes, consist of a thin 'stalk' and a bulbous 'head' that form a signal transduction scaffold between the central pair of microtubules and dynein. Mutations in this gene cause primary ciliary dyskinesia 1, a disease arising from dysmotility of motile cilia and sperm. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2009]. Component of the axonemal radial spoke head which plays an important role in ciliary motility (PubMed:19200523). Essential for triplet radial spokes (RS1, RS2 and RS3) head assembly in the motile cilia (By similarity). Interacts with RSPH6A. Cytoplasm, cytoskeleton, cilium axoneme Cell projection, cilium Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q5TD94-1; Sequence=Displayed; Name=2; IsoId=Q5TD94-2; Sequence=VSP_030125; Name=3; IsoId=Q5TD94-3; Sequence=VSP_030126, VSP_030127; Expressed in trachea, lungs, and testes (PubMed:23993197). Very strong expression is detected in nasal brushings (PubMed:19200523). Ciliary dyskinesia, primary, 11 (CILD11) [MIM:612649]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit situs inversus, due to dysfunction of monocilia at the embryonic node and randomization of left-right body asymmetry. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the flagellar radial spoke RSP4/6 family. radial spoke cilium movement molecular_function nucleus nucleoplasm nucleolus cytoplasm cytoskeleton cilium axoneme motile cilium axoneme assembly cell projection cilium assembly cilium movement involved in cell motility uc003pxe.1 uc003pxe.2 uc003pxe.3 uc003pxe.4 
ENST00000229563.6 TMEM14C ENST00000229563.6 transmembrane protein 14C, transcript variant 2 (from RefSeq NM_016462.4) C6orf53 ENST00000229563.1 ENST00000229563.2 ENST00000229563.3 ENST00000229563.4 ENST00000229563.5 HSPC194 NM_016462 Q5T4I6 Q9P0S9 TM14C_HUMAN uc003mzh.1 uc003mzh.2 uc003mzh.3 uc003mzh.4 uc003mzh.5 Required for normal heme biosynthesis. Q9P0S9; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2339195, EBI-11343438; Q9P0S9; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-2339195, EBI-747430; Q9P0S9; Q13323: BIK; NbExp=3; IntAct=EBI-2339195, EBI-700794; Q9P0S9; O00501: CLDN5; NbExp=3; IntAct=EBI-2339195, EBI-18400628; Q9P0S9; P21964: COMT; NbExp=3; IntAct=EBI-2339195, EBI-372265; Q9P0S9; O75208: COQ9; NbExp=3; IntAct=EBI-2339195, EBI-724524; Q9P0S9; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-2339195, EBI-6942903; Q9P0S9; P00387: CYB5R3; NbExp=3; IntAct=EBI-2339195, EBI-1046040; Q9P0S9; Q15125: EBP; NbExp=3; IntAct=EBI-2339195, EBI-3915253; Q9P0S9; A1L3X0: ELOVL7; NbExp=3; IntAct=EBI-2339195, EBI-10285373; Q9P0S9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2339195, EBI-18304435; Q9P0S9; P08034: GJB1; NbExp=3; IntAct=EBI-2339195, EBI-17565645; Q9P0S9; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-2339195, EBI-3917143; Q9P0S9; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2339195, EBI-13345167; Q9P0S9; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-2339195, EBI-18053395; Q9P0S9; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2339195, EBI-749265; Q9P0S9; Q5T0T0: MARCHF8; NbExp=3; IntAct=EBI-2339195, EBI-14061946; Q9P0S9; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-2339195, EBI-11956541; Q9P0S9; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-2339195, EBI-6163737; Q9P0S9; Q96E29: MTERF3; NbExp=3; IntAct=EBI-2339195, EBI-7825321; Q9P0S9; P15941-11: MUC1; NbExp=3; IntAct=EBI-2339195, EBI-17263240; Q9P0S9; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-2339195, EBI-10247000; Q9P0S9; Q68D85: NCR3LG1; NbExp=3; IntAct=EBI-2339195, EBI-14061804; Q9P0S9; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-2339195, EBI-716063; Q9P0S9; O60664: PLIN3; NbExp=3; IntAct=EBI-2339195, EBI-725795; Q9P0S9; A0A0S2Z4U3: SDC3; NbExp=3; IntAct=EBI-2339195, EBI-10204280; Q9P0S9; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2339195, EBI-18159983; Q9P0S9; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-2339195, EBI-17280858; Q9P0S9; Q16623: STX1A; NbExp=3; IntAct=EBI-2339195, EBI-712466; Q9P0S9; P21579: SYT1; NbExp=3; IntAct=EBI-2339195, EBI-524909; Q9P0S9; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2339195, EBI-8638294; Q9P0S9; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-2339195, EBI-11722971; Q9P0S9; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-2339195, EBI-18178701; Q9P0S9; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-2339195, EBI-8649725; Q9P0S9; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2339195, EBI-2548832; Q9P0S9; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2339195, EBI-6447886; Q9P0S9; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-2339195, EBI-744988; Q9P0S9; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-2339195, EBI-12837904; Q9P0S9; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-2339195, EBI-3892947; Mitochondrion membrane ; Multi-pass membrane protein Belongs to the TMEM14 family. protein binding mitochondrion mitochondrial inner membrane heme biosynthetic process mitochondrial transport membrane integral component of membrane erythrocyte differentiation mitochondrial membrane regulation of heme biosynthetic process uc003mzh.1 uc003mzh.2 uc003mzh.3 uc003mzh.4 uc003mzh.5 
ENST00000229595.6 ASF1A ENST00000229595.6 anti-silencing function 1A histone chaperone (from RefSeq NM_014034.3) ASF1A ASF1A_HUMAN CGI-98 ENST00000229595.1 ENST00000229595.2 ENST00000229595.3 ENST00000229595.4 ENST00000229595.5 HSPC146 NM_014034 Q6IA08 Q9P014 Q9Y294 uc011ebn.1 uc011ebn.2 uc011ebn.3 uc011ebn.4 This gene encodes a member of the H3/H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 gene in yeast. The protein is a key component of a histone donor complex that functions in nucleosome assembly. It interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660803.80138.1, SRR1660805.154207.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229595.6/ ENSP00000229595.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed:29478807). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol (PubMed:21454524, PubMed:29408485). Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit (PubMed:15621527). Interacts with histone H3 (including both histone H3.1 and H3.3) and histone H4 (PubMed:10759893, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:33857403, PubMed:15840725). Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1 complex (PubMed:11897662, PubMed:16980972). Interacts with CABIN1, HAT1, HIRA, NASP, TAF1 and UBN1 (PubMed:12093919, PubMed:14680630, PubMed:14718166, PubMed:15621527, PubMed:16980972, PubMed:19029251). Interacts with CDAN1 (PubMed:22407294). Found in a cytosolic complex with IPO4 and histones H3 and H4 (PubMed:21454524, PubMed:22407294). Interacts with CREBBP (PubMed:24616510). Q9Y294; Q13112: CHAF1B; NbExp=3; IntAct=EBI-749553, EBI-1052944; Q9Y294; P03372: ESR1; NbExp=4; IntAct=EBI-749553, EBI-78473; Q9Y294; P62805: H4C9; NbExp=15; IntAct=EBI-749553, EBI-302023; Q9Y294; P54198: HIRA; NbExp=14; IntAct=EBI-749553, EBI-372342; Q9Y294; P49736: MCM2; NbExp=10; IntAct=EBI-749553, EBI-374819; Q9Y294; P49321-2: NASP; NbExp=3; IntAct=EBI-749553, EBI-7038920; Q9Y294; P79522: PRR3; NbExp=6; IntAct=EBI-749553, EBI-2803328; Q9Y294; Q86UE8: TLK2; NbExp=8; IntAct=EBI-749553, EBI-1047967; Nucleus romosome Ubiquitously expressed. Phosphorylated by TLK1 and TLK2 (PubMed:11470414, PubMed:20016786, PubMed:35136069). Highly phosphorylated in S-phase and at lower levels in M-phase (PubMed:11470414). TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation (PubMed:20016786). Phosphorylation at Ser-192 by PRKDC in response to DNA damage promotes the histone chaperone activity and ability to replace histones at double-strand breaks (DSBs) at stalled or collapsed replication forks, leading to RAD51 recruitment (PubMed:29478807). Belongs to the ASF1 family. nuclear chromatin osteoblast differentiation chromatin binding protein binding nucleus nucleoplasm DNA repair chromatin organization chromatin assembly or disassembly nucleosome assembly DNA replication-dependent nucleosome assembly DNA replication-independent nucleosome assembly negative regulation of chromatin silencing macromolecular complex histone binding muscle cell differentiation uc011ebn.1 uc011ebn.2 uc011ebn.3 uc011ebn.4 
ENST00000229633.7 HINT3 ENST00000229633.7 histidine triad nucleotide binding protein 3 (from RefSeq NM_138571.5) B3KQ91 ENST00000229633.1 ENST00000229633.2 ENST00000229633.3 ENST00000229633.4 ENST00000229633.5 ENST00000229633.6 HINT3_HUMAN NM_138571 Q8N0Y9 Q9NQE9 uc003qal.1 uc003qal.2 uc003qal.3 uc003qal.4 uc003qal.5 uc003qal.6 Histidine triad proteins, such as HINT3, are nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides (Brenner, 2002 [PubMed 12119013]).[supplied by OMIM, Mar 2008]. ##Evidence-Data-START## Transcript exon combination :: BX647228.1, SRR1660807.176584.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229633.7/ ENSP00000229633.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:17870088). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N- alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase (PubMed:17870088). Hydrolyzes 3-indolepropionic acyl-adenylate and fluorogenic purine nucleoside tryptamine phosphoramidates in vitro (PubMed:17870088). Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+); Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57890, ChEBI:CHEBI:456215; Evidence=; Kinetic parameters: KM=1.5 uM for indolepropinoic acyl-adenylate ; KM=22 uM for tryptamine adenine phosphoramidate monoester ; KM=29 uM for tryptamine guanine phosphoramidate monoester ; KM=32 uM for tryptamine hypoxanthine phosphoramidate monoester ; KM=121 uM for tryptamine uracil phosphoramidate monoester ; KM=181 uM for tryptamine cytosine phosphoramidate monoester ; Note=HINT3 prefers purine over pyrimidine-based substrates.; Forms dimers to octamers and even larger oligomer (PubMed:17870088). Interacts with CALM1 (By similarity). Cytoplasm Nucleus Note=Localized as aggregates in the cytoplasm and the nucleus. Belongs to the HINT family. nucleotide binding catalytic activity nucleus cytoplasm hydrolase activity identical protein binding protein homodimerization activity protein homotetramerization uc003qal.1 uc003qal.2 uc003qal.3 uc003qal.4 uc003qal.5 uc003qal.6 
ENST00000229708.4 ULBP1 ENST00000229708.4 UL16 binding protein 1, transcript variant 3 (from RefSeq NR_133659.2) ENST00000229708.1 ENST00000229708.2 ENST00000229708.3 N2DL1 NR_133659 Q5VY81 Q8IZW3 Q8IZX6 Q9BZM6 RAET1I ULBP1_HUMAN uc003qnp.1 uc003qnp.2 uc003qnp.3 uc003qnp.4 uc003qnp.5 uc003qnp.6 The protein encoded by this gene is a ligand of natural killer group 2, member D (NKG2D), an immune system-activating receptor on NK cells and T-cells. Binding of the encoded ligand to NKG2D leads to activation of several signal transduction pathways, including those of JAK2, STAT5, ERK and PI3K kinase/Akt. Also, in cytomegalovirus-infected cells, this ligand binds the UL16 glycoprotein and is prevented from activating the immune system. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015]. Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity. Interacts with KLRK1/NKG2D (PubMed:11777960). Does not bind to beta2-microglobulin (PubMed:12782710). (Microbial infection) In CMV-infected cells, interacts with the viral glycoprotein UL16; this interaction causes ULBP1 retention in the endoplasmic reticulum and cis-Golgi and prevents binding to and activation of KLRK1/NKG2D, providing CMV with an immune evasion mechanism. Q9BZM6; P26718: KLRK1; NbExp=2; IntAct=EBI-16365037, EBI-458344; Cell membrane ; Lipid-anchor, GPI-anchor Endoplasmic reticulum Note=In CMV-infected fibroblasts, detected in the endoplasmic reticulum/cis-Golgi. Expressed in T-cells, B-cells, erythroleukemia cell lines and in a wide range of tissues including heart, brain, lung, liver, testis, lymph node, thymus, tonsil and bone marrow. Also found in fetal heart, brain, lung and liver. UL16-binding proteins (ULBPs) are unusual members of the extended MHC class I superfamily. They do not contain the alpha 3 domain and lack a transmembrane domain. Belongs to the MHC class I family. immune system process protein binding extracellular space endoplasmic reticulum cytosol plasma membrane immune response external side of plasma membrane actin cytoskeleton membrane viral process natural killer cell activation anchored component of membrane natural killer cell mediated cytotoxicity anchored component of plasma membrane natural killer cell lectin-like receptor binding regulation of immune response uc003qnp.1 uc003qnp.2 uc003qnp.3 uc003qnp.4 uc003qnp.5 uc003qnp.6 
ENST00000229725.4 NEU1 ENST00000229725.4 neuraminidase 1 (from RefSeq NM_000434.4) ENST00000229725.1 ENST00000229725.2 ENST00000229725.3 NANH NEUR1_HUMAN NM_000434 Q99519 uc302whk.1 The protein encoded by this gene is a lysosomal enzyme that cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter is also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis, a lysosomal storage disease that can be type 1 (cherry red spot-myoclonus syndrome or normosomatic type), which is late-onset, or type 2 (the dysmorphic type), which occurs at an earlier age with increased severity. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660807.50482.1, SRR1803611.166177.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000375631.5/ ENSP00000364782.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- (2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence= pH dependence: Optimum pH is 4.6.; Interacts with cathepsin A (protective protein), beta- galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex. Q99519; Q13520: AQP6; NbExp=3; IntAct=EBI-721517, EBI-13059134; Q99519; P11912: CD79A; NbExp=3; IntAct=EBI-721517, EBI-7797864; Q99519; Q8IU89: CERS3; NbExp=3; IntAct=EBI-721517, EBI-18202821; Q99519; Q9HA82: CERS4; NbExp=3; IntAct=EBI-721517, EBI-2622997; Q99519; O43889-2: CREB3; NbExp=3; IntAct=EBI-721517, EBI-625022; Q99519; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-721517, EBI-6942903; Q99519; Q15125: EBP; NbExp=3; IntAct=EBI-721517, EBI-3915253; Q99519; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-721517, EBI-781551; Q99519; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-721517, EBI-712073; Q99519; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-721517, EBI-13345167; Q99519; Q8TED1: GPX8; NbExp=3; IntAct=EBI-721517, EBI-11721746; Q99519; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-721517, EBI-1052304; Q99519; O14880: MGST3; NbExp=3; IntAct=EBI-721517, EBI-724754; Q99519; P15941-11: MUC1; NbExp=3; IntAct=EBI-721517, EBI-17263240; Q99519; Q14973: SLC10A1; NbExp=3; IntAct=EBI-721517, EBI-3923031; Q99519; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-721517, EBI-18159983; Q99519; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-721517, EBI-17595455; Q99519; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-721517, EBI-2823239; Q99519; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-721517, EBI-8638294; Lysosome membrane; Peripheral membrane protein; Lumenal side. Lysosome lumen. Cell membrane. Cytoplasmic vesicle. Lysosome Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. Highly expressed in pancreas, followed by skeletal muscle, kidney, placenta, heart, lung and liver. Weakly expressed in brain. A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes. N-glycosylated. Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane. Sialidosis (SIALIDOSIS) [MIM:256550]: Lysosomal storage disease occurring as two types with various manifestations. Type 1 sialidosis (cherry red spot-myoclonus syndrome or normosomatic type) is late-onset and it is characterized by the formation of cherry red macular spots in childhood, progressive debilitating myoclonus, insiduous visual loss and rarely ataxia. The diagnosis can be confirmed by the screening of the urine for sialyloligosaccharides. Type 2 sialidosis (also known as dysmorphic type) occurs as several variants of increasing severity with earlier age of onset. It is characterized by the presence of abnormal somatic features including coarse facies and dysostosis multiplex, vertebral deformities, intellectual disability, cherry-red spot/myoclonus, sialuria, cytoplasmic vacuolation of peripheral lymphocytes, bone marrow cells and conjunctival epithelial cells. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyl hydrolase 33 family. Name=Wikipedia; Note=Neuraminidase entry; URL="https://en.wikipedia.org/wiki/Neuraminidase"; exo-alpha-sialidase activity protein binding extracellular region cytoplasm lysosome lysosomal membrane plasma membrane carbohydrate metabolic process lipid metabolic process glycosphingolipid metabolic process ganglioside catabolic process metabolic process oligosaccharide catabolic process membrane lipid catabolic process hydrolase activity hydrolase activity, acting on glycosyl bonds alpha-sialidase activity cell junction cytoplasmic vesicle specific granule lumen lysosomal lumen intracellular membrane-bounded organelle neutrophil degranulation exo-alpha-(2->3)-sialidase activity exo-alpha-(2->6)-sialidase activity exo-alpha-(2->8)-sialidase activity extracellular exosome uc302whk.1 
ENST00000229729.11 SLC44A4 ENST00000229729.11 solute carrier family 44 member 4, transcript variant 1 (from RefSeq NM_025257.3) A2BED3 B0UXX8 B0UZY8 B4DU94 B4DWM2 C6orf29 CTL4 CTL4_HUMAN E9PEK7 ENST00000229729.1 ENST00000229729.10 ENST00000229729.2 ENST00000229729.3 ENST00000229729.4 ENST00000229729.5 ENST00000229729.6 ENST00000229729.7 ENST00000229729.8 ENST00000229729.9 NG22 NM_025257 Q53GD3 Q5JP84 Q5JQ93 Q658S8 Q6UX89 Q8TEW4 Q96C58 Q96K59 Q9Y332 SLC44A4 TPPT1 UNQ441/PRO874 uc010jti.1 uc010jti.2 uc010jti.3 uc010jti.4 uc010jti.5 The protein encoded by this gene may be a sodium-dependent transmembrane transport protein involved in the uptake of choline by cholinergic neurons. Defects in this gene can cause sialidosis, a lysosomal storage disease. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2010]. Choline transporter that plays a role in the choline- acetylcholine system and is required to the efferent innervation of hair cells in the olivocochlear bundle for the maintenance of physiological function of outer hair cells and the protection of hair cells from acoustic injury (By similarity) (PubMed:23651124, PubMed:28013291). Also described as a thiamine pyrophosphate transporter in colon, may mediate the absorption of microbiota- generated thiamine pyrophosphate and contribute to host thiamine (vitamin B1) homeostasis (PubMed:24379411, PubMed:26741288). [Isoform 3]: Has also thiamine pyrophosphate transporter activity. Reaction=choline(out) + n H(+)(in) = choline(in) + n H(+)(out); Xref=Rhea:RHEA:75463, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378; Evidence=; Reaction=thiamine diphosphate(out) = thiamine diphosphate(in); Xref=Rhea:RHEA:75471, ChEBI:CHEBI:58937; Evidence=; Kinetic parameters: KM=0.17 uM for thiamine pyrophosphate ; Vmax=18.19 pmol/min/mg enzyme ; Membrane ulti-pass membrane protein Apical cell membrane Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q53GD3-1; Sequence=Displayed; Name=2; IsoId=Q53GD3-2; Sequence=VSP_030998; Name=3; IsoId=Q53GD3-3; Sequence=VSP_046236; Name=4; IsoId=Q53GD3-4; Sequence=VSP_046821; Highly expressed in colon, also detected in prostate, trachea and lung (PubMed:24379411). Isoform 3 is also expressed in colon but a lower levels (PubMed:24379411). [Isoform 3]: Expressed in colon at low levels. N-glycosylated; N-glycosylation of Asn-69, Asn-155 and Asn-393 is required for a proper thiamine pyrophosphate uptake. Note=An interstitial deletion causing the fusion of exon 10 of CTL4 with the 3'-UTR of NEU has been detected in two patients affected by sialidosis. Deafness, autosomal dominant, 72 (DFNA72) [MIM:617606]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA72 primarily affects the middle frequencies. It gradually progresses to whole-frequency hearing loss. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the CTL (choline transporter-like) family. plasma membrane phosphatidylcholine biosynthetic process acetylcholine biosynthetic process choline transmembrane transporter activity choline transport membrane integral component of membrane apical plasma membrane positive regulation of cell growth thiamine pyrophosphate transport otolith formation neuromast hair cell development transmembrane transport acetylcholine secretion extracellular exosome thiamine pyrophosphate transporter activity uc010jti.1 uc010jti.2 uc010jti.3 uc010jti.4 uc010jti.5 
ENST00000229758.8 FBXO5 ENST00000229758.8 F-box protein 5, transcript variant 1 (from RefSeq NM_012177.5) B3KNX5 EMI1 ENST00000229758.1 ENST00000229758.2 ENST00000229758.3 ENST00000229758.4 ENST00000229758.5 ENST00000229758.6 ENST00000229758.7 FBX5 FBX5_HUMAN FBXO5 NM_012177 Q5TF47 Q8WV29 Q9UGC8 Q9UKT4 uc003qpg.1 uc003qpg.2 uc003qpg.3 uc003qpg.4 uc003qpg.5 This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. This protein is similar to xenopus early mitotic inhibitor-1 (Emi1), which is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Dec 2008]. Regulator of APC activity during mitotic and meiotic cell cycle (PubMed:17485488, PubMed:17234884, PubMed:17875940, PubMed:23708001, PubMed:23708605, PubMed:16921029). During mitotic cell cycle plays a role as both substrate and inhibitor of APC-FZR1 complex (PubMed:29875408, PubMed:17485488, PubMed:17234884, PubMed:17875940, PubMed:23708001, PubMed:23708605, PubMed:16921029). During G1 phase, plays a role as substrate of APC-FZR1 complex E3 ligase (PubMed:29875408). Then switches as an inhibitor of APC-FZR1 complex during S and G2 leading to cell-cycle commitment (PubMed:29875408). As APC inhibitor, prevents the degradation of APC substrates at multiple levels: by interacting with APC and blocking access of APC substrates to the D-box coreceptor, formed by FZR1 and ANAPC10; by suppressing ubiquitin ligation and chain elongation by APC by preventing the UBE2C and UBE2S activities (PubMed:23708605, PubMed:23708001, PubMed:16921029). Plays a role in genome integrity preservation by coordinating DNA replication with mitosis through APC inhibition in interphase to stabilize CCNA2 and GMNN in order to promote mitosis and prevent rereplication and DNA damage-induced cellular senescence (PubMed:17234884, PubMed:17485488, PubMed:17875940). During oocyte maturation, plays a role in meiosis through inactivation of APC-FZR1 complex. Inhibits APC through RPS6KA2 interaction that increases FBXO5 affiniy for CDC20 leading to the metaphase arrest of the second meiotic division before fertilization (By similarity). Controls entry into the first meiotic division through inactivation of APC-FZR1 complex (By similarity). Promotes migration and osteogenic differentiation of mesenchymal stem cells (PubMed:29850565). Protein modification; protein ubiquitination. Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). Interacts with BTRC; mediates proteolysis by the SCF ubiquitin ligase complex leading to activation of APC in late mitosis and subsequent mitotic progression (PubMed:12791267). Interacts with FZR1/CDH1 and the N-terminal substrate-binding domain of CDC20; prevents APC activation (PubMed:11988738). Also interacts with EVI5 which blocks its phosphorylation by PLK1 and prevents its subsequent binding to BTRC and degradation (PubMed:16439210). Interacts simultaneously with anaphase promoting complex (APC), through at least ANAPC2, CDC23, CDC27, the APC substrate GMNN and the APC activator FZR1 (PubMed:23708001, PubMed:26083744). Interacts with UBE2S; interferes with the activity of UBE2S mainly by disrupting the dynamic electrostatic association between the C-terminal tail of UBE2S and ANAPC2 (PubMed:23708001). Interacts with RPS6KA2; cooperates to induce the metaphase arrest of early blastomeres; increases and stabilizes interaction of FBXO5 with CDC20 (By similarity). Q9UKT4; P30260: CDC27; NbExp=2; IntAct=EBI-852298, EBI-994813; Q9UKT4; O60447: EVI5; NbExp=6; IntAct=EBI-852298, EBI-852291; Q9UKT4; P63208: SKP1; NbExp=5; IntAct=EBI-852298, EBI-307486; Q9UKT4-1; Q9UJX6: ANAPC2; NbExp=7; IntAct=EBI-16059332, EBI-396211; Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle Note=In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration (PubMed:11988738). In mitotic cells, localizes throughout the cell, particularly at the spindle (PubMed:15469984). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UKT4-1; Sequence=Displayed; Name=2; IsoId=Q9UKT4-2; Sequence=VSP_041362; Accumulates in late G1 phase, levels rise during S phase and drop in early mitosis. Up-regulated at 7 days after osteogenic induction (PubMed:29850565). Down-regulated in late G2 phase or mitosis (PubMed:17485488). Down-regulated in G2 phase after DNA damage in a CDKN1A-dependent manner (PubMed:19211842). Down-regulated in G1 phase when APC-FZR1 complex is active and accumulates at the G1-S transition, coincident with the inactivation of APC-FZR1 complex (PubMed:29875408). At the G1-S transition, transcriptionally induced by the E2F transcription factor (PubMed:11988738). Phosphorylation by CDK2 and subsequently by PLK1 triggers degradation during early mitosis through ubiquitin-mediated proteolysis by the SCF ubiquitin ligase complex containing the F-box protein BTRC. This degradation is necessary for the activation of APC in late mitosis and subsequent mitotic progression (PubMed:12791267, PubMed:15469984). Phosphorylated by RPS6KA2; increases and stabilizes interaction with CDC20 (By similarity). Ubiquitinated by the SCF(BTRC) complex following phosphorylation by PLK1 (PubMed:15469984). Undergoes both 'Lys-11' and 'Lys-48'-linked polyubiquitination by APC-FZR1 complex leading to degradation by proteasome during G1 phase (PubMed:29875408). Degraded through the SCF(BTRC) complex; degradation occurs during oocyte maturation, between germinal vesicle breakdown (GVBD) and meiosis I, and is required for the meiosis I-meiosis II transition (By similarity). regulation of transcription involved in G1/S transition of mitotic cell cycle oocyte maturation protein binding nucleus nucleoplasm cytoplasm spindle cytosol cytoskeleton regulation of DNA replication cell cycle spindle assembly involved in female meiosis I regulation of mitotic cell cycle positive regulation of cell proliferation positive regulation of G2/M transition of mitotic cell cycle anaphase-promoting complex binding vesicle organization protein ubiquitination protein kinase binding anaphase-promoting complex-dependent catabolic process negative regulation of DNA endoreduplication regulation of meiotic nuclear division positive regulation of osteoblast differentiation negative regulation of meiotic nuclear division negative regulation of mitotic metaphase/anaphase transition microtubule polymerization metal ion binding spindle assembly cell division negative regulation of ubiquitin-protein transferase activity positive regulation of biomineral tissue development meiotic spindle regulation of mitotic cell cycle phase transition negative regulation of ubiquitin protein ligase activity positive regulation of mesenchymal stem cell migration ubiquitin ligase inhibitor activity negative regulation of cellular senescence negative regulation of response to DNA damage stimulus uc003qpg.1 uc003qpg.2 uc003qpg.3 uc003qpg.4 uc003qpg.5 
ENST00000229769.3 FANCE ENST00000229769.3 FA complementation group E, transcript variant 1 (from RefSeq NM_021922.3) A8K907 ENST00000229769.1 ENST00000229769.2 FACE FANCE_HUMAN NM_021922 Q4ZGH2 Q9HB96 uc003oko.1 uc003oko.2 uc003oko.3 The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, FANCI, FANCJ (also called BRIP1), FANCL, FANCM and FANCN (also called PALB2). The previously defined group FANCH is the same as FANCA. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group E. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF265210.1, BC046359.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229769.3/ ENSP00000229769.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2. Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. Interacts with FANCC and FANCD2. Nucleus Phosphorylated. Phosphorylation by CHEK1 at Thr-346 and Ser-374 regulates its function in DNA cross-links repair. Ubiquitinated. Phosphorylation by CHEK1 induces polyubiquitination and degradation. Fanconi anemia complementation group E (FANCE) [MIM:600901]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Note=The disease is caused by variants affecting the gene represented in this entry. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/293/FANCE"; Name=Fanconi Anemia Mutation Database; URL="https://www2.rockefeller.edu/fanconi/genes/jumpe"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fance/"; molecular_function nucleus nucleoplasm DNA repair cellular response to DNA damage stimulus interstrand cross-link repair Fanconi anaemia nuclear complex uc003oko.1 uc003oko.2 uc003oko.3 
ENST00000229771.11 TULP1 ENST00000229771.11 TUB like protein 1, transcript variant 1 (from RefSeq NM_003322.6) ENST00000229771.1 ENST00000229771.10 ENST00000229771.2 ENST00000229771.3 ENST00000229771.4 ENST00000229771.5 ENST00000229771.6 ENST00000229771.7 ENST00000229771.8 ENST00000229771.9 NM_003322 O00294 O43536 Q5TGM5 Q8N571 TUBL1 TULP1_HUMAN uc003okv.1 uc003okv.2 uc003okv.3 uc003okv.4 uc003okv.5 uc003okv.6 uc003okv.7 This gene encodes a member of the tubby-like gene family (TULPs). Members of this family have been identified in plants, vertebrates, and invertebrates. TULP proteins share a conserved C-terminal region of approximately 200 amino acid residues. The protein encoded by this gene is thought to play a role in the physiology of photoreceptors. Mutations in this gene are associated with recessive juvenile retinitis pigmentosa and Leber congenital amaurosis-15. [provided by RefSeq, Nov 2016]. Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells (By similarity). Binds lipids, especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5- bisphosphate, phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and phosphatidic acid (in vitro). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages. Homodimer (Probable). May interact with ABCF1, PSIP1, ZEB1 and HMGB2 (Potential). Interacts with DNM1 (By similarity). Interacts with F-actin. Interacts with TUB (By similarity). Interacts with TYRO3 (By similarity). O00294; P16333: NCK1; NbExp=2; IntAct=EBI-1756778, EBI-389883; Cytoplasm Cell membrane ; Peripheral membrane protein ; Cytoplasmic side Secreted Synapse Note=Detected at synapses between photoreceptor cells and second-order neurons. Does not have a cleavable signal peptide and is secreted by an alternative pathway (By similarity). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O00294-1; Sequence=Displayed; Name=2; IsoId=O00294-2; Sequence=VSP_023031; Retina-specific. Retinitis pigmentosa 14 (RP14) [MIM:600132]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. te=The disease is caused by variants affecting the gene represented in this entry. Leber congenital amaurosis 15 (LCA15) [MIM:613843]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TUB family. Name=Mutations of the TULP1 gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/tulpmut.htm"; photoreceptor outer segment retina homeostasis photoreceptor inner segment protein binding phosphatidylinositol-4,5-bisphosphate binding extracellular region cytoplasm cytosol plasma membrane cilium phagocytosis phagocytosis, recognition visual perception membrane vesicle-mediated transport dendrite development cell junction eye photoreceptor cell development cell projection axon terminus synapse photoreceptor cell maintenance positive regulation of phagocytosis response to stimulus detection of light stimulus involved in visual perception actin filament binding retina development in camera-type eye protein localization to cilium protein localization to photoreceptor outer segment uc003okv.1 uc003okv.2 uc003okv.3 uc003okv.4 uc003okv.5 uc003okv.6 uc003okv.7 
ENST00000229794.9 MAPK14 ENST00000229794.9 mitogen-activated protein kinase 14, transcript variant 2 (from RefSeq NM_139012.3) A6ZJ92 A8K6P4 B0LPH0 B5TY32 CSBP CSBP1 CSBP2 CSPB1 ENST00000229794.1 ENST00000229794.2 ENST00000229794.3 ENST00000229794.4 ENST00000229794.5 ENST00000229794.6 ENST00000229794.7 ENST00000229794.8 MAPK14 MK14_HUMAN MXI2 NM_139012 O60776 Q13083 Q14084 Q16539 Q8TDX0 SAPK2A uc003olq.1 uc003olq.2 uc003olq.3 uc003olq.4 uc003olq.5 The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various environmental stresses and proinflammatory cytokines. The activation requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase. The substrates of this kinase include transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of this kinase in stress related transcription and cell cycle regulation, as well as in genotoxic stress response. Four alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1 (PubMed:9687510, PubMed:9792677). RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery (PubMed:9687510, PubMed:9792677). On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2 (PubMed:11154262). MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53 (PubMed:10747897). In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3 (PubMed:17003045). MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9 (PubMed:19893488). Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors (PubMed:16932740). Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane- associated metalloprotease ADAM17 (PubMed:20188673). Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A (PubMed:9430721, PubMed:9858528, PubMed:10330143). The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF- kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation (PubMed:11333986). Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation (PubMed:20932473). The p38 MAPKs may also have kinase- independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid- fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression (PubMed:10943842). Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113' (PubMed:15905572). Phosphorylates NLRP1 downstream of MAP3K20/ZAK in response to UV-B irradiation and ribosome collisions, promoting activation of the NLRP1 inflammasome and pyroptosis (PubMed:35857590). (Microbial infection) Activated by phosphorylation by M.tuberculosis EsxA in T-cells leading to inhibition of IFN-gamma production; phosphorylation is apparent within 15 minutes and is inhibited by kinase-specific inhibitors SB203580 and siRNA (PubMed:21586573). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Activated by cell stresses such as DNA damage, heat shock, osmotic shock, anisomycin and sodium arsenite, as well as pro-inflammatory stimuli such as bacterial lipopolysaccharide (LPS) and interleukin-1. Activation occurs through dual phosphorylation of Thr- 180 and Tyr-182 by either of two dual specificity kinases, MAP2K3/MKK3 or MAP2K6/MKK6, and potentially also MAP2K4/MKK4, as well as by TAB1- mediated autophosphorylation. MAPK14 phosphorylated on both Thr-180 and Tyr-182 is 10-20-fold more active than MAPK14 phosphorylated only on Thr-180, whereas MAPK14 phosphorylated on Tyr-182 alone is inactive. whereas Thr-180 is necessary for catalysis, Tyr-182 may be required for auto-activation and substrate recognition. Phosphorylated at Tyr-323 by ZAP70 in an alternative activation pathway in response to TCR signaling in T-cells. This alternative pathway is inhibited by GADD45A. Inhibited by dual specificity phosphatases, such as DUSP1, DUSP10, and DUSP16. Specifically inhibited by the binding of pyridinyl-imidazole compounds, which are cytokine-suppressive anti-inflammatory drugs (CSAID). Isoform Mxi2 is 100-fold less sensitive to these agents than the other isoforms and is not inhibited by DUSP1. Isoform Exip is not activated by MAP2K6. SB203580 is an inhibitor of MAPK14. Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (PubMed:21224381). Binds to a kinase interaction motif within the protein tyrosine phosphatase, PTPRR (By similarity). This interaction retains MAPK14 in the cytoplasm and prevents nuclear accumulation (By similarity). Interacts with SPAG9 and GADD45A (By similarity). Interacts with CDC25B, CDC25C, DUSP1, DUSP10, DUSP16, NP60, SUPT20H and TAB1. Interacts with casein kinase II subunits CSNK2A1 and CSNK2B. Interacts with PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14 and may regulate its dephosphorylation (PubMed:21283629). Interacts with DUSP2; this interaction does not lead to catalytic activation of DUSP2 and dephosphrylation of MAPK14 (By similarity). Q16539; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-73946, EBI-9087876; Q16539; P28562: DUSP1; NbExp=4; IntAct=EBI-73946, EBI-975493; Q16539; Q99956: DUSP9; NbExp=4; IntAct=EBI-73946, EBI-3906678; Q16539; P68104: EEF1A1; NbExp=3; IntAct=EBI-73946, EBI-352162; Q16539; P46734: MAP2K3; NbExp=5; IntAct=EBI-73946, EBI-602462; Q16539; P52564: MAP2K6; NbExp=3; IntAct=EBI-73946, EBI-448135; Q16539; P27361: MAPK3; NbExp=5; IntAct=EBI-73946, EBI-73995; Q16539; P49137: MAPKAPK2; NbExp=10; IntAct=EBI-73946, EBI-993299; Q16539; Q16644: MAPKAPK3; NbExp=10; IntAct=EBI-73946, EBI-1384657; Q16539; Q9BUB5: MKNK1; NbExp=5; IntAct=EBI-73946, EBI-73837; Q16539; Q9HBH9: MKNK2; NbExp=4; IntAct=EBI-73946, EBI-2864341; Q16539; P35813: PPM1A; NbExp=2; IntAct=EBI-73946, EBI-989143; Q16539; Q15256: PTPRR; NbExp=3; IntAct=EBI-73946, EBI-2265659; Q16539; P06400: RB1; NbExp=4; IntAct=EBI-73946, EBI-491274; Q16539; O75676: RPS6KA4; NbExp=6; IntAct=EBI-73946, EBI-73933; Q16539; Q8NEM7: SUPT20H; NbExp=5; IntAct=EBI-73946, EBI-946984; Q16539; Q92574: TSC1; NbExp=2; IntAct=EBI-73946, EBI-1047085; Q16539; Q07352: ZFP36L1; NbExp=2; IntAct=EBI-73946, EBI-721823; Q16539; O43257: ZNHIT1; NbExp=7; IntAct=EBI-73946, EBI-347522; Q16539-1; P22736-1: NR4A1; NbExp=5; IntAct=EBI-15834191, EBI-16085263; Q16539-1; Q15256-1: PTPRR; NbExp=6; IntAct=EBI-15834191, EBI-16067395; Q16539-1; P54830-1: Ptpn5; Xeno; NbExp=6; IntAct=EBI-15834191, EBI-16067443; Q16539-3; P28482: MAPK1; NbExp=5; IntAct=EBI-6932370, EBI-959949; Q16539-3; P49790: NUP153; NbExp=2; IntAct=EBI-6932370, EBI-286779; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=5; Name=CSBP2; IsoId=Q16539-1; Sequence=Displayed; Name=CSBP1; IsoId=Q16539-2; Sequence=VSP_004842; Name=Mxi2; IsoId=Q16539-3; Sequence=VSP_004844; Name=Exip; Synonyms=Exon skip; IsoId=Q16539-4; Sequence=VSP_004843, VSP_004845; Name=5; IsoId=Q16539-5; Sequence=VSP_057194; Brain, heart, placenta, pancreas and skeletal muscle. Expressed to a lesser extent in lung, liver and kidney. The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. Dual phosphorylation can also be mediated by TAB1-mediated autophosphorylation. TCR engagement in T-cells also leads to Tyr-323 phosphorylation by ZAP70. Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16. PPM1D also mediates dephosphorylation and inactivation of MAPK14 (PubMed:21283629). Acetylated at Lys-53 and Lys-152 by KAT2B and EP300. Acetylation at Lys-53 increases the affinity for ATP and enhances kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3. Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Name=Wikipedia; Note=P38 mitogen-activated protein kinases entry; URL="https://en.wikipedia.org/wiki/P38_mitogen-activated_protein_kinases"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41292/MAPK14"; DNA damage checkpoint nucleotide binding activation of MAPK activity cell morphogenesis spindle pole cartilage condensation angiogenesis placenta development chondrocyte differentiation positive regulation of cytokine secretion involved in immune response protein kinase activity protein serine/threonine kinase activity MAP kinase activity MAP kinase kinase activity protein binding ATP binding extracellular region cell nucleus nucleoplasm cytoplasm mitochondrion cytosol glucose metabolic process regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter protein phosphorylation apoptotic process chemotaxis cellular response to DNA damage stimulus signal transduction cell surface receptor signaling pathway transmembrane receptor protein serine/threonine kinase signaling pathway Ras protein signal transduction skeletal muscle tissue development regulation of gene expression positive regulation of gene expression positive regulation of macrophage chemotaxis positive regulation of myotube differentiation kinase activity phosphorylation nuclear speck transferase activity peptidyl-serine phosphorylation fatty acid oxidation enzyme binding protein phosphatase binding regulation of ossification osteoclast differentiation positive regulation of cyclase activity lipopolysaccharide-mediated signaling pathway response to muramyl dipeptide response to lipopolysaccharide secretory granule lumen intracellular signal transduction cellular response to vascular endothelial growth factor stimulus response to muscle stretch p38MAPK cascade positive regulation of protein import into nucleus signal transduction in response to DNA damage neutrophil degranulation positive regulation of erythrocyte differentiation positive regulation of myoblast differentiation positive regulation of transcription from RNA polymerase II promoter positive regulation of glucose import vascular endothelial growth factor receptor signaling pathway mitogen-activated protein kinase p38 binding regulation of sequence-specific DNA binding transcription factor activity striated muscle cell differentiation positive regulation of muscle cell differentiation NFAT protein binding positive regulation of cardiac muscle cell proliferation 3'-UTR-mediated mRNA stabilization cellular response to lipopolysaccharide cellular response to lipoteichoic acid cellular response to tumor necrosis factor cellular response to ionizing radiation negative regulation of canonical Wnt signaling pathway positive regulation of brown fat cell differentiation stress-induced premature senescence cellular response to virus glutamatergic synapse regulation of cytokine production involved in inflammatory response positive regulation of myoblast fusion regulation of signal transduction by p53 class mediator ficolin-1-rich granule lumen positive regulation of metallopeptidase activity positive regulation of reactive oxygen species metabolic process positive regulation of interleukin-12 secretion positive regulation of blood vessel endothelial cell migration uc003olq.1 uc003olq.2 uc003olq.3 uc003olq.4 uc003olq.5 
ENST00000229812.8 STK38 ENST00000229812.8 serine/threonine kinase 38, transcript variant 1 (from RefSeq NM_007271.4) ENST00000229812.1 ENST00000229812.2 ENST00000229812.3 ENST00000229812.4 ENST00000229812.5 ENST00000229812.6 ENST00000229812.7 NDR1 NM_007271 Q15208 Q503A1 STK38 STK38_HUMAN uc003omh.1 uc003omh.2 uc003omh.3 uc003omh.4 This gene encodes a member of the AGC serine/threonine kinase family of proteins. The kinase activity of this protein is regulated by autophosphorylation and phosphorylation by other upstream kinases. This protein has been shown to function in the cell cycle and apoptosis. This protein has also been found to regulate the protein stability and transcriptional activity of the MYC oncogene. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2015]. Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Activated by binding of S100B which releases autoinhibitory N-lobe interactions, enabling ATP to bind and the autophosphorylation of Ser-281. Thr-444 then undergoes calcium- dependent phosphorylation by STK24/MST3. Interactions between phosphorylated Thr-444 and the N-lobe promote additional structural changes that complete the activation of the kinase. Autoinhibition is also released by the binding of MOB1/MOBKL1A and MOB2/HCCA2 to the N- terminal of STK38. Homodimeric S100B binds two molecules of STK38 (PubMed:14661952). Interacts with MOB1 and MOB2 (PubMed:15067004, PubMed:15197186). Interacts with MAP3K1 and MAP3K2 (via the kinase catalytic domain) (PubMed:17906693). Forms a tripartite complex with MOBKL1B and STK3/MST2 (PubMed:18362890). Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4 (By similarity). Q15208; P49407: ARRB1; NbExp=3; IntAct=EBI-458376, EBI-743313; Q15208; P32121: ARRB2; NbExp=3; IntAct=EBI-458376, EBI-714559; Q15208; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-458376, EBI-11524452; Q15208; Q03135: CAV1; NbExp=3; IntAct=EBI-458376, EBI-603614; Q15208; P08238: HSP90AB1; NbExp=2; IntAct=EBI-458376, EBI-352572; Q15208; Q9H8S9: MOB1A; NbExp=3; IntAct=EBI-458376, EBI-748229; Q15208; P16333: NCK1; NbExp=3; IntAct=EBI-458376, EBI-389883; Q15208; P30086: PEBP1; NbExp=3; IntAct=EBI-458376, EBI-716384; Q15208; P02638: S100B; Xeno; NbExp=3; IntAct=EBI-458376, EBI-458452; Nucleus. Cytoplasm. Ubiquitously expressed with highest levels observed in peripheral blood leukocytes. ISGylated. Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). nucleotide binding magnesium ion binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding nucleus cytoplasm cytosol cellular protein modification process protein phosphorylation kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation mitogen-activated protein kinase kinase kinase binding intracellular signal transduction negative regulation of MAP kinase activity cadherin binding metal ion binding uc003omh.1 uc003omh.2 uc003omh.3 uc003omh.4 
ENST00000229829.7 HLA-DOA ENST00000229829.7 major histocompatibility complex, class II, DO alpha (from RefSeq NM_002119.4) ENST00000229829.1 ENST00000229829.2 ENST00000229829.3 ENST00000229829.4 ENST00000229829.5 ENST00000229829.6 HLA-DOA NM_002119 X5CF87 X5CF87_HUMAN uc003ocr.1 uc003ocr.2 uc003ocr.3 uc003ocr.4 uc003ocr.5 HLA-DOA belongs to the HLA class II alpha chain paralogues. HLA-DOA forms a heterodimer with HLA-DOB. The heterodimer, HLA-DO, is found in lysosomes in B cells and regulates HLA-DM-mediated peptide loading on MHC class II molecules. In comparison with classical HLA class II molecules, this gene exhibits very little sequence variation, especially at the protein level. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803612.110203.1, BC013183.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000229829.7/ ENSP00000229829.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Endosome membrane ; Single-pass type I membrane protein Lysosome membrane ; Single-pass type I membrane protein Belongs to the MHC class II family. adaptive immune response immune system process antigen processing and presentation of peptide or polysaccharide antigen via MHC class II immune response membrane integral component of membrane antigen processing and presentation antigen processing and presentation of exogenous peptide antigen via MHC class II MHC class II protein complex regulation of T cell differentiation uc003ocr.1 uc003ocr.2 uc003ocr.3 uc003ocr.4 uc003ocr.5 
ENST00000229903.5 SAYSD1 ENST00000229903.5 SAYSVFN motif domain containing 1, transcript variant 1 (from RefSeq NM_018322.3) C6orf64 ENST00000229903.1 ENST00000229903.2 ENST00000229903.3 ENST00000229903.4 NM_018322 Q9H0D8 Q9NPB0 SMDC1_HUMAN uc003ook.1 uc003ook.2 uc003ook.3 Cytoplasmic vesicle membrane ; Single-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NPB0-1; Sequence=Displayed; Name=2; IsoId=Q9NPB0-2; Sequence=VSP_014597, VSP_014598; membrane integral component of membrane cytoplasmic vesicle membrane cytoplasmic vesicle intracellular membrane-bounded organelle uc003ook.1 uc003ook.2 uc003ook.3 
ENST00000229922.7 CAP2 ENST00000229922.7 cyclase associated actin cytoskeleton regulatory protein 2, transcript variant 1 (from RefSeq NM_006366.3) B2R5Y3 B7Z1C4 B7Z214 CAP2_HUMAN ENST00000229922.1 ENST00000229922.2 ENST00000229922.3 ENST00000229922.4 ENST00000229922.5 ENST00000229922.6 NM_006366 P40123 Q6IAY2 uc003ncb.1 uc003ncb.2 uc003ncb.3 uc003ncb.4 uc003ncb.5 This gene was identified by its similarity to the gene for human adenylyl cyclase-associated protein. The function of the protein encoded by this gene is unknown. However, the protein appears to be able to interact with adenylyl cyclase-associated protein and actin. [provided by RefSeq, Jul 2008]. May have a regulatory bifunctional role. P40123; P60709: ACTB; NbExp=5; IntAct=EBI-1051165, EBI-353944; P40123; P63261: ACTG1; NbExp=12; IntAct=EBI-1051165, EBI-351292; P40123; Q96SZ5: ADO; NbExp=3; IntAct=EBI-1051165, EBI-11102284; P40123; P13196: ALAS1; NbExp=3; IntAct=EBI-1051165, EBI-3905054; P40123; P40123: CAP2; NbExp=4; IntAct=EBI-1051165, EBI-1051165; P40123; Q549N0: CFL2; NbExp=3; IntAct=EBI-1051165, EBI-10201319; P40123; A8MXD5: GRXCR1; NbExp=3; IntAct=EBI-1051165, EBI-5235612; P40123; Q1KLZ0: PS1TP5BP1; NbExp=3; IntAct=EBI-1051165, EBI-9978131; Cell membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P40123-1; Sequence=Displayed; Name=2; IsoId=P40123-2; Sequence=VSP_055520; Name=3; IsoId=P40123-3; Sequence=VSP_055519; Belongs to the CAP family. cell morphogenesis actin binding protein binding plasma membrane cytoskeleton organization establishment or maintenance of cell polarity signal transduction activation of adenylate cyclase activity actin polymerization or depolymerization adenylate cyclase binding postsynaptic density membrane cortical actin cytoskeleton identical protein binding uc003ncb.1 uc003ncb.2 uc003ncb.3 uc003ncb.4 uc003ncb.5 
ENST00000229955.4 GPR63 ENST00000229955.4 G protein-coupled receptor 63, transcript variant 2 (from RefSeq NM_030784.4) ENST00000229955.1 ENST00000229955.2 ENST00000229955.3 GPR63_HUMAN NM_030784 PSP24B Q9BZJ6 Q9UJH3 uc003pou.1 uc003pou.2 uc003pou.3 uc003pou.4 uc003pou.5 This gene encodes a G protein-coupled receptor. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Dec 2011]. Orphan receptor. May play a role in brain function. Cell membrane; Multi-pass membrane protein. Expressed in brain; detected in the frontal cortex, with lower levels in the thalamus, caudate, hypothalamus and midbrain. Belongs to the G-protein coupled receptor 1 family. molecular_function G-protein coupled receptor activity nucleus cytosol plasma membrane signal transduction G-protein coupled receptor signaling pathway biological_process membrane integral component of membrane receptor complex uc003pou.1 uc003pou.2 uc003pou.3 uc003pou.4 uc003pou.5 
ENST00000230036.2 GPLD1 ENST00000230036.2 glycosylphosphatidylinositol specific phospholipase D1 (from RefSeq NM_001503.4) ENST00000230036.1 NM_001503 P80108 PHLD_HUMAN PIGPLD1 Q15127 Q15128 Q2M2F2 Q5T3Y0 Q7Z6T8 Q8TCV0 Q8WW82 Q96ID6 Q9H167 Q9H4M1 Q9UJC9 uc003ned.1 uc003ned.2 uc003ned.3 uc003ned.4 Many proteins are tethered to the extracellular face of eukaryotic plasma membranes by a glycosylphosphatidylinositol (GPI) anchor. The GPI-anchor is a glycolipid found on many blood cells. The protein encoded by this gene is a GPI degrading enzyme. Glycosylphosphatidylinositol specific phospholipase D1 hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, thereby releasing the attached protein from the plasma membrane. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: L11702.1, AJ308108.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230036.2/ ENSP00000230036.1 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane. Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D- myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997, ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1.4.50; Monomer. Secreted. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P80108-1; Sequence=Displayed; Name=2; IsoId=P80108-2; Sequence=VSP_023261, VSP_023262; Belongs to the GPLD1 family. Sequence=AAA36444.1; Type=Miscellaneous discrepancy; Note=This sequence has numerous of conflicts with the human genome.; Evidence=; ossification cell migration involved in sprouting angiogenesis chondrocyte differentiation complement receptor mediated signaling pathway glycosylphosphatidylinositol phospholipase D activity phospholipase D activity extracellular region extracellular space cytoplasm lysosomal membrane C-terminal protein lipidation GPI anchor release negative regulation of cell proliferation insulin receptor signaling pathway response to glucose positive regulation of endothelial cell migration positive regulation of alkaline phosphatase activity positive regulation of triglyceride biosynthetic process negative regulation of triglyceride catabolic process positive regulation of glucose metabolic process positive regulation of high-density lipoprotein particle clearance hydrolase activity sodium channel regulator activity extracellular matrix cellular response to insulin stimulus cellular response to drug hematopoietic stem cell migration positive regulation of insulin secretion involved in cellular response to glucose stimulus positive regulation of apoptotic process intracellular membrane-bounded organelle positive regulation of cytolysis phosphatidylcholine metabolic process positive regulation of membrane protein ectodomain proteolysis positive regulation of secretion extracellular exosome transepithelial transport cellular response to calcium ion cellular response to cholesterol cellular response to triglyceride cellular response to pH hematopoietic stem cell migration to bone marrow regulation of cellular response to insulin stimulus uc003ned.1 uc003ned.2 uc003ned.3 uc003ned.4 
ENST00000230048.5 ACOT13 ENST00000230048.5 acyl-CoA thioesterase 13, transcript variant 1 (from RefSeq NM_018473.4) ACO13_HUMAN ACOT13 ENST00000230048.1 ENST00000230048.2 ENST00000230048.3 ENST00000230048.4 F5H2L4 HT012 NM_018473 O95549 PNAS-27 Q9NPJ3 THEM2 uc003nek.1 uc003nek.2 uc003nek.3 uc003nek.4 uc003nek.5 This gene encodes a member of the thioesterase superfamily. In humans, the protein co-localizes with microtubules and is essential for sustained cell proliferation. The orthologous mouse protein forms a homotetramer and is associated with mitochondria. The mouse protein functions as a medium- and long-chain acyl-CoA thioesterase. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, May 2009]. Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:16934754, PubMed:19170545). Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates (By similarity) (PubMed:16934754, PubMed:19170545). Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro) (By similarity) (PubMed:16934754, PubMed:19170545). May play a role in controlling adaptive thermogenesis (By similarity). Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782; Evidence=; Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence=; Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate; Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence=; Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+); Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; Evidence=; Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; Evidence=; Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence=; Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence=; Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence=; Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)- eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence=; Kinetic parameters: KM=4.9 uM for n-decanoyl-CoA ; KM=26 uM for n-octanoyl-CoA ; KM=70 uM for n-hexanoyl-CoA ; KM=600 uM for n-butyryl-CoA ; KM=220 uM for 2-butenoyl-CoA ; KM=120 uM for beta-methylcrotonyl-CoA ; KM=180 uM for crotonyl-CoA ; KM=250 uM for tiglyl-CoA ; KM=190 uM for n-propionyl-CoA ; KM=290 uM for acetyl-CoA ; KM=9.9 uM for lauroyl-CoA/dodecanoyl-CoA ; KM=5 uM for myristoyl-CoA/tetradecanoyl-CoA (at 25 degrees Celsius) ; KM=9 uM for myristoyl-CoA/tetradecanoyl-CoA (at 37 degrees Celsius) ; KM=16 uM for n-palmitoyl-CoA ; KM=9 uM for palmitoleoyl-CoA ; KM=20 uM for stearoyl-CoA ; KM=9 uM for oleoyl-CoA ; KM=310 uM for linoleoyl-CoA ; KM=20 uM for arachidonoyl-CoA/(5Z,8Z,11Z,14Z)-eicosatetraenoate ; KM=41 uM for 3-hydroxyphenylacetyl-CoA ; KM=10 uM for 3,4-dihydroxyphenylacetyl-CoA ; KM=25 uM for 3,5-dihydroxyphenylacetyl-CoA ; KM=49 uM for 4-hydroxyphenylacetyl-CoA ; KM=240 uM for phenylacetyl-CoA ; KM=32 uM for 3-hydroxybenzoyl-CoA ; KM=13 uM for 4-chlorobenzoyl-CoA ; KM=110 uM for beta-hydroxybutyryl-CoA ; KM=670 uM for glutaryl-CoA ; KM=2900 uM for 3-hydroxy-3-methylglutaryl-CoA ; KM=280 uM for malonyl-CoA ; KM=210 uM for methylmalonyl-CoA ; Note=kcat is 0.016 sec(-1) for n-decanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.0047 sec(-1) for n-octanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.022 sec(-1) for n- hexanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.047 sec(-1) for n-butyryl-CoA hydrolase activity (PubMed:19170545). kcat is 0.014 sec(-1) for 2-butenoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.023 sec(-1) for beta-methylcrotonyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.0076 sec(-1) for crotonyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.02 sec(- 1) for tiglyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.036 sec(-1) for n-propionyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.054 sec(-1) for acetyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.019 sec(-1) for lauroyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.02 sec(-1) for myristoyl-CoA (at 25 degrees Celsius) hydrolase activity (PubMed:19170545). kcat is 0.07 sec(-1) for myristoyl-CoA (at 37 degrees Celsius) hydrolase activity (PubMed:19170545). kcat is 0.0044 sec(-1) for n-palmitoyl- CoA hydrolase activity (PubMed:19170545). kcat is 0.017 sec(-1) for palmitoleoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.011 sec(-1) for stearoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.011 sec(-1) for oleoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.017 sec(-1) for linoleoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.022 sec(-1) for arachidonoyl-CoA hydrolase activity (PubMed:19170545). kcat is 1.4 sec(-1) for 3- hydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.19 sec(-1) for 3,4-dihydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.19 sec(-1) for 3,5- dihydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.14 sec(-1) for 4-hydroxyphenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.084 sec(-1) for phenylacetyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.011 sec(-1) for 3- hydroxybenzoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.032 sec(-1) for 4-chlorobenzoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.18 sec(-1) for beta-hydroxybutyryl-CoA hydrolase activity (PubMed:19170545). kcat is 0.05 sec(-1) for glutaryl-CoA hydrolase activity (PubMed:19170545). kcat is 0.079 sec(-1) for 3-hydroxy-3-methylglutaryl-CoA hydrolase activity (PubMed:19170545). kcat is 0.066 sec(-1) for malonyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.083 sec(-1) for methylmalonyl- CoA hydrolase activity (PubMed:19170545). ; Homotetramer (PubMed:16934754, PubMed:19170545). Interacts with PCTP (By similarity). Q9NPJ3; Q92993: KAT5; NbExp=3; IntAct=EBI-1045357, EBI-399080; Q9NPJ3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1045357, EBI-11742507; Q9NPJ3; Q969H8: MYDGF; NbExp=3; IntAct=EBI-1045357, EBI-718622; Q9NPJ3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1045357, EBI-741158; Q9NPJ3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1045357, EBI-9090795; Q9NPJ3; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-1045357, EBI-742688; Q9NPJ3; P61981: YWHAG; NbExp=3; IntAct=EBI-1045357, EBI-359832; Cytoplasm, cytosol Mitochondrion Nucleus Cytoplasm, cytoskeleton, spindle Note=During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NPJ3-1; Sequence=Displayed; Name=2; IsoId=Q9NPJ3-2; Sequence=VSP_046101; Belongs to the thioesterase PaaI family. nucleus cytoplasm mitochondrion spindle cytosol cytoskeleton acyl-CoA metabolic process hydrolase activity acyl-CoA hydrolase activity protein homotetramerization uc003nek.1 uc003nek.2 uc003nek.3 uc003nek.4 uc003nek.5 
ENST00000230050.4 RPS12 ENST00000230050.4 ribosomal protein S12 (from RefSeq NM_001016.4) ENST00000230050.1 ENST00000230050.2 ENST00000230050.3 NM_001016 P25398 Q76M58 RPS12 RS12_HUMAN uc003qdx.1 uc003qdx.2 uc003qdx.3 uc003qdx.4 uc003qdx.5 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S12E family of ribosomal proteins. It is located in the cytoplasm. Increased expression of this gene in colorectal cancers compared to matched normal colonic mucosa has been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BJ990964.1, BM742041.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230050.4/ ENSP00000230050.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre- rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre- ribosomal RNA by the RNA exosome (PubMed:34516797). Subunit of the 40S ribosomal complex (By similarity). Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Subunit of the 40S ribosomal complex (By similarity). P25398; P42858: HTT; NbExp=3; IntAct=EBI-354542, EBI-466029; Nucleus, nucleolus Belongs to the eukaryotic ribosomal protein eS12 family. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay RNA binding structural constituent of ribosome nucleoplasm cytoplasm Golgi apparatus cytosol ribosome translation translational initiation SRP-dependent cotranslational protein targeting to membrane membrane viral transcription cytosolic small ribosomal subunit intracellular membrane-bounded organelle uc003qdx.1 uc003qdx.2 uc003qdx.3 uc003qdx.4 uc003qdx.5 
ENST00000230053.11 B3GAT2 ENST00000230053.11 beta-1,3-glucuronyltransferase 2 (from RefSeq NM_080742.3) B3GA2_HUMAN ENST00000230053.1 ENST00000230053.10 ENST00000230053.2 ENST00000230053.3 ENST00000230053.4 ENST00000230053.5 ENST00000230053.6 ENST00000230053.7 ENST00000230053.8 ENST00000230053.9 GLCATS KIAA1963 NM_080742 Q5JS09 Q8TF38 Q96NK4 Q9NPZ5 uc003pfv.1 uc003pfv.2 uc003pfv.3 uc003pfv.4 uc003pfv.5 The product of this gene is a transmembrane protein belonging to the glucuronyltransferase family, and catalyzes the transfer of a beta-1,3 linked glucuronic acid to a terminal galactose in different glycoproteins or glycolipids containing a Gal-beta-1-4GlcNAc or Gal-beta-1-3GlcNAc residue. The encoded protein is involved in the synthesis of the human natural killer-1 (HNK-1) carbohydrate epitope, a sulfated trisaccharide implicated in cellular migration and adhesion in the nervous system. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB075843.1, SRR1803615.173590.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2145743 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230053.11/ ENSP00000230053.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D- xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D- GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl- [protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571, Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093; EC=2.4.1.135; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Protein modification; protein glycosylation. Homodimer. Golgi apparatus membrane; Single-pass type II membrane protein. Expressed in the trachea, retina, spinal cord, hippocampus and other brain regions, and, at lower levels, in testis and ovary. Belongs to the glycosyltransferase 43 family. Sequence=BAB70889.1; Type=Erroneous initiation; Evidence=; Sequence=BAB85549.1; Type=Erroneous initiation; Evidence=; Golgi membrane Golgi apparatus protein glycosylation galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity membrane integral component of membrane transferase activity glycosaminoglycan metabolic process metal ion binding chondroitin sulfate proteoglycan biosynthetic process uc003pfv.1 uc003pfv.2 uc003pfv.3 uc003pfv.4 uc003pfv.5 
ENST00000230056.8 GMNN ENST00000230056.8 geminin DNA replication inhibitor, transcript variant 1 (from RefSeq NM_015895.5) B3KMM8 ENST00000230056.1 ENST00000230056.2 ENST00000230056.3 ENST00000230056.4 ENST00000230056.5 ENST00000230056.6 ENST00000230056.7 GEMI_HUMAN NM_015895 O75496 Q9H1Z1 uc003nen.1 uc003nen.2 uc003nen.3 uc003nen.4 uc003nen.5 This gene encodes a protein that plays a critical role in cell cycle regulation. The encoded protein inhibits DNA replication by binding to DNA replication factor Cdt1, preventing the incorporation of minichromosome maintenance proteins into the pre-replication complex. The encoded protein is expressed during the S and G2 phases of the cell cycle and is degraded by the anaphase-promoting complex during the metaphase-anaphase transition. Increased expression of this gene may play a role in several malignancies including colon, rectal and breast cancer. Alternatively spliced transcript variants have been observed for this gene, and two pseudogenes of this gene are located on the short arm of chromosome 16. [provided by RefSeq, Oct 2011]. Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:9635433, PubMed:14993212, PubMed:20129055, PubMed:24064211). It is degraded during the mitotic phase of the cell cycle (PubMed:9635433, PubMed:14993212, PubMed:24064211). Its destruction at the metaphase- anaphase transition permits replication in the succeeding cell cycle (PubMed:9635433, PubMed:14993212, PubMed:24064211). Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (PubMed:22615398). Homotetramer (PubMed:15313623, PubMed:15260975, PubMed:15378034, PubMed:19906994). Interacts with CDT1; this inhibits binding of the MCM complex to origins of replication (PubMed:14993212, PubMed:21543332, PubMed:15260975, PubMed:19906994). The complex with CDT1 exists in two forms, a 'permissive' heterotrimer and an 'inhibitory' heterohexamer (PubMed:14993212, PubMed:15260975, PubMed:19906994). Interacts (via coiled-coil domain) with IDAS (via coiled-coil domain); this targets GMNN to the nucleus (PubMed:21543332). The heterodimer formed by GMNN and MCIDAS has much lower affinity for CDT1 than the GMNN homodimer (PubMed:24064211). Interacts with a subset of Hox proteins, affinity increasing from anterior to posterior types, the strongest interaction being with HOXB1, HOXC9 and HOXD10 (PubMed:22615398). Interacts with LRWD1 from G1/S to mitosis (PubMed:22645314). O75496; Q8IYE0: CCDC146; NbExp=4; IntAct=EBI-371669, EBI-10749669; O75496; Q8IYE0-2: CCDC146; NbExp=4; IntAct=EBI-371669, EBI-10247802; O75496; P42771: CDKN2A; NbExp=2; IntAct=EBI-371669, EBI-375053; O75496; Q9H211: CDT1; NbExp=21; IntAct=EBI-371669, EBI-456953; O75496; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-371669, EBI-7251368; O75496; P31274: HOXC9; NbExp=3; IntAct=EBI-371669, EBI-1779423; O75496; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-371669, EBI-2556193; O75496; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-371669, EBI-739832; O75496; D6RGH6: MCIDAS; NbExp=8; IntAct=EBI-371669, EBI-3954372; O75496; Q06124-2: PTPN11; NbExp=3; IntAct=EBI-371669, EBI-17635971; O75496; Q86UD0: SAPCD2; NbExp=3; IntAct=EBI-371669, EBI-2561646; O75496; P15622-3: ZNF250; NbExp=3; IntAct=EBI-371669, EBI-10177272; O75496; Q8NDP4: ZNF439; NbExp=7; IntAct=EBI-371669, EBI-747580; Cytoplasm Nucleus Note=Mainly cytoplasmic but can be relocalized to the nucleus. Absent during G1 phase, accumulates during S, G2, and M phases, and disappears at the time of the metaphase-anaphase transition. Phosphorylated during mitosis. Phosphorylation at Ser-184 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity. Meier-Gorlin syndrome 6 (MGORS6) [MIM:616835]: A form of Meier-Gorlin syndrome, a syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the geminin family. G1/S transition of mitotic cell cycle chromatin binding transcription corepressor activity protein binding nucleus nucleoplasm cytoplasm cytosol regulation of DNA replication cell cycle negative regulation of DNA replication animal organ morphogenesis positive regulation of chromatin binding histone deacetylase binding negative regulation of cell cycle negative regulation of transcription, DNA-templated macromolecular complex assembly repressing transcription factor binding DNA replication preinitiation complex assembly negative regulation of DNA-dependent DNA replication uc003nen.1 uc003nen.2 uc003nen.3 uc003nen.4 uc003nen.5 
ENST00000230085.13 SNX3 ENST00000230085.13 sorting nexin 3, transcript variant 1 (from RefSeq NM_003795.6) A8K0B1 E1P5E4 E1P5E5 ENST00000230085.1 ENST00000230085.10 ENST00000230085.11 ENST00000230085.12 ENST00000230085.2 ENST00000230085.3 ENST00000230085.4 ENST00000230085.5 ENST00000230085.6 ENST00000230085.7 ENST00000230085.8 ENST00000230085.9 NM_003795 O60493 O60718 Q4TT29 Q4TT31 Q5JXJ7 Q5JXJ8 Q96AP9 Q9C0J5 Q9NU45 SNX3 SNX3_HUMAN uc003psh.1 uc003psh.2 uc003psh.3 uc003psh.4 uc003psh.5 This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein does not contain a coiled coil region, like most family members. This protein interacts with phosphatidylinositol-3-phosphate, and is involved in protein trafficking. A pseudogene of this gene is present on the sex chromosomes. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2014]. Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (By similarity). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (PubMed:21725319, PubMed:24344282, PubMed:30213940). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (PubMed:23237080). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor TFRC presumably by delivering the transferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (By similarity). In the case of Salmonella enterica infection plays arole in maturation of the Salmonella-containing vacuole (SCV) and promotes recruitment of LAMP1 to SCVs (PubMed:20482551). Interacts with VPS26A, VPS29 and VPS35; the interaction with VPS35 is direct. The association with the retromer CSC subcomplex subunits is proposed to represent a functional distinct retromer variant described as SNX3-retromer complex (PubMed:21725319, PubMed:24344282, PubMed:30213940). Interacts with USP10 and SCNN1A (By similarity). Interacts with TRFC (By similarity). Interacts with SNX8; 2 molecules of SNX8 seems to associate with one molecule of SNX3 (PubMed:24866125). Interacts with PTPRU (PubMed:17622474). Interacts with MON2 and DOP1B. O60493; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-727209, EBI-714543; O60493; P46108: CRK; NbExp=2; IntAct=EBI-727209, EBI-886; O60493; Q9NS64: RPRM; NbExp=3; IntAct=EBI-727209, EBI-1052363; Early endosome toplasmic vesicle, phagosome Note=Colocalizes to clathrin-coated endosomal vesicles morphologically distinct from retromer-decorated non-branched endosomal tubule structures (PubMed:21725319) Colocalizes with EEA1 on nascent phagosomes in dendritic cells but competes with EEA1 for binding to phagosomal membrane (PubMed:23237080). In the case of Salmonella enterica infection localizes to Salmonella-containing vacuoles (SCVs) from which SNX3-containing tubules form 30-60 min after infection (PubMed:20482551). Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=O60493-1; Sequence=Displayed; Name=2; Synonyms=SNX 3A; IsoId=O60493-2; Sequence=VSP_006190; Name=3; IsoId=O60493-3; Sequence=VSP_012928; Name=4; IsoId=O60493-4; Sequence=VSP_014694; The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10 (By similarity). Note=A chromosomal aberration involving SNX3 has been found in patients with syndromic microphthalmia. Translocation t(6;13)(q21;q12). Belongs to the sorting nexin family. protein binding cytoplasm endosome early endosome cytosol lipid binding response to bacterium endosome membrane phosphatidylinositol-5-phosphate binding membrane invagination positive regulation of neuron projection development protein transport Wnt signaling pathway protein deubiquitination protein phosphatase binding protein to membrane docking regulation of Wnt signaling pathway clathrin-coated vesicle cytoplasmic vesicle early endosome membrane early phagosome phosphatidylinositol-3-phosphate binding phosphatidylinositol binding negative regulation of protein catabolic process phagocytic vesicle negative regulation of viral entry into host cell negative regulation of phagocytosis negative regulation of protein transport extracellular exosome phosphatidylinositol-4-phosphate binding intralumenal vesicle formation phosphatidylinositol-3,5-bisphosphate binding phosphatidylinositol phosphate binding negative regulation of early endosome to late endosome transport retromer complex uc003psh.1 uc003psh.2 uc003psh.3 uc003psh.4 uc003psh.5 
ENST00000230122.4 ZBTB24 ENST00000230122.4 zinc finger and BTB domain containing 24, transcript variant 1 (from RefSeq NM_014797.3) ENST00000230122.1 ENST00000230122.2 ENST00000230122.3 KIAA0441 NM_014797 O43167 Q17RC6 Q5TED5 Q8N455 ZBT24_HUMAN ZNF450 uc003ptl.1 uc003ptl.2 uc003ptl.3 This gene encodes a protein similar to a protein in rodents which is induced by bone morphogenic protein 2 in vitro. [provided by RefSeq, Aug 2011]. May be involved in BMP2-induced transcription. Interacts with MN1. O43167; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-744471, EBI-1642333; O43167; Q9H165-2: BCL11A; NbExp=3; IntAct=EBI-744471, EBI-10183342; O43167; Q9H2G9: BLZF1; NbExp=9; IntAct=EBI-744471, EBI-2548012; O43167; O95273: CCNDBP1; NbExp=3; IntAct=EBI-744471, EBI-748961; O43167; P32320: CDA; NbExp=6; IntAct=EBI-744471, EBI-9250559; O43167; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-744471, EBI-739624; O43167; Q8TAP6: CEP76; NbExp=6; IntAct=EBI-744471, EBI-742887; O43167; Q8NEL9-2: DDHD1; NbExp=3; IntAct=EBI-744471, EBI-11062258; O43167; Q92997: DVL3; NbExp=3; IntAct=EBI-744471, EBI-739789; O43167; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-744471, EBI-11977403; O43167; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-744471, EBI-2548508; O43167; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-744471, EBI-5916454; O43167; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-744471, EBI-2549423; O43167; Q9UIH9: KLF15; NbExp=10; IntAct=EBI-744471, EBI-2796400; O43167; O00505: KPNA3; NbExp=3; IntAct=EBI-744471, EBI-358297; O43167; Q6A162: KRT40; NbExp=3; IntAct=EBI-744471, EBI-10171697; O43167; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-744471, EBI-10172150; O43167; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-744471, EBI-12012928; O43167; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-744471, EBI-10172290; O43167; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-744471, EBI-10171774; O43167; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-744471, EBI-10172052; O43167; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-744471, EBI-14065470; O43167; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-744471, EBI-10172511; O43167; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-744471, EBI-3958099; O43167; O95751: LDOC1; NbExp=7; IntAct=EBI-744471, EBI-740738; O43167; Q68G74: LHX8; NbExp=3; IntAct=EBI-744471, EBI-8474075; O43167; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-744471, EBI-739832; O43167; Q8N456: LRRC18; NbExp=3; IntAct=EBI-744471, EBI-751373; O43167; D6RGH6: MCIDAS; NbExp=3; IntAct=EBI-744471, EBI-3954372; O43167; Q99750: MDFI; NbExp=11; IntAct=EBI-744471, EBI-724076; O43167; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-744471, EBI-10172526; O43167; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-744471, EBI-9640281; O43167; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-744471, EBI-713786; O43167; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-744471, EBI-79165; O43167; Q7Z3K3: POGZ; NbExp=8; IntAct=EBI-744471, EBI-1389308; O43167; P78424: POU6F2; NbExp=3; IntAct=EBI-744471, EBI-12029004; O43167; Q53GL6: RALY; NbExp=3; IntAct=EBI-744471, EBI-9512693; O43167; P98175: RBM10; NbExp=3; IntAct=EBI-744471, EBI-721525; O43167; Q96LM5: SPMIP2; NbExp=3; IntAct=EBI-744471, EBI-12020542; O43167; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-744471, EBI-2212028; O43167; Q08117: TLE5; NbExp=3; IntAct=EBI-744471, EBI-717810; O43167; Q08117-2: TLE5; NbExp=3; IntAct=EBI-744471, EBI-11741437; O43167; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-744471, EBI-12155101; O43167; Q12933: TRAF2; NbExp=3; IntAct=EBI-744471, EBI-355744; O43167; O94972: TRIM37; NbExp=3; IntAct=EBI-744471, EBI-741602; O43167; Q8WV44: TRIM41; NbExp=6; IntAct=EBI-744471, EBI-725997; O43167; Q9Y3Q8: TSC22D4; NbExp=6; IntAct=EBI-744471, EBI-739485; O43167; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-744471, EBI-744794; O43167; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-744471, EBI-947459; O43167; O43298: ZBTB43; NbExp=3; IntAct=EBI-744471, EBI-740718; O43167; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-744471, EBI-742740; O43167; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-744471, EBI-395708; O43167; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-744471, EBI-12949277; O43167; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-744471, EBI-11035148; O43167; Q9UID6: ZNF639; NbExp=3; IntAct=EBI-744471, EBI-947476; O43167; Q9NQZ8: ZNF71; NbExp=4; IntAct=EBI-744471, EBI-7138235; O43167; Q15937: ZNF79; NbExp=3; IntAct=EBI-744471, EBI-10237274; O43167; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-744471, EBI-10240849; O43167; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-744471, EBI-11962574; O43167; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-744471, EBI-527853; O43167-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-25842419, EBI-10976677; O43167-2; P28799: GRN; NbExp=3; IntAct=EBI-25842419, EBI-747754; O43167-2; P42858: HTT; NbExp=9; IntAct=EBI-25842419, EBI-466029; O43167-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25842419, EBI-10975473; O43167-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-25842419, EBI-21251460; O43167-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25842419, EBI-396669; O43167-2; P37840: SNCA; NbExp=3; IntAct=EBI-25842419, EBI-985879; O43167-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25842419, EBI-5235340; O43167-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-25842419, EBI-372899; O43167-2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-25842419, EBI-12806590; O43167-2; O76024: WFS1; NbExp=3; IntAct=EBI-25842419, EBI-720609; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43167-1; Sequence=Displayed; Name=2; IsoId=O43167-2; Sequence=VSP_016221, VSP_016222; Widely expressed, with highest levels in naive B- cells. Regulated expression during B-cell differentiation. Low expression in pro-B cells, pre-B I cells and large pre-B II cells. Levels peak in small pre-B II and then slightly decrease in immature B-cells. Low levels in CD34+ umbilical cord blood cells. Immunodeficiency-centromeric instability-facial anomalies syndrome 2 (ICF2) [MIM:614069]: A rare disorder characterized by a variable immunodeficiency resulting in recurrent infections, facial anomalies, and branching of chromosomes 1, 9, and 16. Other variable symptoms include growth retardation, failure to thrive, and psychomotor retardation. Laboratory studies show limited hypomethylation of DNA in a small fraction of the genome in some, but not all, patients. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=BAA23713.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=Undiagnosed Disease Network; Note=ZBTB24; URL="https://undiagnosed.hms.harvard.edu/updates/genes-of-interest/zbtb24-gene/"; negative regulation of transcription from RNA polymerase II promoter RNA polymerase II transcription factor activity, sequence-specific DNA binding hematopoietic progenitor cell differentiation nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm transcription regulatory region DNA binding positive regulation of transcription from RNA polymerase II promoter metal ion binding uc003ptl.1 uc003ptl.2 uc003ptl.3 
ENST00000230124.8 FIG4 ENST00000230124.8 FIG4 phosphoinositide 5-phosphatase (from RefSeq NM_014845.6) ENST00000230124.1 ENST00000230124.2 ENST00000230124.3 ENST00000230124.4 ENST00000230124.5 ENST00000230124.6 ENST00000230124.7 FIG4 FIG4_HUMAN KIAA0274 NM_014845 Q53H49 Q5TCS6 Q92562 SAC3 uc003ptt.1 uc003ptt.2 uc003ptt.3 uc003ptt.4 The protein encoded by this gene belongs to the SAC domain-containing protein gene family. The SAC domain, approximately 400 amino acids in length and consisting of seven conserved motifs, has been shown to possess phosphoinositide phosphatase activity. The yeast homolog, Sac1p, is involved in the regulation of various phosphoinositides, and affects diverse cellular functions such as actin cytoskeleton organization, Golgi function, and maintenance of vacuole morphology. Membrane-bound phosphoinositides function as signaling molecules and play a key role in vesicle trafficking in eukaryotic cells. Mutations in this gene have been associated with Charcot-Marie-Tooth disease, type 4J. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK291671.1, D87464.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230124.8/ ENSP00000230124.4 RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Dual specificity phosphatase component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:17556371, PubMed:33098764). Catalyzes the dephosphorylation of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) to form phosphatidylinositol 3-phosphate (PubMed:33098764). Has serine-protein phosphatase activity acting on PIKfyve to stimulate its lipid kinase activity, its catalytically activity being required for maximal PI(3,5)P2 production (PubMed:33098764). In vitro, hydrolyzes all three D5-phosphorylated polyphosphoinositide and although displaying preferences for PtdIns(3,5)P2, it is capable of hydrolyzing PtdIns(3,4,5)P3 and PtdIns(4,5)P2, at least in vitro (PubMed:17556371). Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5- bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:32955, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57923, ChEBI:CHEBI:58088; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32956; Evidence=; Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765; Evidence=; Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5- trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:57836; EC=3.1.3.86; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529; Evidence=; Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence=; Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14 nucleates the assembly of the complex and serves as a scaffold by pentamerizing into a star- shaped structure, which can bind a single copy each of PIKFYVE and FIG4 and coordinates their activities. Q92562; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-4290773, EBI-739467; Q92562; Q08AM6: VAC14; NbExp=5; IntAct=EBI-4290773, EBI-2107455; Endosome membrane Note=Localization requires VAC14 and PIKFYVE. Charcot-Marie-Tooth disease 4J (CMT4J) [MIM:611228]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie- Tooth disease are designated CMT4. te=The disease is caused by variants affecting the gene represented in this entry. Amyotrophic lateral sclerosis 11 (ALS11) [MIM:612577]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Note=The disease is caused by variants affecting the gene represented in this entry. Yunis-Varon syndrome (YVS) [MIM:216340]: A severe autosomal recessive disorder characterized by skeletal defects, including cleidocranial dysplasia and digital anomalies, and severe neurologic involvement with neuronal loss. Enlarged cytoplasmic vacuoles are found in neurons, muscle, and cartilage. The disorder is usually lethal in infancy. Note=The disease is caused by variants affecting the gene represented in this entry. Polymicrogyria, bilateral temporooccipital (BTOP) [MIM:612691]: A disease characterized by temporo-occipital polymicrogyria, psychiatric manifestations, and epilepsy. Note=The disease is caused by variants affecting the gene represented in this entry. Sequence=BAA13403.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Golgi membrane phosphatidylinositol-3-phosphatase activity protein binding endosome endoplasmic reticulum Golgi apparatus lipid particle phosphatidylinositol biosynthetic process vacuole organization locomotory behavior endosome membrane positive regulation of neuron projection development membrane dephosphorylation hydrolase activity negative regulation of myelination early endosome membrane late endosome membrane myelin assembly phosphatidylinositol bisphosphate phosphatase activity phosphatidylinositol-3-phosphate biosynthetic process phosphoric ester hydrolase activity intracellular membrane-bounded organelle pigmentation phosphatidylinositol-4-phosphate phosphatase activity phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity phosphatidylinositol metabolic process neuron development recycling endosome uc003ptt.1 uc003ptt.2 uc003ptt.3 uc003ptt.4 
ENST00000230221.5 OR14J1 ENST00000230221.5 olfactory receptor family 14 subfamily J member 1 (from RefSeq NM_030946.2) A2BEC2 B0V078 ENST00000230221.1 ENST00000230221.2 ENST00000230221.3 ENST00000230221.4 NM_030946 O14J1_HUMAN OR5U1 Q5ST27 Q9UGF5 uc302whl.1 Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms. [provided by RefSeq, Jul 2008]. ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Odorant receptor. Cell membrane; Multi-pass membrane protein. Belongs to the G-protein coupled receptor 1 family. Name=Human Olfactory Receptor Data Exploratorium (HORDE); URL="http://genome.weizmann.ac.il/horde/card/index/symbol:OR14J1"; G-protein coupled receptor activity olfactory receptor activity odorant binding plasma membrane signal transduction G-protein coupled receptor signaling pathway sensory perception of smell membrane integral component of membrane response to stimulus detection of chemical stimulus involved in sensory perception of smell uc302whl.1 
ENST00000230236.4 HSD17B8 ENST00000230236.4 hydroxysteroid 17-beta dehydrogenase 8 (from RefSeq NM_014234.5) A6NLX7 DHB8_HUMAN ENST00000230236.1 ENST00000230236.2 ENST00000230236.3 FABGL HKE6 NM_014234 Q5STP7 Q92506 Q9UIQ1 RING2 SDR30C1 uc302whn.1 In mice, the Ke6 protein is a 17-beta-hydroxysteroid dehydrogenase that can regulate the concentration of biologically active estrogens and androgens. It is preferentially an oxidative enzyme and inactivates estradiol, testosterone, and dihydrotestosterone. However, the enzyme has some reductive activity and can synthesize estradiol from estrone. The protein encoded by this gene is similar to Ke6 and is a member of the short-chain dehydrogenase superfamily. An alternatively spliced transcript of this gene has been detected, but the full-length nature of this variant has not been determined. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.81525.1, BC008185.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968832 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000374662.4/ ENSP00000363794.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Required for the solubility and assembly of the heterotetramer 3-ketoacyl-[acyl carrier protein] (ACP) reductase functional complex (KAR or KAR1) that forms part of the mitochondrial fatty acid synthase (mtFAS). Alpha-subunit of the KAR complex that acts as a scaffold protein required for the stability of carbonyl reductase type-4 (CBR4, beta-subunit of the KAR complex) and for its 3-ketoacyl- ACP reductase activity, thereby participating in mitochondrial fatty acid biosynthesis. Catalyzes the NAD-dependent conversion of (3R)-3- hydroxyacyl-CoA into 3-ketoacyl-CoA (3-oxoacyl-CoA) with no chain length preference; this enzymatic activity is not needed for the KAR function (PubMed:19571038, PubMed:25203508, PubMed:30508570). Prefers (3R)-3-hydroxyacyl-CoA over (3S)-3-hydroxyacyl-CoA and displays enzymatic activity only in the presence of NAD(+) (PubMed:19571038). Cooperates with enoyl-CoA hydratase 1 in mitochondria, together they constitute an alternative route to the auxiliary enzyme pathways for the breakdown of Z-PUFA (cis polyunsaturated fatty acid) enoyl-esters (Probable) (PubMed:30508570). NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol (17beta-estradiol or E2). Has very low activity towards testosterone and dihydrotestosterone (17beta-hydroxy-5alpha-androstan-3-one). Primarily an oxidative enzyme, it can switch to a reductive mode determined in the appropriate physiologic milieu and catalyze the reduction of estrone (E1) to form biologically active 17beta-estradiol (PubMed:17978863). Reaction=a (3R)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:32711, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.n12; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32712; Evidence=; Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24614; Evidence=; Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.239; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930; Evidence=; Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha- androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41993; Evidence=; Steroid biosynthesis; estrogen biosynthesis. Lipid metabolism; fatty acid biosynthesis. Lipid metabolism; mitochondrial fatty acid beta-oxidation. Heterotetramer with CBR4; contains two molecules of HSD17B8 and CBR4. Mitochondrion matrix Widely expressed, particularly abundant in prostate, placenta and kidney (PubMed:17978863). Expressed at protein level in various tissues like brain, cerebellum, heart, lung, kidney, ovary, testis, adrenals and prostate (PubMed:30508570). Up-regulated by estradiol. The fatty acyl-CoA dehydrogenase activity is several thousand times higher than the estradiol and testosterone 17beta- hydroxysteroid dehydrogenase conversion. Belongs to the short-chain dehydrogenases/reductases (SDR) family. 3-hydroxyacyl-CoA dehydrogenase activity estradiol 17-beta-dehydrogenase activity protein binding mitochondrion mitochondrial envelope mitochondrial matrix plasma membrane lipid metabolic process fatty acid metabolic process fatty acid biosynthetic process steroid biosynthetic process estrogen biosynthetic process androgen metabolic process estrogen metabolic process membrane oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor fatty-acyl-CoA biosynthetic process 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity testosterone dehydrogenase (NAD+) activity quinone binding protein heterotetramerization oxidation-reduction process NADH binding uc302whn.1 
ENST00000230256.8 UNC93A ENST00000230256.8 unc-93 homolog A, transcript variant 1 (from RefSeq NM_018974.4) B3KRP5 ENST00000230256.1 ENST00000230256.2 ENST00000230256.3 ENST00000230256.4 ENST00000230256.5 ENST00000230256.6 ENST00000230256.7 NM_018974 Q4QQJ4 Q5JZD6 Q86WB7 UN93A_HUMAN uc003qvq.1 uc003qvq.2 uc003qvq.3 uc003qvq.4 uc003qvq.5 Q86WB7-2; O95870: ABHD16A; NbExp=3; IntAct=EBI-13356252, EBI-348517; Q86WB7-2; Q13520: AQP6; NbExp=3; IntAct=EBI-13356252, EBI-13059134; Q86WB7-2; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-13356252, EBI-12069500; Q86WB7-2; P13236: CCL4; NbExp=3; IntAct=EBI-13356252, EBI-2873970; Q86WB7-2; Q08708: CD300C; NbExp=3; IntAct=EBI-13356252, EBI-3915344; Q86WB7-2; O14735: CDIPT; NbExp=3; IntAct=EBI-13356252, EBI-358858; Q86WB7-2; P48165: GJA8; NbExp=3; IntAct=EBI-13356252, EBI-17458373; Q86WB7-2; Q96P66: GPR101; NbExp=3; IntAct=EBI-13356252, EBI-17935713; Q86WB7-2; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-13356252, EBI-11955647; Q86WB7-2; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-13356252, EBI-12133176; Q86WB7-2; Q02094: RHAG; NbExp=3; IntAct=EBI-13356252, EBI-14772355; Q86WB7-2; Q6ICL7: SLC35E4; NbExp=3; IntAct=EBI-13356252, EBI-12867720; Q86WB7-2; Q92504: SLC39A7; NbExp=3; IntAct=EBI-13356252, EBI-1051105; Q86WB7-2; Q6P1K1: SLC48A1; NbExp=3; IntAct=EBI-13356252, EBI-1222191; Q86WB7-2; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-13356252, EBI-12187159; Q86WB7-2; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-13356252, EBI-6268651; Q86WB7-2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-13356252, EBI-8638294; Q86WB7-2; Q96Q45-2: TMEM237; NbExp=6; IntAct=EBI-13356252, EBI-10982110; Q86WB7-2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-13356252, EBI-6447886; Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q86WB7-1; Sequence=Displayed; Name=2; IsoId=Q86WB7-2; Sequence=VSP_042772; Expressed in testis, small intestine, spleen, prostate and ovary. Although UNC93A gene is located in a region of the genome frequently associated with ovarian cancer, no evidence have been found for a tumor suppressor function. Belongs to the unc-93 family. molecular_function plasma membrane biological_process membrane integral component of membrane uc003qvq.1 uc003qvq.2 uc003qvq.3 uc003qvq.4 uc003qvq.5 
ENST00000230301.9 C6orf118 ENST00000230301.9 chromosome 6 open reading frame 118 (from RefSeq NM_144980.4) CF118_HUMAN ENST00000230301.1 ENST00000230301.2 ENST00000230301.3 ENST00000230301.4 ENST00000230301.5 ENST00000230301.6 ENST00000230301.7 ENST00000230301.8 NM_144980 Q5T5N4 Q8TC11 uc003qum.1 uc003qum.2 uc003qum.3 uc003qum.4 uc003qum.5 uc003qum.6 uc003qum.1 uc003qum.2 uc003qum.3 uc003qum.4 uc003qum.5 uc003qum.6 
ENST00000230321.11 MDFI ENST00000230321.11 MyoD family inhibitor, transcript variant 3 (from RefSeq NM_005586.4) ENST00000230321.1 ENST00000230321.10 ENST00000230321.2 ENST00000230321.3 ENST00000230321.4 ENST00000230321.5 ENST00000230321.6 ENST00000230321.7 ENST00000230321.8 ENST00000230321.9 MDFI_HUMAN NM_005586 Q99750 uc003oqq.1 uc003oqq.2 uc003oqq.3 uc003oqq.4 uc003oqq.5 uc003oqq.6 This protein is a transcription factor that negatively regulates other myogenic family proteins. Studies of the mouse homolog, I-mf, show that it interferes with myogenic factor function by masking nuclear localization signals and preventing DNA binding. Knockout mouse studies show defects in the formation of vertebrae and ribs that also involve cartilage formation in these structures. [provided by RefSeq, Jul 2008]. Inhibits the transactivation activity of the Myod family of myogenic factors and represses myogenesis. Acts by associating with Myod family members and retaining them in the cytoplasm by masking their nuclear localization signals. Can also interfere with the DNA- binding activity of Myod family members. Plays an important role in trophoblast and chondrogenic differentiation. Regulates the transcriptional activity of TCF7L1/TCF3 by interacting directly with TCF7L1/TCF3 and preventing it from binding DNA. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways (By similarity). The C-terminus interacts with AXIN1 and LEF1 (By similarity). Interacts with CCNT2 (PubMed:17289077). Q99750; Q16613: AANAT; NbExp=6; IntAct=EBI-724076, EBI-7451846; Q99750; A0A0S2Z645: ABCF3; NbExp=3; IntAct=EBI-724076, EBI-16432404; Q99750; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-724076, EBI-12318443; Q99750; P82987: ADAMTSL3; NbExp=6; IntAct=EBI-724076, EBI-10221726; Q99750; P18825: ADRA2C; NbExp=3; IntAct=EBI-724076, EBI-12015266; Q99750; Q6ZN18-2: AEBP2; NbExp=3; IntAct=EBI-724076, EBI-10255023; Q99750; P21549: AGXT; NbExp=5; IntAct=EBI-724076, EBI-727098; Q99750; Q02040-3: AKAP17A; NbExp=3; IntAct=EBI-724076, EBI-10222656; Q99750; Q9XRX5-2: ANKRD13C-DT; NbExp=3; IntAct=EBI-724076, EBI-12051311; Q99750; P29972: AQP1; NbExp=7; IntAct=EBI-724076, EBI-745213; Q99750; P55064: AQP5; NbExp=3; IntAct=EBI-724076, EBI-746103; Q99750; A7KAX9: ARHGAP32; NbExp=3; IntAct=EBI-724076, EBI-308663; Q99750; Q03989: ARID5A; NbExp=5; IntAct=EBI-724076, EBI-948603; Q99750; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-724076, EBI-742909; Q99750; Q7L5A3: ATOSB; NbExp=4; IntAct=EBI-724076, EBI-745689; Q99750; P30049: ATP5F1D; NbExp=3; IntAct=EBI-724076, EBI-1049505; Q99750; Q5T686: AVPI1; NbExp=7; IntAct=EBI-724076, EBI-8640233; Q99750; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-724076, EBI-16429430; Q99750; O15169: AXIN1; NbExp=3; IntAct=EBI-724076, EBI-710484; Q99750; O95817: BAG3; NbExp=3; IntAct=EBI-724076, EBI-747185; Q99750; Q8TBE0: BAHD1; NbExp=7; IntAct=EBI-724076, EBI-742750; Q99750; A0A0S2Z5G4: BANP; NbExp=3; IntAct=EBI-724076, EBI-16429704; Q99750; B4DE54: BANP; NbExp=3; IntAct=EBI-724076, EBI-16429313; Q99750; Q8N9N5-2: BANP; NbExp=6; IntAct=EBI-724076, EBI-11524452; Q99750; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-724076, EBI-16429296; Q99750; Q9BXC9: BBS2; NbExp=7; IntAct=EBI-724076, EBI-748297; Q99750; P50895: BCAM; NbExp=3; IntAct=EBI-724076, EBI-10212133; Q99750; A8KA13: BCL6B; NbExp=3; IntAct=EBI-724076, EBI-10174813; Q99750; Q9HBH7: BEX1; NbExp=6; IntAct=EBI-724076, EBI-7162175; Q99750; Q9BXY8: BEX2; NbExp=4; IntAct=EBI-724076, EBI-745073; Q99750; Q00994: BEX3; NbExp=3; IntAct=EBI-724076, EBI-741753; Q99750; Q5T681: C10orf62; NbExp=7; IntAct=EBI-724076, EBI-744052; Q99750; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-724076, EBI-747505; Q99750; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-724076, EBI-7317823; Q99750; Q9H7E9: C8orf33; NbExp=5; IntAct=EBI-724076, EBI-715389; Q99750; Q96LL4: C8orf48; NbExp=6; IntAct=EBI-724076, EBI-751596; Q99750; Q8NEC5: CATSPER1; NbExp=4; IntAct=EBI-724076, EBI-744545; Q99750; O43439: CBFA2T2; NbExp=4; IntAct=EBI-724076, EBI-748628; Q99750; Q8N7E2: CBLL2; NbExp=3; IntAct=EBI-724076, EBI-12196065; Q99750; Q14781: CBX2; NbExp=3; IntAct=EBI-724076, EBI-745934; Q99750; Q14781-2: CBX2; NbExp=3; IntAct=EBI-724076, EBI-11974585; Q99750; Q9HC52: CBX8; NbExp=3; IntAct=EBI-724076, EBI-712912; Q99750; Q5T0F9: CC2D1B; NbExp=3; IntAct=EBI-724076, EBI-10245204; Q99750; Q5T0F9-3: CC2D1B; NbExp=3; IntAct=EBI-724076, EBI-13176876; Q99750; Q8IYX3: CCDC116; NbExp=7; IntAct=EBI-724076, EBI-744311; Q99750; Q8N715: CCDC185; NbExp=4; IntAct=EBI-724076, EBI-740814; Q99750; Q9NVL8: CCDC198; NbExp=3; IntAct=EBI-724076, EBI-10238351; Q99750; Q96S94-5: CCNL2; NbExp=3; IntAct=EBI-724076, EBI-12024864; Q99750; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-724076, EBI-11983537; Q99750; Q16543: CDC37; NbExp=3; IntAct=EBI-724076, EBI-295634; Q99750; Q96GN5: CDCA7L; NbExp=6; IntAct=EBI-724076, EBI-5278764; Q99750; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-724076, EBI-3919850; Q99750; Q8IYX8: CEP57L1; NbExp=6; IntAct=EBI-724076, EBI-1104570; Q99750; O43745: CHP2; NbExp=3; IntAct=EBI-724076, EBI-8525536; Q99750; P07510-2: CHRNG; NbExp=6; IntAct=EBI-724076, EBI-11979451; Q99750; A8MYP8: CIMAP1B; NbExp=3; IntAct=EBI-724076, EBI-12010090; Q99750; Q8NE01: CNNM3; NbExp=6; IntAct=EBI-724076, EBI-741032; Q99750; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-724076, EBI-739773; Q99750; Q02930-3: CREB5; NbExp=8; IntAct=EBI-724076, EBI-10192698; Q99750; P06850: CRH; NbExp=3; IntAct=EBI-724076, EBI-3870390; Q99750; Q9Y6M4-3: CSNK1G3; NbExp=3; IntAct=EBI-724076, EBI-11045281; Q99750; Q99895: CTRC; NbExp=3; IntAct=EBI-724076, EBI-10295404; Q99750; Q6DCB0: DAAM2; NbExp=3; IntAct=EBI-724076, EBI-10249414; Q99750; Q8NFT6-2: DBF4B; NbExp=3; IntAct=EBI-724076, EBI-12205861; Q99750; Q58WW2: DCAF6; NbExp=3; IntAct=EBI-724076, EBI-2559044; Q99750; Q5TAQ9: DCAF8; NbExp=6; IntAct=EBI-724076, EBI-740686; Q99750; Q8TF63: DCANP1; NbExp=7; IntAct=EBI-724076, EBI-10275670; Q99750; Q96LJ7: DHRS1; NbExp=4; IntAct=EBI-724076, EBI-746300; Q99750; O94907: DKK1; NbExp=4; IntAct=EBI-724076, EBI-742864; Q99750; Q9NQL9: DMRT3; NbExp=6; IntAct=EBI-724076, EBI-9679045; Q99750; P59910: DNAJB13; NbExp=3; IntAct=EBI-724076, EBI-11514233; Q99750; Q9Y6K1: DNMT3A; NbExp=3; IntAct=EBI-724076, EBI-923653; Q99750; Q92608: DOCK2; NbExp=8; IntAct=EBI-724076, EBI-448771; Q99750; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-724076, EBI-10694655; Q99750; Q5JR98: DYNLT4; NbExp=3; IntAct=EBI-724076, EBI-4311709; Q99750; O95967: EFEMP2; NbExp=3; IntAct=EBI-724076, EBI-743414; Q99750; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-724076, EBI-10232522; Q99750; Q14241: ELOA; NbExp=6; IntAct=EBI-724076, EBI-742350; Q99750; Q9H0I2: ENKD1; NbExp=8; IntAct=EBI-724076, EBI-744099; Q99750; Q92731-3: ESR2; NbExp=3; IntAct=EBI-724076, EBI-12259414; Q99750; Q0VG06-3: FAAP100; NbExp=3; IntAct=EBI-724076, EBI-10226932; Q99750; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-724076, EBI-3943864; Q99750; Q5T036: FAM120AOS; NbExp=3; IntAct=EBI-724076, EBI-12420808; Q99750; Q9H5Z6: FAM124B; NbExp=4; IntAct=EBI-724076, EBI-741626; Q99750; Q3B820: FAM161A; NbExp=6; IntAct=EBI-724076, EBI-719941; Q99750; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-724076, EBI-7225287; Q99750; Q08E93: FAM27E3; NbExp=3; IntAct=EBI-724076, EBI-2602739; Q99750; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-724076, EBI-6658203; Q99750; O95363: FARS2; NbExp=3; IntAct=EBI-724076, EBI-2513774; Q99750; Q96D16: FBXL18; NbExp=5; IntAct=EBI-724076, EBI-744419; Q99750; Q9NWN3: FBXO34; NbExp=3; IntAct=EBI-724076, EBI-719816; Q99750; A0PJY2: FEZF1; NbExp=3; IntAct=EBI-724076, EBI-11988727; Q99750; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-724076, EBI-744935; Q99750; Q12950: FOXD4; NbExp=3; IntAct=EBI-724076, EBI-11317801; Q99750; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-724076, EBI-11320806; Q99750; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-724076, EBI-11961494; Q99750; Q3SYB3: FOXD4L6; NbExp=6; IntAct=EBI-724076, EBI-6425864; Q99750; O14764: GABRD; NbExp=3; IntAct=EBI-724076, EBI-744352; Q99750; P15976-2: GATA1; NbExp=5; IntAct=EBI-724076, EBI-9090198; Q99750; P23769: GATA2; NbExp=4; IntAct=EBI-724076, EBI-2806671; Q99750; Q99988: GDF15; NbExp=5; IntAct=EBI-724076, EBI-2116863; Q99750; P04899: GNAI2; NbExp=5; IntAct=EBI-724076, EBI-353997; Q99750; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-724076, EBI-11975289; Q99750; P63218: GNG5; NbExp=3; IntAct=EBI-724076, EBI-10220734; Q99750; O95872: GPANK1; NbExp=3; IntAct=EBI-724076, EBI-751540; Q99750; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-724076, EBI-5666657; Q99750; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-724076, EBI-11959863; Q99750; O60565: GREM1; NbExp=3; IntAct=EBI-724076, EBI-944395; Q99750; Q9Y5Q8: GTF3C5; NbExp=3; IntAct=EBI-724076, EBI-1045409; Q99750; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-724076, EBI-11956675; Q99750; Q8TF76: HASPIN; NbExp=3; IntAct=EBI-724076, EBI-1237328; Q99750; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-724076, EBI-10188461; Q99750; B4DNA4: hCG_20425; NbExp=3; IntAct=EBI-724076, EBI-7399002; Q99750; Q9NQ87: HEYL; NbExp=7; IntAct=EBI-724076, EBI-751092; Q99750; Q03014: HHEX; NbExp=3; IntAct=EBI-724076, EBI-747421; Q99750; Q8WVV9: HNRNPLL; NbExp=4; IntAct=EBI-724076, EBI-535849; Q99750; P49639: HOXA1; NbExp=7; IntAct=EBI-724076, EBI-740785; Q99750; P17482: HOXB9; NbExp=6; IntAct=EBI-724076, EBI-745290; Q99750; P37235: HPCAL1; NbExp=3; IntAct=EBI-724076, EBI-749311; Q99750; P28222: HTR1B; NbExp=7; IntAct=EBI-724076, EBI-1056863; Q99750; Q12894: IFRD2; NbExp=3; IntAct=EBI-724076, EBI-2512448; Q99750; Q8NA54: IQUB; NbExp=3; IntAct=EBI-724076, EBI-10220600; Q99750; P16144-2: ITGB4; NbExp=3; IntAct=EBI-724076, EBI-11051601; Q99750; Q15040: JOSD1; NbExp=3; IntAct=EBI-724076, EBI-2510602; Q99750; Q92993: KAT5; NbExp=3; IntAct=EBI-724076, EBI-399080; Q99750; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-724076, EBI-11954971; Q99750; A0A384DVV8: KIAA0040; NbExp=6; IntAct=EBI-724076, EBI-20764875; Q99750; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-724076, EBI-6426443; Q99750; P52292: KPNA2; NbExp=3; IntAct=EBI-724076, EBI-349938; Q99750; Q7Z794: KRT77; NbExp=3; IntAct=EBI-724076, EBI-3045529; Q99750; A0A0S2Z3Z3: LAMB3; NbExp=3; IntAct=EBI-724076, EBI-16435132; Q99750; Q14847: LASP1; NbExp=3; IntAct=EBI-724076, EBI-742828; Q99750; Q14847-2: LASP1; NbExp=3; IntAct=EBI-724076, EBI-9088686; Q99750; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-724076, EBI-11962058; Q99750; Q5T7P3: LCE1B; NbExp=4; IntAct=EBI-724076, EBI-10245913; Q99750; Q5T752: LCE1D; NbExp=3; IntAct=EBI-724076, EBI-11741311; Q99750; Q5T754: LCE1F; NbExp=3; IntAct=EBI-724076, EBI-11958008; Q99750; O14633: LCE2B; NbExp=3; IntAct=EBI-724076, EBI-11478468; Q99750; Q5TA76: LCE3A; NbExp=5; IntAct=EBI-724076, EBI-9394625; Q99750; Q5T5A8: LCE3C; NbExp=5; IntAct=EBI-724076, EBI-10245291; Q99750; Q9BYE3: LCE3D; NbExp=4; IntAct=EBI-724076, EBI-6658837; Q99750; Q5T5B0: LCE3E; NbExp=8; IntAct=EBI-724076, EBI-10245456; Q99750; Q5TA78: LCE4A; NbExp=6; IntAct=EBI-724076, EBI-10246358; Q99750; Q7Z4I7-5: LIMS2; NbExp=3; IntAct=EBI-724076, EBI-10257651; Q99750; O14910: LIN7A; NbExp=3; IntAct=EBI-724076, EBI-2513988; Q99750; O75427: LRCH4; NbExp=3; IntAct=EBI-724076, EBI-718707; Q99750; Q8TD91-2: MAGEC3; NbExp=3; IntAct=EBI-724076, EBI-10694180; Q99750; Q9Y5V3: MAGED1; NbExp=6; IntAct=EBI-724076, EBI-716006; Q99750; Q9HAY2: MAGEF1; NbExp=4; IntAct=EBI-724076, EBI-5525855; Q99750; P28482: MAPK1; NbExp=3; IntAct=EBI-724076, EBI-959949; Q99750; O60336: MAPKBP1; NbExp=6; IntAct=EBI-724076, EBI-947402; Q99750; Q8NHZ7: MBD3L2; NbExp=3; IntAct=EBI-724076, EBI-11989378; Q99750; Q99750: MDFI; NbExp=4; IntAct=EBI-724076, EBI-724076; Q99750; Q9H7H0: METTL17; NbExp=5; IntAct=EBI-724076, EBI-749353; Q99750; Q9H7H0-2: METTL17; NbExp=6; IntAct=EBI-724076, EBI-11098807; Q99750; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-724076, EBI-14086479; Q99750; P50539-3: MXI1; NbExp=3; IntAct=EBI-724076, EBI-10211940; Q99750; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-724076, EBI-2858213; Q99750; Q92692: NECTIN2; NbExp=4; IntAct=EBI-724076, EBI-718419; Q99750; Q92692-2: NECTIN2; NbExp=3; IntAct=EBI-724076, EBI-6979889; Q99750; Q8WWR8: NEU4; NbExp=4; IntAct=EBI-724076, EBI-746964; Q99750; Q86XR2: NIBAN3; NbExp=3; IntAct=EBI-724076, EBI-2796690; Q99750; Q969G9: NKD1; NbExp=3; IntAct=EBI-724076, EBI-1538217; Q99750; Q9NQX5: NPDC1; NbExp=8; IntAct=EBI-724076, EBI-748927; Q99750; Q8NDH3-5: NPEPL1; NbExp=3; IntAct=EBI-724076, EBI-12329915; Q99750; F1D8P7: NR1H2; NbExp=6; IntAct=EBI-724076, EBI-10177172; Q99750; P55055: NR1H2; NbExp=3; IntAct=EBI-724076, EBI-745354; Q99750; Q13133: NR1H3; NbExp=3; IntAct=EBI-724076, EBI-781356; Q99750; Q13133-2: NR1H3; NbExp=3; IntAct=EBI-724076, EBI-12699353; Q99750; Q13133-3: NR1H3; NbExp=3; IntAct=EBI-724076, EBI-11952806; Q99750; Q96L73-2: NSD1; NbExp=3; IntAct=EBI-724076, EBI-11110981; Q99750; Q9Y5Y2: NUBP2; NbExp=3; IntAct=EBI-724076, EBI-1048886; Q99750; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-724076, EBI-1210753; Q99750; Q17RF5: ODAPH; NbExp=6; IntAct=EBI-724076, EBI-10239029; Q99750; Q14990: ODF1; NbExp=3; IntAct=EBI-724076, EBI-10234557; Q99750; Q7RTU3: OLIG3; NbExp=6; IntAct=EBI-724076, EBI-10225049; Q99750; P32242: OTX1; NbExp=9; IntAct=EBI-724076, EBI-740446; Q99750; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-724076, EBI-11022007; Q99750; Q96AQ6: PBXIP1; NbExp=4; IntAct=EBI-724076, EBI-740845; Q99750; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-724076, EBI-11956269; Q99750; P04085-2: PDGFA; NbExp=3; IntAct=EBI-724076, EBI-11995148; Q99750; Q14554: PDIA5; NbExp=3; IntAct=EBI-724076, EBI-953879; Q99750; Q29RF7-3: PDS5A; NbExp=3; IntAct=EBI-724076, EBI-12067280; Q99750; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-724076, EBI-448407; Q99750; O43189: PHF1; NbExp=3; IntAct=EBI-724076, EBI-530034; Q99750; A2BDE7: PHLDA1; NbExp=3; IntAct=EBI-724076, EBI-14084211; Q99750; Q8WV24: PHLDA1; NbExp=3; IntAct=EBI-724076, EBI-738731; Q99750; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-724076, EBI-14066006; Q99750; Q7Z2X4: PID1; NbExp=3; IntAct=EBI-724076, EBI-10256685; Q99750; Q9HB75: PIDD1; NbExp=3; IntAct=EBI-724076, EBI-520427; Q99750; Q8WWB5: PIH1D2; NbExp=6; IntAct=EBI-724076, EBI-10232538; Q99750; Q13526: PIN1; NbExp=7; IntAct=EBI-724076, EBI-714158; Q99750; P78337: PITX1; NbExp=3; IntAct=EBI-724076, EBI-748265; Q99750; Q13563: PKD2; NbExp=3; IntAct=EBI-724076, EBI-7813714; Q99750; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-724076, EBI-949255; Q99750; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-724076, EBI-10320765; Q99750; O43741: PRKAB2; NbExp=12; IntAct=EBI-724076, EBI-1053424; Q99750; Q99633: PRPF18; NbExp=3; IntAct=EBI-724076, EBI-2798416; Q99750; Q8WWY3: PRPF31; NbExp=5; IntAct=EBI-724076, EBI-1567797; Q99750; Q9NV39: PRR34; NbExp=3; IntAct=EBI-724076, EBI-11959565; Q99750; Q13308: PTK7; NbExp=3; IntAct=EBI-724076, EBI-2803245; Q99750; Q8WUK0: PTPMT1; NbExp=7; IntAct=EBI-724076, EBI-7199479; Q99750; Q3YEC7: RABL6; NbExp=2; IntAct=EBI-724076, EBI-742029; Q99750; P63000: RAC1; NbExp=3; IntAct=EBI-724076, EBI-413628; Q99750; Q9Y272: RASD1; NbExp=5; IntAct=EBI-724076, EBI-740818; Q99750; Q06141: REG3A; NbExp=3; IntAct=EBI-724076, EBI-10223932; Q99750; Q96EN9: REX1BD; NbExp=6; IntAct=EBI-724076, EBI-745810; Q99750; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-724076, EBI-372094; Q99750; Q13671: RIN1; NbExp=3; IntAct=EBI-724076, EBI-366017; Q99750; Q0D2K3: RIPPLY1; NbExp=6; IntAct=EBI-724076, EBI-10226430; Q99750; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-724076, EBI-16428950; Q99750; Q14D33: RTP5; NbExp=6; IntAct=EBI-724076, EBI-10217913; Q99750; Q86UD0: SAPCD2; NbExp=3; IntAct=EBI-724076, EBI-2561646; Q99750; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-724076, EBI-4403649; Q99750; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-724076, EBI-748391; Q99750; Q8WWX9: SELENOM; NbExp=3; IntAct=EBI-724076, EBI-10277687; Q99750; Q13214-2: SEMA3B; NbExp=3; IntAct=EBI-724076, EBI-11017428; Q99750; Q9NUL5: SHFL; NbExp=3; IntAct=EBI-724076, EBI-10313866; Q99750; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-724076, EBI-11955083; Q99750; P34896: SHMT1; NbExp=3; IntAct=EBI-724076, EBI-715117; Q99750; Q15475: SIX1; NbExp=2; IntAct=EBI-724076, EBI-743675; Q99750; Q86YT5: SLC13A5; NbExp=3; IntAct=EBI-724076, EBI-12002412; Q99750; Q8IY34: SLC15A3; NbExp=3; IntAct=EBI-724076, EBI-12179023; Q99750; Q9UBX3: SLC25A10; NbExp=7; IntAct=EBI-724076, EBI-750394; Q99750; Q9UBX3-2: SLC25A10; NbExp=3; IntAct=EBI-724076, EBI-12056597; Q99750; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-724076, EBI-8463848; Q99750; Q96RF0: SNX18; NbExp=3; IntAct=EBI-724076, EBI-298169; Q99750; O14512: SOCS7; NbExp=3; IntAct=EBI-724076, EBI-1539606; Q99750; Q86W54-2: SPATA24; NbExp=3; IntAct=EBI-724076, EBI-12041693; Q99750; Q6RVD6: SPATA8; NbExp=6; IntAct=EBI-724076, EBI-8635958; Q99750; Q9UQ90: SPG7; NbExp=7; IntAct=EBI-724076, EBI-717201; Q99750; Q9P2T0: SPMAP2; NbExp=3; IntAct=EBI-724076, EBI-751020; Q99750; Q96LM5: SPMIP2; NbExp=3; IntAct=EBI-724076, EBI-12020542; Q99750; Q9HCB6: SPON1; NbExp=3; IntAct=EBI-724076, EBI-2431846; Q99750; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-724076, EBI-7082156; Q99750; O43609: SPRY1; NbExp=7; IntAct=EBI-724076, EBI-3866665; Q99750; O43597: SPRY2; NbExp=3; IntAct=EBI-724076, EBI-742487; Q99750; P51687: SUOX; NbExp=3; IntAct=EBI-724076, EBI-3921347; Q99750; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-724076, EBI-747797; Q99750; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-724076, EBI-745958; Q99750; Q6DHY5: TBC1D3G; NbExp=3; IntAct=EBI-724076, EBI-13092532; Q99750; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-724076, EBI-11955057; Q99750; A0A0S2Z4E5: TEAD4; NbExp=3; IntAct=EBI-724076, EBI-16432288; Q99750; A0A0S2Z4F2: TEAD4; NbExp=3; IntAct=EBI-724076, EBI-16429215; Q99750; Q7L2K0: TEDC2; NbExp=3; IntAct=EBI-724076, EBI-8465456; Q99750; Q15583: TGIF1; NbExp=4; IntAct=EBI-724076, EBI-714215; Q99750; P07101-3: TH; NbExp=3; IntAct=EBI-724076, EBI-12001016; Q99750; Q08117-2: TLE5; NbExp=3; IntAct=EBI-724076, EBI-11741437; Q99750; P19237: TNNI1; NbExp=3; IntAct=EBI-724076, EBI-746692; Q99750; Q05952: TNP2; NbExp=4; IntAct=EBI-724076, EBI-12039775; Q99750; Q4VB56: TNP2; NbExp=3; IntAct=EBI-724076, EBI-10241829; Q99750; O14656: TOR1A; NbExp=3; IntAct=EBI-724076, EBI-524257; Q99750; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-724076, EBI-492476; Q99750; P43897: TSFM; NbExp=3; IntAct=EBI-724076, EBI-1049298; Q99750; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-724076, EBI-10241197; Q99750; O14817: TSPAN4; NbExp=3; IntAct=EBI-724076, EBI-8652667; Q99750; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-724076, EBI-723389; Q99750; Q8N831: TSPYL6; NbExp=3; IntAct=EBI-724076, EBI-12023322; Q99750; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-724076, EBI-6447954; Q99750; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-724076, EBI-9090990; Q99750; Q6ZVT0: TTLL10; NbExp=3; IntAct=EBI-724076, EBI-7844656; Q99750; Q6ZVT0-3: TTLL10; NbExp=3; IntAct=EBI-724076, EBI-11979997; Q99750; O75896: TUSC2; NbExp=7; IntAct=EBI-724076, EBI-1052725; Q99750; Q99757: TXN2; NbExp=3; IntAct=EBI-724076, EBI-2932492; Q99750; Q8TAI1: TYMSOS; NbExp=4; IntAct=EBI-724076, EBI-742060; Q99750; Q06418: TYRO3; NbExp=3; IntAct=EBI-724076, EBI-3951628; Q99750; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-724076, EBI-14096082; Q99750; Q9Y2K6: USP20; NbExp=3; IntAct=EBI-724076, EBI-2511991; Q99750; Q6EMK4: VASN; NbExp=3; IntAct=EBI-724076, EBI-10249550; Q99750; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-724076, EBI-11957216; Q99750; P40337: VHL; NbExp=4; IntAct=EBI-724076, EBI-301246; Q99750; P40337-2: VHL; NbExp=4; IntAct=EBI-724076, EBI-12157263; Q99750; Q15906: VPS72; NbExp=4; IntAct=EBI-724076, EBI-399189; Q99750; Q8IW00: VSTM4; NbExp=3; IntAct=EBI-724076, EBI-4311759; Q99750; O96014: WNT11; NbExp=9; IntAct=EBI-724076, EBI-8058160; Q99750; P25490: YY1; NbExp=3; IntAct=EBI-724076, EBI-765538; Q99750; O43167: ZBTB24; NbExp=11; IntAct=EBI-724076, EBI-744471; Q99750; P24278: ZBTB25; NbExp=2; IntAct=EBI-724076, EBI-739899; Q99750; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-724076, EBI-12287587; Q99750; Q96C00: ZBTB9; NbExp=6; IntAct=EBI-724076, EBI-395708; Q99750; Q7Z2W4: ZC3HAV1; NbExp=3; IntAct=EBI-724076, EBI-922540; Q99750; Q8WTX9: ZDHHC1; NbExp=3; IntAct=EBI-724076, EBI-2818796; Q99750; Q9Y260: ZFAB; NbExp=4; IntAct=EBI-724076, EBI-750052; Q99750; Q68DK2-5: ZFYVE26; NbExp=7; IntAct=EBI-724076, EBI-8656416; Q99750; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-724076, EBI-11962760; Q99750; Q8IZC7: ZNF101; NbExp=6; IntAct=EBI-724076, EBI-5278328; Q99750; P17014: ZNF12; NbExp=3; IntAct=EBI-724076, EBI-11278550; Q99750; Q15973: ZNF124; NbExp=6; IntAct=EBI-724076, EBI-2555767; Q99750; P52737: ZNF136; NbExp=12; IntAct=EBI-724076, EBI-749129; Q99750; P52744: ZNF138; NbExp=3; IntAct=EBI-724076, EBI-10746567; Q99750; P52744-2: ZNF138; NbExp=3; IntAct=EBI-724076, EBI-10213071; Q99750; Q12901: ZNF155; NbExp=3; IntAct=EBI-724076, EBI-10747670; Q99750; Q12901-2: ZNF155; NbExp=3; IntAct=EBI-724076, EBI-10227379; Q99750; Q9UK13: ZNF221; NbExp=3; IntAct=EBI-724076, EBI-14513896; Q99750; Q9UK11: ZNF223; NbExp=7; IntAct=EBI-724076, EBI-10322867; Q99750; P17027: ZNF23; NbExp=3; IntAct=EBI-724076, EBI-5657766; Q99750; Q9UIE0: ZNF230; NbExp=3; IntAct=EBI-724076, EBI-1105361; Q99750; O43296: ZNF264; NbExp=3; IntAct=EBI-724076, EBI-4395808; Q99750; Q14C61: ZNF264; NbExp=3; IntAct=EBI-724076, EBI-2826570; Q99750; Q14584: ZNF266; NbExp=6; IntAct=EBI-724076, EBI-7115319; Q99750; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-724076, EBI-373456; Q99750; Q9H9D4: ZNF408; NbExp=6; IntAct=EBI-724076, EBI-347633; Q99750; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-724076, EBI-744257; Q99750; Q8TAU3: ZNF417; NbExp=7; IntAct=EBI-724076, EBI-740727; Q99750; Q8N7K0: ZNF433; NbExp=3; IntAct=EBI-724076, EBI-10267553; Q99750; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-724076, EBI-11962468; Q99750; Q8NDP4: ZNF439; NbExp=8; IntAct=EBI-724076, EBI-747580; Q99750; Q8IYI8: ZNF440; NbExp=10; IntAct=EBI-724076, EBI-726439; Q99750; Q8N8Z8: ZNF441; NbExp=3; IntAct=EBI-724076, EBI-17216366; Q99750; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-724076, EBI-740232; Q99750; Q8TAF7: ZNF461; NbExp=3; IntAct=EBI-724076, EBI-10271693; Q99750; Q96JC4: ZNF479; NbExp=3; IntAct=EBI-724076, EBI-10820574; Q99750; Q9ULM2: ZNF490; NbExp=7; IntAct=EBI-724076, EBI-1105370; Q99750; Q8N8L2: ZNF491; NbExp=5; IntAct=EBI-724076, EBI-12019860; Q99750; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-724076, EBI-10486136; Q99750; Q96KM6: ZNF512B; NbExp=3; IntAct=EBI-724076, EBI-1049952; Q99750; Q96C55: ZNF524; NbExp=3; IntAct=EBI-724076, EBI-10283126; Q99750; Q9BR84: ZNF559; NbExp=8; IntAct=EBI-724076, EBI-746605; Q99750; Q8TBZ8: ZNF564; NbExp=6; IntAct=EBI-724076, EBI-10273713; Q99750; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-724076, EBI-10172590; Q99750; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-724076, EBI-14069183; Q99750; Q3MI94: ZNF578; NbExp=3; IntAct=EBI-724076, EBI-10241108; Q99750; Q96N58: ZNF578; NbExp=3; IntAct=EBI-724076, EBI-11955189; Q99750; Q9UK33: ZNF580; NbExp=3; IntAct=EBI-724076, EBI-746277; Q99750; Q9P0T4: ZNF581; NbExp=8; IntAct=EBI-724076, EBI-745520; Q99750; Q96SQ5: ZNF587; NbExp=8; IntAct=EBI-724076, EBI-6427977; Q99750; Q96SK3: ZNF607; NbExp=4; IntAct=EBI-724076, EBI-747175; Q99750; Q6PF04: ZNF613; NbExp=3; IntAct=EBI-724076, EBI-12062855; Q99750; O15015: ZNF646; NbExp=3; IntAct=EBI-724076, EBI-745608; Q99750; Q5T619: ZNF648; NbExp=5; IntAct=EBI-724076, EBI-11985915; Q99750; Q6ZS27-3: ZNF662; NbExp=3; IntAct=EBI-724076, EBI-10255155; Q99750; Q96BR6: ZNF669; NbExp=3; IntAct=EBI-724076, EBI-12006574; Q99750; Q9BS34: ZNF670; NbExp=5; IntAct=EBI-724076, EBI-745276; Q99750; Q8IYX0: ZNF679; NbExp=4; IntAct=EBI-724076, EBI-745567; Q99750; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-724076, EBI-16429014; Q99750; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-724076, EBI-11090299; Q99750; Q96C28: ZNF707; NbExp=5; IntAct=EBI-724076, EBI-748111; Q99750; Q96H86: ZNF764; NbExp=4; IntAct=EBI-724076, EBI-745775; Q99750; Q8NCA9: ZNF784; NbExp=3; IntAct=EBI-724076, EBI-7138303; Q99750; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-724076, EBI-3925400; Q99750; Q8N393: ZNF786; NbExp=3; IntAct=EBI-724076, EBI-10265203; Q99750; Q15937: ZNF79; NbExp=3; IntAct=EBI-724076, EBI-10237274; Q99750; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-724076, EBI-11962574; Q99750; Q08AG5: ZNF844; NbExp=6; IntAct=EBI-724076, EBI-10225757; Q99750; O43257: ZNHIT1; NbExp=3; IntAct=EBI-724076, EBI-347522; Q99750; Q5BKY6; NbExp=3; IntAct=EBI-724076, EBI-10243533; Q99750; Q5W150; NbExp=3; IntAct=EBI-724076, EBI-10248148; Q99750; Q5XG85; NbExp=3; IntAct=EBI-724076, EBI-10248413; Q99750; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-724076, EBI-3957603; Nucleus Cytoplasm Belongs to the MDFI family. negative regulation of transcription from RNA polymerase II promoter protein binding nucleus cytoplasm multicellular organism development transcription factor binding dorsal/ventral axis specification cell differentiation negative regulation of Wnt signaling pathway identical protein binding cytoplasmic sequestering of transcription factor negative regulation of DNA binding embryonic skeletal system morphogenesis trophoblast giant cell differentiation uc003oqq.1 uc003oqq.2 uc003oqq.3 uc003oqq.4 uc003oqq.5 uc003oqq.6 
ENST00000230340.9 BYSL ENST00000230340.9 bystin like (from RefSeq NM_004053.4) BYSL BYST_HUMAN ENP1 ENST00000230340.1 ENST00000230340.2 ENST00000230340.3 ENST00000230340.4 ENST00000230340.5 ENST00000230340.6 ENST00000230340.7 ENST00000230340.8 NM_004053 Q13895 Q6P5W4 Q86W44 Q96IP8 uc003orl.1 uc003orl.2 uc003orl.3 uc003orl.4 uc003orl.5 Bystin is expressed as a 2-kb major transcript and a 3.6-kb minor transcript in SNG-M cells and in human trophoblastic teratocarcinoma HT-H cells. Protein binding assays determined that bystin binds directly to trophinin and tastin, and that binding is enhanced when cytokeratins 8 and 18 are present. Immunocytochemistry of HT-H cells showed that bystin colocalizes with trophinin, tastin, and the cytokeratins, suggesting that these molecules form a complex in trophectoderm cells at the time of implantation. Using immunohistochemistry it was determined that trophinin and bystin are found in the placenta from the sixth week of pregnancy. Both proteins were localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the levels of trophinin, tastin, and bystin decreased and then disappeared from placental villi. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC007340.2, SRR3476690.380103.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230340.9/ ENSP00000230340.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. May be required for trophinin- dependent regulation of cell adhesion during implantation of human embryos. Binds trophinin, tastin and cytokeratins. Q13895; Q13155: AIMP2; NbExp=5; IntAct=EBI-358049, EBI-745226; Q13895; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-358049, EBI-746752; Q13895; P06576: ATP5F1B; NbExp=3; IntAct=EBI-358049, EBI-356231; Q13895; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-358049, EBI-4400025; Q13895; Q8N7W2-2: BEND7; NbExp=8; IntAct=EBI-358049, EBI-10181188; Q13895; Q12934-2: BFSP1; NbExp=3; IntAct=EBI-358049, EBI-12123320; Q13895; O14503: BHLHE40; NbExp=3; IntAct=EBI-358049, EBI-711810; Q13895; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-358049, EBI-946029; Q13895; P20807-4: CAPN3; NbExp=3; IntAct=EBI-358049, EBI-11532021; Q13895; O14958: CASQ2; NbExp=3; IntAct=EBI-358049, EBI-6859557; Q13895; Q5BKX8: CAVIN4; NbExp=3; IntAct=EBI-358049, EBI-12836558; Q13895; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-358049, EBI-10171570; Q13895; Q96JN2-2: CCDC136; NbExp=5; IntAct=EBI-358049, EBI-10171416; Q13895; Q9UJX2: CDC23; NbExp=5; IntAct=EBI-358049, EBI-396137; Q13895; Q96GN5: CDCA7L; NbExp=5; IntAct=EBI-358049, EBI-5278764; Q13895; Q9C0F1: CEP44; NbExp=5; IntAct=EBI-358049, EBI-744115; Q13895; Q8IYX8-2: CEP57L1; NbExp=5; IntAct=EBI-358049, EBI-10181988; Q13895; Q8NHQ1: CEP70; NbExp=8; IntAct=EBI-358049, EBI-739624; Q13895; P38432: COIL; NbExp=11; IntAct=EBI-358049, EBI-945751; Q13895; Q92841: DDX17; NbExp=6; IntAct=EBI-358049, EBI-746012; Q13895; Q8NF50-2: DOCK8; NbExp=5; IntAct=EBI-358049, EBI-10174653; Q13895; Q56P03: EAPP; NbExp=3; IntAct=EBI-358049, EBI-748732; Q13895; P50402: EMD; NbExp=6; IntAct=EBI-358049, EBI-489887; Q13895; Q12929: EPS8; NbExp=3; IntAct=EBI-358049, EBI-375576; Q13895; Q15303: ERBB4; NbExp=3; IntAct=EBI-358049, EBI-80371; Q13895; Q86W67: FAM228A; NbExp=3; IntAct=EBI-358049, EBI-12958227; Q13895; Q8IZU0: FAM9B; NbExp=5; IntAct=EBI-358049, EBI-10175124; Q13895; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-358049, EBI-11977403; Q13895; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-358049, EBI-10172181; Q13895; P51114-2: FXR1; NbExp=3; IntAct=EBI-358049, EBI-11022345; Q13895; P51116: FXR2; NbExp=8; IntAct=EBI-358049, EBI-740459; Q13895; O95995: GAS8; NbExp=3; IntAct=EBI-358049, EBI-1052570; Q13895; Q96IK5: GMCL1; NbExp=5; IntAct=EBI-358049, EBI-2548508; Q13895; Q08379: GOLGA2; NbExp=8; IntAct=EBI-358049, EBI-618309; Q13895; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-358049, EBI-5916454; Q13895; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-358049, EBI-717919; Q13895; Q6NT76: HMBOX1; NbExp=8; IntAct=EBI-358049, EBI-2549423; Q13895; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-358049, EBI-740641; Q13895; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-358049, EBI-10961706; Q13895; O75031: HSF2BP; NbExp=3; IntAct=EBI-358049, EBI-7116203; Q13895; Q13422: IKZF1; NbExp=5; IntAct=EBI-358049, EBI-745305; Q13895; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-358049, EBI-11522367; Q13895; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-358049, EBI-747204; Q13895; O75564-2: JRK; NbExp=3; IntAct=EBI-358049, EBI-17181882; Q13895; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-358049, EBI-743591; Q13895; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-358049, EBI-3437878; Q13895; Q9BVG8-5: KIFC3; NbExp=5; IntAct=EBI-358049, EBI-14069005; Q13895; O95198: KLHL2; NbExp=3; IntAct=EBI-358049, EBI-746999; Q13895; Q8WZ60: KLHL6; NbExp=3; IntAct=EBI-358049, EBI-6426464; Q13895; Q15323: KRT31; NbExp=3; IntAct=EBI-358049, EBI-948001; Q13895; Q6A162: KRT40; NbExp=8; IntAct=EBI-358049, EBI-10171697; Q13895; P60370: KRTAP10-5; NbExp=5; IntAct=EBI-358049, EBI-10172150; Q13895; P60409: KRTAP10-7; NbExp=5; IntAct=EBI-358049, EBI-10172290; Q13895; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-358049, EBI-10172511; Q13895; Q96JM7: L3MBTL3; NbExp=5; IntAct=EBI-358049, EBI-2686809; Q13895; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-358049, EBI-11985629; Q13895; O95751: LDOC1; NbExp=4; IntAct=EBI-358049, EBI-740738; Q13895; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-358049, EBI-12039345; Q13895; P25800: LMO1; NbExp=3; IntAct=EBI-358049, EBI-8639312; Q13895; P25791-3: LMO2; NbExp=3; IntAct=EBI-358049, EBI-11959475; Q13895; Q17RB8: LONRF1; NbExp=8; IntAct=EBI-358049, EBI-2341787; Q13895; Q96GA3: LTV1; NbExp=11; IntAct=EBI-358049, EBI-2558389; Q13895; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-358049, EBI-1216080; Q13895; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-358049, EBI-741037; Q13895; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-358049, EBI-11323212; Q13895; D6RGH6: MCIDAS; NbExp=3; IntAct=EBI-358049, EBI-3954372; Q13895; Q9HAF1: MEAF6; NbExp=3; IntAct=EBI-358049, EBI-399266; Q13895; P50221: MEOX1; NbExp=3; IntAct=EBI-358049, EBI-2864512; Q13895; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-358049, EBI-16439278; Q13895; O15344: MID1; NbExp=4; IntAct=EBI-358049, EBI-2340316; Q13895; Q9UJV3-2: MID2; NbExp=8; IntAct=EBI-358049, EBI-10172526; Q13895; Q8TD10: MIPOL1; NbExp=8; IntAct=EBI-358049, EBI-2548751; Q13895; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-358049, EBI-373524; Q13895; O00566: MPHOSPH10; NbExp=3; IntAct=EBI-358049, EBI-5235884; Q13895; Q96HT8: MRFAP1L1; NbExp=13; IntAct=EBI-358049, EBI-748896; Q13895; Q8NCY6: MSANTD4; NbExp=3; IntAct=EBI-358049, EBI-7850168; Q13895; Q5JR59: MTUS2; NbExp=5; IntAct=EBI-358049, EBI-742948; Q13895; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-358049, EBI-11522433; Q13895; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-358049, EBI-10172876; Q13895; P35240-4: NF2; NbExp=3; IntAct=EBI-358049, EBI-1014514; Q13895; Q7RTU3: OLIG3; NbExp=5; IntAct=EBI-358049, EBI-10225049; Q13895; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-358049, EBI-1051317; Q13895; Q5VU43: PDE4DIP; NbExp=5; IntAct=EBI-358049, EBI-1105124; Q13895; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-358049, EBI-9640281; Q13895; Q8IXK0: PHC2; NbExp=6; IntAct=EBI-358049, EBI-713786; Q13895; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-358049, EBI-79165; Q13895; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-358049, EBI-357318; Q13895; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-358049, EBI-302345; Q13895; Q9UL42: PNMA2; NbExp=7; IntAct=EBI-358049, EBI-302355; Q13895; Q96MT3: PRICKLE1; NbExp=3; IntAct=EBI-358049, EBI-2348662; Q13895; P62333: PSMC6; NbExp=3; IntAct=EBI-358049, EBI-357669; Q13895; Q9H0H5: RACGAP1; NbExp=3; IntAct=EBI-358049, EBI-717233; Q13895; P63244: RACK1; NbExp=3; IntAct=EBI-358049, EBI-296739; Q13895; Q53GL6: RALY; NbExp=3; IntAct=EBI-358049, EBI-9512693; Q13895; Q86SE5: RALYL; NbExp=3; IntAct=EBI-358049, EBI-741520; Q13895; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-358049, EBI-1210429; Q13895; Q8TA86: RP9; NbExp=3; IntAct=EBI-358049, EBI-630339; Q13895; Q92622: RUBCN; NbExp=3; IntAct=EBI-358049, EBI-2952709; Q13895; Q16637: SMN2; NbExp=8; IntAct=EBI-358049, EBI-395421; Q13895; Q13573: SNW1; NbExp=3; IntAct=EBI-358049, EBI-632715; Q13895; Q9Y2D8: SSX2IP; NbExp=5; IntAct=EBI-358049, EBI-2212028; Q13895; O75558: STX11; NbExp=8; IntAct=EBI-358049, EBI-714135; Q13895; Q969V4: TEKT1; NbExp=6; IntAct=EBI-358049, EBI-10180409; Q13895; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-358049, EBI-1105213; Q13895; Q9NVV9: THAP1; NbExp=8; IntAct=EBI-358049, EBI-741515; Q13895; Q08117: TLE5; NbExp=5; IntAct=EBI-358049, EBI-717810; Q13895; Q08117-2: TLE5; NbExp=5; IntAct=EBI-358049, EBI-11741437; Q13895; Q15025: TNIP1; NbExp=8; IntAct=EBI-358049, EBI-357849; Q13895; Q12933: TRAF2; NbExp=3; IntAct=EBI-358049, EBI-355744; Q13895; Q9BUZ4: TRAF4; NbExp=9; IntAct=EBI-358049, EBI-3650647; Q13895; Q14142: TRIM14; NbExp=3; IntAct=EBI-358049, EBI-2820256; Q13895; P14373: TRIM27; NbExp=6; IntAct=EBI-358049, EBI-719493; Q13895; O94972: TRIM37; NbExp=9; IntAct=EBI-358049, EBI-741602; Q13895; O00635: TRIM38; NbExp=3; IntAct=EBI-358049, EBI-2130415; Q13895; Q8WV44: TRIM41; NbExp=5; IntAct=EBI-358049, EBI-725997; Q13895; Q9BYV2: TRIM54; NbExp=7; IntAct=EBI-358049, EBI-2130429; Q13895; Q9BYV6-2: TRIM55; NbExp=3; IntAct=EBI-358049, EBI-11522718; Q13895; Q15654: TRIP6; NbExp=6; IntAct=EBI-358049, EBI-742327; Q13895; Q12816: TRO; NbExp=4; IntAct=EBI-358049, EBI-950001; Q13895; Q12815: TROAP; NbExp=9; IntAct=EBI-358049, EBI-2349743; Q13895; A4D1L5: UBE2H; NbExp=3; IntAct=EBI-358049, EBI-10230777; Q13895; Q495M9: USH1G; NbExp=3; IntAct=EBI-358049, EBI-8601749; Q13895; P08670: VIM; NbExp=3; IntAct=EBI-358049, EBI-353844; Q13895; Q9H9H4: VPS37B; NbExp=8; IntAct=EBI-358049, EBI-4400866; Q13895; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-358049, EBI-2799833; Q13895; Q9UPY6-2: WASF3; NbExp=3; IntAct=EBI-358049, EBI-12026286; Q13895; Q15007: WTAP; NbExp=3; IntAct=EBI-358049, EBI-751647; Q13895; O43829: ZBTB14; NbExp=8; IntAct=EBI-358049, EBI-10176632; Q13895; Q96BR9: ZBTB8A; NbExp=8; IntAct=EBI-358049, EBI-742740; Q13895; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-358049, EBI-14104088; Q13895; Q9NTW7: ZFP64; NbExp=5; IntAct=EBI-358049, EBI-711679; Q13895; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-358049, EBI-7850213; Q13895; Q9UDV6: ZNF212; NbExp=3; IntAct=EBI-358049, EBI-1640204; Q13895; Q9HBT8: ZNF286A; NbExp=3; IntAct=EBI-358049, EBI-10754950; Q13895; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-358049, EBI-743265; Q13895; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-358049, EBI-8489702; Q13895; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-358049, EBI-11962468; Q13895; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-358049, EBI-12006434; Q13895; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-358049, EBI-745520; Q13895; Q8N720: ZNF655; NbExp=3; IntAct=EBI-358049, EBI-625509; Q13895; Q96K58-2: ZNF668; NbExp=3; IntAct=EBI-358049, EBI-12817597; Q13895; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-358049, EBI-7138235; Q13895; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-358049, EBI-10251462; Q13895; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-358049, EBI-5667516; Q13895; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-358049, EBI-527853; Q13895; P10073: ZSCAN22; NbExp=3; IntAct=EBI-358049, EBI-10178224; Q13895; P0DTC9: N; Xeno; NbExp=5; IntAct=EBI-358049, EBI-25475856; Cytoplasm Nucleus, nucleolus Note=Associated with 40S ribosomal subunits. Found in the placenta from the sixth week of pregnancy. Was localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the level decreased and then disappeared from placental villi. HeLa cells lacking BYSL show a delay in the processing of the 18S rRNA component of the 40S ribosomal subunit. HT-H cells lacking BYSL show trophinin-independent signaling through ERBB4. Belongs to the bystin family. Sequence=AAC16603.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) in utero embryonic development blastocyst formation trophectodermal cell differentiation RNA binding protein binding nucleus nucleoplasm nucleolus cytoplasm cytosol rRNA processing cell proliferation membrane snoRNA binding preribosome, small subunit precursor ribosome biogenesis intracellular membrane-bounded organelle apical part of cell regulation of protein localization to nucleolus uc003orl.1 uc003orl.2 uc003orl.3 uc003orl.4 uc003orl.5 
ENST00000230361.4 GUCA1B ENST00000230361.4 guanylate cyclase activator 1B (from RefSeq NM_002098.6) ENST00000230361.1 ENST00000230361.2 ENST00000230361.3 GCAP2 GUC1B_HUMAN NM_002098 Q9NU15 Q9UMX6 uc003orz.1 uc003orz.2 uc003orz.3 uc003orz.4 uc003orz.5 The protein encoded by this gene is a calcium-binding protein that activates photoreceptor guanylate cyclases. This gene may have arisen due to a gene duplication event since there is a highly similar gene clustered with it on chromosome 6. Mutations in this gene can cause a form of retinitis pigmentosa. [provided by RefSeq, Nov 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BX537393.1, BQ636025.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1968968 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## CDS uses downstream in-frame AUG :: upstream AUG and CDS extension is not conserved MANE Ensembl match :: ENST00000230361.4/ ENSP00000230361.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Stimulates two retinal guanylyl cyclases (GCs) GUCY2D and GUCY2F when free calcium ions concentration is low, and inhibits GUCY2D and GUCY2F when free calcium ions concentration is elevated (By similarity). This Ca(2+)-sensitive regulation of GCs is a key event in recovery of the dark state of rod photoreceptors following light exposure (By similarity). May be involved in cone photoreceptor response and recovery of response in bright light (By similarity). Q9UMX6; P32243-2: OTX2; NbExp=3; IntAct=EBI-12896859, EBI-9087860; Cell membrane ; Lipid-anchor Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Note=Subcellular location is not affected by light or dark conditions. In the retina, it is expressed in cone and rod photoreceptor cells. The N-terminus is blocked. Retinitis pigmentosa 48 (RP48) [MIM:613827]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note=The disease is caused by variants affecting the gene represented in this entry. Binds three calcium ions. photoreceptor outer segment photoreceptor inner segment calcium ion binding plasma membrane receptor guanylyl cyclase signaling pathway cell-cell signaling body fluid secretion visual perception phototransduction calcium sensitive guanylate cyclase activator activity membrane regulation of rhodopsin mediated signaling pathway guanylate cyclase regulator activity regulation of guanylate cyclase activity positive regulation of guanylate cyclase activity metal ion binding response to stimulus photoreceptor disc membrane uc003orz.1 uc003orz.2 uc003orz.3 uc003orz.4 uc003orz.5 
ENST00000230381.7 PRPH2 ENST00000230381.7 peripherin 2 (from RefSeq NM_000322.5) ENST00000230381.1 ENST00000230381.2 ENST00000230381.3 ENST00000230381.4 ENST00000230381.5 ENST00000230381.6 NM_000322 P23942 PRPH PRPH2_HUMAN Q5TFH5 Q6DK65 RDS TSPAN22 uc003osk.1 uc003osk.2 uc003osk.3 uc003osk.4 uc003osk.5 The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein found in the outer segment of both rod and cone photoreceptor cells. It may function as an adhesion molecule involved in stabilization and compaction of outer segment disks or in the maintenance of the curvature of the rim. This protein is essential for disk morphogenesis. Defects in this gene are associated with both central and peripheral retinal degenerations. Some of the various phenotypically different disorders are autosomal dominant retinitis pigmentosa, progressive macular degeneration, macular dystrophy and retinitis pigmentosa digenic. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.105378.1, SRR1803614.121211.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230381.7/ ENSP00000230381.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Essential for retina photoreceptor outer segment disk morphogenesis, may also play a role with ROM1 in the maintenance of outer segment disk structure (By similarity). Required for the maintenance of retinal outer nuclear layer thickness (By similarity). Required for the correct development and organization of the photoreceptor inner segment (By similarity). Homodimer; disulfide-linked (By similarity). Forms a homotetramer (By similarity). Forms a heterotetramer with ROM1 (By similarity). Homotetramer and heterotetramer core complexes go on to form higher order complexes by formation of intermolecular disulfide bonds (By similarity). Interacts with MREG (By similarity). Interacts with STX3 (By similarity). Interacts with SNAP25 (By similarity). P23942; P06307: CCK; NbExp=3; IntAct=EBI-25836834, EBI-6624398; P23942; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25836834, EBI-21591415; P23942; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25836834, EBI-5280197; P23942; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-25836834, EBI-2623095; Membrane ; Multi- pass membrane protein Cell projection, cilium, photoreceptor outer segment Photoreceptor inner segment Retina (photoreceptor). In rim region of ROS (rod outer segment) disks. Retinitis pigmentosa 7 (RP7) [MIM:608133]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. te=The disease is caused by variants affecting the gene represented in this entry. Retinitis punctata albescens (RPA) [MIM:136880]: A form of fleck retina disease characterized by aggregation of white flecks posteriorly in the retina, causing night blindness and delayed dark adaptation. It differs from fundus albipunctatus in being progressive and evolving to generalized atrophy of the retina. Note=The disease is caused by variants affecting the gene represented in this entry. Macular dystrophy, vitelliform, 3 (VMD3) [MIM:608161]: A form of vitelliform macular dystrophy, a retinal disease characterized by yellow, lipofuscin-containing deposits, usually localized at the center of the macula. Patients usually become symptomatic in the fourth or fifth decade of life with a protracted disease of decreased visual acuity. te=The disease is caused by variants affecting the gene represented in this entry. Macular dystrophy, patterned, 1 (MDPT1) [MIM:169150]: A form of retinal patterned dystrophy, a heterogeneous group of macular disorders that includes reticular (fishnet-like) dystrophy, macroreticular (spider-shaped) dystrophy and butterfly-shaped pigment dystrophy. te=The disease is caused by variants affecting the gene represented in this entry. Choroidal dystrophy, central areolar 2 (CACD2) [MIM:613105]: A form of central areolar choroidal dystrophy, a retinal disease that affects the macula and results in a well-demarcated circumscribed area of atrophy of the pigment epithelium and choriocapillaris. te=The disease is caused by variants affecting the gene represented in this entry. Note=Defects in PRPH2 are found in different retinal diseases including cone-rod dystrophy, retinitis pigmentosa, macular degeneration. The mutations underlying autosomal dominant retinitis pigmentosa and severe macular degeneration are largely missense or small in-frame deletions in a large intradiscal loop between the third and fourth transmembrane domains. In contrast, those associated with the milder pattern phenotypes or with digenic RP are scattered more evenly through the gene and are often nonsense mutations. This observation correlates with the hypothesis that the large loop is an important site of interaction between PRPH2 molecules and other protein components in the disk. Belongs to the PRPH2/ROM1 family. Name=Mutations of the RDS gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/rdsmut.htm"; photoreceptor outer segment integral component of plasma membrane cell adhesion visual perception membrane integral component of membrane retina development in camera-type eye uc003osk.1 uc003osk.2 uc003osk.3 uc003osk.4 uc003osk.5 
ENST00000230419.9 PTK7 ENST00000230419.9 protein tyrosine kinase 7 (inactive), transcript variant PTK7-1 (from RefSeq NM_002821.5) A8K974 B7Z477 CCK4 E9PFZ5 ENST00000230419.1 ENST00000230419.2 ENST00000230419.3 ENST00000230419.4 ENST00000230419.5 ENST00000230419.6 ENST00000230419.7 ENST00000230419.8 NM_002821 PTK7_HUMAN Q13308 Q13417 Q5T650 Q6IQ54 Q8NFA5 Q8NFA6 Q8NFA7 Q8NFA8 uc003oub.1 uc003oub.2 uc003oub.3 uc003oub.4 This gene encodes a member of the receptor protein tyrosine kinase family of proteins that transduce extracellular signals across the cell membrane. The encoded protein lacks detectable catalytic tyrosine kinase activity, is involved in the Wnt signaling pathway and plays a role in multiple cellular processes including polarity and adhesion. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jul 2012]. Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis. Interacts with CTNNB1. Q13308; P35222: CTNNB1; NbExp=5; IntAct=EBI-2803245, EBI-491549; Q13308; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2803245, EBI-11749135; Q13308; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2803245, EBI-10171774; Q13308; Q99750: MDFI; NbExp=3; IntAct=EBI-2803245, EBI-724076; Q13308; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2803245, EBI-11522433; Q13308; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2803245, EBI-22310682; Membrane ; Single- pass type I membrane protein Cell junction Note=Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells. Event=Alternative splicing; Named isoforms=6; Name=1; Synonyms=PTK7-1; IsoId=Q13308-1; Sequence=Displayed; Name=2; Synonyms=PTK7-2; IsoId=Q13308-2; Sequence=VSP_037182; Name=3; Synonyms=PTK7-3; IsoId=Q13308-3; Sequence=VSP_037181; Name=4; Synonyms=PTK7-4; IsoId=Q13308-4; Sequence=VSP_037183; Name=5; Synonyms=PTK7-5; IsoId=Q13308-5; Sequence=VSP_037184, VSP_037185; Name=6; IsoId=Q13308-6; Sequence=VSP_044775; Highly expressed in lung, liver, pancreas, kidney, placenta and melanocytes. Weakly expressed in thyroid gland, ovary, brain, heart and skeletal muscle. Also expressed in erythroleukemia cells. But not expressed in colon. Higher expression in cell lines established from normal non- tumorigenic tissues compared to cell lines established from highly metastatic invasive carcinomas (at protein level). The protein kinase domain is predicted to be catalytically inactive. MMP14 cleaves PTK7 between Pro-621 and Leu-622 generating an N- terminal soluble (70 kDa) fragment and a membrane C-terminal (50 kDa) fragment. Proteolysis by MMP14 regulates PTK7 function in non-canonical Wnt signaling pathway. [Isoform 5]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41901/PTK7"; establishment of planar polarity neural tube closure ventricular septum development axis elongation protein kinase activity protein binding ATP binding plasma membrane integral component of plasma membrane cell-cell junction focal adhesion protein phosphorylation cell adhesion signal transduction heart development positive regulation of neuron projection development membrane integral component of membrane Wnt signaling pathway cell migration cell junction actin cytoskeleton reorganization wound healing establishment of epithelial cell apical/basal polarity convergent extension lung-associated mesenchyme development coronary vasculature development cellular response to retinoic acid cochlea morphogenesis planar cell polarity pathway involved in neural tube closure positive regulation of canonical Wnt signaling pathway coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway uc003oub.1 uc003oub.2 uc003oub.3 uc003oub.4 
ENST00000230431.11 DNPH1 ENST00000230431.11 2'-deoxynucleoside 5'-phosphate N-hydrolase 1, transcript variant 1 (from RefSeq NM_006443.3) B2LUJ9 C6orf108 DNPH1 DNPH1_HUMAN ENST00000230431.1 ENST00000230431.10 ENST00000230431.2 ENST00000230431.3 ENST00000230431.4 ENST00000230431.5 ENST00000230431.6 ENST00000230431.7 ENST00000230431.8 ENST00000230431.9 NM_006443 O43598 RCL uc003ouo.1 uc003ouo.2 uc003ouo.3 uc003ouo.4 uc003ouo.5 This gene was identified on the basis of its stimulation by c-Myc protein. The latter is a transcription factor that participates in the regulation of cell proliferation, differentiation, and apoptosis. The exact function of this gene is not known but studies in rat suggest a role in cellular proliferation and c-Myc-mediated transformation. Two alternative transcripts encoding different proteins have been described. [provided by RefSeq, Jul 2008]. Part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate) (PubMed:33833118). Catalyzes the second step in that pathway, the hydrolysis of the N-glycosidic bond in hmdUMP, degrading this cytotoxic nucleotide to avoid its genomic integration (PubMed:33833118). Reaction=5-hydroxymethyl-dUMP + H2O = 2-deoxy-D-ribose 5-phosphate + 5- hydroxymethyluracil; Xref=Rhea:RHEA:77099, ChEBI:CHEBI:15377, ChEBI:CHEBI:16964, ChEBI:CHEBI:62877, ChEBI:CHEBI:90409; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77100; Evidence=; Kinetic parameters: KM=57 uM for dGMP ; KM=97 uM for dAMP ; KM=104 uM for dIMP ; KM=2500 uM for dCMP ; KM=7800 uM for dUMP ; KM=25000 uM for dTMP ; Note=kcat is 0.002 sec(-1) with dGMP as substrate. kcat is 0.0025 sec(-1) with dAMP as substrate. kcat is 0.0016 sec(-1) with dIMP as substrate. kcat is 0.2 sec(-1) with dUMP as substrate. kcat is 0.0083 sec(-1) with dCMP as substrate. kcat is 0.025 sec(-1) with dTMP as substrate. ; Monomer and homodimer. O43598; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-748674, EBI-742054; O43598; O43598: DNPH1; NbExp=5; IntAct=EBI-748674, EBI-748674; O43598; Q92993: KAT5; NbExp=3; IntAct=EBI-748674, EBI-399080; O43598; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-748674, EBI-11742507; O43598; P17252: PRKCA; NbExp=3; IntAct=EBI-748674, EBI-1383528; O43598; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-748674, EBI-9090795; O43598; P54274: TERF1; NbExp=2; IntAct=EBI-748674, EBI-710997; O43598; P61981: YWHAG; NbExp=3; IntAct=EBI-748674, EBI-359832; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O43598-1; Sequence=Displayed; Name=2; IsoId=O43598-2; Sequence=VSP_040509, VSP_040510; Expressed at low levels in brain, colon, lung, peripheral blood leukocytes, placenta, small intestine, and thymus. Expressed at high levels in heart, kidney, liver, skeletal muscle and spleen. Overexpressed in a significant proportion of breast cancers. Expression is induced by ETV1. Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family. Originally described for its in vitro hydrolytic activity towards dGMP, dAMP and dIMP (PubMed:24260472, PubMed:25108359). However, this was not confirmed in vivo (PubMed:33833118). protein binding nucleus cytoplasm cytosol purine nucleotide catabolic process metabolic process nucleoside metabolic process nucleotide metabolic process deoxyribonucleoside monophosphate catabolic process hydrolase activity hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing N-glycosyl compounds positive regulation of cell growth epithelial cell differentiation identical protein binding protein homodimerization activity extracellular exosome deoxyribonucleoside 5'-monophosphate N-glycosidase activity uc003ouo.1 uc003ouo.2 uc003ouo.3 uc003ouo.4 uc003ouo.5 
ENST00000230449.9 EXOC2 ENST00000230449.9 exocyst complex component 2, transcript variant 2 (from RefSeq NR_073064.2) B2RBE6 ENST00000230449.1 ENST00000230449.2 ENST00000230449.3 ENST00000230449.4 ENST00000230449.5 ENST00000230449.6 ENST00000230449.7 ENST00000230449.8 EXOC2_HUMAN NR_073064 Q5JPC8 Q96AN6 Q96KP1 Q9NUZ8 Q9UJM7 SEC5 SEC5L1 uc003mtd.1 uc003mtd.2 uc003mtd.3 uc003mtd.4 uc003mtd.5 uc003mtd.6 The protein encoded by this gene is a component of the exocyst complex, a multi-protein complex essential for the polarized targeting of exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and the functions of the exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. This interaction has been shown to mediate filopodia formation in fibroblasts. This protein has been shown to interact with the Ral subfamily of GTPases and thereby mediate exocytosis by tethering vesicles to the plasma membrane. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2012]. Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1 (By similarity). Interacts with GNEFR/DELGEF; this interaction occurs only in the presence of magnesium or manganese and is stimulated by dCTP or GTP (PubMed:12459492). Interacts with RALA and RALB (PubMed:18756269, PubMed:19166349, PubMed:12459492) (By similarity). Interacts with ARL13B; regulates ARL13B localization to the cilium membrane. Q96KP1; Q9NV70: EXOC1; NbExp=6; IntAct=EBI-465715, EBI-1045313; Midbody, Midbody ring Note=Recruitment to the midbody does not require RALA, nor RALB (PubMed:18756269). Colocalizes with CNTRL/centriolin at the midbody ring (PubMed:16213214). Widely expressed with highest levels in brain and placenta. Interacts with RALA through the TIG domain. Neurodevelopmental disorder with dysmorphic facies and cerebellar hypoplasia (NEDFACH) [MIM:619306]: An autosomal recessive disorder characterized by global developmental delay, intellectual disability, facial dysmorphism, and abnormalities of the cerebellum observed on brain imaging. Disease severity is variable. Some affected individuals have poor overall growth with microcephaly, delayed walking, spasticity, and poor or absent speech. Others may achieve more significant developmental milestones. Additional variable manifestations may include cardiac ventricular septal defect, spasticity, cataracts, optic nerve hypoplasia, seizures, and joint contractures. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the SEC5 family. Sequence=BAA91963.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; exocyst protein binding cytosol plasma membrane exocytosis Golgi to plasma membrane transport protein transport membrane vesicle-mediated transport Ral GTPase binding protein kinase binding protein N-terminus binding Flemming body regulation of entry of bacterium into host cell uc003mtd.1 uc003mtd.2 uc003mtd.3 uc003mtd.4 uc003mtd.5 uc003mtd.6 
ENST00000230461.11 TMEM30A ENST00000230461.11 transmembrane protein 30A, transcript variant 1 (from RefSeq NM_018247.4) A8K9V8 C6orf67 CC50A_HUMAN CDC50A E1P539 ENST00000230461.1 ENST00000230461.10 ENST00000230461.2 ENST00000230461.3 ENST00000230461.4 ENST00000230461.5 ENST00000230461.6 ENST00000230461.7 ENST00000230461.8 ENST00000230461.9 NM_018247 Q658Z3 Q96H09 Q9NSL9 Q9NV96 TMEM30A uc003phw.1 uc003phw.2 uc003phw.3 uc003phw.4 Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediates the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations. Component of various P4-ATPase flippase complexes which consists of a catalytic alpha subunit and an accessory beta subunit (PubMed:31416931). Interacts with ATP8A1 to form a flippase complex; this complex forms an intermediate phosphoenzyme (PubMed:31416931). The ATP8A2:TMEM30A flippase complex has been purified, and ATP8B1:TMEM30A and ATP8B2:TMEM30A flippase complexes have been shown to form intermediate phosphoenzymes in vitro. Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C. Q9NV96; O60312: ATP10A; NbExp=3; IntAct=EBI-2836942, EBI-26444318; Q9NV96; P98196: ATP11A; NbExp=4; IntAct=EBI-2836942, EBI-21519640; Q9NV96; Q9Y2G3: ATP11B; NbExp=2; IntAct=EBI-2836942, EBI-20857228; Q9NV96; Q8NB49: ATP11C; NbExp=2; IntAct=EBI-2836942, EBI-11279131; Q9NV96; Q9Y2Q0: ATP8A1; NbExp=5; IntAct=EBI-2836942, EBI-9539324; Q9NV96; Q9Y2Q0-2: ATP8A1; NbExp=2; IntAct=EBI-2836942, EBI-21654619; Q9NV96; O43520: ATP8B1; NbExp=9; IntAct=EBI-2836942, EBI-9524729; Q9NV96; P98198: ATP8B2; NbExp=4; IntAct=EBI-2836942, EBI-9539266; Q9NV96; Q8TF62: ATP8B4; NbExp=4; IntAct=EBI-2836942, EBI-9527207; Q9NV96-1; O94823-1: ATP10B; NbExp=2; IntAct=EBI-26444832, EBI-26444823; Q9NV96-2; P54253: ATXN1; NbExp=6; IntAct=EBI-12921610, EBI-930964; Q9NV96-2; P42858: HTT; NbExp=3; IntAct=EBI-12921610, EBI-466029; Q9NV96-2; P21145: MAL; NbExp=3; IntAct=EBI-12921610, EBI-3932027; Membrane ; Multi-pass membrane protein Cell membrane. Golgi apparatus. Cytoplasmic vesicle, secretory vesicle membrane Apical cell membrane Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NV96-1; Sequence=Displayed; Name=2; IsoId=Q9NV96-2; Sequence=VSP_019568; Name=3; IsoId=Q9NV96-3; Sequence=VSP_019567; The N-terminal domain seems to play a role in the reaction cycle of the catalytic subunit such as ATP8A2. N-glycosylated. Contains high mannose-type oligosaccharides (By similarity). Belongs to the CDC50/LEM3 family. protein binding endoplasmic reticulum Golgi apparatus plasma membrane drug transmembrane transport lipid transport positive regulation of neuron projection development aminophospholipid transporter activity phospholipid transport aminophospholipid transport membrane integral component of membrane apical plasma membrane transport vesicle membrane cytoplasmic vesicle azurophil granule membrane specific granule membrane protein localization to endosome neutrophil degranulation phospholipid translocation positive regulation of protein exit from endoplasmic reticulum uc003phw.1 uc003phw.2 uc003phw.3 uc003phw.4 
ENST00000230538.12 LAMA4 ENST00000230538.12 laminin subunit alpha 4, transcript variant 1 (from RefSeq NM_001105206.3) A0A0A0MQS9 A0A0A0MQS9_HUMAN ENST00000230538.1 ENST00000230538.10 ENST00000230538.11 ENST00000230538.2 ENST00000230538.3 ENST00000230538.4 ENST00000230538.5 ENST00000230538.6 ENST00000230538.7 ENST00000230538.8 ENST00000230538.9 LAMA4 NM_001105206 uc003pvu.1 uc003pvu.2 uc003pvu.3 uc003pvu.4 uc003pvu.5 Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the alpha chain isoform laminin, alpha 4. The domain structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the N-terminus (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the C-terminal G domain which distinguishes all alpha chains from the beta and gamma chains. The RNA analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known. Tissue-specific utilization of alternative polyA-signal has been described in literature. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Aug 2011]. Membrane Lacks conserved residue(s) required for the propagation of feature annotation. blood vessel development receptor binding basement membrane cell adhesion regulation of cell adhesion regulation of cell migration neuromuscular junction synaptic cleft regulation of embryonic development brown fat cell differentiation uc003pvu.1 uc003pvu.2 uc003pvu.3 uc003pvu.4 uc003pvu.5 
ENST00000230568.5 LY86 ENST00000230568.5 lymphocyte antigen 86 (from RefSeq NM_004271.4) ENST00000230568.1 ENST00000230568.2 ENST00000230568.3 ENST00000230568.4 LY86_HUMAN MD1 NM_004271 O95711 Q9UQC4 uc003mwy.1 uc003mwy.2 uc003mwy.3 May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression (By similarity). M-shaped tetramer of two CD180-LY86 heterodimers. O95711; Q99467: CD180; NbExp=3; IntAct=EBI-12203791, EBI-15940363; O95711; P57678: GEMIN4; NbExp=3; IntAct=EBI-12203791, EBI-356700; Secreted, extracellular space. Note=Associated with CD180 at the cell surface. Highly expressed in B-cells, monocytes and tonsil. In monocytes, down-regulated by the cell-wall fraction of Mycobacterium bovis (BCG-CWS). Sequence=BAA76410.1; Type=Erroneous initiation; Evidence=; immune system process protein binding extracellular region extracellular space inflammatory response immune response positive regulation of lipopolysaccharide-mediated signaling pathway innate immune response uc003mwy.1 uc003mwy.2 uc003mwy.3 
ENST00000230582.8 PRSS16 ENST00000230582.8 serine protease 16 (from RefSeq NM_005865.4) ENST00000230582.1 ENST00000230582.2 ENST00000230582.3 ENST00000230582.4 ENST00000230582.5 ENST00000230582.6 ENST00000230582.7 NM_005865 O75416 Q9NQE7 TSSP TSSP_HUMAN uc003nja.1 uc003nja.2 uc003nja.3 uc003nja.4 uc003nja.5 This gene encodes a serine protease expressed exclusively in the thymus. It is thought to play a role in the alternative antigen presenting pathway used by cortical thymic epithelial cells during the positive selection of T cells. The gene is found in the large histone gene cluster on chromosome 6, near the major histocompatibility complex (MHC) class I region. A second transcript variant has been described, but its full length nature has not been determined. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF052514.1, AK314037.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN03465418 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230582.8/ ENSP00000230582.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Protease that may play a role in T-cell development. Cytoplasmic vesicle. Note=Vesicular, either lysosomal or endosomal. Expressed predominantly in cortical thymic epithelial cells. Expressed in fetal thymus. Belongs to the peptidase S28 family. lysosome endosome proteolysis peptidase activity serine-type peptidase activity dipeptidyl-peptidase activity hydrolase activity protein catabolic process cytoplasmic vesicle uc003nja.1 uc003nja.2 uc003nja.3 uc003nja.4 uc003nja.5 
ENST00000230588.9 MEP1A ENST00000230588.9 meprin A subunit alpha (from RefSeq NM_005588.3) A2RRM4 B0AZP9 B2RCS2 ENST00000230588.1 ENST00000230588.2 ENST00000230588.3 ENST00000230588.4 ENST00000230588.5 ENST00000230588.6 ENST00000230588.7 ENST00000230588.8 MEP1A_HUMAN NM_005588 Q16819 Q8TDC9 Q9H1R1 uc010jzh.1 uc010jzh.2 uc010jzh.3 Reaction=Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.; EC=3.4.24.18; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. Inhibited by several hydroxamate compounds, the most potent inhibitor is actinonin. Kinetic parameters: KM=110 uM for GRP ; KM=18.0 uM for PTH 12-34 ; KM=33.9 uM for secretin ; KM=41.3 uM for substance P ; KM=56.5 uM for LHRH ; KM=73.2 uM for orcokinin ; KM=292 uM for alpha-MSH ; KM=125 uM for bradykinin ; KM=200 uM for gastrin ; Homotetramer consisting of disulfide-linked alpha subunits, homooligomer consisting of disulfide-linked alpha subunit homodimers, or heterotetramer of two alpha and two beta subunits formed by non- covalent association of two disulfide-linked heterodimers (By similarity). Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity (By similarity). Q16819; P14780: MMP9; NbExp=2; IntAct=EBI-8153734, EBI-1382326; Membrane; Single-pass type I membrane protein. N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose. metalloendopeptidase activity protein binding extracellular space integral component of plasma membrane proteolysis peptidase activity metallopeptidase activity zinc ion binding membrane integral component of membrane hydrolase activity meprin A complex metal ion binding extracellular exosome uc010jzh.1 uc010jzh.2 uc010jzh.3 
ENST00000230640.10 MTREX ENST00000230640.10 Mtr4 exosome RNA helicase (from RefSeq NM_015360.5) DOB1 ENST00000230640.1 ENST00000230640.2 ENST00000230640.3 ENST00000230640.4 ENST00000230640.5 ENST00000230640.6 ENST00000230640.7 ENST00000230640.8 ENST00000230640.9 KIAA0052 MTR4 MTREX MTREX_HUMAN NM_015360 P42285 Q2M386 Q6MZZ8 Q6P170 Q8N5R0 Q8TAG2 SKIV2L2 uc003jpy.1 uc003jpy.2 uc003jpy.3 uc003jpy.4 uc003jpy.5 uc003jpy.6 Catalyzes the ATP-dependent unwinding of RNA duplexes with a single-stranded 3' RNA extension (PubMed:27871484, PubMed:29844170, PubMed:29906447). Central subunit of many protein complexes, namely TRAMP-like, nuclear exosome targeting (NEXT) and poly(A) tail exosome targeting (PAXT) (PubMed:27871484, PubMed:29844170, PubMed:21855801). NEXT functions as an RNA exosome cofactor that directs a subset of non- coding short-lived RNAs for exosomal degradation. NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs (PubMed:27871484, PubMed:29844170). PAXT directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor ZCCHC8, which links to RNA-binding protein adapters (PubMed:27871484). Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA (PubMed:17412707, PubMed:29107693). May be involved in pre-mRNA splicing. In the context of NEXT complex can also in vitro unwind DNA:RNA heteroduplexes with a 3' poly (A) RNA tracking strand (PubMed:29844170). Can promote unwinding and degradation of structured RNA substrates when associated with the nuclear exosome and its cofactors. Can displace a DNA strand while translocating on RNA to ultimately degrade the RNA within a DNA/RNA heteroduplex (PubMed:29906447). Plays a role in DNA damage response (PubMed:29902117). Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence=; Activated when MTREX is incorporated into NEXT complex an the nuclear RNA exosome complex. Component of a TRAMP-like complex, an ATP-dependent exosome regulatory complex consisting of a helicase (MTREX), an oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes exist with specific compositions and are associated with nuclear, or nucleolar RNA exosomes (PubMed:21855801). Identified in the spliceosome C complex. Component of the poly(A) tail exosome targeting (PAXT) complex made of PABPN1, ZFC3H1 and MTREX that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation (PubMed:27871484). Component of the nuclear exosome targeting (NEXT) complex composed of MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding short-lived RNAs for exosomal degradation (PubMed:27905398, PubMed:27871484). Interacts with ZCCHC8; this interaction bridges the interaction between RBM7 and MTREX (PubMed:27905398, PubMed:16263084, PubMed:29844170, PubMed:31358741). Binds to ZFC3H1 and RBM7 in a RNase-insensitive manner (PubMed:27871484). Interacts with EXOSC10; the interaction mediates the association of MTREX with nuclear RNA exosomes (PubMed:26166824). Interacts with isoform 1 of NVL in an ATP-dependent manner; the interaction is required to associate NVL with nuclear RNA exosome (PubMed:16782053, PubMed:26166824, PubMed:11991638, PubMed:16263084, PubMed:21855801, PubMed:27871484, PubMed:27905398, PubMed:31358741). Interacts with WDR74; the interaction dissociation in a late stage of rRNA synthesis is required for appropriate maturation of pre-60S particles and depends on the ATPase activity of NVL (PubMed:26456651, PubMed:29107693). Interacts with MPHOSPH6 (PubMed:17412707). Interacts with the RNA cap-binding complex proteins NCBP1 and SRRT (PubMed:30842217). Interacts with NRDE2; the interaction is direct and negatively regulates MTREX function in exosomal degradation by changing its conformation precluding interaction with ZFC3H1, the RNA cap-binding complex proteins NCBP1 and SRRT, and association with the exosome (PubMed:30842217, PubMed:30538148, PubMed:29902117). Interacts with the nuclear RNA exosome complex (PubMed:29906447). P42285; Q99547: MPHOSPH6; NbExp=2; IntAct=EBI-347612, EBI-373187; Nucleus, nucleoplasm Nucleus, nucleolus Nucleus Nucleus speckle Belongs to the helicase family. SKI2 subfamily. Sequence=AAH65258.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=BAA06124.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleotide binding mRNA splicing, via spliceosome maturation of 5.8S rRNA nucleic acid binding RNA binding RNA helicase activity helicase activity protein binding ATP binding nucleus nucleoplasm spliceosomal complex nucleolus rRNA processing mRNA processing RNA catabolic process RNA splicing hydrolase activity TRAMP complex catalytic step 2 spliceosome nuclear exosome (RNase complex) exosome (RNase complex) uc003jpy.1 uc003jpy.2 uc003jpy.3 uc003jpy.4 uc003jpy.5 uc003jpy.6 
ENST00000230658.12 ISL1 ENST00000230658.12 ISL LIM homeobox 1 (from RefSeq NM_002202.3) ENST00000230658.1 ENST00000230658.10 ENST00000230658.11 ENST00000230658.2 ENST00000230658.3 ENST00000230658.4 ENST00000230658.5 ENST00000230658.6 ENST00000230658.7 ENST00000230658.8 ENST00000230658.9 ISL1_HUMAN NM_002202 P20663 P47894 P61371 uc003jor.1 uc003jor.2 uc003jor.3 uc003jor.4 uc003jor.5 This gene encodes a member of the LIM/homeodomain family of transcription factors. The encoded protein binds to the enhancer region of the insulin gene, among others, and may play an important role in regulating insulin gene expression. The encoded protein is central to the development of pancreatic cell lineages and may also be required for motor neuron generation. Mutations in this gene have been associated with maturity-onset diabetes of the young. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U07559.1, BC031213.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000230658.12/ ENSP00000230658.7 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## DNA-binding transcriptional activator. Recognizes and binds to the consensus octamer binding site 5'-ATAATTAA-3' in promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Cooperates with the transcription factor POU4F2 to achieve maximal levels of expression of RGC target genes and RGC fate specification in the developing retina. Involved in the specification of motor neurons in cooperation with LHX3 and LDB1 (By similarity). Binds to insulin gene enhancer sequences (By similarity). Essential for heart development. Marker of one progenitor cell population that give rise to the outflow tract, right ventricle, a subset of left ventricular cells, and a large number of atrial cells as well, its function is required for these progenitors to contribute to the heart. Controls the expression of FGF and BMP growth factors in this cell population and is required for proliferation and survival of cells within pharyngeal foregut endoderm and adjacent splanchnic mesoderm as well as for migration of cardiac progenitors into the heart (By similarity). At neuronal promoters, displaces LDB1 from LHX3 LIM domain to form a ternary complex in which ISL1 contacts both LHX3 and LDB1; allosteric structural changes in the DNA binding domain of LHX3, induced by the ISL1:LHX3 interaction, may explain differences in sequence specificity of the different complexes. Interacts with LHX3. Interacts (via C-terminus) with POU4F2 (via C-terminus) isoform 1. Interacts with POU3F2. Interacts with POU4F3. Interacts (via N-terminal domain) with MLIP; the interaction represses ISL1 transactivator activity. Interacts with GCN5/KAT2A. Interactions of ISL1 with MLIP1 or KAT2A may be mutually exclusive (By similarity). P61371; Q86U70-2: LDB1; NbExp=7; IntAct=EBI-3906896, EBI-11979761; P61371; Q969G2: LHX4; NbExp=3; IntAct=EBI-3906896, EBI-2865388; P61371; Q8NB15: ZNF511; NbExp=7; IntAct=EBI-3906896, EBI-10269136; Nucleus Expressed in subsets of neurons of the adrenal medulla and dorsal root ganglion, inner nuclear and ganglion cell layers in the retina, the pineal and some regions of the brain. Expressed in the forming heart in the stage 9 embryo, in the myocardial trough, and then at stages 10 to 11, in the nondifferentiated mesodermal cells at the venous and arterial poles, as well as cells of the dorsal coelomic wall and ruptured mesocardium (at protein level). Ubiquitinated probably by WWP1 E3 ubiquitin ligase; ubiquitination is followed by protein degradation. Phosphorylated. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding RNA polymerase II activating transcription factor binding enhancer sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding neural crest cell migration heart morphogenesis secondary heart field specification outflow tract septum morphogenesis outflow tract morphogenesis endocardial cushion morphogenesis cardiac right ventricle morphogenesis regulation of secondary heart field cardioblast proliferation DNA binding chromatin binding transcription coactivator activity protein binding nucleus nucleoplasm cytoplasm regulation of transcription, DNA-templated multicellular organism development axonogenesis heart development positive regulation of cell proliferation regulation of gene expression positive regulation of vascular endothelial growth factor production positive regulation of epithelial to mesenchymal transition ligand-dependent nuclear receptor binding spinal cord motor neuron cell fate specification spinal cord motor neuron differentiation visceral motor neuron differentiation trigeminal nerve development pituitary gland development cell differentiation neuron differentiation estrogen receptor binding pancreas development axon regeneration retinal ganglion cell axon guidance positive regulation of insulin secretion positive regulation of granulocyte macrophage colony-stimulating factor production positive regulation of interferon-gamma production positive regulation of interleukin-1 alpha production positive regulation of interleukin-1 beta production positive regulation of interleukin-12 production positive regulation of interleukin-6 production positive regulation of tumor necrosis factor production negative regulation of intracellular estrogen receptor signaling pathway positive regulation of histone acetylation positive regulation of tyrosine phosphorylation of STAT protein positive regulation of DNA binding bHLH transcription factor binding negative regulation of neuron apoptotic process sequence-specific DNA binding positive regulation of cell differentiation negative regulation of neuron differentiation positive regulation of angiogenesis positive regulation of transcription from RNA polymerase II promoter metal ion binding neuron fate commitment neuron fate specification mesenchymal cell differentiation sensory system development peripheral nervous system neuron development peripheral nervous system neuron axonogenesis negative regulation of epithelial cell proliferation negative regulation of inflammatory response ventricular cardiac muscle tissue morphogenesis pharyngeal system development cardiac muscle cell myoblast differentiation innervation atrial septum morphogenesis cardiac cell fate determination cellular response to glucocorticoid stimulus positive regulation of granulocyte colony-stimulating factor production negative regulation of protein homodimerization activity negative regulation of canonical Wnt signaling pathway positive regulation of macrophage colony-stimulating factor production promoter-specific chromatin binding uc003jor.1 uc003jor.2 uc003jor.3 uc003jor.4 uc003jor.5 
ENST00000230671.7 SLC6A7 ENST00000230671.7 solute carrier family 6 member 7 (from RefSeq NM_014228.5) ENST00000230671.1 ENST00000230671.2 ENST00000230671.3 ENST00000230671.4 ENST00000230671.5 ENST00000230671.6 NM_014228 PROT Q0VG81 Q52LU6 Q99884 SC6A7_HUMAN SLC6A7 uc003lrr.1 uc003lrr.2 uc003lrr.3 uc003lrr.4 This gene is a member of the gamma-aminobutyric acid (GABA) neurotransmitter gene family and encodes a high-affinity mammalian brain L-proline transporter protein. This transporter protein differs from other sodium-dependent plasma membrane carriers by its pharmacological specificity, kinetic properties, and ionic requirements. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript matching the genomic sequence was available for the full length of the gene. The extent of this transcript is supported by transcript alignments. ##Evidence-Data-START## Transcript exon combination :: AK096607.1, SRR1803614.50508.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145743, SAMEA2154665 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## CDS uses downstream in-frame AUG :: upstream AUG and CDS extension is not conserved MANE Ensembl match :: ENST00000230671.7/ ENSP00000230671.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Brain specific sodium (and chloride)-dependent proline transporter (PubMed:7651355). Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals (Probable). Reaction=chloride(out) + L-proline(out) + 2 Na(+)(out) = chloride(in) + L-proline(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71263, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039; Evidence=; Reaction=chloride(out) + L-pipecolate(out) + 2 Na(+)(out) = chloride(in) + L-pipecolate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71267, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:61185; Evidence=; Kinetic parameters: KM=6.2 uM for L-proline ; Synaptic cell membrane ; Multi-pass membrane protein Brain specific (at protein level) (PubMed:7651355). Highly expressed in hippocampus, corpus striatum and temporal cortex. Also expressed in frontal cortex, occipital cortex and, at lower levels, in cerebellum and parietal cortex (at protein level) (PubMed:7651355). Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A7 subfamily. proline:sodium symporter activity neurotransmitter:sodium symporter activity plasma membrane integral component of plasma membrane neurotransmitter transport amino acid transport L-proline transmembrane transporter activity symporter activity proline transport membrane integral component of membrane proline transmembrane transport uc003lrr.1 uc003lrr.2 uc003lrr.3 uc003lrr.4 
ENST00000230771.9 HARS2 ENST00000230771.9 histidyl-tRNA synthetase 2, mitochondrial, transcript variant 1 (from RefSeq NM_012208.4) B4DDY8 ENST00000230771.1 ENST00000230771.2 ENST00000230771.3 ENST00000230771.4 ENST00000230771.5 ENST00000230771.6 ENST00000230771.7 ENST00000230771.8 HARSL HARSR HO3 NM_012208 P49590 SYHM_HUMAN uc003lgx.1 uc003lgx.2 uc003lgx.3 uc003lgx.4 uc003lgx.5 uc003lgx.6 uc003lgx.7 Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is an enzyme belonging to the class II family of aminoacyl-tRNA synthetases. Functioning in the synthesis of histidyl-transfer RNA, the enzyme plays an accessory role in the regulation of protein biosynthesis. The gene is located in a head-to-head orientation with HARS on chromosome five, where the homologous genes likely share a bidirectional promoter. Mutations in this gene are associated with the pathogenesis of Perrault syndrome, which involves ovarian dysgenesis and sensorineural hearing loss. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jul 2013]. Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L- histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21; Evidence=; Homodimer. P49590; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-3909030, EBI-741181; Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49590-1; Sequence=Displayed; Name=2; IsoId=P49590-2; Sequence=VSP_055133; A high level expression is seen in the heart, kidney and skeletal muscle while a lower level expression is seen in the brain and liver. Perrault syndrome 2 (PRLTS2) [MIM:614926]: A sex-influenced disorder characterized by sensorineural deafness in both males and females and ovarian dysgenesis in females. Affected females have primary amenorrhea, streak gonads, and infertility, whereas affected males show normal pubertal development and are fertile. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the class-II aminoacyl-tRNA synthetase family. nucleotide binding RNA binding aminoacyl-tRNA ligase activity histidine-tRNA ligase activity protein binding ATP binding cytoplasm mitochondrion mitochondrial matrix cytosol translation tRNA aminoacylation for protein translation histidyl-tRNA aminoacylation ligase activity identical protein binding protein homodimerization activity uc003lgx.1 uc003lgx.2 uc003lgx.3 uc003lgx.4 uc003lgx.5 uc003lgx.6 uc003lgx.7 
ENST00000230792.7 NUDT12 ENST00000230792.7 nudix hydrolase 12, transcript variant 1 (from RefSeq NM_031438.4) B3KUW2 B4E1W3 ENST00000230792.1 ENST00000230792.2 ENST00000230792.3 ENST00000230792.4 ENST00000230792.5 ENST00000230792.6 NM_031438 NUD12_HUMAN NUDT12 Q8TAL7 Q9BQG2 uc003koi.1 uc003koi.2 uc003koi.3 uc003koi.4 uc003koi.5 Nucleotides are involved in numerous biochemical reactions and pathways within the cell as substrates, cofactors, and effectors. Nudix hydrolases, such as NUDT12, regulate the concentrations of individual nucleotides and of nucleotide ratios in response to changing circumstances (Abdelraheim et al., 2003 [PubMed 12790796]).[supplied by OMIM, Mar 2008]. mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA (PubMed:31101919, PubMed:31875550). The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed:31101919). Preferentially acts on NAD- capped transcripts in response to nutrient stress (PubMed:31101919). Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'- ADP (PubMed:12790796). May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (PubMed:12790796). Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity). Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'- end phospho-adenosine-phospho-ribonucleoside in mRNA + beta- nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876, Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029, ChEBI:CHEBI:144051; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877; Evidence=; Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215; EC=3.6.1.22; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11801; Evidence=; Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D- ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832, ChEBI:CHEBI:456215; EC=3.6.1.22; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48869; Evidence=; Reaction=H2O + NADPH = adenosine 2',5'-bisphosphate + 2 H(+) + reduced beta-nicotinamide D-ribonucleotide; Xref=Rhea:RHEA:60820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:90832, ChEBI:CHEBI:194156; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60821; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Binds 3 Mg(2+) ions per subunit. ; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Kinetic parameters: KM=11 uM for NADH ; KM=16 uM for NADPH ; KM=190 uM for NAD ; pH dependence: Optimum pH is 8-9. ; Homodimer (PubMed:31875550). Homodimerization is essential for its catalytic activity and protein stability (PubMed:31875550). Interacts (via ANK repeats) with BLMH (PubMed:31875550). Q9BQG2; Q13867: BLMH; NbExp=8; IntAct=EBI-10230612, EBI-718504; Cytoplasm Peroxisome Cytoplasmic granule Note=Localizes to cytoplasmic granules in the presence of BLMH. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BQG2-1; Sequence=Displayed; Name=2; IsoId=Q9BQG2-2; Sequence=VSP_060395; Belongs to the Nudix hydrolase family. NudC subfamily. NAD+ diphosphatase activity protein binding nucleus cytoplasm peroxisome peroxisomal matrix cytosol NADH metabolic process NADP catabolic process hydrolase activity NAD catabolic process NAD biosynthesis via nicotinamide riboside salvage pathway NADH pyrophosphatase activity metal ion binding uc003koi.1 uc003koi.2 uc003koi.3 uc003koi.4 uc003koi.5 
ENST00000230859.8 TENT4A ENST00000230859.8 terminal nucleotidyltransferase 4A, transcript variant 1 (from RefSeq NM_006999.6) A0A0X1KG68 A8K1E2 ENST00000230859.1 ENST00000230859.2 ENST00000230859.3 ENST00000230859.4 ENST00000230859.5 ENST00000230859.6 ENST00000230859.7 M1JCE6 NM_006999 O43289 PAPD7 PAPD7_HUMAN POLS Q17RZ1 Q5XG87 Q9Y6C1 TENT4A TRF4 uc003jdx.1 uc003jdx.2 uc003jdx.3 The protein encoded by this gene is a DNA polymerase that is likely involved in DNA repair. In addition, the encoded protein may be required for sister chromatid adhesion. Alternatively spliced transcript variants that encode different isoforms have been described. [provided by RefSeq, Jan 2010]. Terminal nucleotidyltransferase that catalyzes preferentially the transfer of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation (PubMed:23376078, PubMed:30026317). Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Has no terminal uridylyltransferase activity, and does not play a role in replication- dependent histone mRNA degradation via uridylation (PubMed:23376078). Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Component of a nuclear TRAMP-like complex, an ATP-dependent exosome regulatory complex consisting of a helicase (MTREX), an oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes exist with specific compositions and are associated with nuclear, or nucleolar RNA exosomes. Cytoplasm Nucleus, nucleoplasm Note=Excluded from nucleolus, weak staining detected in the cytoplasm. Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=l; IsoId=Q5XG87-1; Sequence=Displayed; Name=2; Synonyms=s; IsoId=Q5XG87-2; Sequence=VSP_053732; [Isoform 2]: Exhibits poor nucleotidyl transferase activity. Belongs to the DNA polymerase type-B-like family. Was originally thought to have DNA polymerase activity. Sequence=AAD45198.1; Type=Frameshift; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/pols/"; nucleotide binding polynucleotide adenylyltransferase activity ATP binding nucleus nucleoplasm nucleolus cytoplasm Golgi apparatus double-strand break repair mRNA processing sister chromatid cohesion mitotic chromosome condensation transferase activity nucleotidyltransferase activity TRAMP complex nuclear membrane response to drug SMC family protein binding RNA polyadenylation metal ion binding negative regulation of nuclear-transcribed mRNA poly(A) tail shortening guanylyltransferase activity histone mRNA catabolic process snoRNA polyadenylation RNA 3' uridylation uc003jdx.1 uc003jdx.2 uc003jdx.3 
ENST00000230882.9 GHR ENST00000230882.9 growth hormone receptor, transcript variant 9 (from RefSeq NM_001242406.2) ENST00000230882.1 ENST00000230882.2 ENST00000230882.3 ENST00000230882.4 ENST00000230882.5 ENST00000230882.6 ENST00000230882.7 ENST00000230882.8 GHR_HUMAN NM_001242406 P10912 Q9HCX2 uc003jmt.1 uc003jmt.2 uc003jmt.3 uc003jmt.4 uc003jmt.5 This gene encodes a member of the type I cytokine receptor family, which is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. In humans and rabbits, but not rodents, growth hormone binding protein (GHBP) is generated by proteolytic cleavage of the extracellular ligand-binding domain from the mature growth hormone receptor protein. Multiple alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Jun 2011]. Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity). The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling. Isoform 2 up-regulates the production of GHBP and acts as a negative inhibitor of GH signaling. On growth hormone (GH) binding, forms homodimers and binds JAK2 via a box 1-containing domain. Binding to SOCS3 inhibits JAK2 activation, binding to CIS and SOCS2 inhibits STAT5 activation. Interacts with ADAM17. P10912; Q16829: DUSP7; NbExp=2; IntAct=EBI-286316, EBI-1265847; P10912; P01241: GH1; NbExp=4; IntAct=EBI-286316, EBI-1026046; P10912; P10912: GHR; NbExp=4; IntAct=EBI-286316, EBI-286316; P10912; P16333: NCK1; NbExp=3; IntAct=EBI-286316, EBI-389883; P10912; P18031: PTPN1; NbExp=5; IntAct=EBI-286316, EBI-968788; P10912; P17706: PTPN2; NbExp=8; IntAct=EBI-286316, EBI-984930; P10912; P26045: PTPN3; NbExp=4; IntAct=EBI-286316, EBI-1047946; P10912; P43378: PTPN9; NbExp=2; IntAct=EBI-286316, EBI-742898; P10912; P23467: PTPRB; NbExp=3; IntAct=EBI-286316, EBI-1265766; P10912; Q9HD43: PTPRH; NbExp=4; IntAct=EBI-286316, EBI-1267176; P10912; Q12913: PTPRJ; NbExp=2; IntAct=EBI-286316, EBI-2264500; P10912; Q9JLI4: Ncoa6; Xeno; NbExp=2; IntAct=EBI-286316, EBI-286271; Cell membrane; Single-pass type I membrane protein. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non- degradative pathway. [Isoform 2]: Cell membrane; Single-pass type I membrane protein. Note=Remains fixed to the cell membrane and is not internalized. [Growth hormone-binding protein]: Secreted. Note=Complexed to a substantial fraction of circulating GH. Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=GHRfl; IsoId=P10912-1; Sequence=Displayed; Name=2; Synonyms=GHRtr, GHR1-279; IsoId=P10912-2; Sequence=VSP_010227, VSP_010228; Name=3; Synonyms=GHR1-277; IsoId=P10912-3; Sequence=VSP_010229, VSP_010230; Name=4; Synonyms=GHRd3; IsoId=P10912-4; Sequence=VSP_010225, VSP_010226; Expressed in various tissues with high expression in liver and skeletal muscle. Isoform 4 is predominantly expressed in kidney, bladder, adrenal gland and brain stem. Isoform 1 expression in placenta is predominant in chorion and decidua. Isoform 4 is highly expressed in placental villi. Isoform 2 is expressed in lung, stomach and muscle. Low levels in liver. The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box 1 motif is required for JAK interaction and/or activation. The extracellular domain is the ligand-binding domain representing the growth hormone-binding protein (GHBP). The ubiquitination-dependent endocytosis motif (UbE) is required for recruitment of the ubiquitin conjugation system on to the receptor and for its internalization. The soluble form (GHBP) is produced by phorbol ester-promoted proteolytic cleavage at the cell surface (shedding) by ADAM17/TACE. Shedding is inhibited by growth hormone (GH) binding to the receptor probably due to a conformational change in GHR rendering the receptor inaccessible to ADAM17 (By similarity). On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2. On ligand binding, ubiquitinated on lysine residues in the cytoplasmic domain. This ubiquitination is not sufficient for GHR internalization (By similarity). Genetic variation in GHR may act as phenotype modifier in familial hypercholesterolemia [MIM:143890] patients carrying a mutation in the LDLR gene. Laron syndrome (LARS) [MIM:262500]: A severe form of growth hormone insensitivity characterized by growth impairment, short stature, dysfunctional growth hormone receptor, and failure to generate insulin-like growth factor I in response to growth hormone. te=The disease is caused by variants affecting the gene represented in this entry. Growth hormone insensitivity, partial (GHIP) [MIM:604271]: A disease characterized by partial resistance to growth hormone resulting in short stature. Short stature is defined by a standing height more than 2 standard deviations below the mean (or below the 2.5 percentile) for sex and chronological age, compared with a well-nourished, healthy, genetically relevant population. Note=The disease is caused by variants affecting the gene represented in this entry. [Isoform 4]: Arises by species-specific retrovirus- mediated alternative splice mimicry. Belongs to the type I cytokine receptor family. Type 1 subfamily. activation of MAPK activity cytokine receptor activity growth hormone receptor activity protein binding extracellular region extracellular space cytosol plasma membrane integral component of plasma membrane endocytosis JAK-STAT cascade external side of plasma membrane cell surface membrane integral component of membrane peptide hormone binding cytokine-mediated signaling pathway taurine metabolic process growth factor binding protein kinase binding cytokine binding receptor internalization response to estradiol cellular response to hormone stimulus cytoplasmic ribonucleoprotein granule regulation of multicellular organism growth positive regulation of multicellular organism growth hormone metabolic process positive regulation of tyrosine phosphorylation of STAT protein identical protein binding protein homodimerization activity activation of Janus kinase activity receptor complex positive regulation of JAK-STAT cascade response to cycloheximide insulin-like growth factor receptor signaling pathway positive regulation of peptidyl-tyrosine phosphorylation growth hormone receptor signaling pathway JAK-STAT cascade involved in growth hormone signaling pathway proline-rich region binding growth hormone receptor complex uc003jmt.1 uc003jmt.2 uc003jmt.3 uc003jmt.4 uc003jmt.5 
ENST00000230895.11 DAP ENST00000230895.11 death associated protein, transcript variant 2 (from RefSeq NM_004394.3) DAP DAP1 DAP1_HUMAN ENST00000230895.1 ENST00000230895.10 ENST00000230895.2 ENST00000230895.3 ENST00000230895.4 ENST00000230895.5 ENST00000230895.6 ENST00000230895.7 ENST00000230895.8 ENST00000230895.9 NM_004394 P51397 Q6FGC3 Q9BUC9 uc003jez.1 uc003jez.2 uc003jez.3 uc003jez.4 uc003jez.5 uc003jez.6 This gene encodes a basic, proline-rich, 15-kD protein. The protein acts as a positive mediator of programmed cell death that is induced by interferon-gamma. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, May 2014]. Ribosome-binding protein involved in ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with eiF5a (EIF5A and EIF5A2) at the polypeptide exit tunnel of the ribosome, preventing mRNA translation (By similarity). Involved in ribosome hibernation in the mature oocyte by preventing mRNA translation, leading to ribosome inactivation (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also acts as a negative regulator of autophagy (PubMed:20537536). Involved in mediating interferon-gamma-induced cell death (PubMed:7828849). Associates with ribosomes; inhibiting translation (By similarity). Interacts with eiF5a (EIF5A and EIF5A2); inhibiting translation (By similarity). Phosphorylated. Phosphorylation by MTOR inhibits the suppressive activity of DAP toward autophagy. Belongs to the DAP-DAPL1 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/dap/"; autophagy apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process negative regulation of autophagy negative regulation of NF-kappaB transcription factor activity cellular response to amino acid starvation negative regulation of transcription, DNA-templated death domain binding apoptotic signaling pathway uc003jez.1 uc003jez.2 uc003jez.3 uc003jez.4 uc003jez.5 uc003jez.6 
ENST00000230990.7 HBEGF ENST00000230990.7 heparin binding EGF like growth factor (from RefSeq NM_001945.3) B2R821 DTR DTS ENST00000230990.1 ENST00000230990.2 ENST00000230990.3 ENST00000230990.4 ENST00000230990.5 ENST00000230990.6 HBEGF_HUMAN HEGFL NM_001945 Q99075 uc003lfi.1 uc003lfi.2 uc003lfi.3 uc003lfi.4 uc003lfi.5 Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor. Interacts with FBLN1 (By similarity). Interacts with EGFR and ERBB4. Q99075; P00533: EGFR; NbExp=3; IntAct=EBI-7211558, EBI-297353; Q99075; Q15303: ERBB4; NbExp=2; IntAct=EBI-7211558, EBI-80371; Q99075; P22607: FGFR3; NbExp=3; IntAct=EBI-7211558, EBI-348399; Q99075; P06396: GSN; NbExp=3; IntAct=EBI-7211558, EBI-351506; [Heparin-binding EGF-like growth factor]: Secreted, extracellular space. Note=Mature HB-EGF is released into the extracellular space and probably binds to a receptor. [Proheparin-binding EGF-like growth factor]: Cell membrane; Single-pass type I membrane protein. Several N-termini have been identified by direct sequencing. The forms with N-termini 63, 73 and 74 have been tested and found to be biologically active. O-glycosylated with core 1 or possibly core 8 glycans. Thr-47 is a minor glycosylation site compared to Thr-44. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/dtr/"; MAPK cascade epidermal growth factor receptor binding extracellular region extracellular space plasma membrane integral component of plasma membrane signal transduction epidermal growth factor receptor signaling pathway muscle organ development regulation of heart contraction growth factor activity heparin binding positive regulation of cell proliferation cell surface membrane integral component of membrane cell migration positive regulation of cell growth positive regulation of cell migration clathrin-coated vesicle membrane endocytic vesicle membrane clathrin-coated endocytic vesicle membrane wound healing, spreading of epidermal cells ERBB2 signaling pathway negative regulation of epidermal growth factor receptor signaling pathway positive regulation of smooth muscle cell proliferation positive regulation of peptidyl-tyrosine phosphorylation negative regulation of elastin biosynthetic process positive regulation of keratinocyte migration positive regulation of protein kinase B signaling cell chemotaxis membrane organization positive regulation of wound healing regulation of cell motility uc003lfi.1 uc003lfi.2 uc003lfi.3 uc003lfi.4 uc003lfi.5 
ENST00000231004.5 LOX ENST00000231004.5 lysyl oxidase, transcript variant 1 (from RefSeq NM_002317.7) B2R5Q3 ENST00000231004.1 ENST00000231004.2 ENST00000231004.3 ENST00000231004.4 LYOX_HUMAN NM_002317 P28300 Q5FWF0 uc003ksu.1 uc003ksu.2 uc003ksu.3 uc003ksu.4 uc003ksu.5 This gene encodes a member of the lysyl oxidase family of proteins. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate a regulatory propeptide and the mature enzyme. The copper-dependent amine oxidase activity of this enzyme functions in the crosslinking of collagens and elastin, while the propeptide may play a role in tumor suppression. In addition, defects in this gene have been linked with predisposition to thoracic aortic aneurysms and dissections. [provided by RefSeq, Jul 2016]. Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:26838787). Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity). Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl- [protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence=; Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence=; Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence=; Note=Contains 1 lysine tyrosylquinone. ; Interacts with MFAP4 (PubMed:26601954). Interacts (via propeptide) with EFEMP2; this interaction is strong and facilitates formation of ternary complexes with ELN during elastic fiber assembly; this interaction limits interaction of EFEMP2 with FBLN5 (PubMed:19855011). P28300; O95967: EFEMP2; NbExp=7; IntAct=EBI-3893481, EBI-743414; P28300; P15502: ELN; NbExp=2; IntAct=EBI-3893481, EBI-1222108; P28300; Q9UBX5: FBLN5; NbExp=2; IntAct=EBI-3893481, EBI-947897; P28300; P35555: FBN1; NbExp=2; IntAct=EBI-3893481, EBI-2505934; P28300; Q15262: PTPRK; NbExp=4; IntAct=EBI-3893481, EBI-474052; PRO_0000018520; Q07507: DPT; NbExp=2; IntAct=EBI-20724846, EBI-719535; PRO_0000018520; PRO_0000007541 [P01133]: EGF; NbExp=2; IntAct=EBI-20724846, EBI-9076336; PRO_0000018520; P02751: FN1; NbExp=2; IntAct=EBI-20724846, EBI-1220319; PRO_0000018520; PRO_0000390479 [P02751]: FN1; NbExp=3; IntAct=EBI-20724846, EBI-15482592; PRO_0000018520; P00747: PLG; NbExp=2; IntAct=EBI-20724846, EBI-999394; PRO_0000018520; P21980: TGM2; NbExp=3; IntAct=EBI-20724846, EBI-727668; Secreted Secreted, extracellular space. Heart, placenta, skeletal muscle, kidney, lung and pancreas. The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. Proteolytically cleaved by BMP1 which removes the propeptide (PubMed:31152061). Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream of the BMP1 cleavage site (PubMed:31152061). The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin (By similarity). Cleavage by BMP1 to remove the propeptide does not increase enzymatic activity but increases binding to collagen (PubMed:31152061). Cleavage by ADAMTS2 produces a form with reduced collagen-binding activity (PubMed:31152061). Sulfated at Tyr-187 and also at either Tyr-183 or Tyr-184 which enhances binding to collagen. Aortic aneurysm, familial thoracic 10 (AAT10) [MIM:617168]: A form of thoracic aortic aneurysm, a disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the lysyl oxidase family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41191/LOX"; blood vessel development osteoblast differentiation regulation of protein phosphorylation protein-lysine 6-oxidase activity copper ion binding protein binding collagen binding extracellular region collagen trimer extracellular space nucleus cellular protein modification process heart development response to hormone regulation of gene expression regulation of striated muscle tissue development oxidoreductase activity oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor regulation of transforming growth factor beta receptor signaling pathway peptidyl-lysine oxidation protein oxidation extracellular matrix organization collagen fibril organization bone mineralization lung development extracellular matrix platelet-derived growth factor receptor-beta signaling pathway aorta development ascending aorta development descending aorta development wound healing response to drug regulation of apoptotic process protein kinase B signaling regulation of megakaryocyte differentiation muscle cell cellular homeostasis metal ion binding elastic fiber assembly blood vessel morphogenesis response to steroid hormone muscle fiber development oxidation-reduction process cell chemotaxis connective tissue development cellular response to organic substance DNA biosynthetic process regulation of receptor binding regulation of bone development cellular response to chemokine regulation of platelet-derived growth factor receptor-beta signaling pathway uc003ksu.1 uc003ksu.2 uc003ksu.3 uc003ksu.4 uc003ksu.5 
ENST00000231009.3 GZMK ENST00000231009.3 granzyme K (from RefSeq NM_002104.3) B2R563 ENST00000231009.1 ENST00000231009.2 GRAK_HUMAN NM_002104 P49863 TRYP2 uc003jpl.1 uc003jpl.2 uc003jpl.3 This gene product is a member of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes (CTL) and natural killer (NK) cells share the remarkable ability to recognize, bind, and lyse specific target cells. They are thought to protect their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein described here lacks consensus sequences for N-glycosylation present in other granzymes. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189667.268483.1, AK312074.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231009.3/ ENSP00000231009.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## P49863; P55061: TMBIM6; NbExp=3; IntAct=EBI-3910072, EBI-1045825; Secreted. Cytoplasmic granule. Expressed in lung, spleen, thymus and peripheral blood leukocytes. Belongs to the peptidase S1 family. Granzyme subfamily. serine-type endopeptidase activity extracellular region proteolysis peptidase activity serine-type peptidase activity hydrolase activity positive regulation of apoptotic process negative regulation of oxidoreductase activity uc003jpl.1 uc003jpl.2 uc003jpl.3 
ENST00000231021.9 CDH9 ENST00000231021.9 cadherin 9 (from RefSeq NM_016279.4) CADH9_HUMAN ENST00000231021.1 ENST00000231021.2 ENST00000231021.3 ENST00000231021.4 ENST00000231021.5 ENST00000231021.6 ENST00000231021.7 ENST00000231021.8 NM_016279 Q3B7I5 Q9ULB4 uc003jgs.1 uc003jgs.2 uc003jgs.3 This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. The extracellular domain consists of 5 subdomains, each containing a cadherin motif, and appears to determine the specificity of the protein's homophilic cell adhesion activity. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB035302.1, SRR1660809.172028.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968540, SAMEA1968968 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231021.9/ ENSP00000231021.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cell membrane ; Single-pass type I membrane protein Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. cell morphogenesis molecular_function calcium ion binding plasma membrane cell-cell adherens junction cell-cell junction assembly cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules synapse assembly cytoskeletal protein binding cell surface membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules catenin complex adherens junction organization protein homodimerization activity cell-cell adhesion mediated by cadherin cadherin binding metal ion binding cell-cell adhesion integral component of postsynaptic membrane integral component of presynaptic membrane synaptic membrane adhesion uc003jgs.1 uc003jgs.2 uc003jgs.3 
ENST00000231061.9 SPARC ENST00000231061.9 secreted protein acidic and cysteine rich, transcript variant 1 (from RefSeq NM_003118.4) D3DQH9 ENST00000231061.1 ENST00000231061.2 ENST00000231061.3 ENST00000231061.4 ENST00000231061.5 ENST00000231061.6 ENST00000231061.7 ENST00000231061.8 NM_003118 ON P09486 Q6IBK4 SPRC_HUMAN uc003lui.1 uc003lui.2 uc003lui.3 uc003lui.4 uc003lui.5 uc003lui.6 This gene encodes a cysteine-rich acidic matrix-associated protein. The encoded protein is required for the collagen in bone to become calcified but is also involved in extracellular matrix synthesis and promotion of changes to cell shape. The gene product has been associated with tumor suppression but has also been correlated with metastasis based on changes to cell shape which can promote tumor cell invasion. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2015]. Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity. P09486; P02461-1: COL3A1; NbExp=4; IntAct=EBI-2800983, EBI-15740444; P09486; Q99972: MYOC; NbExp=3; IntAct=EBI-2800983, EBI-11692272; P09486; Q2TV77: faf; Xeno; NbExp=4; IntAct=EBI-2800983, EBI-6405263; Secreted, extracellular space, extracellular matrix, basement membrane te=In or around the basement membrane. Expressed at high levels in tissues undergoing morphogenesis, remodeling and wound repair. Osteogenesis imperfecta 17 (OI17) [MIM:616507]: An autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the SPARC family. Sequence=AAA60993.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence=; Name=Wikipedia; Note=Osteonectin entry; URL="https://en.wikipedia.org/wiki/Osteonectin"; ossification negative regulation of endothelial cell proliferation platelet degranulation extracellular matrix structural constituent calcium ion binding protein binding collagen binding extracellular region basement membrane extracellular space nucleus cytoplasm receptor-mediated endocytosis heart development response to gravity cell surface response to lead ion positive regulation of endothelial cell migration nuclear matrix negative regulation of angiogenesis regulation of cell morphogenesis extracellular matrix organization lung development extracellular matrix platelet alpha granule platelet alpha granule membrane platelet alpha granule lumen vesicle response to lipopolysaccharide response to L-ascorbic acid response to cytokine wound healing regulation of cell proliferation response to peptide hormone pigmentation synapse response to ethanol response to cadmium ion metal ion binding inner ear development regulation of synapse organization extracellular matrix binding response to glucocorticoid response to cAMP response to calcium ion bone development cellular response to growth factor stimulus endocytic vesicle lumen glutamatergic synapse mitochondrion plasma membrane uc003lui.1 uc003lui.2 uc003lui.3 uc003lui.4 uc003lui.5 uc003lui.6 
ENST00000231121.3 HAND1 ENST00000231121.3 heart and neural crest derivatives expressed 1 (from RefSeq NM_004821.3) BHLHA27 EHAND ENST00000231121.1 ENST00000231121.2 HAND1_HUMAN NM_004821 O96004 uc003lvn.1 uc003lvn.2 uc003lvn.3 uc003lvn.4 The protein encoded by this gene belongs to the basic helix-loop-helix family of transcription factors. This gene product is one of two closely related family members, the HAND proteins, which are asymmetrically expressed in the developing ventricular chambers and play an essential role in cardiac morphogenesis. Working in a complementary fashion, they function in the formation of the right ventricle and aortic arch arteries, implicating them as mediators of congenital heart disease. In addition, it has been suggested that this transcription factor may be required for early trophoblast differentiation. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC021190.2, AF061756.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2148874, SAMEA2153932 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231121.3/ ENSP00000231121.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Transcription factor that plays an essential role in both trophoblast giant cell differentiation and in cardiac morphogenesis (By similarity). Binds the DNA sequence 5'-NRTCTG-3' (non-canonical E-box) (By similarity). Acts as a transcriptional repressor of SOX15 (By similarity). In the adult, could be required for ongoing expression of cardiac-specific genes (PubMed:9931445). Efficient DNA binding requires dimerization with another bHLH protein. Forms homodimers and heterodimers with TCF3 gene products E12 and E47, HAND2 and HEY1, HEY2 and HEYL (hairy-related transcription factors). Interacts with MDFIC (By similarity). Interacts with SOX15; the interaction enhances HAND1-induced differentiation of trophoblast giant cells (By similarity). O96004; G5E9A7: DMWD; NbExp=3; IntAct=EBI-11320290, EBI-10976677; O96004; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-11320290, EBI-12012928; O96004; D3DTS7: PMP22; NbExp=3; IntAct=EBI-11320290, EBI-25882629; O96004; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-11320290, EBI-5235340; O96004; Q99081-3: TCF12; NbExp=3; IntAct=EBI-11320290, EBI-11952764; O96004; P15923-3: TCF3; NbExp=3; IntAct=EBI-11320290, EBI-12000326; O96004; Q86WV8: TSC1; NbExp=3; IntAct=EBI-11320290, EBI-12806590; Nucleus, nucleoplasm Nucleus, nucleolus Note=Interaction with MDFIC sequesters it into the nucleolus, preventing the transcription factor activity. Phosphorylation by PLK4 disrupts the interaction with MDFIC and releases it from the nucleolus, leading to transcription factor activity (By similarity). Heart. Phosphorylation by PLK4 disrupts the interaction with MDFIC and leads to translocation into the nucleoplasm, allowing dimerization and transcription factor activity. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding angiogenesis in utero embryonic development mesoderm formation blastocyst development trophectodermal cell differentiation heart looping embryonic heart tube formation cardiac left ventricle formation cardiac right ventricle formation DNA binding transcription coactivator activity protein binding nucleus nucleoplasm nucleolus cytoplasm transcription from RNA polymerase II promoter multicellular organism development heart development transcription factor binding enzyme binding cell differentiation embryonic heart tube development odontogenesis of dentin-containing tooth identical protein binding protein homodimerization activity bHLH transcription factor binding negative regulation of sequence-specific DNA binding transcription factor activity sequence-specific DNA binding negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity protein dimerization activity ventricular cardiac muscle tissue morphogenesis cardiac septum morphogenesis mesenchyme development cartilage morphogenesis trophoblast giant cell differentiation determination of heart left/right asymmetry RNA polymerase II transcription factor complex negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding transcription regulatory region DNA binding uc003lvn.1 uc003lvn.2 uc003lvn.3 uc003lvn.4 
ENST00000231130.3 PCDHB3 ENST00000231130.3 protocadherin beta 3 (from RefSeq NM_018937.5) B2R8P2 ENST00000231130.1 ENST00000231130.2 NM_018937 PCDB3_HUMAN Q9Y5E6 uc003lio.1 uc003lio.2 uc003lio.3 uc003lio.4 uc003lio.5 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: AK313451.1, AF217755.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231130.3/ ENSP00000231130.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Q9Y5E6; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-24224850, EBI-11139477; Cell membrane ; Single-pass type I membrane protein calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules chemical synaptic transmission nervous system development synapse assembly membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules uc003lio.1 uc003lio.2 uc003lio.3 uc003lio.4 uc003lio.5 
ENST00000231134.8 PCDHB5 ENST00000231134.8 protocadherin beta 5 (from RefSeq NM_015669.5) ENST00000231134.1 ENST00000231134.2 ENST00000231134.3 ENST00000231134.4 ENST00000231134.5 ENST00000231134.6 ENST00000231134.7 NM_015669 PCDB5_HUMAN Q549F4 Q9UFU9 Q9Y5E4 uc003liq.1 uc003liq.2 uc003liq.3 uc003liq.4 uc003liq.5 uc003liq.6 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: SRR1660807.168422.1, SRR1660803.263366.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231134.8/ ENSP00000231134.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Cell membrane ; Single-pass type I membrane protein calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules chemical synaptic transmission synapse assembly membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules uc003liq.1 uc003liq.2 uc003liq.3 uc003liq.4 uc003liq.5 uc003liq.6 
ENST00000231136.4 PCDHB6 ENST00000231136.4 protocadherin beta 6, transcript variant 1 (from RefSeq NM_018939.4) B2R8R9 ENST00000231136.1 ENST00000231136.2 ENST00000231136.3 NM_018939 PCDB6_HUMAN PCDHB6 Q9Y5E3 uc003lir.1 uc003lir.2 uc003lir.3 uc003lir.4 uc003lir.5 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. Unlike the alpha and gamma clusters, the transcripts from these genes do not share common 3' exons. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell neural connections. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]. Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain. Forms homodimers in trans (molecules expressed by two different cells). Forms promiscuous heterodimers in cis (at the plasma membrane of the same cell) with other protocadherins. Cell membrane ; Single-pass type I membrane protein Cadherin 1 to cadherin 4 domains mediate homophilic trans- interaction, the interaction with an identical protocadherin expressed by a neighboring cell. This is a head-to-tail interaction, the cadherin 1 domain interacting with the cadherin 4 domain and the cadherin 2 domain interacting the cadherin 3 domain of the other protocadherin. The cadherin 6 domain mediates promiscuous interactions with protocadherins on the same cell membrane. Each cadherin domain binds three calcium ions. calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules chemical synaptic transmission nervous system development synapse assembly cell-cell recognition membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules identical protein binding metal ion binding uc003lir.1 uc003lir.2 uc003lir.3 uc003lir.4 uc003lir.5 
ENST00000231137.6 PCDHB7 ENST00000231137.6 protocadherin beta 7 (from RefSeq NM_018940.4) A1L3Y8 ENST00000231137.1 ENST00000231137.2 ENST00000231137.3 ENST00000231137.4 ENST00000231137.5 NM_018940 PCDB7_HUMAN Q9Y5E2 uc003lit.1 uc003lit.2 uc003lit.3 uc003lit.4 uc003lit.5 uc003lit.6 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. The transcript for this particular family member uses more than one polyadenylation site. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: SRR1803616.27540.1, AF217750.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231137.6/ ENSP00000231137.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Cell membrane ; Single-pass type I membrane protein calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules membrane integral component of membrane uc003lit.1 uc003lit.2 uc003lit.3 uc003lit.4 uc003lit.5 uc003lit.6 
ENST00000231173.6 PCDHB15 ENST00000231173.6 protocadherin beta 15 (from RefSeq NM_018935.4) ENST00000231173.1 ENST00000231173.2 ENST00000231173.3 ENST00000231173.4 ENST00000231173.5 NM_018935 PCDBF_HUMAN Q8IUX5 Q9Y5E8 uc003lje.1 uc003lje.2 uc003lje.3 uc003lje.4 uc003lje.5 uc003lje.6 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: SRR1803616.131073.1, SRR1803615.178351.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231173.6/ ENSP00000231173.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Cell membrane ; Single-pass type I membrane protein calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules nervous system development membrane integral component of membrane photoreceptor connecting cilium uc003lje.1 uc003lje.2 uc003lje.3 uc003lje.4 uc003lje.5 uc003lje.6 
ENST00000231198.12 THG1L ENST00000231198.12 tRNA-histidine guanylyltransferase 1 like, transcript variant 1 (from RefSeq NM_017872.5) D3DQJ5 ENST00000231198.1 ENST00000231198.10 ENST00000231198.11 ENST00000231198.2 ENST00000231198.3 ENST00000231198.4 ENST00000231198.5 ENST00000231198.6 ENST00000231198.7 ENST00000231198.8 ENST00000231198.9 ICF45 NM_017872 Q53G12 Q7L5R3 Q9H0S2 Q9NWX6 THG1_HUMAN uc003lxd.1 uc003lxd.2 uc003lxd.3 uc003lxd.4 uc003lxd.5 The protein encoded by this gene is a mitochondrial protein that is induced by high levels of glucose and is associated with diabetic nephropathy. The encoded protein appears to increase mitochondrial biogenesis, which could lead to renal fibrosis. Another function of this protein is that of a guanyltransferase, adding GMP to the 5' end of tRNA(His). Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2015]. Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis (Probable). Also functions as a guanyl-nucleotide exchange factor/GEF for the MFN1 and MFN2 mitofusins thereby regulating mitochondrial fusion (PubMed:25008184, PubMed:27307223). By regulating both mitochondrial dynamics and bioenergetic function, it contributes to cell survival following oxidative stress (PubMed:25008184, PubMed:27307223). Reaction=a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate + H(+); Xref=Rhea:RHEA:54564, Rhea:RHEA-COMP:14193, Rhea:RHEA- COMP:14917, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:138282, ChEBI:CHEBI:141847, ChEBI:CHEBI:456215; EC=2.7.7.79; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Binds 2 magnesium ions per subunit. ; Homotetramer (PubMed:21059936). Interacts with MFN1 and MFN2; functions as a guanyl-nucleotide exchange factor/GEF for MFN2 and also probably MFN1 (PubMed:25008184). Q9NWX6; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-746510, EBI-739832; Q9NWX6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746510, EBI-741158; Q9NWX6; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-746510, EBI-742388; Q9NWX6; O00560: SDCBP; NbExp=3; IntAct=EBI-746510, EBI-727004; Q9NWX6; P54274: TERF1; NbExp=2; IntAct=EBI-746510, EBI-710997; Q9NWX6; Q9NWX6: THG1L; NbExp=4; IntAct=EBI-746510, EBI-746510; Cytoplasm Mitochondrion outer membrane Expressed in many tissues. Spinocerebellar ataxia, autosomal recessive, 28 (SCAR28) [MIM:618800]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR28 patients manifest mild motor developmental delay, gait ataxia, and dysarthria. Some patients show mildly impaired intellectual development. Disease onset is in early childhood. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the tRNA(His) guanylyltransferase family. Sequence=AAH01523.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAH01852.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; tRNA binding nucleotide binding magnesium ion binding protein binding ATP binding GTP binding cytoplasm mitochondrion cytosol tRNA modification tRNA processing tRNA guanylyltransferase activity transferase activity nucleotidyltransferase activity identical protein binding metal ion binding protein homotetramerization tRNA 5'-end processing transferase complex uc003lxd.1 uc003lxd.2 uc003lxd.3 uc003lxd.4 uc003lxd.5 
ENST00000231228.3 IL12B ENST00000231228.3 interleukin 12B (from RefSeq NM_002187.3) ENST00000231228.1 ENST00000231228.2 IL12B_HUMAN NKSF2 NM_002187 P29460 uc003lxr.1 uc003lxr.2 uc003lxr.3 This gene encodes a subunit of interleukin 12, a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. Interleukin 12 is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit encoded by this gene, and a 35 kD subunit encoded by IL12A. This cytokine is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. This cytokine has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Overexpression of this gene was observed in the central nervous system of patients with multiple sclerosis (MS), suggesting a role of this cytokine in the pathogenesis of the disease. The promoter polymorphism of this gene has been reported to be associated with the severity of atopic and non-atopic asthma in children. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M65290.1, M65272.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231228.3/ ENSP00000231228.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC. Associates with IL23A to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of pro-inflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis. Heterodimer with IL12A; disulfide-linked. The heterodimer is known as interleukin IL-12. Heterodimer with IL23A; disulfide-linked. The heterodimer is known as interleukin IL-23. Also secreted as a monomer. Interacts with NBR1; this interaction promotes IL-12 secretion (By similarity). P29460; P29459: IL12A; NbExp=2; IntAct=EBI-1029614, EBI-1029636; P29460; P29460: IL12B; NbExp=2; IntAct=EBI-1029614, EBI-1029614; P29460; Q9NPF7: IL23A; NbExp=6; IntAct=EBI-1029614, EBI-2481154; P29460; Q9EQ14: Il23a; Xeno; NbExp=2; IntAct=EBI-1029614, EBI-2481329; Secreted. Known to be C-mannosylated in the recombinant protein; it is not yet known for sure if the wild-type protein is also modified. Immunodeficiency 29 (IMD29) [MIM:614890]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous- like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD29 is characterized by undetectable IL12B secretion from leukocytes. Affected individuals generally present with BCG disease after vaccination in childhood, and at least half also have Salmonella infection. Disease phenotype is relatively mild, and patients have a good prognosis. te=The disease is caused by variants affecting the gene represented in this entry. Psoriasis 11 (PSORS11) [MIM:612599]: A common, chronic inflammatory disease of the skin with multifactorial etiology. It is characterized by red, scaly plaques usually found on the scalp, elbows and knees. These lesions are caused by abnormal keratinocyte proliferation and infiltration of inflammatory cells into the dermis and epidermis. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the IL-12B family. Name=IL12Bbase; Note=IL12B mutation db; URL="http://structure.bmc.lu.se/idbase/IL12Bbase/"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/il12b/"; positive regulation of T cell mediated cytotoxicity positive regulation of defense response to virus by host natural killer cell activation involved in immune response positive regulation of T-helper 1 type immune response positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target negative regulation of inflammatory response to antigenic stimulus cytokine receptor activity cytokine activity cytokine receptor binding interleukin-12 receptor binding protein binding extracellular region extracellular space cytoplasm endoplasmic reticulum lumen cytosol cell cycle arrest cell surface receptor signaling pathway cell proliferation external side of plasma membrane cell surface response to organic substance response to UV-B positive regulation of activation of Janus kinase activity membrane cell migration cytokine-mediated signaling pathway sensory perception of pain sexual reproduction cytokine binding natural killer cell activation late endosome lumen negative regulation of interleukin-10 production negative regulation of interleukin-17 production positive regulation of granulocyte macrophage colony-stimulating factor production positive regulation of interferon-gamma production positive regulation of interleukin-10 production positive regulation of interleukin-12 production positive regulation of interleukin-17 production positive regulation of tumor necrosis factor production positive regulation of natural killer cell activation positive regulation of natural killer cell proliferation positive regulation of mononuclear cell proliferation positive regulation of tissue remodeling positive regulation of smooth muscle cell apoptotic process interleukin-12-mediated signaling pathway T-helper 1 cell cytokine production interleukin-23-mediated signaling pathway regulation of cytokine biosynthetic process T-helper 1 type immune response T-helper cell differentiation interferon-gamma biosynthetic process positive regulation of T cell proliferation positive regulation of activated T cell proliferation interleukin-12 alpha subunit binding regulation of tyrosine phosphorylation of STAT protein positive regulation of tyrosine phosphorylation of STAT protein identical protein binding protein homodimerization activity defense response to protozoan receptor complex positive regulation of memory T cell differentiation interleukin-12 complex positive regulation of interferon-gamma biosynthetic process positive regulation of osteoclast differentiation positive regulation of cell adhesion protein heterodimerization activity negative regulation of smooth muscle cell proliferation positive regulation of lymphocyte proliferation positive regulation of inflammatory response defense response to Gram-negative bacterium positive regulation of NK T cell activation positive regulation of NK T cell proliferation defense response to virus interleukin-23 complex cellular response to lipopolysaccharide cellular response to interferon-gamma positive regulation of NIK/NF-kappaB signaling positive regulation of T-helper 17 type immune response positive regulation of T-helper 17 cell lineage commitment growth factor activity interleukin-23 receptor binding uc003lxr.1 uc003lxr.2 uc003lxr.3 
ENST00000231238.10 TTC1 ENST00000231238.10 tetratricopeptide repeat domain 1, transcript variant 1 (from RefSeq NM_003314.3) B2RCT2 D3DQJ8 ENST00000231238.1 ENST00000231238.2 ENST00000231238.3 ENST00000231238.4 ENST00000231238.5 ENST00000231238.6 ENST00000231238.7 ENST00000231238.8 ENST00000231238.9 NM_003314 Q99614 Q9BVT3 TPR1 TTC1_HUMAN uc003lxu.1 uc003lxu.2 uc003lxu.3 uc003lxu.4 uc003lxu.5 uc003lxu.6 This gene encodes a protein that belongs to the tetratrico peptide repeat superfamily of proteins. The encoded protein plays a role in protein-protein interactions, and binds to the Galpha subunit of G protein-coupled receptors to activate the Ras signaling pathway. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]. Interacts with the GAP domain of NF1 (PubMed:8836031). Interacts (via TPR repeats) with HSP90AA1 and HSPA8 (PubMed:15708368). Q99614; Q9UHQ9: CYB5R1; NbExp=3; IntAct=EBI-742074, EBI-953870; Q99614; P28799: GRN; NbExp=3; IntAct=EBI-742074, EBI-747754; Q99614; P04792: HSPB1; NbExp=3; IntAct=EBI-742074, EBI-352682; Q99614; P42858: HTT; NbExp=9; IntAct=EBI-742074, EBI-466029; Q99614; A0A0S2Z528: PSTPIP1; NbExp=3; IntAct=EBI-742074, EBI-16430249; Q99614; Q9H4P4: RNF41; NbExp=10; IntAct=EBI-742074, EBI-2130266; Q99614; O76024: WFS1; NbExp=3; IntAct=EBI-742074, EBI-720609; protein binding peroxisomal membrane cytosol protein folding unfolded protein binding uc003lxu.1 uc003lxu.2 uc003lxu.3 uc003lxu.4 uc003lxu.5 uc003lxu.6 
ENST00000231357.7 IRX4 ENST00000231357.7 iroquois homeobox 4, transcript variant 5 (from RefSeq NM_016358.3) B2RMW5 D3DTC5 ENST00000231357.1 ENST00000231357.2 ENST00000231357.3 ENST00000231357.4 ENST00000231357.5 ENST00000231357.6 H1AFL0 H1AFL1 IRX4_HUMAN IRXA3 NM_016358 P78413 Q2NL64 Q9UHR2 uc003jcz.1 uc003jcz.2 uc003jcz.3 Likely to be an important mediator of ventricular differentiation during cardiac development. Interacts with the vitamin D receptor VDR but doesn't affect its transactivation activity. P78413; P78424: POU6F2; NbExp=3; IntAct=EBI-12073510, EBI-12029004; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P78413-1; Sequence=Displayed; Name=2; IsoId=P78413-2; Sequence=VSP_054304; Predominantly expressed in cardiac ventricles. Belongs to the TALE/IRO homeobox family. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter heart development sequence-specific DNA binding establishment of animal organ orientation uc003jcz.1 uc003jcz.2 uc003jcz.3 
ENST00000231368.10 LNPEP ENST00000231368.10 leucyl and cystinyl aminopeptidase, transcript variant 1 (from RefSeq NM_005575.3) ENST00000231368.1 ENST00000231368.2 ENST00000231368.3 ENST00000231368.4 ENST00000231368.5 ENST00000231368.6 ENST00000231368.7 ENST00000231368.8 ENST00000231368.9 LCAP_HUMAN NM_005575 O00769 OTASE Q15145 Q59H76 Q9TNQ2 Q9TNQ3 Q9UIQ6 Q9UIQ7 uc003kmv.1 uc003kmv.2 uc003kmv.3 This gene encodes a zinc-dependent aminopeptidase that cleaves vasopressin, oxytocin, lys-bradykinin, met-enkephalin, dynorphin A and other peptide hormones. The protein can be secreted in maternal serum, reside in intracellular vesicles with the insulin-responsive glucose transporter GLUT4, or form a type II integral membrane glycoprotein. The protein catalyzes the final step in the conversion of angiotensinogen to angiotensin IV (AT4) and is also a receptor for AT4. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]. Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain. Reaction=Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however.; EC=3.4.11.3; Evidence= Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Homodimer. Binds tankyrases 1 and 2. Q9UIQ6; Q969F0: FATE1; NbExp=3; IntAct=EBI-2805360, EBI-743099; Q9UIQ6; Q04864: REL; NbExp=3; IntAct=EBI-2805360, EBI-307352; Q9UIQ6; P15884: TCF4; NbExp=3; IntAct=EBI-2805360, EBI-533224; Q9UIQ6; Q9H2K2: TNKS2; NbExp=3; IntAct=EBI-2805360, EBI-4398527; Q9UIQ6-2; Q13520: AQP6; NbExp=3; IntAct=EBI-12133176, EBI-13059134; Q9UIQ6-2; P07307-3: ASGR2; NbExp=3; IntAct=EBI-12133176, EBI-12808270; Q9UIQ6-2; Q99675: CGRRF1; NbExp=3; IntAct=EBI-12133176, EBI-2130213; Q9UIQ6-2; P78358: CTAG1B; NbExp=3; IntAct=EBI-12133176, EBI-1188472; Q9UIQ6-2; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-12133176, EBI-18938272; Q9UIQ6-2; Q969F0: FATE1; NbExp=3; IntAct=EBI-12133176, EBI-743099; Q9UIQ6-2; Q9UJ14: GGT7; NbExp=3; IntAct=EBI-12133176, EBI-1058791; Q9UIQ6-2; O15529: GPR42; NbExp=3; IntAct=EBI-12133176, EBI-18076404; Q9UIQ6-2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12133176, EBI-11721746; Q9UIQ6-2; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-12133176, EBI-1052304; Q9UIQ6-2; P80188: LCN2; NbExp=3; IntAct=EBI-12133176, EBI-11911016; Q9UIQ6-2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12133176, EBI-2820517; Q9UIQ6-2; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-12133176, EBI-6163737; Q9UIQ6-2; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12133176, EBI-7545592; Q9UIQ6-2; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-12133176, EBI-13389236; Q9UIQ6-2; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-12133176, EBI-2823239; Q9UIQ6-2; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12133176, EBI-17280858; Q9UIQ6-2; P27105: STOM; NbExp=3; IntAct=EBI-12133176, EBI-1211440; Q9UIQ6-2; P59542: TAS2R19; NbExp=3; IntAct=EBI-12133176, EBI-12847034; Q9UIQ6-2; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-12133176, EBI-12947623; Q9UIQ6-2; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-12133176, EBI-11722971; Q9UIQ6-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12133176, EBI-741480; Q9UIQ6-2; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-12133176, EBI-13356252; Cell membrane ; Single-pass type II membrane protein Note=In brain only the membrane-bound form is found. The protein resides in intracellular vesicles together with GLUT4 and can then translocate to the cell surface in response to insulin and/or oxytocin. Localization may be determined by dileucine internalization motifs, and/or by interaction with tankyrases. [Leucyl-cystinyl aminopeptidase, pregnancy serum form]: Secreted. Note=During pregnancy serum levels are low in the first trimester, rise progressively during the second and third trimester and decrease rapidly after parturition. Event=Alternative splicing; Named isoforms=3; Comment=Experimental confirmation may be lacking for some isoforms.; Name=1; IsoId=Q9UIQ6-1; Sequence=Displayed; Name=2; IsoId=Q9UIQ6-2; Sequence=VSP_005448; Name=3; IsoId=Q9UIQ6-3; Sequence=VSP_005449; Highly expressed in placenta, heart, kidney and small intestine. Detected at lower levels in neuronal cells in the brain, in skeletal muscle, spleen, liver, testes and colon. The pregnancy serum form is derived from the membrane-bound form by proteolytic processing. N-glycosylated. Belongs to the peptidase M1 family. Sequence=BAA09436.1; Type=Erroneous initiation; Evidence=; Sequence=BAD92120.1; Type=Frameshift; Evidence=; protein polyubiquitination antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent aminopeptidase activity protein binding extracellular region cytoplasm lysosomal membrane cytosol plasma membrane integral component of plasma membrane proteolysis cell-cell signaling female pregnancy peptidase activity metallopeptidase activity zinc ion binding membrane integral component of membrane hydrolase activity protein catabolic process cytoplasmic vesicle membrane early endosome lumen peptide binding peptide catabolic process metal ion binding perinuclear region of cytoplasm SMAD protein signal transduction metalloaminopeptidase activity uc003kmv.1 uc003kmv.2 uc003kmv.3 
ENST00000231420.11 AGXT2 ENST00000231420.11 alanine--glyoxylate aminotransferase 2, transcript variant 1 (from RefSeq NM_031900.4) AGT2 AGT2_HUMAN B7ZM47 E9PDL7 ENST00000231420.1 ENST00000231420.10 ENST00000231420.2 ENST00000231420.3 ENST00000231420.4 ENST00000231420.5 ENST00000231420.6 ENST00000231420.7 ENST00000231420.8 ENST00000231420.9 NM_031900 Q53FB4 Q53FY7 Q53G03 Q5W7Q1 Q9BYV1 uc003jjf.1 uc003jjf.2 uc003jjf.3 uc003jjf.4 uc003jjf.5 The protein encoded by this gene is a class III pyridoxal-phosphate-dependent mitochondrial aminotransferase. It catalyzes the conversion of glyoxylate to glycine using L-alanine as the amino donor. It is an important regulator of methylarginines and is involved in the control of blood pressure in kidney. Polymorphisms in this gene affect methylarginine and beta-aminoisobutyrate metabolism, and are associated with carotid atherosclerosis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2015]. Multifunctional aminotransferase with a broad substrate specifcity (PubMed:20018850, PubMed:24586340, PubMed:23023372). Catalyzes the conversion of glyoxylate to glycine using alanine as the amino donor (By similarity). Catalyzes metabolism of not L- but the D- isomer of D-beta-aminoisobutyric acid to generate 2-methyl-3- oxopropanoate and alanine (PubMed:24586340). Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L-alanine and 3- oxopropanoate (By similarity). Can metabolize NG-monomethyl-L-arginine (NMMA), asymmetric NG,NG-dimethyl-L-arginine (ADMA) and symmetric NG,N'G-dimethyl-L-arginine (SDMA) (PubMed:20018850, PubMed:23023372). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure (PubMed:20018850, PubMed:23023372). Reaction=glyoxylate + L-alanine = glycine + pyruvate; Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249; Evidence=; Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3- oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361, ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18394; Evidence=; Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate; Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190, ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14079; Evidence=; Reaction=2-oxobutanoate + L-alanine = (2S)-2-aminobutanoate + pyruvate; Xref=Rhea:RHEA:77355, ChEBI:CHEBI:15361, ChEBI:CHEBI:16763, ChEBI:CHEBI:57972, ChEBI:CHEBI:74359; EC=2.6.1.44; Evidence=; Reaction=N(omega),N(omega)-dimethyl-L-arginine + pyruvate = 5-(3,3- dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77303, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence=; Reaction=N(omega),N('omega)-dimethyl-L-arginine + pyruvate = 5-(3,3'- dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77307, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:197308, ChEBI:CHEBI:197310; Evidence=; Reaction=glyoxylate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3- dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77311, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence=; Reaction=glyoxylate + N(omega),N('omega)-dimethyl-L-arginine = 5-(3,3'- dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77315, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:197308, ChEBI:CHEBI:197310; Evidence=; Reaction=N(omega)-methyl-L-arginine + pyruvate = 5-(3-methylguanidino)- 2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77319, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; Evidence=; Reaction=glyoxylate + N(omega)-methyl-L-arginine = 5-(3- methylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77323, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; Evidence=; Reaction=L-ornithine + pyruvate = 5-amino-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77327, ChEBI:CHEBI:15361, ChEBI:CHEBI:46911, ChEBI:CHEBI:57972, ChEBI:CHEBI:58802; Evidence=; Reaction=glyoxylate + L-ornithine = 5-amino-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77331, ChEBI:CHEBI:36655, ChEBI:CHEBI:46911, ChEBI:CHEBI:57305, ChEBI:CHEBI:58802; Evidence=; Reaction=(2S)-2-aminobutanoate + glyoxylate = 2-oxobutanoate + glycine; Xref=Rhea:RHEA:77339, ChEBI:CHEBI:16763, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:74359; Evidence=; Reaction=N(omega),N(omega)-dimethyl-L-arginine + oxaloacetate = 5-(3,3- dimethylguanidino)-2-oxopentanoate + L-aspartate; Xref=Rhea:RHEA:77343, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence=; Reaction=L-alanine + oxaloacetate = L-aspartate + pyruvate; Xref=Rhea:RHEA:77347, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:57972; Evidence=; Reaction=2-oxobutanoate + N(omega),N(omega)-dimethyl-L-arginine = (2S)- 2-aminobutanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate; Xref=Rhea:RHEA:77351, ChEBI:CHEBI:16763, ChEBI:CHEBI:58326, ChEBI:CHEBI:74359, ChEBI:CHEBI:197301; Evidence=; Reaction=2-oxopentanoate + N(omega),N(omega)-dimethyl-L-arginine = 5- (3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminopentanoate; Xref=Rhea:RHEA:77359, ChEBI:CHEBI:28644, ChEBI:CHEBI:58326, ChEBI:CHEBI:58441, ChEBI:CHEBI:197301; Evidence=; Reaction=2-oxohexanoate + N(omega),N(omega)-dimethyl-L-arginine = 5- (3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminohexanoate; Xref=Rhea:RHEA:77363, ChEBI:CHEBI:35177, ChEBI:CHEBI:58326, ChEBI:CHEBI:58455, ChEBI:CHEBI:197301; Evidence=; Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence=; Homotetramer. Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BYV1-1; Sequence=Displayed; Name=2; IsoId=Q9BYV1-2; Sequence=VSP_055802; Expressed in the convoluted tubule in the kidney and in the liver hepatocytes (at protein level). Genetic variants in AGXT2 are association with beta- aminoisobutyric aciduria (BAIBA)[MIM:210100]. Excretion of beta- aminoisobutyric acid in urine is a common, benign, metabolic trait. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. catalytic activity mitochondrion mitochondrial matrix alanine-glyoxylate transaminase activity transaminase activity glyoxylate catabolic process transferase activity glycine biosynthetic process, by transamination of glyoxylate L-alanine catabolic process, by transamination pyridoxal phosphate binding positive regulation of nitric oxide biosynthetic process glyoxylate metabolic process (R)-3-amino-2-methylpropionate-pyruvate transaminase activity uc003jjf.1 uc003jjf.2 uc003jjf.3 uc003jjf.4 uc003jjf.5 
ENST00000231449.7 IL4 ENST00000231449.7 interleukin 4, transcript variant 1 (from RefSeq NM_000589.4) ENST00000231449.1 ENST00000231449.2 ENST00000231449.3 ENST00000231449.4 ENST00000231449.5 ENST00000231449.6 IL4_HUMAN NM_000589 P05112 Q14630 Q6NZ77 uc003kxk.1 uc003kxk.2 uc003kxk.3 uc003kxk.4 The protein encoded by this gene is a pleiotropic cytokine produced by activated T cells. This cytokine is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. This gene, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. IL4 is considered an important cytokine for tissue repair, counterbalancing the effects of proinflammatory type 1 cytokines, however, it also promotes allergic airway inflammation. Moreover, IL-4, a type 2 cytokine, mediates and regulates a variety of human host responses such as allergic, anti-parasitic, wound healing, and acute inflammation. This cytokine has been reported to promote resolution of neutrophil-mediated acute lung injury. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2020]. Cytokine secreted primarily by mast cells, T-cells, eosinophils, and basophils that plays a role in regulating antibody production, hematopoiesis and inflammation, and the development of effector T-cell responses (PubMed:3016727, PubMed:1993171). Induces the expression of class II MHC molecules on resting B-cells. Enhances both secretion and cell surface expression of IgE and IgG1 (PubMed:1993171). Regulates also the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes (PubMed:2521231). Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4. In addition, plays a critical role in higher functions of the normal brain, such as memory and learning (By similarity). Upon binding to IL4, IL4R receptor dimerizes either with the common IL2R gamma chain/IL2RG to produce the type 1 signaling complex, located mainly on hematopoietic cells, or with the IL13RA1 to produce the type 2 complex, which is expressed also on nonhematopoietic cells (PubMed:10219247, PubMed:11526337, PubMed:18243101). Engagement of both types of receptors initiates JAK3 and to a lower extend JAK1 phosphorylation leading to activation of the signal transducer and activator of transcription 6/STAT6 (PubMed:7721895). Interacts with IL4R (PubMed:10219247, PubMed:11526337). Interacts with IL13RA1 (PubMed:18243101). P05112; P78552: IL13RA1; NbExp=3; IntAct=EBI-367025, EBI-1391535; P05112; P24394: IL4R; NbExp=7; IntAct=EBI-367025, EBI-367009; Secreted. Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Long; IsoId=P05112-1; Sequence=Displayed; Name=2; Synonyms=Short, IL-4delta2; IsoId=P05112-2; Sequence=VSP_002672; Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the IL-4/IL-13 family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/il4/"; cytokine activity cytokine receptor binding interleukin-4 receptor binding protein binding extracellular region extracellular space immune response growth factor activity cholesterol metabolic process positive regulation of gene expression negative regulation of epithelial cell migration positive regulation of macroautophagy cytokine-mediated signaling pathway B cell differentiation positive regulation of B cell proliferation positive regulation of interleukin-13 production T-helper 2 cell cytokine production type 2 immune response positive regulation of T cell proliferation T cell activation B cell activation regulation of phosphorylation positive regulation of tyrosine phosphorylation of STAT protein negative regulation of tumor necrosis factor biosynthetic process activation of Janus kinase activity myeloid dendritic cell differentiation negative regulation of apoptotic process connective tissue growth factor biosynthetic process regulation of isotype switching positive regulation of MHC class II biosynthetic process positive regulation of T cell differentiation negative regulation of osteoclast differentiation negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter positive regulation of receptor-mediated endocytosis positive regulation of isotype switching to IgE isotypes positive regulation of isotype switching to IgG isotypes regulation of immune response dendritic cell differentiation positive regulation of beta-amyloid clearance positive regulation of cellular respiration negative regulation of complement-dependent cytotoxicity negative regulation of endothelial cell apoptotic process positive regulation of ATP biosynthetic process uc003kxk.1 uc003kxk.2 uc003kxk.3 uc003kxk.4 
ENST00000231454.6 IL5 ENST00000231454.6 interleukin 5 (from RefSeq NM_000879.3) ENST00000231454.1 ENST00000231454.2 ENST00000231454.3 ENST00000231454.4 ENST00000231454.5 IL5_HUMAN NM_000879 P05113 Q13840 uc003kxe.1 uc003kxe.2 This gene encodes a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. The encoded cytokine plays a major role in the regulation of eosinophil formation, maturation, recruitment and survival. The increased production of this cytokine may be related to pathogenesis of eosinophil-dependent inflammatory diseases. This cytokine functions by binding to its receptor, which is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene is located on chromosome 5 within a cytokine gene cluster which includes interleukin 4 (IL4), interleukin 13 (IL13), and CSF2 . This gene, IL4, and IL13 may be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31. [provided by RefSeq, Jul 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X04688.1, X12705.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231454.6/ ENSP00000231454.1 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils (PubMed:2653458, PubMed:9010276). Acts also on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation (By similarity). Mechanistically, exerts its biological effects through a receptor composed of IL5RA subunit and the cytokine receptor common subunit beta/CSF2RB (PubMed:1495999, PubMed:22528658). Binding to the receptor leads to activation of various kinases including LYN, SYK and JAK2 and thereby propagates signals through the RAS-MAPK and JAK-STAT5 pathways respectively (PubMed:7613138). Homodimer; disulfide-linked (PubMed:8483502, PubMed:22528658). Interacts with IL5RA (PubMed:1495999, PubMed:22153509). Interacts with CSF2RB (PubMed:1495999). P05113; P32927: CSF2RB; NbExp=2; IntAct=EBI-2435811, EBI-1809771; P05113; Q01344: IL5RA; NbExp=2; IntAct=EBI-2435811, EBI-1759442; P05113; Q01344-2: IL5RA; NbExp=4; IntAct=EBI-2435811, EBI-15957545; Secreted Belongs to the IL-5 family. Name=Wikipedia; Note=Interleukin-5 entry; URL="https://en.wikipedia.org/wiki/Interleukin_5"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/il5/"; MAPK cascade cytokine activity interleukin-5 receptor binding protein binding extracellular region extracellular space inflammatory response immune response growth factor activity positive regulation of cell proliferation cytokine-mediated signaling pathway positive regulation of B cell proliferation positive regulation of eosinophil differentiation positive regulation of transcription, DNA-templated positive regulation of JAK-STAT cascade positive regulation of peptidyl-tyrosine phosphorylation positive regulation of immunoglobulin secretion positive regulation of sequence-specific DNA binding transcription factor activity positive regulation of podosome assembly uc003kxe.1 uc003kxe.2 
ENST00000231461.10 ST8SIA4 ENST00000231461.10 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4, transcript variant 1 (from RefSeq NM_005668.6) A8KA07 ENST00000231461.1 ENST00000231461.2 ENST00000231461.3 ENST00000231461.4 ENST00000231461.5 ENST00000231461.6 ENST00000231461.7 ENST00000231461.8 ENST00000231461.9 G3V104 NM_005668 PST PST1 Q8N1F4 Q92187 Q92693 SIA8D_HUMAN SIAT8D uc003knk.1 uc003knk.2 uc003knk.3 uc003knk.4 uc003knk.5 uc003knk.6 The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells. Protein modification; protein glycosylation. Golgi apparatus membrane ; Single- pass type II membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q92187-1; Sequence=Displayed; Name=2; IsoId=Q92187-2; Sequence=VSP_044867; Highly expressed in fetal brain, lung and kidney and in adult heart, spleen and thymus. Present to a lesser extent in adult brain, placenta, lung, large and small intestine and peripheral blood leukocytes. Belongs to the glycosyltransferase 29 family. Name=Functional Glycomics Gateway - GTase; Note=ST8Sia IV; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_639"; Golgi membrane ganglioside biosynthetic process alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity Golgi apparatus cellular protein modification process protein glycosylation N-glycan processing nervous system development sialyltransferase activity oligosaccharide metabolic process membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups sialic acid binding sialylation uc003knk.1 uc003knk.2 uc003knk.3 uc003knk.4 uc003knk.5 uc003knk.6 
ENST00000231484.4 PCDH12 ENST00000231484.4 protocadherin 12 (from RefSeq NM_016580.4) ENST00000231484.1 ENST00000231484.2 ENST00000231484.3 NM_016580 PCD12_HUMAN PCDH12 Q6UXB6 Q96KB8 Q9H7Y6 Q9H8E0 Q9NPG4 UNQ395/PRO731 uc003llx.1 uc003llx.2 uc003llx.3 uc003llx.4 uc003llx.5 This gene belongs to the protocadherin gene family, a subfamily of the cadherin superfamily. The encoded protein consists of an extracellular domain containing 6 cadherin repeats, a transmembrane domain and a cytoplasmic tail that differs from those of the classical cadherins. The gene localizes to the region on chromosome 5 where the protocadherin gene clusters reside. The exon organization of this transcript is similar to that of the gene cluster transcripts, notably the first large exon, but no significant sequence homology exists. The function of this cellular adhesion protein is undetermined but mouse protocadherin 12 does not bind catenins and appears to have no affect on cell migration or growth. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF240635.1, AF231025.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions (By similarity). Acts as a regulator of cell migration, probably via increasing cell- cell adhesion (PubMed:21402705). Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions (By similarity). Unable to bind to catenins, weakly associates with the cytoskeleton (By similarity). [Protocadherin-12]: Cell membrane ; Single-pass type I membrane protein Cell junction [Protocadherin-12, secreted form]: Secreted Note=The secreted form is produced following cleavage by ADAM10. Expressed in highly vascularized tissues including the heart and placenta, but most tissues contain a low level of expression (PubMed:11063261). Prominent expression in the spleen (PubMed:11063261). Present in villous and extravillous trophoblast (at protein level) (PubMed:21402705). [Protocadherin-12]: Cleaved by ADAM10 close to the transmembrane domain to release the Protocadherin-12, secreted form in the serum. Cleavage results in reduced cellular adhesion in a cell migration assay. Diencephalic-mesencephalic junction dysplasia syndrome 1 (DMJDS1) [MIM:251280]: An autosomal recessive syndrome characterized by severe global developmental delay with profound intellectual disability, spasticity or dystonia, and congenital microcephaly. Brain imaging shows hypothalamic midbrain dysplasia, diencephalic- mesencephalic dysplasia, and intracerebral calcifications. Note=The disease is caused by variants affecting the gene represented in this entry. calcium ion binding extracellular region plasma membrane integral component of plasma membrane cell-cell junction glycogen metabolic process cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules neuron recognition membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules cell junction labyrinthine layer development extracellular exosome uc003llx.1 uc003llx.2 uc003llx.3 uc003llx.4 uc003llx.5 
ENST00000231498.8 NUP155 ENST00000231498.8 nucleoporin 155, transcript variant 1 (from RefSeq NM_153485.3) ENST00000231498.1 ENST00000231498.2 ENST00000231498.3 ENST00000231498.4 ENST00000231498.5 ENST00000231498.6 ENST00000231498.7 KIAA0791 NM_153485 NU155_HUMAN O75694 Q9UBE9 Q9UFL5 uc003jku.1 uc003jku.2 uc003jku.3 uc003jku.4 Nucleoporins are proteins that play an important role in the assembly and functioning of the nuclear pore complex (NPC) which regulates the movement of macromolecules across the nuclear envelope (NE). The protein encoded by this gene plays a role in the fusion of NE vesicles and formation of the double membrane NE. The protein may also be involved in cardiac physiology and may be associated with the pathogenesis of atrial fibrillation. Alternative splicing results in multiple transcript variants of this gene. A pseudogene associated with this gene is located on chromosome 6. [provided by RefSeq, May 2013]. Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. Interacts with GLE1. Able to form a heterotrimer with GLE1 and NUP42 in vitro. Forms a complex with NUP35, NUP93, NUP205 and lamin B. O75694; O43281: EFS; NbExp=3; IntAct=EBI-1050769, EBI-718488; O75694; P02545: LMNA; NbExp=6; IntAct=EBI-1050769, EBI-351935; Nucleus, nuclear pore complex Nucleus membrane ; Peripheral membrane protein ; Cytoplasmic side Nucleus membrane ; Peripheral membrane protein ; Nucleoplasmic side Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75694-1; Sequence=Displayed; Name=2; IsoId=O75694-2; Sequence=VSP_014437; Expressed in all tissues tested, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Phosphorylated. Phosphorylation and dephosphorylation may be important for the function of NUP155 and may play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity). Disulfide-linked to NUP62. The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC (By similarity). Atrial fibrillation, familial, 15 (ATFB15) [MIM:615770]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the non-repetitive/WGA-negative nucleoporin family. Sequence=AAD52966.1; Type=Erroneous gene model prediction; Evidence=; Sequence=BAA34511.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery protein binding nucleus nuclear envelope nuclear pore regulation of glycolytic process mRNA export from nucleus tRNA export from nucleus protein import into nucleus nucleocytoplasmic transport nuclear envelope organization protein transport membrane viral process protein sumoylation structural constituent of nuclear pore viral transcription nuclear membrane protein targeting to nuclear inner membrane host cell nuclear pore inner ring mRNA transport regulation of gene silencing by miRNA intracellular transport of virus atrial cardiac muscle cell action potential regulation of cellular response to heat uc003jku.1 uc003jku.2 uc003jku.3 uc003jku.4 
ENST00000231512.5 C5orf15 ENST00000231512.5 chromosome 5 open reading frame 15 (from RefSeq NM_020199.3) B2RD10 D3DQ92 ENST00000231512.1 ENST00000231512.2 ENST00000231512.3 ENST00000231512.4 HTGN29 KCT2 KCT2_HUMAN NM_020199 Q8NC54 Q9NRG2 uc003kyo.1 uc003kyo.2 uc003kyo.3 uc003kyo.4 uc003kyo.5 Membrane ; Single-pass type I membrane protein Widely expressed. membrane integral component of membrane uc003kyo.1 uc003kyo.2 uc003kyo.3 uc003kyo.4 uc003kyo.5 
ENST00000231524.14 TRIM23 ENST00000231524.14 tripartite motif containing 23, transcript variant alpha (from RefSeq NM_001656.4) ARD1 ARFD1 ENST00000231524.1 ENST00000231524.10 ENST00000231524.11 ENST00000231524.12 ENST00000231524.13 ENST00000231524.2 ENST00000231524.3 ENST00000231524.4 ENST00000231524.5 ENST00000231524.6 ENST00000231524.7 ENST00000231524.8 ENST00000231524.9 NM_001656 P36406 Q9BZY4 Q9BZY5 RNF46 TRI23_HUMAN uc003jty.1 uc003jty.2 uc003jty.3 uc003jty.4 uc003jty.5 The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described. [provided by RefSeq, Jul 2008]. Acts as an E3 ubiquitin-protein ligase. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes (PubMed:28871090). (Microbial infection) Mediates TRAF6 auto-ubiquitination in the presence of human cytomegalovirus protein UL144, resulting in the virally controlled activation of NF-kappa-B stimulation at early times of HCMV infection. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Protein modification; protein ubiquitination. Homodimer. Interacts with PSCD1. Interacts with UBE2D2 (PubMed:28681414). Interacts with TBK1 (via N-terminal kinase domain) and p62/SQSTM1. (Microbial infection) Interacts with human cytomegalovirus protein UL144; this interaction might cause autoubiquitination of TRAF6, leading to NF-kappa-B activation. P36406; A0A0S2Z3G1: ACTN4; NbExp=3; IntAct=EBI-740098, EBI-16430749; P36406; Q96IX9: ANKRD36BP1; NbExp=3; IntAct=EBI-740098, EBI-744859; P36406; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-740098, EBI-14493093; P36406; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-740098, EBI-2371151; P36406; P29972: AQP1; NbExp=6; IntAct=EBI-740098, EBI-745213; P36406; Q8N6T3: ARFGAP1; NbExp=3; IntAct=EBI-740098, EBI-716933; P36406; Q9NR81: ARHGEF3; NbExp=5; IntAct=EBI-740098, EBI-10312733; P36406; Q8N5M1: ATPAF2; NbExp=7; IntAct=EBI-740098, EBI-1166928; P36406; P54253: ATXN1; NbExp=6; IntAct=EBI-740098, EBI-930964; P36406; Q99933: BAG1; NbExp=5; IntAct=EBI-740098, EBI-1030678; P36406; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-740098, EBI-1012434; P36406; Q0VDD7: BRME1; NbExp=4; IntAct=EBI-740098, EBI-741210; P36406; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-740098, EBI-739879; P36406; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-740098, EBI-715389; P36406; Q9H257: CARD9; NbExp=4; IntAct=EBI-740098, EBI-751319; P36406; P55212: CASP6; NbExp=3; IntAct=EBI-740098, EBI-718729; P36406; Q9HC52: CBX8; NbExp=3; IntAct=EBI-740098, EBI-712912; P36406; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-740098, EBI-10961312; P36406; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-740098, EBI-10247802; P36406; Q86WR0: CCDC25; NbExp=3; IntAct=EBI-740098, EBI-2690264; P36406; Q86Y33: CDC20B; NbExp=3; IntAct=EBI-740098, EBI-10260504; P36406; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-740098, EBI-930143; P36406; Q01850: CDR2; NbExp=6; IntAct=EBI-740098, EBI-1181367; P36406; Q96M91: CFAP53; NbExp=3; IntAct=EBI-740098, EBI-742422; P36406; O43247-2: CIMIP4; NbExp=3; IntAct=EBI-740098, EBI-12093053; P36406; P10606: COX5B; NbExp=5; IntAct=EBI-740098, EBI-1053725; P36406; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-740098, EBI-12012272; P36406; Q02930-3: CREB5; NbExp=3; IntAct=EBI-740098, EBI-10192698; P36406; Q16527: CSRP2; NbExp=3; IntAct=EBI-740098, EBI-2959737; P36406; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-740098, EBI-5453285; P36406; O95715: CXCL14; NbExp=3; IntAct=EBI-740098, EBI-2798068; P36406; O43602: DCX; NbExp=3; IntAct=EBI-740098, EBI-8646694; P36406; Q14565: DMC1; NbExp=3; IntAct=EBI-740098, EBI-930865; P36406; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-740098, EBI-9679045; P36406; Q92608: DOCK2; NbExp=3; IntAct=EBI-740098, EBI-448771; P36406; Q96CJ1: EAF2; NbExp=3; IntAct=EBI-740098, EBI-1245604; P36406; Q08426: EHHADH; NbExp=3; IntAct=EBI-740098, EBI-2339219; P36406; O15371: EIF3D; NbExp=3; IntAct=EBI-740098, EBI-353818; P36406; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-740098, EBI-744099; P36406; O95208-2: EPN2; NbExp=3; IntAct=EBI-740098, EBI-12135243; P36406; Q8N2X6: EXOC3-AS1; NbExp=3; IntAct=EBI-740098, EBI-749333; P36406; Q9BQ89: FAM110A; NbExp=6; IntAct=EBI-740098, EBI-1752811; P36406; Q8N9E0: FAM133A; NbExp=6; IntAct=EBI-740098, EBI-10268158; P36406; Q96PV7-2: FAM193B; NbExp=3; IntAct=EBI-740098, EBI-10292648; P36406; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-740098, EBI-1384254; P36406; Q86YD7: FAM90A1; NbExp=6; IntAct=EBI-740098, EBI-6658203; P36406; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-740098, EBI-10244131; P36406; P22607: FGFR3; NbExp=3; IntAct=EBI-740098, EBI-348399; P36406; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-740098, EBI-11526128; P36406; C0H5X2: FLJ38668; NbExp=3; IntAct=EBI-740098, EBI-10176227; P36406; A0A0S2Z4D9: GAD1; NbExp=3; IntAct=EBI-740098, EBI-16430771; P36406; P23769: GATA2; NbExp=4; IntAct=EBI-740098, EBI-2806671; P36406; P55040: GEM; NbExp=7; IntAct=EBI-740098, EBI-744104; P36406; Q9NZ52-2: GGA3; NbExp=3; IntAct=EBI-740098, EBI-12075758; P36406; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-740098, EBI-745707; P36406; O95872: GPANK1; NbExp=7; IntAct=EBI-740098, EBI-751540; P36406; Q92917: GPKOW; NbExp=4; IntAct=EBI-740098, EBI-746309; P36406; Q14957: GRIN2C; NbExp=3; IntAct=EBI-740098, EBI-8285963; P36406; P06396: GSN; NbExp=3; IntAct=EBI-740098, EBI-351506; P36406; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-740098, EBI-11956675; P36406; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-740098, EBI-2514791; P36406; O14964: HGS; NbExp=3; IntAct=EBI-740098, EBI-740220; P36406; O00291: HIP1; NbExp=3; IntAct=EBI-740098, EBI-473886; P36406; P09067: HOXB5; NbExp=6; IntAct=EBI-740098, EBI-3893317; P36406; P01112: HRAS; NbExp=3; IntAct=EBI-740098, EBI-350145; P36406; P04792: HSPB1; NbExp=3; IntAct=EBI-740098, EBI-352682; P36406; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-740098, EBI-739361; P36406; Q14005-2: IL16; NbExp=3; IntAct=EBI-740098, EBI-17178971; P36406; Q8NA54: IQUB; NbExp=7; IntAct=EBI-740098, EBI-10220600; P36406; Q15040: JOSD1; NbExp=3; IntAct=EBI-740098, EBI-2510602; P36406; O75564-2: JRK; NbExp=3; IntAct=EBI-740098, EBI-17181882; P36406; Q92993: KAT5; NbExp=3; IntAct=EBI-740098, EBI-399080; P36406; O60333-2: KIF1B; NbExp=3; IntAct=EBI-740098, EBI-10975473; P36406; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-740098, EBI-2125614; P36406; Q9P2K6: KLHL42; NbExp=6; IntAct=EBI-740098, EBI-739890; P36406; P02538: KRT6A; NbExp=8; IntAct=EBI-740098, EBI-702198; P36406; O95678: KRT75; NbExp=3; IntAct=EBI-740098, EBI-2949715; P36406; Q01546: KRT76; NbExp=3; IntAct=EBI-740098, EBI-2952745; P36406; Q14657: LAGE3; NbExp=3; IntAct=EBI-740098, EBI-1052105; P36406; P13473-2: LAMP2; NbExp=3; IntAct=EBI-740098, EBI-21591415; P36406; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-740098, EBI-726510; P36406; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-740098, EBI-10274069; P36406; O00214: LGALS8; NbExp=4; IntAct=EBI-740098, EBI-740058; P36406; Q96FQ7: LINC00526; NbExp=3; IntAct=EBI-740098, EBI-10286106; P36406; P25791: LMO2; NbExp=3; IntAct=EBI-740098, EBI-739696; P36406; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-740098, EBI-11742507; P36406; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740098, EBI-739832; P36406; Q8NDC4: MORN4; NbExp=6; IntAct=EBI-740098, EBI-10269566; P36406; Q9BYD3: MRPL4; NbExp=3; IntAct=EBI-740098, EBI-721368; P36406; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-740098, EBI-2514313; P36406; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-740098, EBI-10699187; P36406; Q6P444: MTFR2; NbExp=3; IntAct=EBI-740098, EBI-10252703; P36406; Q9P2K5-2: MYEF2; NbExp=3; IntAct=EBI-740098, EBI-10318831; P36406; P52179-2: MYOM1; NbExp=3; IntAct=EBI-740098, EBI-12010196; P36406; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-740098, EBI-744402; P36406; Q15742: NAB2; NbExp=3; IntAct=EBI-740098, EBI-8641936; P36406; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-740098, EBI-11746523; P36406; Q9HC98: NEK6; NbExp=4; IntAct=EBI-740098, EBI-740364; P36406; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-740098, EBI-725252; P36406; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-740098, EBI-12025760; P36406; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-740098, EBI-741158; P36406; O43809: NUDT21; NbExp=3; IntAct=EBI-740098, EBI-355720; P36406; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-740098, EBI-752122; P36406; O43189: PHF1; NbExp=4; IntAct=EBI-740098, EBI-530034; P36406; O75928: PIAS2; NbExp=3; IntAct=EBI-740098, EBI-348555; P36406; O00459: PIK3R2; NbExp=3; IntAct=EBI-740098, EBI-346930; P36406; P78337: PITX1; NbExp=4; IntAct=EBI-740098, EBI-748265; P36406; Q99569: PKP4; NbExp=3; IntAct=EBI-740098, EBI-726447; P36406; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-740098, EBI-4401947; P36406; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-740098, EBI-10320765; P36406; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-740098, EBI-11956563; P36406; Q13356: PPIL2; NbExp=3; IntAct=EBI-740098, EBI-7705988; P36406; Q5SWA1: PPP1R15B; NbExp=3; IntAct=EBI-740098, EBI-2815482; P36406; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-740098, EBI-2557469; P36406; Q99633: PRPF18; NbExp=3; IntAct=EBI-740098, EBI-2798416; P36406; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-740098, EBI-1567797; P36406; P25786: PSMA1; NbExp=5; IntAct=EBI-740098, EBI-359352; P36406; P20618: PSMB1; NbExp=3; IntAct=EBI-740098, EBI-372273; P36406; Q9BTL3: RAMAC; NbExp=6; IntAct=EBI-740098, EBI-744023; P36406; P62826: RAN; NbExp=3; IntAct=EBI-740098, EBI-286642; P36406; Q9UKA8: RCAN3; NbExp=3; IntAct=EBI-740098, EBI-9091952; P36406; Q8N443: RIBC1; NbExp=3; IntAct=EBI-740098, EBI-10265323; P36406; Q13671: RIN1; NbExp=3; IntAct=EBI-740098, EBI-366017; P36406; Q63HN8-6: RNF213; NbExp=3; IntAct=EBI-740098, EBI-10248548; P36406; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-740098, EBI-16428950; P36406; Q7L4I2-2: RSRC2; NbExp=3; IntAct=EBI-740098, EBI-10256202; P36406; Q14D33: RTP5; NbExp=3; IntAct=EBI-740098, EBI-10217913; P36406; Q96T51-2: RUFY1; NbExp=3; IntAct=EBI-740098, EBI-12192715; P36406; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-740098, EBI-748391; P36406; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-747035; P36406; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-10308083; P36406; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-740098, EBI-747107; P36406; P12236: SLC25A6; NbExp=3; IntAct=EBI-740098, EBI-356254; P36406; Q9H0W8: SMG9; NbExp=6; IntAct=EBI-740098, EBI-2872322; P36406; O95863: SNAI1; NbExp=7; IntAct=EBI-740098, EBI-1045459; P36406; O43623: SNAI2; NbExp=3; IntAct=EBI-740098, EBI-9876238; P36406; P14678-2: SNRPB; NbExp=3; IntAct=EBI-740098, EBI-372475; P36406; P08579: SNRPB2; NbExp=3; IntAct=EBI-740098, EBI-1053651; P36406; Q13573: SNW1; NbExp=3; IntAct=EBI-740098, EBI-632715; P36406; O60504: SORBS3; NbExp=6; IntAct=EBI-740098, EBI-741237; P36406; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-740098, EBI-742688; P36406; B7ZLI8: STK19; NbExp=3; IntAct=EBI-740098, EBI-10176124; P36406; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-740098, EBI-10175576; P36406; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-740098, EBI-747797; P36406; Q13148: TARDBP; NbExp=3; IntAct=EBI-740098, EBI-372899; P36406; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-740098, EBI-10172380; P36406; Q9NU19: TBC1D22B; NbExp=8; IntAct=EBI-740098, EBI-8787464; P36406; Q15560: TCEA2; NbExp=3; IntAct=EBI-740098, EBI-710310; P36406; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-740098, EBI-11955057; P36406; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-740098, EBI-11139477; P36406; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-740098, EBI-10226570; P36406; P21580: TNFAIP3; NbExp=6; IntAct=EBI-740098, EBI-527670; P36406; Q13077: TRAF1; NbExp=3; IntAct=EBI-740098, EBI-359224; P36406; P36406: TRIM23; NbExp=7; IntAct=EBI-740098, EBI-740098; P36406; Q0P6H7: TRIM29; NbExp=3; IntAct=EBI-740098, EBI-10226710; P36406; Q14134: TRIM29; NbExp=4; IntAct=EBI-740098, EBI-702370; P36406; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-740098, EBI-5235829; P36406; Q9BYV6: TRIM55; NbExp=2; IntAct=EBI-740098, EBI-2341179; P36406; Q12815: TROAP; NbExp=5; IntAct=EBI-740098, EBI-2349743; P36406; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-740098, EBI-2559824; P36406; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-740098, EBI-9053916; P36406; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-740098, EBI-2825190; P36406; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-740098, EBI-10180829; P36406; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-740098, EBI-741480; P36406; O75604: USP2; NbExp=3; IntAct=EBI-740098, EBI-743272; P36406; Q9Y2K6: USP20; NbExp=3; IntAct=EBI-740098, EBI-2511991; P36406; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-740098, EBI-5457544; P36406; Q99990: VGLL1; NbExp=3; IntAct=EBI-740098, EBI-11983165; P36406; Q64LD2: WDR25; NbExp=3; IntAct=EBI-740098, EBI-744560; P36406; O76024: WFS1; NbExp=3; IntAct=EBI-740098, EBI-720609; P36406; Q05516: ZBTB16; NbExp=3; IntAct=EBI-740098, EBI-711925; P36406; Q9P1Z0: ZBTB4; NbExp=3; IntAct=EBI-740098, EBI-2564133; P36406; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-740098, EBI-740767; P36406; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-740098, EBI-14104088; P36406; Q8N6M9: ZFAND2A; NbExp=3; IntAct=EBI-740098, EBI-3921109; P36406; P17024: ZNF20; NbExp=3; IntAct=EBI-740098, EBI-717634; P36406; P15622-3: ZNF250; NbExp=3; IntAct=EBI-740098, EBI-10177272; P36406; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-740098, EBI-347633; P36406; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-740098, EBI-740727; P36406; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-740098, EBI-17269964; P36406; Q8TBZ8: ZNF564; NbExp=6; IntAct=EBI-740098, EBI-10273713; P36406; Q9P0T4: ZNF581; NbExp=8; IntAct=EBI-740098, EBI-745520; P36406; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-740098, EBI-6427977; P36406; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-740098, EBI-16429014; P36406; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-740098, EBI-16429989; P36406; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-740098, EBI-5667516; P36406; P09022: Hoxa1; Xeno; NbExp=2; IntAct=EBI-740098, EBI-3957603; Cytoplasm Endomembrane system Golgi apparatus membrane Lysosome membrane Note=Membrane-associated with the Golgi complex and lysosomal structures. Event=Alternative splicing; Named isoforms=3; Name=Alpha; IsoId=P36406-1; Sequence=Displayed; Name=Beta; IsoId=P36406-2; Sequence=VSP_000296; Name=Gamma; IsoId=P36406-3; Sequence=VSP_000297; The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity. This domain is catalytically active as a dimer. In the C-terminal section; belongs to the small GTPase superfamily. Arf family. Golgi membrane nucleotide binding immune system process nucleic acid binding GTPase activity ubiquitin-protein transferase activity protein binding GTP binding nucleus cytoplasm lysosome lysosomal membrane Golgi apparatus plasma membrane intracellular protein transport enzyme activator activity zinc ion binding endomembrane system membrane viral process vesicle-mediated transport protein ubiquitination transferase activity GDP binding identical protein binding positive regulation of catalytic activity innate immune response metal ion binding uc003jty.1 uc003jty.2 uc003jty.3 uc003jty.4 uc003jty.5 
ENST00000231572.8 RARS1 ENST00000231572.8 arginyl-tRNA synthetase 1 (from RefSeq NM_002887.4) B2RBS9 ENST00000231572.1 ENST00000231572.2 ENST00000231572.3 ENST00000231572.4 ENST00000231572.5 ENST00000231572.6 ENST00000231572.7 NM_002887 P54136 Q53GY4 Q9BWA1 RARS RARS1 SYRC_HUMAN uc003lzx.1 uc003lzx.2 uc003lzx.3 uc003lzx.4 uc003lzx.5 Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1146952.1, SRR1803616.190698.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231572.8/ ENSP00000231572.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (PubMed:25288775). Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 (PubMed:17443684). Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl- tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA- COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215; EC=6.1.1.19; Evidence= Kinetic parameters: KM=3.9 uM for arginine (ATP-PPi exchange at 37 degrees Celsius) ; KM=3.5 uM for arginine (arginylation at 37 degrees Celsius) ; KM=1183 uM for ATP (ATP-PPi exchange at 37 Celsius) ; KM=910 uM for ATP (arginylation at 37 Celsius) ; KM=0.05 uM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius) ; KM=0.41 uM for calf liver tRNA-Arg (arginylation at 37 Celsius) ; Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity (PubMed:10358004, PubMed:25288775). Interacts (via N-terminus) with LARS2 (via C-terminus) (PubMed:16055448, PubMed:17443684). Monomer (PubMed:24859084). Part of a multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:19131329, PubMed:19289464). Interacts with QARS1 (PubMed:24656866). Part of a complex composed of RARS1, QARS1 and AIMP1 (PubMed:25288775). P54136; Q12904-2: AIMP1; NbExp=3; IntAct=EBI-355482, EBI-12412735; P54136; Q96NT0: CCDC115; NbExp=3; IntAct=EBI-355482, EBI-2810325; P54136; Q9P2J5: LARS1; NbExp=4; IntAct=EBI-355482, EBI-356077; P54136; Q96K83: ZNF521; NbExp=3; IntAct=EBI-355482, EBI-6597673; Cytoplasm toplasm, cytosol Event=Alternative initiation; Named isoforms=2; Name=Complexed; IsoId=P54136-1; Sequence=Displayed; Name=Monomeric; IsoId=P54136-2; Sequence=VSP_018905; The alpha-helical N-terminus (residues 1-72) mediates interaction with AIMP1 and thereby contributes to the assembly of the multisynthetase complex. Leukodystrophy, hypomyelinating, 9 (HLD9) [MIM:616140]: An autosomal recessive neurodegenerative disorder characterized by delayed psychomotor development, severe spasticity, nystagmus, and ataxia associated with diffuse hypomyelination apparent on brain MRI. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the class-I aminoacyl-tRNA synthetase family. tRNA binding nucleotide binding aminoacyl-tRNA ligase activity arginine-tRNA ligase activity protein binding ATP binding nucleus nucleoplasm cytoplasm cytosol translation tRNA aminoacylation for protein translation arginyl-tRNA aminoacylation membrane ligase activity aminoacyl-tRNA synthetase multienzyme complex arginine binding cadherin binding extracellular exosome uc003lzx.1 uc003lzx.2 uc003lzx.3 uc003lzx.4 uc003lzx.5 
ENST00000231656.13 CDX1 ENST00000231656.13 caudal type homeobox 1 (from RefSeq NM_001804.3) CDX1_HUMAN ENST00000231656.1 ENST00000231656.10 ENST00000231656.11 ENST00000231656.12 ENST00000231656.2 ENST00000231656.3 ENST00000231656.4 ENST00000231656.5 ENST00000231656.6 ENST00000231656.7 ENST00000231656.8 ENST00000231656.9 NM_001804 P47902 Q4VAU4 Q9NYK8 uc003lrq.1 uc003lrq.2 uc003lrq.3 uc003lrq.4 uc003lrq.5 This gene is a member of the caudal-related homeobox transcription factor gene family. The encoded DNA-binding protein regulates intestine-specific gene expression and enterocyte differentiation. It has been shown to induce expression of the intestinal alkaline phosphatase gene, and inhibit beta-catenin/T-cell factor transcriptional activity. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: U51095.1, U15212.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231656.13/ ENSP00000231656.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plays a role in transcriptional regulation (PubMed:24623306). Involved in activated KRAS-mediated transcriptional activation of PRKD1 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the PRKD1 promoter in colorectal cancer (CRC) cells (PubMed:24623306). Could play a role in the terminal differentiation of the intestine. Binds preferentially to methylated DNA (PubMed:28473536). P47902; P49715: CEBPA; NbExp=3; IntAct=EBI-8514176, EBI-1172054; Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P47902-1; Sequence=Displayed; Name=2; IsoId=P47902-2; Sequence=VSP_021030; Intestinal epithelium. Belongs to the Caudal homeobox family. nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development pattern specification process methyl-CpG binding animal organ morphogenesis anterior/posterior axis specification anterior/posterior pattern specification regulation of somitogenesis cell differentiation sequence-specific DNA binding transcription regulatory region DNA binding positive regulation of transcription from RNA polymerase II promoter bone morphogenesis uc003lrq.1 uc003lrq.2 uc003lrq.3 uc003lrq.4 uc003lrq.5 
ENST00000231706.6 SLC7A14 ENST00000231706.6 solute carrier family 7 member 14 (from RefSeq NM_020949.3) B3KV33 ENST00000231706.1 ENST00000231706.2 ENST00000231706.3 ENST00000231706.4 ENST00000231706.5 KIAA1613 NM_020949 Q8TBB6 Q9HCF9 S7A14_HUMAN SLC7A14 uc003fgz.1 uc003fgz.2 uc003fgz.3 uc003fgz.4 This gene is predicted to encode a glycosylated, cationic amino acid transporter protein with 14 transmembrane domains. This gene is primarily expressed in skin fibroblasts, neural tissue, and primary endothelial cells and its protein is predicted to mediate lysosomal uptake of cationic amino acids. Mutations in this gene are associated with autosomal recessive retinitis pigmentosa. In mice, this gene is expressed in the photoreceptor layer of the retina where its expression increases over the course of retinal development and persists in the mature retina. [provided by RefSeq, Apr 2014]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.185681.1, SRR1660805.215668.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2145743 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231706.6/ ENSP00000231706.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Imports 4-aminobutanoate (GABA) into lysosomes. May act as a GABA sensor that regulates mTORC2-dependent INS signaling and gluconeogenesis. The transport mechanism and substrate selectivity remain to be elucidated. Reaction=4-aminobutanoate(in) = 4-aminobutanoate(out); Xref=Rhea:RHEA:35035, ChEBI:CHEBI:59888; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35037; Evidence=; Q8TBB6; Q9ULC5: ACSL5; NbExp=3; IntAct=EBI-5235586, EBI-2876927; Q8TBB6; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-5235586, EBI-11277970; Q8TBB6; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-5235586, EBI-11522760; Q8TBB6; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-5235586, EBI-11957045; Q8TBB6; O95236-2: APOL3; NbExp=3; IntAct=EBI-5235586, EBI-11976321; Q8TBB6; O15155: BET1; NbExp=3; IntAct=EBI-5235586, EBI-749204; Q8TBB6; Q12981: BNIP1; NbExp=3; IntAct=EBI-5235586, EBI-4402847; Q8TBB6; Q12982: BNIP2; NbExp=3; IntAct=EBI-5235586, EBI-752094; Q8TBB6; P27352: CBLIF; NbExp=3; IntAct=EBI-5235586, EBI-3953638; Q8TBB6; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-5235586, EBI-9083477; Q8TBB6; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-5235586, EBI-10271156; Q8TBB6; P19397: CD53; NbExp=3; IntAct=EBI-5235586, EBI-6657396; Q8TBB6; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-5235586, EBI-11522780; Q8TBB6; Q96PD2-2: DCBLD2; NbExp=3; IntAct=EBI-5235586, EBI-12135455; Q8TBB6; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-5235586, EBI-398977; Q8TBB6; Q5NDL2-3: EOGT; NbExp=3; IntAct=EBI-5235586, EBI-13052900; Q8TBB6; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-5235586, EBI-10976398; Q8TBB6; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-5235586, EBI-18304435; Q8TBB6; O75063: FAM20B; NbExp=3; IntAct=EBI-5235586, EBI-11090967; Q8TBB6; Q969F0: FATE1; NbExp=3; IntAct=EBI-5235586, EBI-743099; Q8TBB6; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-5235586, EBI-3918971; Q8TBB6; Q13651: IL10RA; NbExp=3; IntAct=EBI-5235586, EBI-1031656; Q8TBB6; Q16873: LTC4S; NbExp=3; IntAct=EBI-5235586, EBI-12241118; Q8TBB6; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-5235586, EBI-11956541; Q8TBB6; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-5235586, EBI-12866138; Q8TBB6; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-5235586, EBI-6163737; Q8TBB6; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-5235586, EBI-10317425; Q8TBB6; P42857: NSG1; NbExp=3; IntAct=EBI-5235586, EBI-6380741; Q8TBB6; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-5235586, EBI-11721828; Q8TBB6; A5D903: PRB1; NbExp=3; IntAct=EBI-5235586, EBI-10173935; Q8TBB6; Q14162: SCARF1; NbExp=3; IntAct=EBI-5235586, EBI-12056025; Q8TBB6; O00767: SCD; NbExp=3; IntAct=EBI-5235586, EBI-2684237; Q8TBB6; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-5235586, EBI-8640191; Q8TBB6; Q9NZ01: TECR; NbExp=3; IntAct=EBI-5235586, EBI-2877718; Q8TBB6; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-5235586, EBI-10694905; Q8TBB6; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-5235586, EBI-16746122; Q8TBB6; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-5235586, EBI-11988865; Q8TBB6; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-5235586, EBI-2819725; Q8TBB6; P63027: VAMP2; NbExp=3; IntAct=EBI-5235586, EBI-520113; Q8TBB6; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-5235586, EBI-6256462; Q8TBB6; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-5235586, EBI-751253; Q8TBB6; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-5235586, EBI-751210; Q8TBB6; O95159: ZFPL1; NbExp=3; IntAct=EBI-5235586, EBI-718439; Lysosome membrane ulti-pass membrane protein Note=Exhibits a punctated pattern in the cytoplasm, which partially ovelaps with lysosomes. Expressed in skin fibroblasts. Retinitis pigmentosa 68 (RP68) [MIM:615725]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the amino acid-polyamine-organocation (APC) superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family. Initially postulated to transport L-arginine based on studies with a chimeric protein, which was not confirmed by other groups using the wild-type protein. It was latter shown to rather function as a GABA importer. Sequence=BAB13439.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence=; lysosome lysosomal membrane amino acid transport negative regulation of phosphatase activity membrane integral component of membrane transmembrane transporter activity transmembrane transport uc003fgz.1 uc003fgz.2 uc003fgz.3 uc003fgz.4 
ENST00000231721.7 SEMA3G ENST00000231721.7 semaphorin 3G (from RefSeq NM_020163.3) ENST00000231721.1 ENST00000231721.2 ENST00000231721.3 ENST00000231721.4 ENST00000231721.5 ENST00000231721.6 NM_020163 Q7L9D9 Q9H7Q3 Q9NS98 SEM3G_HUMAN uc003dea.1 uc003dea.2 uc003dea.3 The transcription of this gene is activated by PPAR-gamma, and the resulting protein product plays a role in endothelial cell migration. Expression of this gene also inhibits tumor cell migration and invasion. [provided by RefSeq, Jul 2016]. ##Evidence-Data-START## Transcript exon combination :: AB029496.1, SRR1803615.101779.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000231721.7/ ENSP00000231721.2 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Has chemorepulsive activities for sympathetic axons. Ligand of NRP2 (By similarity). Q9NS98; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-17574989, EBI-12878374; Secreted Belongs to the semaphorin family. neural crest cell migration receptor binding extracellular region extracellular space integral component of plasma membrane semaphorin receptor binding positive regulation of cell migration negative regulation of axon extension chemorepellent activity negative regulation of axon extension involved in axon guidance negative chemotaxis extracellular exosome semaphorin-plexin signaling pathway uc003dea.1 uc003dea.2 uc003dea.3 
ENST00000231749.8 ZMYND10 ENST00000231749.8 zinc finger MYND-type containing 10, transcript variant 1 (from RefSeq NM_015896.4) A6NK41 B3KU54 BLU ENST00000231749.1 ENST00000231749.2 ENST00000231749.3 ENST00000231749.4 ENST00000231749.5 ENST00000231749.6 ENST00000231749.7 LUCA12.4 NM_015896 O14570 O75800 O75801 Q53FE6 Q8N4R6 Q8NDN6 ZMY10_HUMAN ZMYND10 uc003dag.1 uc003dag.2 uc003dag.3 This gene encodes a protein containing a MYND-type zinc finger domain that likely functions in assembly of the dynein motor. Mutations in this gene can cause primary ciliary dyskinesia. This gene is also considered a tumor suppressor gene and is often mutated, deleted, or hypermethylated and silenced in cancer cells. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2015]. Plays a role in axonemal structure organization and motility (PubMed:23891469, PubMed:23891471). Involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility (By similarity). May act by indirectly regulating transcription of dynein proteins (By similarity). Interacts (via C-terminus) with DNAAF11 (via CS domain); this interaction stabilizes DNAAF11 at the protein level (PubMed:23891469, PubMed:23891471, PubMed:29601588). Interacts (via C-terminus) with DNAL1; this interaction stabilizes DNAL1 at the protein level (PubMed:29601588). Interacts with DNAAF4, HSPA8, IQUB, RUVBL2 and DYNTL5 (PubMed:29601588). O75800; P51861: CDR1; NbExp=6; IntAct=EBI-747061, EBI-2836538; O75800; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-747061, EBI-3867333; O75800; Q7L2H7: EIF3M; NbExp=3; IntAct=EBI-747061, EBI-353901; O75800; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-747061, EBI-10220102; O75800; Q96FT9: IFT43; NbExp=3; IntAct=EBI-747061, EBI-10189681; O75800; Q96FT9-2: IFT43; NbExp=3; IntAct=EBI-747061, EBI-11944538; O75800; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-747061, EBI-11522433; O75800; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-747061, EBI-10178410; O75800; P57052: RBM11; NbExp=3; IntAct=EBI-747061, EBI-741332; O75800; Q9Y5W9: SNX11; NbExp=3; IntAct=EBI-747061, EBI-10329449; O75800; Q99593: TBX5; NbExp=3; IntAct=EBI-747061, EBI-297043; O75800; P15884-3: TCF4; NbExp=3; IntAct=EBI-747061, EBI-13636688; O75800; Q9Y3Q8: TSC22D4; NbExp=5; IntAct=EBI-747061, EBI-739485; O75800; Q96G27: WBP1; NbExp=3; IntAct=EBI-747061, EBI-3867685; Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Apical cell membrane Dynein axonemal particle Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=Lung; IsoId=O75800-1; Sequence=Displayed; Name=2; Synonyms=Testis; IsoId=O75800-2; Sequence=VSP_003328; Ciliary dyskinesia, primary, 22 (CILD22) [MIM:615444]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. Patients may exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the ZMYND10 family. Sequence=AAB67311.1; Type=Erroneous gene model prediction; Evidence=; protein binding cytoplasm microtubule organizing center cytoskeleton plasma membrane membrane apical plasma membrane centriolar satellite outer dynein arm assembly inner dynein arm assembly motile cilium assembly metal ion binding positive regulation of motile cilium assembly uc003dag.1 uc003dag.2 uc003dag.3 
ENST00000231751.9 LTF ENST00000231751.9 lactotransferrin, transcript variant 1 (from RefSeq NM_002343.6) ENST00000231751.1 ENST00000231751.2 ENST00000231751.3 ENST00000231751.4 ENST00000231751.5 ENST00000231751.6 ENST00000231751.7 ENST00000231751.8 HEL110 NM_002343 V9HWI4 V9HWI4_HUMAN uc003cpq.1 uc003cpq.2 uc003cpq.3 uc003cpq.4 uc003cpq.5 uc003cpq.6 This gene is a member of the transferrin family of genes and its protein product is found in the secondary granules of neutrophils. The protein is a major iron-binding protein in milk and body secretions with an antimicrobial activity, making it an important component of the non-specific immune system. The protein demonstrates a broad spectrum of properties, including regulation of iron homeostasis, host defense against a broad range of microbial infections, anti-inflammatory activity, regulation of cellular growth and differentiation and protection against cancer development and metastasis. Antimicrobial, antiviral, antifungal and antiparasitic activity has been found for this protein and its peptides. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2014]. Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Cytoplasmic granule Secreted Belongs to the transferrin family. regulation of cytokine production serine-type endopeptidase activity iron ion binding extracellular region extracellular space cytoplasm proteolysis peptidase activity antibacterial humoral response antifungal humoral response uc003cpq.1 uc003cpq.2 uc003cpq.3 uc003cpq.4 uc003cpq.5 uc003cpq.6 
ENST00000231790.8 MLH1 ENST00000231790.8 mutL homolog 1, transcript variant 1 (from RefSeq NM_000249.4) B4DI13 B4DQ11 COCA2 E9PCU2 ENST00000231790.1 ENST00000231790.2 ENST00000231790.3 ENST00000231790.4 ENST00000231790.5 ENST00000231790.6 ENST00000231790.7 MLH1_HUMAN NM_000249 P40692 uc003cgl.1 uc003cgl.2 uc003cgl.3 uc003cgl.4 uc003cgl.5 The protein encoded by this gene can heterodimerize with mismatch repair endonuclease PMS2 to form MutL alpha, part of the DNA mismatch repair system. When MutL alpha is bound by MutS beta and some accessory proteins, the PMS2 subunit of MutL alpha introduces a single-strand break near DNA mismatches, providing an entry point for exonuclease degradation. The encoded protein is also involved in DNA damage signaling and can heterodimerize with DNA mismatch repair protein MLH3 to form MutL gamma, which is involved in meiosis. This gene was identified as a locus frequently mutated in hereditary nonpolyposis colon cancer (HNPCC). [provided by RefSeq, Aug 2017]. Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis. Component of the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). Heterodimer of MLH1 and PMS2 (MutL alpha), MLH1 and PMS1 (MutL beta) or MLH1 and MLH3 (MutL gamma). Forms a ternary complex with MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3). Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex (PubMed:10783165). This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains (PubMed:10097147). Interacts with MCM9; the interaction recruits MLH1 to chromatin (PubMed:26300262). Interacts with MCM8 (PubMed:26300262). Interacts with PMS2 (PubMed:11427529, PubMed:22753075). Interacts with MBD4 (PubMed:10097147). Interacts with EXO1 (PubMed:11427529, PubMed:11429708, PubMed:12414623, PubMed:14676842, PubMed:22753075). Interacts with MTMR15/FAN1 (PubMed:20603073). P40692; P63261: ACTG1; NbExp=7; IntAct=EBI-744248, EBI-351292; P40692; P07355: ANXA2; NbExp=7; IntAct=EBI-744248, EBI-352622; P40692; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-744248, EBI-11978055; P40692; P63010-2: AP2B1; NbExp=8; IntAct=EBI-744248, EBI-11529439; P40692; Q9BX63: BRIP1; NbExp=18; IntAct=EBI-744248, EBI-3509650; P40692; Q9BX70: BTBD2; NbExp=3; IntAct=EBI-744248, EBI-710091; P40692; Q5JTZ5: C9orf152; NbExp=3; IntAct=EBI-744248, EBI-18560658; P40692; Q8NA61: CBY2; NbExp=6; IntAct=EBI-744248, EBI-741724; P40692; Q8NA61-2: CBY2; NbExp=11; IntAct=EBI-744248, EBI-11524851; P40692; Q8N5R6: CCDC33; NbExp=4; IntAct=EBI-744248, EBI-740841; P40692; Q96LY2-2: CCDC74B; NbExp=3; IntAct=EBI-744248, EBI-17967022; P40692; Q96GN5: CDCA7L; NbExp=4; IntAct=EBI-744248, EBI-5278764; P40692; O76039: CDKL5; NbExp=4; IntAct=EBI-744248, EBI-1752465; P40692; P07858: CTSB; NbExp=7; IntAct=EBI-744248, EBI-715062; P40692; P17661: DES; NbExp=7; IntAct=EBI-744248, EBI-1055572; P40692; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-744248, EBI-744099; P40692; Q86W67: FAM228A; NbExp=3; IntAct=EBI-744248, EBI-12958227; P40692; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-744248, EBI-742802; P40692; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-744248, EBI-6658203; P40692; Q96NE9: FRMD6; NbExp=3; IntAct=EBI-744248, EBI-741729; P40692; Q96NE9-2: FRMD6; NbExp=4; IntAct=EBI-744248, EBI-13213391; P40692; Q16658: FSCN1; NbExp=7; IntAct=EBI-744248, EBI-351076; P40692; P11142: HSPA8; NbExp=2; IntAct=EBI-744248, EBI-351896; P40692; Q9ULR0: ISY1; NbExp=3; IntAct=EBI-744248, EBI-2557660; P40692; P52292: KPNA2; NbExp=9; IntAct=EBI-744248, EBI-349938; P40692; O15131: KPNA5; NbExp=3; IntAct=EBI-744248, EBI-540602; P40692; Q5T749: KPRP; NbExp=3; IntAct=EBI-744248, EBI-10981970; P40692; O95232-2: LUC7L3; NbExp=3; IntAct=EBI-744248, EBI-19157865; P40692; P43361: MAGEA8; NbExp=7; IntAct=EBI-744248, EBI-10182930; P40692; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-744248, EBI-12516603; P40692; O95243-2: MBD4; NbExp=3; IntAct=EBI-744248, EBI-6448717; P40692; Q9NXL9: MCM9; NbExp=4; IntAct=EBI-744248, EBI-2804985; P40692; Q9UHC1: MLH3; NbExp=4; IntAct=EBI-744248, EBI-3893094; P40692; Q6PF18: MORN3; NbExp=3; IntAct=EBI-744248, EBI-9675802; P40692; P29372-4: MPG; NbExp=3; IntAct=EBI-744248, EBI-10695618; P40692; P20585: MSH3; NbExp=5; IntAct=EBI-744248, EBI-1164205; P40692; P15173: MYOG; NbExp=12; IntAct=EBI-744248, EBI-3906629; P40692; P60323-2: NANOS3; NbExp=3; IntAct=EBI-744248, EBI-18012223; P40692; Q9H3P2: NELFA; NbExp=3; IntAct=EBI-744248, EBI-5461341; P40692; Q14938-5: NFIX; NbExp=3; IntAct=EBI-744248, EBI-12024662; P40692; O00746: NME4; NbExp=3; IntAct=EBI-744248, EBI-744871; P40692; Q969T7: NT5C3B; NbExp=3; IntAct=EBI-744248, EBI-2932564; P40692; O15055: PER2; NbExp=3; IntAct=EBI-744248, EBI-1054296; P40692; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-744248, EBI-11532361; P40692; P54277: PMS1; NbExp=5; IntAct=EBI-744248, EBI-2893308; P40692; P54278: PMS2; NbExp=22; IntAct=EBI-744248, EBI-1162561; P40692; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-744248, EBI-1105153; P40692; Q6MZQ0: PRR5L; NbExp=3; IntAct=EBI-744248, EBI-1567866; P40692; P25786: PSMA1; NbExp=5; IntAct=EBI-744248, EBI-359352; P40692; P26045: PTPN3; NbExp=3; IntAct=EBI-744248, EBI-1047946; P40692; Q6NSI4: RADX; NbExp=9; IntAct=EBI-744248, EBI-8634209; P40692; Q5RL73: RBM48; NbExp=3; IntAct=EBI-744248, EBI-473821; P40692; Q86UC2: RSPH3; NbExp=3; IntAct=EBI-744248, EBI-6873025; P40692; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-744248, EBI-8635958; P40692; Q13813: SPTAN1; NbExp=7; IntAct=EBI-744248, EBI-351450; P40692; O95926: SYF2; NbExp=3; IntAct=EBI-744248, EBI-2557644; P40692; Q5VWN6: TASOR2; NbExp=6; IntAct=EBI-744248, EBI-745958; P40692; Q7Z6R9: TFAP2D; NbExp=5; IntAct=EBI-744248, EBI-11952651; P40692; Q08117-2: TLE5; NbExp=3; IntAct=EBI-744248, EBI-11741437; P40692; P62328: TMSB4X; NbExp=16; IntAct=EBI-744248, EBI-712598; P40692; Q96PP4: TSGA13; NbExp=3; IntAct=EBI-744248, EBI-12390276; P40692; Q01081: U2AF1; NbExp=3; IntAct=EBI-744248, EBI-632461; P40692; O94941: UBOX5; NbExp=7; IntAct=EBI-744248, EBI-751901; P40692; O75152: ZC3H11A; NbExp=7; IntAct=EBI-744248, EBI-748480; P40692; Q9NU63-3: ZFP57; NbExp=3; IntAct=EBI-744248, EBI-12879708; P40692; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-744248, EBI-11419867; P40692; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-744248, EBI-7850213; P40692; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-744248, EBI-12272076; P40692; Q9UDV6: ZNF212; NbExp=3; IntAct=EBI-744248, EBI-1640204; P40692; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-744248, EBI-17269964; P40692; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-744248, EBI-10251462; Nucleus romosome Note=Recruited to chromatin in a MCM9-dependent manner. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P40692-1; Sequence=Displayed; Name=2; IsoId=P40692-2; Sequence=VSP_045201; Name=3; IsoId=P40692-3; Sequence=VSP_047023; Colon, lymphocytes, breast, lung, spleen, testis, prostate, thyroid, gall bladder and heart. Lynch syndrome 2 (LYNCH2) [MIM:609310]: A form of Lynch syndrome, an autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra- colonic tumors of the gastrointestinal, urological and female reproductive tracts. Lynch syndrome is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, it is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical Lynch syndrome is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected Lynch syndrome' or 'incomplete Lynch syndrome' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. te=The disease is caused by variants affecting the gene represented in this entry. Mismatch repair cancer syndrome 1 (MMRCS1) [MIM:276300]: An autosomal recessive form of mismatch repair cancer syndrome, a childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. te=The disease is caused by variants affecting the gene represented in this entry. Muir-Torre syndrome (MRTES) [MIM:158320]: Rare autosomal dominant disorder characterized by sebaceous neoplasms and visceral malignancy. Note=The disease is caused by variants affecting the gene represented in this entry. Note=Defects in MLH1 may contribute to lobular carcinoma in situ (LCIS), a non-invasive neoplastic disease of the breast. Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Note=Some epigenetic changes can be transmitted unchanged through the germline (termed 'epigenetic inheritance'). Evidence that this mechanism occurs in humans is provided by the identification of individuals in whom 1 allele of the MLH1 gene is epigenetically silenced throughout the soma (implying a germline event). These individuals are affected by Lynch syndrome but does not have identifiable mutations in MLH1, even though it is silenced, which demonstrates that an epimutation can phenocopy a genetic disease. Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. te=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the DNA mismatch repair MutL/HexB family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/149/MLH1"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mlh1/"; Name=Colon cancer gene variant databases MutL homolog 1 (E.coli) (MLH1); Note=Leiden Open Variation Database (LOVD); URL="https://databases.lovd.nl/shared/genes/MLH1"; nucleotide binding nuclear-transcribed mRNA poly(A) tail shortening resolution of meiotic recombination intermediates condensed chromosome condensed nuclear chromosome synaptonemal complex male germ cell nucleus somatic recombination of immunoglobulin genes involved in immune response chromatin binding protein binding ATP binding nucleus nucleoplasm chromosome chiasma late recombination nodule DNA repair mismatch repair double-strand break repair via nonhomologous end joining cellular response to DNA damage stimulus cell cycle male meiosis chromosome segregation synapsis reciprocal meiotic recombination male meiosis spermatogenesis intrinsic apoptotic signaling pathway in response to DNA damage response to bacterium membrane female meiosis chromosome segregation somatic hypermutation of immunoglobulin genes somatic recombination of immunoglobulin gene segments ATPase activity enzyme binding mismatched DNA binding guanine/thymine mispair binding mismatch repair complex MutLalpha complex meiotic metaphase I plate congression meiotic chromosome segregation meiotic telomere clustering homologous chromosome segregation isotype switching negative regulation of mitotic recombination positive regulation of isotype switching to IgA isotypes positive regulation of isotype switching to IgG isotypes oogenesis meiotic spindle midzone assembly meiotic cell cycle single-stranded DNA binding MutSalpha complex binding uc003cgl.1 uc003cgl.2 uc003cgl.3 uc003cgl.4 uc003cgl.5 
ENST00000231887.8 EHHADH ENST00000231887.8 enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase, transcript variant 1 (from RefSeq NM_001966.4) A8K6Y3 B4DWG3 D3DNU0 ECHD ECHP_HUMAN EHHADH ENST00000231887.1 ENST00000231887.2 ENST00000231887.3 ENST00000231887.4 ENST00000231887.5 ENST00000231887.6 ENST00000231887.7 NM_001966 Q08426 Q58EZ5 uc003fpf.1 uc003fpf.2 uc003fpf.3 uc003fpf.4 The protein encoded by this gene is a bifunctional enzyme and is one of the four enzymes of the peroxisomal beta-oxidation pathway. The N-terminal region of the encoded protein contains enoyl-CoA hydratase activity while the C-terminal region contains 3-hydroxyacyl-CoA dehydrogenase activity. Defects in this gene are a cause of peroxisomal disorders such as Zellweger syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2009]. Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl- CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (By similarity). Can also use branched-chain fatty acids such as 2-methyl- 2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3- hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species (Probable). Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (PubMed:15060085). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta- oxidation (PubMed:15060085). Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16106; Evidence=; Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20725; Evidence=; Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901; Evidence=; Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229; Evidence=; Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433; Evidence=; Reaction=(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA = (2E)-2-methylbut-2- enoyl-CoA + H2O; Xref=Rhea:RHEA:31119, ChEBI:CHEBI:15377, ChEBI:CHEBI:57312, ChEBI:CHEBI:57337; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31121; Evidence=; Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378, ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62613; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160; Evidence=; Reaction=(3S)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O; Xref=Rhea:RHEA:31163, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526, ChEBI:CHEBI:62613; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31165; Evidence=; Reaction=(2E)-hexadecenedioyl-CoA + H2O = (3S)-hydroxyhexadecanedioyl- CoA; Xref=Rhea:RHEA:40259, ChEBI:CHEBI:15377, ChEBI:CHEBI:77075, ChEBI:CHEBI:77080; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40260; Evidence=; Reaction=(3S)-hydroxyhexadecanedioyl-CoA + NAD(+) = 3- oxohexadecanedioyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:40267, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77080, ChEBI:CHEBI:77081; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40268; Evidence=; Reaction=(3E,5Z)-tetradecadienoyl-CoA = (2E,5Z)-tetradecadienoyl-CoA; Xref=Rhea:RHEA:47464, ChEBI:CHEBI:71586, ChEBI:CHEBI:87701; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47466; Evidence=; Reaction=(3E,5Z)-octadienoyl-CoA = (2E,5Z)-octadienoyl-CoA; Xref=Rhea:RHEA:49932, ChEBI:CHEBI:85108, ChEBI:CHEBI:131990; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49934; Evidence=; Reaction=(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:62616; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31188; Evidence=; Reaction=(3E)-decenoyl-CoA = (2E)-decenoyl-CoA; Xref=Rhea:RHEA:45752, ChEBI:CHEBI:61406, ChEBI:CHEBI:84793; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45753; Evidence=; Reaction=(3Z)-hexenoyl-CoA = (2E)-hexenoyl-CoA; Xref=Rhea:RHEA:45748, ChEBI:CHEBI:62077, ChEBI:CHEBI:85415; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45749; Evidence=; Reaction=(3E)-hexenoyl-CoA = (2E)-hexenoyl-CoA; Xref=Rhea:RHEA:45736, ChEBI:CHEBI:62077, ChEBI:CHEBI:84790; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45737; Evidence=; Reaction=(3S)-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2O; Xref=Rhea:RHEA:31191, ChEBI:CHEBI:15377, ChEBI:CHEBI:61406, ChEBI:CHEBI:62616; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31193; Evidence=; Reaction=(3S)-hydroxyhexanoyl-CoA = (2E)-hexenoyl-CoA + H2O; Xref=Rhea:RHEA:30547, ChEBI:CHEBI:15377, ChEBI:CHEBI:62075, ChEBI:CHEBI:62077; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30549; Evidence=; Enzyme activity enhanced by acetylation. Kinetic parameters: KM=0.3 uM for (3S)-hydroxyhexadecanedioyl-CoA ; KM=10 uM for (3S)-hydroxyhexadecanoyl-CoA ; Lipid metabolism; fatty acid beta-oxidation. Monomer. Q08426; Q5JTZ9: AARS2; NbExp=3; IntAct=EBI-2339219, EBI-308736; Q08426; P60709: ACTB; NbExp=4; IntAct=EBI-2339219, EBI-353944; Q08426; P63261: ACTG1; NbExp=4; IntAct=EBI-2339219, EBI-351292; Q08426; P78563-4: ADARB1; NbExp=3; IntAct=EBI-2339219, EBI-12002366; Q08426; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-2339219, EBI-12170453; Q08426; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-2339219, EBI-36513937; Q08426; Q9UH62: ARMCX3; NbExp=3; IntAct=EBI-2339219, EBI-717832; Q08426; O14503: BHLHE40; NbExp=3; IntAct=EBI-2339219, EBI-711810; Q08426; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-2339219, EBI-11983447; Q08426; Q9BV19: C1orf50; NbExp=3; IntAct=EBI-2339219, EBI-2874661; Q08426; P20807-4: CAPN3; NbExp=3; IntAct=EBI-2339219, EBI-11532021; Q08426; P35520: CBS; NbExp=4; IntAct=EBI-2339219, EBI-740135; Q08426; Q68D86: CCDC102B; NbExp=4; IntAct=EBI-2339219, EBI-10171570; Q08426; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-2339219, EBI-10961312; Q08426; Q86X02: CDR2L; NbExp=3; IntAct=EBI-2339219, EBI-11063830; Q08426; Q9Y592-2: CEP83; NbExp=3; IntAct=EBI-2339219, EBI-11123098; Q08426; Q9Y281: CFL2; NbExp=3; IntAct=EBI-2339219, EBI-351218; Q08426; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-2339219, EBI-1045797; Q08426; P56856: CLDN18; NbExp=3; IntAct=EBI-2339219, EBI-16354902; Q08426; O00501: CLDN5; NbExp=3; IntAct=EBI-2339219, EBI-18400628; Q08426; P49760: CLK2; NbExp=3; IntAct=EBI-2339219, EBI-750020; Q08426; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-2339219, EBI-1054315; Q08426; O75208: COQ9; NbExp=3; IntAct=EBI-2339219, EBI-724524; Q08426; P49447: CYB561; NbExp=3; IntAct=EBI-2339219, EBI-8646596; Q08426; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-2339219, EBI-10269179; Q08426; Q96Q80: DERL3; NbExp=3; IntAct=EBI-2339219, EBI-12831318; Q08426; P17661: DES; NbExp=6; IntAct=EBI-2339219, EBI-1055572; Q08426; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-2339219, EBI-517508; Q08426; Q15125: EBP; NbExp=3; IntAct=EBI-2339219, EBI-3915253; Q08426; P54849: EMP1; NbExp=3; IntAct=EBI-2339219, EBI-4319440; Q08426; Q969X5: ERGIC1; NbExp=3; IntAct=EBI-2339219, EBI-781527; Q08426; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2339219, EBI-781551; Q08426; P60508: ERVFRD-1; NbExp=3; IntAct=EBI-2339219, EBI-17973325; Q08426; Q92915-2: FGF14; NbExp=3; IntAct=EBI-2339219, EBI-12836320; Q08426; Q8IVP5: FUNDC1; NbExp=4; IntAct=EBI-2339219, EBI-3059266; Q08426; O95995: GAS8; NbExp=3; IntAct=EBI-2339219, EBI-1052570; Q08426; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-2339219, EBI-2548508; Q08426; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-2339219, EBI-717919; Q08426; Q8IV36: HID1; NbExp=3; IntAct=EBI-2339219, EBI-743438; Q08426; O00291: HIP1; NbExp=3; IntAct=EBI-2339219, EBI-473886; Q08426; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-2339219, EBI-740641; Q08426; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-2339219, EBI-1052304; Q08426; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-2339219, EBI-12937691; Q08426; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2339219, EBI-747204; Q08426; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2339219, EBI-10266796; Q08426; Q8NC69: KCTD6; NbExp=5; IntAct=EBI-2339219, EBI-2511344; Q08426; Q7L273: KCTD9; NbExp=4; IntAct=EBI-2339219, EBI-4397613; Q08426; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-2339219, EBI-10172290; Q08426; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-2339219, EBI-10302392; Q08426; P80188: LCN2; NbExp=3; IntAct=EBI-2339219, EBI-11911016; Q08426; O95214: LEPROTL1; NbExp=5; IntAct=EBI-2339219, EBI-750776; Q08426; P36941: LTBR; NbExp=3; IntAct=EBI-2339219, EBI-3509981; Q08426; Q6UWN5: LYPD5; NbExp=3; IntAct=EBI-2339219, EBI-17200970; Q08426; Q9NQ48: LZTFL1; NbExp=3; IntAct=EBI-2339219, EBI-2824799; Q08426; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2339219, EBI-741037; Q08426; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-2339219, EBI-10268010; Q08426; O15344: MID1; NbExp=8; IntAct=EBI-2339219, EBI-2340316; Q08426; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2339219, EBI-11522433; Q08426; Q96RE7: NACC1; NbExp=3; IntAct=EBI-2339219, EBI-7950997; Q08426; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-2339219, EBI-10172876; Q08426; P35372-10: OPRM1; NbExp=3; IntAct=EBI-2339219, EBI-12807478; Q08426; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-2339219, EBI-1054848; Q08426; Q8TEZ7: PAQR8; NbExp=3; IntAct=EBI-2339219, EBI-12847818; Q08426; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2339219, EBI-79165; Q08426; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-2339219, EBI-302345; Q08426; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-2339219, EBI-10171633; Q08426; Q9BZL4: PPP1R12C; NbExp=3; IntAct=EBI-2339219, EBI-721802; Q08426; O75569: PRKRA; NbExp=3; IntAct=EBI-2339219, EBI-713955; Q08426; O14744: PRMT5; NbExp=3; IntAct=EBI-2339219, EBI-351098; Q08426; Q1KLZ0: PS1TP5BP1; NbExp=3; IntAct=EBI-2339219, EBI-9978131; Q08426; O43586: PSTPIP1; NbExp=3; IntAct=EBI-2339219, EBI-1050964; Q08426; O14684: PTGES; NbExp=3; IntAct=EBI-2339219, EBI-11161398; Q08426; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-2339219, EBI-14065960; Q08426; Q04864-2: REL; NbExp=3; IntAct=EBI-2339219, EBI-10829018; Q08426; P78317: RNF4; NbExp=3; IntAct=EBI-2339219, EBI-2340927; Q08426; Q9NS64: RPRM; NbExp=3; IntAct=EBI-2339219, EBI-1052363; Q08426; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-2339219, EBI-8636004; Q08426; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-2339219, EBI-12823227; Q08426; Q8N3Y7: SDR16C5; NbExp=3; IntAct=EBI-2339219, EBI-3923480; Q08426; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-2339219, EBI-2854842; Q08426; Q16585: SGCB; NbExp=3; IntAct=EBI-2339219, EBI-5663627; Q08426; Q15849: SLC14A2; NbExp=3; IntAct=EBI-2339219, EBI-1573290; Q08426; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-2339219, EBI-12898013; Q08426; Q71RC9: SMIM5; NbExp=3; IntAct=EBI-2339219, EBI-12334905; Q08426; Q16637: SMN2; NbExp=3; IntAct=EBI-2339219, EBI-395421; Q08426; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-2339219, EBI-17280858; Q08426; O43805: SSNA1; NbExp=4; IntAct=EBI-2339219, EBI-2515299; Q08426; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-2339219, EBI-2212028; Q08426; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-2339219, EBI-12187159; Q08426; O43761: SYNGR3; NbExp=3; IntAct=EBI-2339219, EBI-11321949; Q08426; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-2339219, EBI-12155101; Q08426; Q86X19: TMEM17; NbExp=3; IntAct=EBI-2339219, EBI-11343485; Q08426; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-2339219, EBI-11722971; Q08426; Q15025: TNIP1; NbExp=4; IntAct=EBI-2339219, EBI-357849; Q08426; P29144: TPP2; NbExp=5; IntAct=EBI-2339219, EBI-1044672; Q08426; Q13077: TRAF1; NbExp=3; IntAct=EBI-2339219, EBI-359224; Q08426; Q12933: TRAF2; NbExp=3; IntAct=EBI-2339219, EBI-355744; Q08426; P19474: TRIM21; NbExp=3; IntAct=EBI-2339219, EBI-81290; Q08426; P36406: TRIM23; NbExp=3; IntAct=EBI-2339219, EBI-740098; Q08426; P14373: TRIM27; NbExp=6; IntAct=EBI-2339219, EBI-719493; Q08426; Q8WV44: TRIM41; NbExp=7; IntAct=EBI-2339219, EBI-725997; Q08426; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-2339219, EBI-12840050; Q08426; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2339219, EBI-2130429; Q08426; Q969Q1: TRIM63; NbExp=3; IntAct=EBI-2339219, EBI-5661333; Q08426; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-2339219, EBI-11530712; Q08426; Q08AM6: VAC14; NbExp=3; IntAct=EBI-2339219, EBI-2107455; Q08426; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-2339219, EBI-12017160; Q08426; Q9HCK0: ZBTB26; NbExp=5; IntAct=EBI-2339219, EBI-3918996; Q08426; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-2339219, EBI-742740; Q08426; Q96C00: ZBTB9; NbExp=6; IntAct=EBI-2339219, EBI-395708; Q08426; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-2339219, EBI-746345; Q08426; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2339219, EBI-527853; Q08426; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-2339219, EBI-25475856; Peroxisome Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q08426-1; Sequence=Displayed; Name=2; IsoId=Q08426-2; Sequence=VSP_042811; Liver and kidney. Strongly expressed in the terminal segments of the proximal tubule. Lower amounts seen in the brain. Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TSA) or with nicotinamide (NAM) with highest increase on Lys-346. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids. Fanconi renotubular syndrome 3 (FRTS3) [MIM:615605]: A form of Fanconi renotubular syndrome, a disease due to a generalized dysfunction of the proximal kidney tubule resulting in decreased solute and water reabsorption. Patients have polydipsia and polyuria with phosphaturia, glycosuria and aminoaciduria. They may develop hypophosphatemic rickets or osteomalacia, acidosis and a tendency toward dehydration. Some eventually develop renal insufficiency. FRTS3 inheritance is autosomal dominant. Note=The disease is caused by variants affecting the gene represented in this entry. Absent in patients suffering with peroxisomal disorders such as Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum disease. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. catalytic activity 3-hydroxyacyl-CoA dehydrogenase activity dodecenoyl-CoA delta-isomerase activity enoyl-CoA hydratase activity protein binding peroxisome peroxisomal matrix cytosol internal protein amino acid acetylation protein targeting to peroxisome lipid metabolic process fatty acid metabolic process fatty acid beta-oxidation metabolic process oxidoreductase activity long-chain-enoyl-CoA hydratase activity lyase activity isomerase activity enzyme binding fatty acid beta-oxidation using acyl-CoA oxidase oxidation-reduction process uc003fpf.1 uc003fpf.2 uc003fpf.3 uc003fpf.4 
ENST00000231948.9 CRBN ENST00000231948.9 cereblon, transcript variant 1 (from RefSeq NM_016302.4) AD-006 B2R6H4 C9IZA9 C9JAH6 CRBN_HUMAN ENST00000231948.1 ENST00000231948.2 ENST00000231948.3 ENST00000231948.4 ENST00000231948.5 ENST00000231948.6 ENST00000231948.7 ENST00000231948.8 NM_016302 Q6AI62 Q6NVZ0 Q96SW2 Q9UHW4 uc003bpq.1 uc003bpq.2 uc003bpq.3 uc003bpq.4 uc003bpq.5 This gene encodes a protein related to the Lon protease protein family. In rodents and other mammals this gene product is found in the cytoplasm localized with a calcium channel membrane protein, and is thought to play a role in brain development. Mutations in this gene are associated with autosomal recessive nonsyndromic cognitive disability. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2010]. Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2 (PubMed:33009960). Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (PubMed:20223979, PubMed:24328678, PubMed:25043012, PubMed:25108355). Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons (PubMed:18414909, PubMed:29530986). Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (PubMed:18414909). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity). Plays a negative role in TLR4 signaling by interacting with TRAF6 and ECSIT, leading to inhibition of ECSIT ubiquitination, an important step of the signaling (PubMed:31620128). Protein modification; protein ubiquitination. Interacts with KCNT1 (By similarity). Component of a DCX (DDB1-CUL4-X-box) protein ligase complex, at least composed of CRBN, CUL4A, DDB1 and RBX1. Interacts directly with DDB1 (PubMed:25043012, PubMed:25108355). Interacts (in pomalidomide-bound form) with IKZF1 and IKZF3 (PubMed:24328678). Interacts with ILF2 (PubMed:33009960). Interacts with TRAF6 and ECSIT (PubMed:31620128). Q96SW2; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-2510250, EBI-21553822; Q96SW2; P48729: CSNK1A1; NbExp=3; IntAct=EBI-2510250, EBI-1383726; Q96SW2; Q16531: DDB1; NbExp=3; IntAct=EBI-2510250, EBI-350322; Q96SW2; O14901: KLF11; NbExp=3; IntAct=EBI-2510250, EBI-948266; Q96SW2; Q8IVT2: MISP; NbExp=3; IntAct=EBI-2510250, EBI-2555085; Q96SW2; Q9P286: PAK5; NbExp=4; IntAct=EBI-2510250, EBI-741896; Q96SW2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2510250, EBI-25882629; Q96SW2; Q93062: RBPMS; NbExp=3; IntAct=EBI-2510250, EBI-740322; Q96SW2-2; Q16531: DDB1; NbExp=7; IntAct=EBI-10693561, EBI-350322; Q96SW2-2; Q13422-7: IKZF1; NbExp=2; IntAct=EBI-10693561, EBI-11522367; Cytoplasm Nucleus Membrane ; Peripheral membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96SW2-1; Sequence=Displayed; Name=2; IsoId=Q96SW2-2; Sequence=VSP_015209; Widely expressed. Highly expressed in brain. The CULT domain binds thalidomide and related drugs, such as pomalidomide and lenalidomide. Drug binding leads to a change in substrate specificity of the human DCX (DDB1-CUL4-X-box) E3 protein ligase complex, while no such change is observed in rodents. Ubiquitinated, ubiquitination is mediated by its own DCX protein ligase complex. Intellectual developmental disorder, autosomal recessive 2 (MRT2) [MIM:607417]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT2 patients display mild intellectual disability with a standard IQ ranged from 50 to 70. IQ scores are lower in males than females. Developmental milestones are mildly delayed. There are no dysmorphic or autistic features. Note=The disease is caused by variants affecting the gene represented in this entry. Thalidomide was widely prescribed to pregnant women in the late 1950s as a sedative and as treatment against morning sickness. Thalidomide was found to be teratogenic, causing multiple birth defects. Recently, thalidomide use has increased for the treatment of multiple myeloma and erythema nodosum leprosum, a painful complication of leprosy. Binding of pomalidomide and other thalidomide-related drugs leads to a change in substrate specificity of the human DCX (DDB1-CUL4- X-box) E3 protein ligase complex, and this is probably the underlying cause of the teratogenic activity of thalidomide, possibly due to abnormal regulation of the BMP and FGF8 signaling pathways (PubMed:20223979). The thalidomide-induced change in substrate specificity leads to decreased degradation of MEIS2 and other target proteins and increased degradation of MYC, IRF4, IKZF1 and IKZF3, and this is probably the reason for the anti-proliferative and immunomodulatory effects of thalidomide and related drugs (PubMed:25108355). Thalidomide is also teratogenic in chicken and zebrafish, but not in mice. Belongs to the CRBN family. Although it contains a Lon N-terminal domain also found in proteases of the peptidase S16 family, it does not contain the ATP- binding and catalytic domains, suggesting that it has no protease activity. Sequence=AAF17211.1; Type=Frameshift; Evidence=; Sequence=BAG35471.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=BAG35471.1; Type=Frameshift; Evidence=; Name=Protein Spotlight; Note=A short story - Issue 117 of May 2010; URL="https://web.expasy.org/spotlight/back_issues/117"; protein binding nucleus nucleolus cytoplasm membrane protein ubiquitination Cul4A-RING E3 ubiquitin ligase complex negative regulation of protein homooligomerization negative regulation of ion transmembrane transport proteasome-mediated ubiquitin-dependent protein catabolic process metal ion binding positive regulation of protein homodimerization activity uc003bpq.1 uc003bpq.2 uc003bpq.3 uc003bpq.4 uc003bpq.5 
ENST00000232003.5 HRG ENST00000232003.5 histidine rich glycoprotein (from RefSeq NM_000412.5) B9EK35 D3DNU7 ENST00000232003.1 ENST00000232003.2 ENST00000232003.3 ENST00000232003.4 HRG_HUMAN NM_000412 P04196 uc003fqq.1 uc003fqq.2 uc003fqq.3 uc003fqq.4 uc003fqq.5 uc003fqq.6 This histidine-rich glycoprotein contains two cystatin-like domains and is located in plasma and platelets. The physiological function has not been determined but it is known that the protein binds heme, dyes and divalent metal ions. The encoded protein also has a peptide that displays antimicrobial activity against C. albicans, E. coli, S. aureus, P. aeruginosa, and E. faecalis. It can inhibit rosette formation and interacts with heparin, thrombospondin and plasminogen. Two of the protein's effects, the inhibition of fibrinolysis and the reduction of inhibition of coagulation, indicate a potential prothrombotic effect. Mutations in this gene lead to thrombophilia due to abnormal histidine-rich glycoprotein levels. [provided by RefSeq, Nov 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M13149.1, BC150591.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232003.5/ ENSP00000232003.4 Protein has antimicrobial activity :: PMID: 17229145, 18797515 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis. Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Interacts (via the HRR domain) with TPM1; the interaction appears to contribute to the antiangiogenic properties of the HRR domain. Interacts with THBS2; the interaction blocks the antiangiogenic effect of THBS2 with CD36 (By similarity). Interacts with THBS1 (via the TSP type I repeats); the interaction blocks the antiangiogenic effect of THBS1 with CD3. Interacts with PLG (via its Kringle domains); the interaction tethers PLG to the cell surface and enhances its activation. Interacts with HPSE; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts (via the HRR domain) with TMP1; the interaction partially mediates the antiangiogenic properties of HRG. Interacts with kappa and lambda light chains of IgG molecules. Interacts with ATP5F1A; the interaction occurs on the surface of T- cells and alters their cell morphology in concert with CONA. Binds IgG molecules containing kappa and lambda light chains and inhibits the formation of insoluble immunoglobulin complexes. Interacts with F12; the interaction, which is enhanced in the presence of zinc ions and inhibited by heparin-binding to HRG, inhibits factor XII autoactivation and contact-initiated coagulation. P04196; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-3915012, EBI-3867333; P04196; Q96PM5: RCHY1; NbExp=3; IntAct=EBI-3915012, EBI-947779; P04196; O76081-6: RGS20; NbExp=3; IntAct=EBI-3915012, EBI-10178530; P04196; Q99XU0: SPy_2034; Xeno; NbExp=4; IntAct=EBI-3915012, EBI-8852705; Secreted Expressed in macrophages and in malignant cells. Expressed by the liver and secreted in plasma (at protein level). The His/Pro-rich (HRR) region contains approximately 12 tandem internal repeats of the 5-residue G[H/P][H/P]PH consensus sequence. HRR binds heparan sulfate and possesses antiangiogenic, antibacterial and antifungal properties through binding Candida cells, and preferentially lysing the ergosterol-containing liposomes at low pH. The tandem repeats also bind divalent metal ions and heme. The cystatin domains can also bind heparan sulfate. Binding is enhanced in the presence of zinc ions. Proteolytic cleavage produces several HRG fragments which are mostly disulfide-linked and, therefore, not released. Cleavage by plasmin is inhibited in the presence of heparin, zinc ions or in an acidic environment. Cleavage reduces binding of HRG to heparan sulfate, but enhances the ability of HRG to bind and tether plasminogen to the cell surface. On platelet activation, releases a 33 kDa antiangiogenic peptide which encompasses the HRR. Also cleaved in the C-terminal by plasmin. N-glycosylated. Thrombophilia due to histidine-rich glycoprotein deficiency (THPH11) [MIM:613116]: A hemostatic disorder characterized by a tendency to thrombosis. te=The disease is caused by variants affecting the gene represented in this entry. angiogenesis platelet degranulation positive regulation of immune response to tumor cell serine-type endopeptidase inhibitor activity cysteine-type endopeptidase inhibitor activity receptor binding protein binding extracellular region plasma membrane chemotaxis negative regulation of cell adhesion blood coagulation hemostasis heparin binding zinc ion binding negative regulation of cell proliferation cell surface regulation of gene expression regulation of platelet activation negative regulation of lamellipodium assembly negative regulation of endopeptidase activity heme transport negative regulation of angiogenesis immunoglobulin binding heme binding platelet activation regulation of blood coagulation negative regulation of cell growth platelet alpha granule lumen regulation of actin cytoskeleton organization negative regulation of cell adhesion mediated by integrin endolysosome fibrinolysis positive regulation of apoptotic process regulation of protein complex assembly heparan sulfate proteoglycan binding negative regulation of blood vessel endothelial cell migration metal ion binding regulation of peptidyl-tyrosine phosphorylation defense response to fungus cytolysis in other organism positive regulation of focal adhesion assembly negative regulation of fibrinolysis extracellular exosome blood microparticle negative regulation of vascular endothelial growth factor signaling pathway positive regulation of blood vessel remodeling negative regulation of endothelial cell chemotaxis uc003fqq.1 uc003fqq.2 uc003fqq.3 uc003fqq.4 uc003fqq.5 uc003fqq.6 
ENST00000232217.6 RBP2 ENST00000232217.6 retinol binding protein 2 (from RefSeq NM_004164.3) A8K7G3 CRBP2 ENST00000232217.1 ENST00000232217.2 ENST00000232217.3 ENST00000232217.4 ENST00000232217.5 NM_004164 P50120 Q6ISQ9 Q6ISS7 RET2_HUMAN uc003eth.1 uc003eth.2 uc003eth.3 uc003eth.4 This gene encodes an abundant protein present in the small intestinal epithelium. It is thought to participate in the uptake and/or intracellular metabolism of vitamin A. Vitamin A is a fat-soluble vitamin necessary for growth, reproduction, differentiation of epithelial tissues, and vision. This protein may also modulate the supply of retinoic acid to the nuclei of endometrial cells during the menstrual cycle. [provided by RefSeq, Aug 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AW772327.1, AK291978.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232217.6/ ENSP00000232217.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Intracellular transport of retinol. Cytoplasm. Higher expression in adult small intestine and to a much lesser extent in fetal kidney. Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family. retinoid metabolic process retinoid binding cytoplasm cytosol vitamin A metabolic process lipid binding epidermis development retinal binding retinol binding uc003eth.1 uc003eth.2 uc003eth.3 uc003eth.4 
ENST00000232375.8 PFKFB4 ENST00000232375.8 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4, transcript variant 2 (from RefSeq NM_004567.4) ENST00000232375.1 ENST00000232375.2 ENST00000232375.3 ENST00000232375.4 ENST00000232375.5 ENST00000232375.6 ENST00000232375.7 F264_HUMAN NM_004567 Q16877 Q5S3G5 Q5XLC2 Q64EX5 uc003ctv.1 uc003ctv.2 uc003ctv.3 uc003ctv.4 uc003ctv.5 The protein encoded by this gene is one of four bifunctional kinase/phosphatases that regulate the concentration of the glycolytic byproduct fructose-2,6-bisphosphate (F2,6BP). The encoded protein is highly expressed in cancer cells and is induced by hypoxia. This protein is essential to the survival of cancer cells under conditions of hypoxia, because it increases the amount of F2,6BP and ATP at a time when the cell cannot produce much of them. This finding suggests that this protein may be a good target for disruption in cancer cells, hopefully imperiling their survival. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015]. Synthesis and degradation of fructose 2,6-bisphosphate. Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6- phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6- bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579, ChEBI:CHEBI:456216; EC=2.7.1.105; The most important regulatory mechanism of these opposing activities is by phosphorylation and dephosphorylation of the enzyme. Homodimer. Q16877; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-764534, EBI-10171570; Q16877; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-764534, EBI-396137; Q16877; Q96L50: LRR1; NbExp=3; IntAct=EBI-764534, EBI-2510106; Q16877; P16118: PFKFB1; NbExp=5; IntAct=EBI-764534, EBI-709807; Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q16877-1; Sequence=Displayed; Name=2; IsoId=Q16877-2; Sequence=VSP_056530; Name=3; IsoId=Q16877-3; Sequence=VSP_056621; In the C-terminal section; belongs to the phosphoglycerate mutase family. nucleotide binding catalytic activity 6-phosphofructo-2-kinase activity fructose-2,6-bisphosphate 2-phosphatase activity ATP binding cytosol fructose metabolic process fructose 2,6-bisphosphate metabolic process metabolic process kinase activity phosphorylation dephosphorylation transferase activity hydrolase activity positive regulation of glycolytic process carbohydrate phosphorylation uc003ctv.1 uc003ctv.2 uc003ctv.3 uc003ctv.4 uc003ctv.5 
ENST00000232424.4 HES1 ENST00000232424.4 hes family bHLH transcription factor 1 (from RefSeq NM_005524.4) BHLHB39 ENST00000232424.1 ENST00000232424.2 ENST00000232424.3 HES1_HUMAN HL HRY NM_005524 Q14469 Q6FHB2 uc003ftq.1 uc003ftq.2 uc003ftq.3 uc003ftq.4 This protein belongs to the basic helix-loop-helix family of transcription factors. It is a transcriptional repressor of genes that require a bHLH protein for their transcription. The protein has a particular type of basic domain that contains a helix interrupting protein that binds to the N-box rather than the canonical E-box. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DA569975.1, AK000415.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232424.4/ ENSP00000232424.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1. Binds DNA on N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'- CANNTG-3' with low affinity (By similarity). May play a role in a functional FA core complex response to DNA cross-link damage, being required for the stability and nuclear localization of FA core complex proteins, as well as for FANCD2 monoubiquitination in response to DNA damage. Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family. Interacts (via WPRW motif) with TLE1, and more weakly with TLE2. Interacts with HES6 (By similarity). Interacts with SIRT1. Interacts with an FA complex, composed of FANCA, FANCF, FANCG and FANCL, but not of FANCC, nor FANCE. Q14469; Q96EB6: SIRT1; NbExp=4; IntAct=EBI-2832522, EBI-1802965; Nucleus Has a particular type of basic domain (presence of a helix- interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG). The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy- related proteins. The bHLH, as well as cooperation between the central Orange domain and the C-terminal WRPW motif, is required for transcriptional repressor activity. (Microbial infection) Ubiquitinated via human cytomegalovirus/HCMV protein IE1 that assembles a HES1 ubiquitination complex; leading to HES1 proteasomal degradation. negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding in utero embryonic development liver development embryonic heart tube morphogenesis outflow tract morphogenesis regulation of secondary heart field cardioblast proliferation ventricular septum development DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm cytoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter cell adhesion Notch signaling pathway smoothened signaling pathway pattern specification process nervous system development transcription factor binding positive regulation of cell proliferation anterior/posterior pattern specification cell migration telencephalon development midbrain-hindbrain boundary morphogenesis oculomotor nerve development trochlear nerve development hindbrain morphogenesis forebrain radial glial cell differentiation neural tube development pituitary gland development adenohypophysis development cell differentiation lung development positive regulation of BMP signaling pathway midbrain development pancreas development somatic stem cell population maintenance aorta morphogenesis ascending aorta morphogenesis positive regulation of T cell proliferation positive regulation of tyrosine phosphorylation of STAT protein protein homodimerization activity histone deacetylase binding positive regulation of DNA binding sequence-specific DNA binding cell fate commitment negative regulation of cell differentiation regulation of fat cell differentiation negative regulation of auditory receptor cell differentiation negative regulation of neuron differentiation positive regulation of Notch signaling pathway negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter positive regulation of mitotic cell cycle, embryonic lateral inhibition regulation of JAK-STAT cascade positive regulation of JAK-STAT cascade protein dimerization activity cell maturation regulation of timing of cell differentiation thymus development cell morphogenesis involved in neuron differentiation positive regulation of astrocyte differentiation negative regulation of oligodendrocyte differentiation artery morphogenesis regulation of epithelial cell proliferation regulation of neurogenesis chaperone binding inner ear receptor stereocilium organization regulation of timing of neuron differentiation negative regulation of glial cell proliferation ventricular septum morphogenesis ureteric bud morphogenesis labyrinthine layer blood vessel development common bile duct development negative regulation of stomach neuroendocrine cell differentiation cardiac neural crest cell development involved in outflow tract morphogenesis pharyngeal arch artery morphogenesis macromolecular complex assembly E-box binding N-box binding glomerulus vasculature development comma-shaped body morphogenesis S-shaped body morphogenesis renal interstitial fibroblast development metanephric nephron tubule morphogenesis cochlea development establishment of epithelial cell polarity vascular smooth muscle cell development neuronal stem cell population maintenance negative regulation of pancreatic A cell differentiation negative regulation of stem cell differentiation negative regulation of pro-B cell differentiation negative regulation of forebrain neuron differentiation negative regulation of inner ear receptor cell differentiation uc003ftq.1 uc003ftq.2 uc003ftq.3 uc003ftq.4 
ENST00000232461.8 GNAT1 ENST00000232461.8 G protein subunit alpha transducin 1, transcript variant 1 (from RefSeq NM_144499.3) ENST00000232461.1 ENST00000232461.2 ENST00000232461.3 ENST00000232461.4 ENST00000232461.5 ENST00000232461.6 ENST00000232461.7 GNAT1_HUMAN GNATR NM_144499 P11488 Q4VBN2 uc003cym.1 uc003cym.2 uc003cym.3 uc003cym.4 Transducin is a 3-subunit guanine nucleotide-binding protein (G protein) which stimulates the coupling of rhodopsin and cGMP-phoshodiesterase during visual impulses. The transducin alpha subunits in rods and cones are encoded by separate genes. This gene encodes the alpha subunit in rods. This gene is also expressed in other cells, and has been implicated in bitter taste transduction in rat taste cells. Mutations in this gene result in autosomal dominant congenital stationary night blindness. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Feb 2009]. Functions as a signal transducer for the rod photoreceptor RHO. Required for normal RHO-mediated light perception by the retina (PubMed:22190596). Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs), such as the photoreceptor RHO. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP- bound state and an inactive, GDP-bound state. Activated RHO promotes GDP release and GTP binding. Signaling is mediated via downstream effector proteins, such as cGMP-phosphodiesterase (By similarity). Heterotrimeric G proteins are composed of 3 subunits alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with RHO. Interacts with RGS9 and PDE6G (By similarity). Interacts (when myristoylated) with UNC119; interaction is required for localization in sensory neurons (PubMed:21642972). Cell projection, cilium, photoreceptor outer segment Membrane ; Peripheral membrane protein Photoreceptor inner segment Note=Localizes mainly in the outer segment in the dark-adapted state, whereas is translocated to the inner part of the photoreceptors in the light-adapted state. During dark- adapted conditions, in the presence of UNC119 mislocalizes from the outer segment to the inner part of rod photoreceptors which leads to decreased photoreceptor damage caused by light. Rod photoreceptor cells (PubMed:1614872). Predominantly expressed in the retina followed by the ciliary body, iris and retinal pigment epithelium (PubMed:22190596). First detected at low levels at approximately postnatal day 7. Subsequently, expression increases rapidly during the first month after birth. Night blindness, congenital stationary, autosomal dominant 3 (CSNBAD3) [MIM:610444]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. Note=The disease is caused by variants affecting the gene represented in this entry. Night blindness, congenital stationary, 1G (CSNB1G) [MIM:616389]: An autosomal recessive form of congenital stationary night blindness, a non-progressive retinal disorder characterized by impaired night vision or in dim light, with good vision only on bright days. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the G-alpha family. G(i/o/t/z) subfamily. Name=Mutations of the GNAT1 gene; Note=Retina International's Scientific Newsletter; URL="https://www.retina-international.org/files/sci-news/gntmut.htm"; acyl binding nucleotide binding detection of chemical stimulus involved in sensory perception of bitter taste G-protein coupled receptor binding photoreceptor outer segment photoreceptor inner segment GTPase activity GTP binding cytoplasm cytosol heterotrimeric G-protein complex plasma membrane protein folding signal transduction G-protein coupled receptor signaling pathway adenylate cyclase-modulating G-protein coupled receptor signaling pathway visual perception phototransduction phototransduction, visible light cell proliferation response to light stimulus response to light intensity membrane rhodopsin mediated signaling pathway apical plasma membrane guanyl nucleotide binding GDP binding protein kinase binding regulation of rhodopsin mediated signaling pathway G-protein beta/gamma-subunit complex binding photoreceptor connecting cilium eye photoreceptor cell development photoreceptor outer segment membrane cell projection neuronal cell body metal ion binding response to stimulus detection of light stimulus involved in visual perception sensory perception of umami taste positive regulation of cyclic-nucleotide phosphodiesterase activity negative regulation of cyclic-nucleotide phosphodiesterase activity retina development in camera-type eye cellular response to electrical stimulus photoreceptor disc membrane uc003cym.1 uc003cym.2 uc003cym.3 uc003cym.4 
ENST00000232496.5 TUSC2 ENST00000232496.5 tumor suppressor 2, mitochondrial calcium regulator (from RefSeq NM_007275.3) B2R4Y9 C3orf11 ENST00000232496.1 ENST00000232496.2 ENST00000232496.3 ENST00000232496.4 FUS1 LGCC NM_007275 O75896 PDAP2 TUSC2_HUMAN uc003czy.1 uc003czy.2 uc003czy.3 This gene is a highly conserved lung cancer candidate gene. No other information about this gene is currently available. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163658.125991.1, AF055479.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2150385, SAMEA2467148 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: inferred from homology RefSeq Select criteria :: based on single protein-coding transcript regulatory uORF :: PMID: 21645495 ##RefSeq-Attributes-END## May function as a tumor suppressor, inhibiting colony formation, causing G1 arrest and ultimately inducing apoptosis in homozygous 3p21.3 120-kb region-deficient cells. O75896; Q5TD97: FHL5; NbExp=3; IntAct=EBI-1052725, EBI-750641; O75896; Q99750: MDFI; NbExp=7; IntAct=EBI-1052725, EBI-724076; O75896; Q93062: RBPMS; NbExp=4; IntAct=EBI-1052725, EBI-740322; Strong expression in heart, lung, skeletal muscle, kidney, and pancreas, followed by brain and liver, lowest levels in placenta. Myristoylation is required for tumor suppressor activity. Belongs to the TUSC2 family. natural killer cell differentiation protein binding mitochondrion phagocytosis inflammatory response cell cycle interleukin-15 production negative regulation of interleukin-17 production positive regulation of interleukin-10 production cell maturation defense response to Gram-negative bacterium regulation of mitochondrial membrane potential response to defense-related host reactive oxygen species production neutrophil mediated killing of gram-negative bacterium chemokine (C-C motif) ligand 5 production regulation of reactive oxygen species metabolic process uc003czy.1 uc003czy.2 uc003czy.3 
ENST00000232501.8 NPRL2 ENST00000232501.8 NPR2 like, GATOR1 complex subunit (from RefSeq NM_006545.5) A8K831 ENST00000232501.1 ENST00000232501.2 ENST00000232501.3 ENST00000232501.4 ENST00000232501.5 ENST00000232501.6 ENST00000232501.7 NM_006545 NPRL2 NPRL2_HUMAN Q6FGS2 Q8WTW4 Q9Y249 Q9Y497 TUSC4 uc003daj.1 uc003daj.2 uc003daj.3 Catalytic component of the GATOR1 complex, a multiprotein complex that functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:29590090, PubMed:35338845). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (PubMed:23723238, PubMed:29590090, PubMed:35338845). In the presence of abundant amino acids, the GATOR1 complex is ubiquitinated and inhibited by GATOR2 (PubMed:23723238, PubMed:36528027). Within the GATOR1 complex, NPRL2 constitutes the catalytic subunit that mediates the GAP activity (PubMed:30651352, PubMed:35338845). Suppresses Src-dependent tyrosine phosphorylation and activation of PDPK1 and its downstream signaling (PubMed:18616680). Down-regulates PDPK1 kinase activity by interfering with tyrosine phosphorylation at 'Tyr-9', 'Tyr-373' and 'Tyr-376' residues (PubMed:18616680). May act as a tumor suppressor (PubMed:18616680). Suppresses cell growth and enhances sensitivity to various anticancer drugs (PubMed:18616680). Within the GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5, NPRL2 and NPRL3 (PubMed:19521502, PubMed:23723238, PubMed:29590090, PubMed:35338845). GATOR1 mediates the strong interaction of the GATOR complex with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) heterodimers (PubMed:23723238, PubMed:29590090). GATOR1 interacts with GPR155/LYCHOS; interaction takes place in presence of cholesterol and prevents interaction between GATOR1 and KICSTOR (PubMed:36007018). Interacts with PDPK1 (PubMed:18616680). Q8WTW4; Q12980: NPRL3; NbExp=6; IntAct=EBI-1043552, EBI-2650314; Lysosome membrane Note=Localization to lysosomes is mediated by the KICSTOR complex and is amino acid-independent. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8WTW4-1; Sequence=Displayed; Name=2; IsoId=Q8WTW4-2; Sequence=VSP_010329, VSP_010330, VSP_010331; Most abundant in skeletal muscle, followed by brain, liver and pancreas, with lower amounts in lung, kidney, placenta and heart. Expressed in the frontal lobe cortex as well as in the temporal, parietal, and occipital lobes (PubMed:27173016, PubMed:26505888). Expressed in most lung cancer cell lines tested. The arginine finger is critical for the GTPase-activating mechanism. In the presence of abundant amino acids, ubiquitinated at Lys-158 and Lys-357 via 'Lys-6'-linked ubiquitination by the WDR24 component of the GATOR2 complex, thereby inhibiting the GATOR1 complex and promoting mTORC1 activation. Note=Inactivating mutations and truncating deletions in the genes encoding GATOR1 proteins, including NPRL2, are detected in glioblastoma and ovarian tumors and are associated with loss of heterozygosity events. Inactivation of GATOR1 proteins promotes constitutive localization of mTORC1 to the lysosomal membrane and blocks mTORC1 inactivation following amino acid withdrawal (PubMed:23723238). Epilepsy, familial focal, with variable foci 2 (FFEVF2) [MIM:617116]: An autosomal dominant form of epilepsy characterized by focal seizures arising from different cortical regions, including the temporal, frontal, parietal, and occipital lobes. Seizure types commonly include temporal lobe epilepsy, frontal lobe epilepsy, and nocturnal frontal lobe epilepsy. Some patients may have intellectual disability or autism spectrum disorders. Seizure onset usually occurs in the first or second decades, although later onset has been reported, and there is phenotypic variability within families. A subset of patients have structural brain abnormalities. Penetrance of the disorder is incomplete. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the NPR2 family. protein kinase activity GTPase activator activity protein binding lysosome lysosomal membrane protein phosphorylation cellular response to nitrogen starvation positive regulation of autophagy membrane negative regulation of TOR signaling negative regulation of kinase activity cellular response to amino acid starvation positive regulation of GTPase activity Iml1 complex regulation of autophagosome assembly uc003daj.1 uc003daj.2 uc003daj.3 
ENST00000232564.8 GNB4 ENST00000232564.8 G protein subunit beta 4 (from RefSeq NM_021629.4) B3KMH5 D3DNR8 ENST00000232564.1 ENST00000232564.2 ENST00000232564.3 ENST00000232564.4 ENST00000232564.5 ENST00000232564.6 ENST00000232564.7 GBB4_HUMAN NM_021629 Q9HAV0 uc003fjv.1 uc003fjv.2 uc003fjv.3 uc003fjv.4 uc003fjv.5 uc003fjv.6 Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.177602.1, SRR1803614.226704.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232564.8/ ENSP00000232564.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. G proteins are composed of 3 units, alpha, beta and gamma. Q9HAV0; P55212: CASP6; NbExp=3; IntAct=EBI-358539, EBI-718729; Q9HAV0; P13473-2: LAMP2; NbExp=3; IntAct=EBI-358539, EBI-21591415; Q9HAV0; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-358539, EBI-2623095; Strongly expressed in lung and placenta, whereas it is weakly expressed in brain and heart. Abundantly expressed in the axons and Schwann cells of peripheral nerves. Charcot-Marie-Tooth disease, dominant intermediate F (CMTDIF) [MIM:615185]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. CMTDIF is characterized by onset around adolescence of slowly progressive distal muscle atrophy and weakness affecting the upper and lower limbs and resulting in steppage gait. There is distal sensory impairment with decreased reflexes. Nerve conduction velocities are variable, ranging from the demyelinating to the axonal range. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the WD repeat G protein beta family. lysosomal membrane cytosol protein folding signal transduction substantia nigra development macromolecular complex binding extracellular exosome uc003fjv.1 uc003fjv.2 uc003fjv.3 uc003fjv.4 uc003fjv.5 uc003fjv.6 
ENST00000232603.10 MORC1 ENST00000232603.10 MORC family CW-type zinc finger 1 (from RefSeq NM_014429.4) B4DYX1 E7ERX1 ENST00000232603.1 ENST00000232603.2 ENST00000232603.3 ENST00000232603.4 ENST00000232603.5 ENST00000232603.6 ENST00000232603.7 ENST00000232603.8 ENST00000232603.9 MORC MORC1 MORC1_HUMAN NM_014429 Q7L8E2 Q86VD1 Q9NSG7 Q9Y6D4 uc003dxl.1 uc003dxl.2 uc003dxl.3 uc003dxl.4 uc003dxl.5 This gene encodes the human homolog of mouse morc and like the mouse protein it is testis-specific. Mouse studies support a testis-specific function since only male knockout mice are infertile; infertility is the only apparent defect. These studies further support a role for this protein early in spermatogenesis, possibly by affecting entry into apoptosis because testis from knockout mice show greatly increased numbers of apoptotic cells. [provided by RefSeq, Jan 2009]. ##Evidence-Data-START## Transcript exon combination :: BC050307.1, AF084946.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1968968 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232603.10/ ENSP00000232603.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Required for spermatogenesis (By similarity). Essential for de novo DNA methylation and silencing of transposable elements in the male embryonic germ cells (By similarity). Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q86VD1-1; Sequence=Displayed; Name=2; IsoId=Q86VD1-2; Sequence=VSP_055495; behavioral fear response male germ cell nucleus nucleus multicellular organism development spermatogenesis zinc ion binding negative regulation of transposition negative regulation of gene expression cell differentiation regulation of gene expression, epigenetic DNA methylation involved in gamete generation DNA hypermethylation metal ion binding negative regulation of DNA-templated transcription, initiation uc003dxl.1 uc003dxl.2 uc003dxl.3 uc003dxl.4 uc003dxl.5 
ENST00000232607.7 UMPS ENST00000232607.7 uridine monophosphate synthetase, transcript variant 2 (from RefSeq NR_033434.2) B5LY68 B5LY72 ENST00000232607.1 ENST00000232607.2 ENST00000232607.3 ENST00000232607.4 ENST00000232607.5 ENST00000232607.6 NR_033434 O00758 O00759 O00760 OK/SW-cl.21 P11172 Q16862 Q9H3Q2 Q9UG49 UMPS UMPS_HUMAN uc003ehl.1 uc003ehl.2 uc003ehl.3 uc003ehl.4 uc003ehl.5 uc003ehl.6 This gene encodes a uridine 5'-monophosphate synthase. The encoded protein is a bifunctional enzyme that catalyzes the final two steps of the de novo pyrimidine biosynthetic pathway. The first reaction is carried out by the N-terminal enzyme orotate phosphoribosyltransferase which converts orotic acid to orotidine-5'-monophosphate. The terminal reaction is carried out by the C-terminal enzyme OMP decarboxylase which converts orotidine-5'-monophosphate to uridine monophosphate. Defects in this gene are the cause of hereditary orotic aciduria. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Mar 2010]. Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP). Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D- ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10382; Evidence=; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11597; Evidence=; Kinetic parameters: KM=16.6 uM for orotidine 5'-phosphate ; Note=kcat is 0.75 sec(-1) with orotidine 5'-phosphate as substrate. ; Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. Homodimer; dimerization is required for enzymatic activity. P11172-1; P11172-1: UMPS; NbExp=2; IntAct=EBI-15679357, EBI-15679357; Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=P11172-1; Sequence=Displayed; Name=2; IsoId=P11172-2; Sequence=VSP_009273; Name=3; IsoId=P11172-3; Sequence=VSP_047611; Name=4; IsoId=P11172-4; Sequence=VSP_009273, VSP_047612; Orotic aciduria 1 (ORAC1) [MIM:258900]: A disorder of pyrimidine metabolism resulting in megaloblastic anemia and orotic acid crystalluria that is frequently associated with some degree of physical and intellectual disability. A minority of cases have additional features, particularly congenital malformations and immune deficiencies. Note=The disease is caused by variants affecting the gene represented in this entry. In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. In the C-terminal section; belongs to the OMP decarboxylase family. Sequence=CAB45710.3; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/umps/"; catalytic activity orotate phosphoribosyltransferase activity orotidine-5'-phosphate decarboxylase activity nucleus cytoplasm cytosol 'de novo' pyrimidine nucleobase biosynthetic process pyrimidine nucleotide biosynthetic process UMP biosynthetic process female pregnancy lactation metabolic process nucleoside metabolic process transferase activity transferase activity, transferring glycosyl groups lyase activity carboxy-lyase activity pyrimidine nucleobase biosynthetic process cellular response to drug identical protein binding 'de novo' UMP biosynthetic process pyrimidine nucleoside biosynthetic process uc003ehl.1 uc003ehl.2 uc003ehl.3 uc003ehl.4 uc003ehl.5 uc003ehl.6 
ENST00000232744.13 ABTB1 ENST00000232744.13 ankyrin repeat and BTB domain containing 1, transcript variant 2 (from RefSeq NM_172027.3) ABTB1 ABTB1_HUMAN BPOZ D3DNB0 ENST00000232744.1 ENST00000232744.10 ENST00000232744.11 ENST00000232744.12 ENST00000232744.2 ENST00000232744.3 ENST00000232744.4 ENST00000232744.5 ENST00000232744.6 ENST00000232744.7 ENST00000232744.8 ENST00000232744.9 NM_172027 PP2259 Q6ZNU9 Q71MF1 Q969K4 Q96S62 Q96S63 uc003ejt.1 uc003ejt.2 uc003ejt.3 uc003ejt.4 uc003ejt.5 This gene encodes a protein with an ankyrin repeat region and two BTB/POZ domains, which are thought to be involved in protein-protein interactions. Expression of this gene is activated by the phosphatase and tensin homolog, a tumor suppressor. Alternate splicing results in three transcript variants. [provided by RefSeq, Mar 2010]. May act as a mediator of the PTEN growth-suppressive signaling pathway. May play a role in developmental processes. Q969K4; P54253: ATXN1; NbExp=3; IntAct=EBI-7223971, EBI-930964; Q969K4; Q13618: CUL3; NbExp=5; IntAct=EBI-7223971, EBI-456129; Q969K4; Q05639: EEF1A2; NbExp=9; IntAct=EBI-7223971, EBI-354943; Q969K4; P29692-2: EEF1D; NbExp=4; IntAct=EBI-7223971, EBI-5280572; Q969K4; Q13148: TARDBP; NbExp=3; IntAct=EBI-7223971, EBI-372899; Cytoplasm Event=Alternative splicing; Named isoforms=4; Name=2 ; Synonyms=BPOZ-2 ; IsoId=Q969K4-1; Sequence=Displayed; Name=1 ; Synonyms=BPOZ-1 ; IsoId=Q969K4-2; Sequence=VSP_052148; Name=3 ; Synonyms=BPOZ-3 ; IsoId=Q969K4-3; Sequence=VSP_052149; Name=4 ; IsoId=Q969K4-4; Sequence=VSP_052150, VSP_052151, VSP_052152, VSP_052153; Ubiquitously expressed in all fetal tissues examined including heart, brain, liver, and kidney. Also expressed at lower levels in both adult heart and hypertrophic heart. Sequence=AAQ04661.1; Type=Frameshift; Evidence=; ubiquitin ligase complex translation elongation factor activity protein binding nucleolus cytoplasm cytosol plasma membrane translation translational elongation uc003ejt.1 uc003ejt.2 uc003ejt.3 uc003ejt.4 uc003ejt.5 
ENST00000232766.6 KLHL18 ENST00000232766.6 kelch like family member 18 (from RefSeq NM_025010.5) A8K612 ENST00000232766.1 ENST00000232766.2 ENST00000232766.3 ENST00000232766.4 ENST00000232766.5 KIAA0795 KLH18_HUMAN NM_025010 O94889 OK/SW-cl.74 Q7Z3E8 Q8N125 uc003crd.1 uc003crd.2 uc003crd.3 uc003crd.4 uc003crd.5 Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis (PubMed:23213400). The BCR(KLHL18) E3 ubiquitin ligase complex mediates the ubiquitination of AURKA leading to its activation at the centrosome which is required for initiating mitotic entry (PubMed:23213400). Regulates light-and dark-dependent alpha-transducin localization changes in rod photoreceptors through UNC119 ubiquitination and degradation (By similarity). Preferentially ubiquitinates the unphosphorylated form of UNC119 over the phosphorylated form (By similarity). In the presence of UNC119, under dark-adapted conditions alpha-transducin mislocalizes from the outer segment to the inner part of rod photoreceptors which leads to decreased photoreceptor damage caused by light (By similarity). Protein modification; protein ubiquitination. Interacts with AURKA (PubMed:23213400). Interacts (via BTB domain) with CUL3 (PubMed:23213400). Interacts (via kelch repeats) with UNC119 (PubMed:31696965). O94889; P13569: CFTR; NbExp=3; IntAct=EBI-2510096, EBI-349854; O94889; P26641-2: EEF1G; NbExp=3; IntAct=EBI-2510096, EBI-10177695; O94889; O60260-5: PRKN; NbExp=3; IntAct=EBI-2510096, EBI-21251460; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O94889-1; Sequence=Displayed; Name=2; IsoId=O94889-2; Sequence=VSP_035974; Sequence=AAH32620.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=CAD97920.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; protein binding protein ubiquitination positive regulation of mitotic cell cycle phase transition uc003crd.1 uc003crd.2 uc003crd.3 uc003crd.4 uc003crd.5 
ENST00000232854.9 HEMK1 ENST00000232854.9 HemK methyltransferase family member 1, transcript variant 1 (from RefSeq NM_016173.5) ENST00000232854.1 ENST00000232854.2 ENST00000232854.3 ENST00000232854.4 ENST00000232854.5 ENST00000232854.6 ENST00000232854.7 ENST00000232854.8 HEMK HEMK1_HUMAN NM_016173 Q9Y5R4 uc003dav.1 uc003dav.2 uc003dav.3 uc003dav.4 uc003dav.5 N5-glutamine methyltransferase responsible for the methylation of the glutamine residue in the universally conserved GGQ motif of the mitochondrial translation release factors MTRF1, MTRF1L, MRPL58/ICT1 and MTRFR. Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L- methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA- COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; EC=2.1.1.297; Evidence=; Q9Y5R4; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-10329202, EBI-357530; Q9Y5R4; Q9NQ33: ASCL3; NbExp=3; IntAct=EBI-10329202, EBI-12108222; Q9Y5R4; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10329202, EBI-396137; Q9Y5R4; P15882: CHN1; NbExp=8; IntAct=EBI-10329202, EBI-718947; Q9Y5R4; P78358: CTAG1B; NbExp=3; IntAct=EBI-10329202, EBI-1188472; Q9Y5R4; Q15038: DAZAP2; NbExp=3; IntAct=EBI-10329202, EBI-724310; Q9Y5R4; A2RTY3: HEATR9; NbExp=3; IntAct=EBI-10329202, EBI-13049042; Q9Y5R4; Q0VD86: INCA1; NbExp=5; IntAct=EBI-10329202, EBI-6509505; Q9Y5R4; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-10329202, EBI-12811111; Q9Y5R4; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-10329202, EBI-716006; Q9Y5R4; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-10329202, EBI-724639; Q9Y5R4; Q16633: POU2AF1; NbExp=3; IntAct=EBI-10329202, EBI-943588; Q9Y5R4; P28070: PSMB4; NbExp=3; IntAct=EBI-10329202, EBI-603350; Q9Y5R4; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-10329202, EBI-748621; Q9Y5R4; O15266-2: SHOX; NbExp=3; IntAct=EBI-10329202, EBI-12825957; Q9Y5R4; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-10329202, EBI-12288855; Q9Y5R4; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-10329202, EBI-11959123; Q9Y5R4; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-10329202, EBI-12408727; Q9Y5R4; Q96RT8: TUBGCP5; NbExp=3; IntAct=EBI-10329202, EBI-2555061; Q9Y5R4; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10329202, EBI-947187; Mitochondrion Belongs to the protein N5-glutamine methyltransferase family. nucleic acid binding DNA binding protein binding mitochondrion DNA methylation protein methylation methyltransferase activity N-methyltransferase activity protein methyltransferase activity transferase activity methylation uc003dav.1 uc003dav.2 uc003dav.3 uc003dav.4 uc003dav.5 
ENST00000232888.7 RRP9 ENST00000232888.7 ribosomal RNA processing 9, U3 small nucleolar RNA binding protein (from RefSeq NM_004704.5) B2R996 ENST00000232888.1 ENST00000232888.2 ENST00000232888.3 ENST00000232888.4 ENST00000232888.5 ENST00000232888.6 NM_004704 O43818 Q8IZ30 RNU3IP2 RRP9 U355K U3IP2_HUMAN uc003dbw.1 uc003dbw.2 uc003dbw.3 uc003dbw.4 This gene encodes a member of the WD-repeat protein family. The encoded protein is a component of the nucleolar small nuclear ribonucleoprotein particle (snoRNP) and is essential for 18s rRNA processing during ribosome synthesis. It contains seven WD domains required for nucleolar localization and specific interaction with the U3 small nucleolar RNA (U3 snoRNA). [provided by RefSeq, Oct 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.439055.1, BC009879.2 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232888.7/ ENSP00000232888.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA (pre-rRNA) (PubMed:26867678). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). Interacts specifically with the U3 small nucleolar RNA (U3 snoRNA) (PubMed:10982864, PubMed:12381732). Binds a sub-fragment of the U3 snoRNA surrounding the B/C motif (3UBC) (PubMed:10982864, PubMed:12381732). This association with the U3BC RNA is dependent on the binding of a protein called 15.5K to the box B/C motif (PubMed:10982864, PubMed:12381732). The association of the protein with the U3BC RNA was found to be also dependent on a conserved RNA structure that flanks the box B/C motif (PubMed:10982864, PubMed:12381732). Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Nucleus, nucleolus The WD domains are required for nucleolar localization and U3 small nucleolar RNAs binding. Acetylation at Lys-12 and Lys-25 by KAT2B/PCAF under stress impairs pre-rRNA processing (PubMed:26867678). Deacetylation by SIRT7 enhances RRP9-binding to U3 snoRNA, which is a prerequisite for pre- rRNA processing (PubMed:26867678). Belongs to the WD repeat RRP9 family. RNA binding nucleus nucleoplasm nucleolus rRNA processing box C/D snoRNP complex small-subunit processome U3 snoRNA binding uc003dbw.1 uc003dbw.2 uc003dbw.3 uc003dbw.4 
ENST00000232892.12 AADAC ENST00000232892.12 arylacetamide deacetylase (from RefSeq NM_001086.3) A8K3L3 AAAD_HUMAN D3DNJ6 DAC ENST00000232892.1 ENST00000232892.10 ENST00000232892.11 ENST00000232892.2 ENST00000232892.3 ENST00000232892.4 ENST00000232892.5 ENST00000232892.6 ENST00000232892.7 ENST00000232892.8 ENST00000232892.9 NM_001086 P22760 Q8N1A9 uc003eze.1 uc003eze.2 uc003eze.3 uc003eze.4 uc003eze.5 Microsomal arylacetamide deacetylase competes against the activity of cytosolic arylamine N-acetyltransferase, which catalyzes one of the initial biotransformation pathways for arylamine and heterocyclic amine carcinogens [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189664.80955.1, SRR5189664.54243.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142363, SAMEA2142586 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232892.12/ ENSP00000232892.6 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity. Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Kinetic parameters: KM=0.8 mM for flutamide KM=0.6 mM for flutamide KM=0.472 mM for flutamide KM=3.05 mM for phenacetin KM=1.8 mM for phenacetin KM=1.42 mM for phenacetin KM=0.2 mM for rifampicin KM=0.154 mM for rifampicin Vmax=1.1 nmol/min/mg enzyme toward flutamide Vmax=0.617 nmol/min/mg enzyme toward flutamide Vmax=1.34 nmol/min/mg enzyme toward phenacetin Vmax=6.4 nmol/min/mg enzyme toward phenacetin Vmax=1.42 nmol/min/mg enzyme toward phenacetin Vmax=0.149 nmol/min/mg enzyme toward rifampicin Vmax=0.060 nmol/min/mg enzyme toward rifampicin P22760; Q92624: APPBP2; NbExp=3; IntAct=EBI-13217105, EBI-743771; Endoplasmic reticulum membrane; Single-pass type II membrane protein. Microsome membrane; Single-pass type II membrane protein. Detected in liver (at protein level). Mainly expressed in liver, small intestine, colon, adrenal gland and bladder. Down-regulated following infection with hepatis C virus which results in impaired triacylglycerol lipolysis and impaired assembly of very low density lipoproteins. This may represent a cellular adaptation to infection that is aimed at limiting viral production. Glycosylation is required for enzyme activity. Three alleles are known: AADAC*1, AADAC*2 and AADAC*3. The sequence shown is that of AADAC*1 which is found in European American, African American, Japanese and Korean populations at allelic frequencies of 39.3 to 47.4%. The AADAC*2 allele is found in European American, African American, Korean, and Japanese populations at allelic frequencies of 52.6 to 63.5% whereas the AADAC*3 allele is found in European American (1.3%) and African American (2.0%) samples but not in Japanese or Korean samples. Can hydrolyze a number of clinical drugs such as flutamide, an antiandrogen drug used for the treatment of prostate cancer; phenacetin, an analgesic antipyretic which has been withdrawn from the market due to its links with renal failure; and rifamycins which have been used as antituberculosis drugs. Belongs to the 'GDXG' lipolytic enzyme family. Sequence=AAA35551.1; Type=Frameshift; Evidence=; catalytic activity triglyceride lipase activity endoplasmic reticulum endoplasmic reticulum membrane xenobiotic metabolic process catabolic process positive regulation of triglyceride catabolic process membrane integral component of membrane lipase activity hydrolase activity serine hydrolase activity deacetylase activity organelle membrane short-chain carboxylesterase activity intracellular membrane-bounded organelle carboxylic ester hydrolase activity uc003eze.1 uc003eze.2 uc003eze.3 uc003eze.4 uc003eze.5 
ENST00000232905.4 EIF1B ENST00000232905.4 eukaryotic translation initiation factor 1B (from RefSeq NM_005875.3) A0A024R2V6 EIF1B ENST00000232905.1 ENST00000232905.2 ENST00000232905.3 GC20 NM_005875 Q6FG85 Q6FG85_HUMAN hCG_16417 uc003ckc.1 uc003ckc.2 uc003ckc.3 uc003ckc.4 uc003ckc.5 uc003ckc.6 Belongs to the SUI1 family. translation initiation factor activity protein binding translational initiation uc003ckc.1 uc003ckc.2 uc003ckc.3 uc003ckc.4 uc003ckc.5 uc003ckc.6 
ENST00000232974.11 ZBTB47 ENST00000232974.11 zinc finger and BTB domain containing 47, transcript variant 2 (from RefSeq NM_145166.4) ENST00000232974.1 ENST00000232974.10 ENST00000232974.2 ENST00000232974.3 ENST00000232974.4 ENST00000232974.5 ENST00000232974.6 ENST00000232974.7 ENST00000232974.8 ENST00000232974.9 H7BXD3 KIAA1190 NM_145166 Q6ZSY6 Q8WTY8 Q9UFB7 Q9ULN0 ZBT47_HUMAN ZNF651 uc003clu.1 uc003clu.2 uc003clu.3 uc003clu.4 May be involved in transcriptional regulation. Q9UFB7; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-7781767, EBI-739624; Q9UFB7; Q92997: DVL3; NbExp=3; IntAct=EBI-7781767, EBI-739789; Q9UFB7; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-7781767, EBI-746704; Q9UFB7; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-7781767, EBI-10961706; Q9UFB7; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-7781767, EBI-11522433; Q9UFB7; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-7781767, EBI-10963850; Q9UFB7; Q9UL41: PNMA3; NbExp=3; IntAct=EBI-7781767, EBI-11278955; Q9UFB7; Q08117-2: TLE5; NbExp=5; IntAct=EBI-7781767, EBI-11741437; Q9UFB7; P17020: ZNF16; NbExp=3; IntAct=EBI-7781767, EBI-3921553; Q9UFB7; Q53GI3: ZNF394; NbExp=3; IntAct=EBI-7781767, EBI-10211248; Q9UFB7; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-7781767, EBI-527853; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UFB7-1; Sequence=Displayed; Name=2; IsoId=Q9UFB7-2; Sequence=VSP_054051; Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=AAH21855.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=CAB61386.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleic acid binding DNA binding nucleus cellular response to DNA damage stimulus metal ion binding uc003clu.1 uc003clu.2 uc003clu.3 uc003clu.4 
ENST00000232975.8 TNNC1 ENST00000232975.8 troponin C1, slow skeletal and cardiac type (from RefSeq NM_003280.3) A0A024R2Z4 ENST00000232975.1 ENST00000232975.2 ENST00000232975.3 ENST00000232975.4 ENST00000232975.5 ENST00000232975.6 ENST00000232975.7 NM_003280 Q6FH91 Q6FH91_HUMAN TNNC1 hCG_42573 uc003deb.1 uc003deb.2 uc003deb.3 uc003deb.4 uc003deb.5 Troponin is a central regulatory protein of striated muscle contraction, and together with tropomyosin, is located on the actin filament. Troponin consists of 3 subunits: TnI, which is the inhibitor of actomyosin ATPase; TnT, which contains the binding site for tropomyosin; and TnC, the protein encoded by this gene. The binding of calcium to TnC abolishes the inhibitory action of TnI, thus allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in this gene are associated with cardiomyopathy dilated type 1Z. [provided by RefSeq, Oct 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189655.140968.1, SRR5189655.222916.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2147920, SAMEA2151741 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000232975.8/ ENSP00000232975.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. Belongs to the troponin C family. diaphragm contraction calcium ion binding response to metal ion transition between fast and slow fiber regulation of muscle filament sliding speed contractile fiber regulation of ATPase activity actin filament binding cardiac muscle contraction uc003deb.1 uc003deb.2 uc003deb.3 uc003deb.4 uc003deb.5 
ENST00000232978.13 NKTR ENST00000232978.13 natural killer cell triggering receptor, transcript variant 1 (from RefSeq NM_005385.4) ENST00000232978.1 ENST00000232978.10 ENST00000232978.11 ENST00000232978.12 ENST00000232978.2 ENST00000232978.3 ENST00000232978.4 ENST00000232978.5 ENST00000232978.6 ENST00000232978.7 ENST00000232978.8 ENST00000232978.9 NKTR NKTR_HUMAN NM_005385 P30414 uc003clo.1 uc003clo.2 uc003clo.3 uc003clo.4 uc003clo.5 This gene encodes a membrane-anchored protein with a hydrophobic amino terminal domain and a cyclophilin-like PPIase domain. It is present on the surface of natural killer cells and facilitates their binding to targets. Its expression is regulated by IL2 activation of the cells. [provided by RefSeq, Jul 2008]. PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Component of a putative tumor-recognition complex involved in the function of NK cells (PubMed:8421688). Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence=; Inhibited by cyclosporin A (CsA). Cell membrane A report has suggested that the protein is expressed at the cell surface, associated with the cell membrane via its N-terminus. However, there is no direct evidence for that localization and the properties of the protein argue against it. protein peptidyl-prolyl isomerization peptidyl-prolyl cis-trans isomerase activity nucleoplasm mitochondrion cytosol plasma membrane protein folding cyclosporin A binding membrane isomerase activity protein refolding unfolded protein binding uc003clo.1 uc003clo.2 uc003clo.3 uc003clo.4 uc003clo.5 
ENST00000233027.10 NEK4 ENST00000233027.10 NIMA related kinase 4, transcript variant 1 (from RefSeq NM_003157.6) A5YM70 B2R633 B7Z200 ENST00000233027.1 ENST00000233027.2 ENST00000233027.3 ENST00000233027.4 ENST00000233027.5 ENST00000233027.6 ENST00000233027.7 ENST00000233027.8 ENST00000233027.9 NEK4_HUMAN NM_003157 P51957 Q6P576 STK2 uc003dfq.1 uc003dfq.2 uc003dfq.3 uc003dfq.4 uc003dfq.5 uc003dfq.6 The protein encoded by this gene is a serine/threonine protein kinase required for normal entry into replicative senescence. The encoded protein also is involved in cell cycle arrest in response to double-stranded DNA damage. Finally, this protein plays a role in maintaining cilium integrity, and defects in this gene have been associated with ciliopathies. [provided by RefSeq, Jan 2017]. Protein kinase that seems to act exclusively upon threonine residues (By similarity). Required for normal entry into proliferative arrest after a limited number of cell divisions, also called replicative senescence. Required for normal cell cycle arrest in response to double-stranded DNA damage. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Interacts with RPGRIP1 and RPGRIP1L. Cell projection, cilium Cytoplasm Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P51957-1; Sequence=Displayed; Name=2; IsoId=P51957-2; Sequence=VSP_037123, VSP_037124; Name=3; IsoId=P51957-3; Sequence=VSP_043334; Highest expression in adult heart, followed by pancreas, skeletal muscle, brain, testis, retina, liver, kidney, lung and placenta. Present in most primary carcinomas. Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily. nucleotide binding mitotic cell cycle protein kinase activity protein serine/threonine kinase activity ATP binding cytoplasm cytosol cilium protein phosphorylation cellular response to DNA damage stimulus cell cycle kinase activity phosphorylation transferase activity signal transduction by protein phosphorylation manganese ion binding activation of protein kinase activity ciliary rootlet ciliary transition zone ciliary basal body cell projection positive regulation of transcription, DNA-templated metal ion binding cell division ciliary plasm regulation of replicative cell aging regulation of cellular senescence regulation of response to DNA damage stimulus uc003dfq.1 uc003dfq.2 uc003dfq.3 uc003dfq.4 uc003dfq.5 uc003dfq.6 
ENST00000233047.9 LDAF1 ENST00000233047.9 lipid droplet assembly factor 1, transcript variant 4 (from RefSeq NM_001301771.2) A6NMA9 B4DEC1 ENST00000233047.1 ENST00000233047.2 ENST00000233047.3 ENST00000233047.4 ENST00000233047.5 ENST00000233047.6 ENST00000233047.7 ENST00000233047.8 LDAF1 LDAF1_HUMAN NM_001301771 O00323 Q96B96 TMEM159 uc002dih.1 uc002dih.2 uc002dih.3 uc002dih.4 uc002dih.5 uc002dih.6 Plays an important role in the formation of lipid droplets (LD) which are storage organelles at the center of lipid and energy homeostasis (PubMed:31708432). In association with BSCL2/seipin, defines the sites of LD formation in the endoplasmic reticulum (PubMed:31708432). Interacts with isoform 1 and isoform 3 of BSCL2/seipin to form an oligomeric complex. Q96B96; Q9UGQ2: CACFD1; NbExp=4; IntAct=EBI-7055862, EBI-8652492; Q96B96; Q8NI60: COQ8A; NbExp=8; IntAct=EBI-7055862, EBI-745535; Q96B96; Q05329: GAD2; NbExp=6; IntAct=EBI-7055862, EBI-9304251; Q96B96; A8MRB1: S100B; NbExp=3; IntAct=EBI-7055862, EBI-16432654; Q96B96; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-7055862, EBI-8652744; Q96B96; Q6P1K1: SLC48A1; NbExp=3; IntAct=EBI-7055862, EBI-1222191; Q96B96; Q17RD7: SYT16; NbExp=3; IntAct=EBI-7055862, EBI-10238936; Q96B96; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-7055862, EBI-741829; Endoplasmic reticulum membrane ; Multi-pass membrane protein Lipid droplet Note=Co- localizes with BSCL2/seipin in the ER, upon LD formation dissociates from BSCL2/seipin and relocalizes to LD surfaces during LD maturation. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96B96-1; Sequence=Displayed; Name=2; IsoId=Q96B96-2; Sequence=VSP_056078; Expressed at high levels in the heart and skeletal muscle. Expressed at low levels in kidney, small intestine, lung and liver. Belongs to the LDAF1 family. protein binding membrane integral component of membrane uc002dih.1 uc002dih.2 uc002dih.3 uc002dih.4 uc002dih.5 uc002dih.6 
ENST00000233055.9 WDFY1 ENST00000233055.9 WD repeat and FYVE domain containing 1 (from RefSeq NM_020830.5) ENST00000233055.1 ENST00000233055.2 ENST00000233055.3 ENST00000233055.4 ENST00000233055.5 ENST00000233055.6 ENST00000233055.7 ENST00000233055.8 FENS1 KIAA1435 NM_020830 Q53S17 Q8IWB7 Q9H9D5 Q9P2B3 WDF1 WDFY1_HUMAN ZFYVE17 uc002vnq.1 uc002vnq.2 uc002vnq.3 uc002vnq.4 uc002vnq.5 The protein encoded by this gene is a phosphatidylinositol 3-phosphate binding protein, which contains a FYVE zinc finger domain and multiple WD-40 repeat domains. When exogenously expressed, it localizes to early endosomes. Mutagenesis analysis demonstrates that this endosomal localization is mediated by the FYVE domain. [provided by RefSeq, Jan 2015]. ##Evidence-Data-START## Transcript exon combination :: BC065934.1, SRR1660807.218551.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233055.9/ ENSP00000233055.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Positively regulates TLR3- and TLR4-mediated signaling pathways by bridging the interaction between TLR3 or TLR4 and TICAM1. Promotes TLR3/4 ligand-induced activation of transcription factors IRF3 and NF-kappa-B, as well as the production of IFN-beta and inflammatory cytokines (PubMed:25736436). Binds PtdIns3P in vitro with high specificity over other phosphoinositides. Interacts (via WD repeat 2) with tyrosine- phosphorylated TLR3 (via TIR domain) in response to poly(I:C) (PubMed:25736436). Interacts with TICAM1 in response to poly(I:C) (By similarity). Interacts with TLR4 in response to LPS (By similarity). Early endosome The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched membranes is substantially increased in acidic conditions. The FYVE domain is required for its function in regulating TLR3 signaling (PubMed:25736436). Sequence=BAA92673.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; protein binding 1-phosphatidylinositol binding nucleus endosome early endosome cytosol zinc ion binding positive regulation of toll-like receptor 3 signaling pathway positive regulation of toll-like receptor 4 signaling pathway metal ion binding uc002vnq.1 uc002vnq.2 uc002vnq.3 uc002vnq.4 uc002vnq.5 
ENST00000233057.9 EIF2AK2 ENST00000233057.9 eukaryotic translation initiation factor 2 alpha kinase 2, transcript variant 1 (from RefSeq NM_002759.4) A8K3P0 D6W584 E2AK2_HUMAN E9PC80 ENST00000233057.1 ENST00000233057.2 ENST00000233057.3 ENST00000233057.4 ENST00000233057.5 ENST00000233057.6 ENST00000233057.7 ENST00000233057.8 NM_002759 P19525 PKR PRKR Q52M43 Q7Z6F6 Q9UIR4 uc010fac.1 uc010fac.2 uc010fac.3 uc010fac.4 uc010fac.5 The protein encoded by this gene is a serine/threonine protein kinase that is activated by autophosphorylation after binding to dsRNA. The activated form of the encoded protein can phosphorylate translation initiation factor EIF2S1, which in turn inhibits protein synthesis. This protein is also activated by manganese ions and heparin. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Oct 2011]. IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19507191, PubMed:19189853, PubMed:21123651, PubMed:21072047, PubMed:22948139, PubMed:23229543, PubMed:22381929). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2- alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:20171114, PubMed:19840259, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:22214662, PubMed:19229320). In addition to serine/threonine- protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Initially produced in an inactive form and is activated by binding to viral dsRNA, which causes dimerization and autophosphorylation in the activation loop and stimulation of function. ISGylation can activate it in the absence of viral infection. Can also be activated by heparin, pro-inflammatory stimuli, growth factors, cytokines, oxidative stress and the cellular protein PRKRA. Activity is markedly stimulated by manganese ions. Activation is blocked by the viral components HIV-1 Tat protein and large amounts of HIV-1 trans- activation response (TAR) RNA element as well as by the cellular proteins TARBP2, DUS2L, NPM1, NCK1 and ADAR. Down-regulated by Toscana virus (TOS) and Rift valley fever virus (RVFV) NSS which promote its proteasomal degradation. Inhibited by vaccinia virus protein E3, probably via dsRNA sequestering. Homodimer (PubMed:16179258, PubMed:31246429). Interacts with STRBP (By similarity). Interacts with DNAJC3. Forms a complex with FANCA, FANCC, FANCG and HSP70. Interacts with ADAR/ADAR1. Interacts with IRS1 (By similarity). The inactive form interacts with NCK1 and GSN. Interacts (via the kinase catalytic domain) with STAT3 (via SH2 domain), TRAF2 (C-terminus), TRAF5 (C-terminus) and TRAF6 (C-terminus). Interacts with MAP2K6, IKBKB/IKKB, NPM1, TARBP2, NLRP1, NLRP3, NLRC4 and AIM2. Interacts (via DRBM 1 domain) with DUS2L (via DRBM domain). Interacts with DHX9 (via N-terminus) and this interaction is dependent upon activation of the kinase. Interacts with EIF2S1/EIF-2ALPHA; this interaction induces a conformational change in EIF2S1 and its phosphorylation by EIF2AK2 (PubMed:16179258). (Microbial infection) Interacts with human cytomegalovirus (HCMV) TRS1; this interaction retains EIF2AK2 to the nucleus and prevents its activation. (Microbial infection) Interacts with vaccinia virus protein K3 (K3L); this interaction inhibits EIF2AK2. (Microbial infection) Interacts with human herpes simplex virus 1 (HHV-1) protein US11 in an RNA-dependent manner. (Microbial infection) The inactive form interacts with Toscana virus (TOS) NSS. (Microbial infection) Interacts with herpes virus 8 protein v- IRF2; this interaction inhibits EIF2AK2 activation. (Microbial infection) Interacts with vaccinia protein E3. (Microbial infection) Interacts (via N-terminus) with Hepatitis C virus (HCV) mature core protein (via N-terminus); this interaction induces the autophosphorylation of EIF2AK2. (Microbial infection) Interacts with Hepatitis C virus (HCV) non-structural protein 5A (NS5A); this interaction leads to disruption of EIF2AK2 dimerization by NS5A. (Microbial infection) Interacts with Hepatitis C virus (HCV) envelope glycoprotein E2; this interaction inhibits EIF2AK2 and blocks its inhibitory effect on protein synthesis and cell growth. (Microbial infection) Interacts with human respiratory syncytial virus (HRSV) nucleoprotein; this interaction inhibits EIF2AK2 phosphorylation of EIF2S1 and blocks EIF2AK2-mediated translation shutoff. P19525; P78563-4: ADARB1; NbExp=3; IntAct=EBI-640775, EBI-12002366; P19525; P06493: CDK1; NbExp=4; IntAct=EBI-640775, EBI-444308; P19525; Q7L2E3: DHX30; NbExp=4; IntAct=EBI-640775, EBI-1211456; P19525; Q96C10: DHX58; NbExp=2; IntAct=EBI-640775, EBI-744193; P19525; Q08211: DHX9; NbExp=2; IntAct=EBI-640775, EBI-352022; P19525; Q9UPY3: DICER1; NbExp=2; IntAct=EBI-640775, EBI-395506; P19525; Q6P2E9: EDC4; NbExp=2; IntAct=EBI-640775, EBI-1006038; P19525; P19525: EIF2AK2; NbExp=2; IntAct=EBI-640775, EBI-640775; P19525; P05198: EIF2S1; NbExp=5; IntAct=EBI-640775, EBI-1056162; P19525; P56537: EIF6; NbExp=2; IntAct=EBI-640775, EBI-372243; P19525; Q8IY81: FTSJ3; NbExp=3; IntAct=EBI-640775, EBI-744088; P19525; Q9HCE1: MOV10; NbExp=3; IntAct=EBI-640775, EBI-1055820; P19525; Q96P20: NLRP3; NbExp=6; IntAct=EBI-640775, EBI-6253230; P19525; P06748: NPM1; NbExp=3; IntAct=EBI-640775, EBI-78579; P19525; O75569: PRKRA; NbExp=6; IntAct=EBI-640775, EBI-713955; P19525; O75569-1: PRKRA; NbExp=3; IntAct=EBI-640775, EBI-15588172; P19525; Q9NUL3: STAU2; NbExp=3; IntAct=EBI-640775, EBI-722938; P19525; Q15633: TARBP2; NbExp=2; IntAct=EBI-640775, EBI-978581; P19525; Q9H0E2: TOLLIP; NbExp=2; IntAct=EBI-640775, EBI-74615; P19525; Q9UL40: ZNF346; NbExp=3; IntAct=EBI-640775, EBI-2462313; P19525; Q27968: DNAJC3; Xeno; NbExp=5; IntAct=EBI-640775, EBI-640793; P19525; P0DTC9: N; Xeno; NbExp=8; IntAct=EBI-640775, EBI-25475856; P19525; P20639: OPG041; Xeno; NbExp=3; IntAct=EBI-640775, EBI-8674942; P19525; P04487: US11; Xeno; NbExp=3; IntAct=EBI-640775, EBI-6150681; P19525; Q2HR71: vIRF-2; Xeno; NbExp=2; IntAct=EBI-640775, EBI-8876177; P19525; PRO_0000278746 [O92972]; Xeno; NbExp=2; IntAct=EBI-640775, EBI-6918883; P19525; PRO_0000037570 [P27958]; Xeno; NbExp=4; IntAct=EBI-640775, EBI-6904269; P19525; PRO_0000037576 [P27958]; Xeno; NbExp=5; IntAct=EBI-640775, EBI-8753518; Cytoplasm cleus Cytoplasm, perinuclear region Note=Nuclear localization is elevated in acute leukemia, myelodysplastic syndrome (MDS), melanoma, breast, colon, prostate and lung cancer patient samples or cell lines as well as neurocytes from advanced Creutzfeldt- Jakob disease patients. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P19525-1; Sequence=Displayed; Name=2; IsoId=P19525-2; Sequence=VSP_046177; Highly expressed in thymus, spleen and bone marrow compared to non-hematopoietic tissues such as small intestine, liver, or kidney tissues. Colocalizes with GSK3B and TAU in the Alzheimer disease (AD) brain. Elevated levels seen in breast and colon carcinomas, and which correlates with tumor progression and invasiveness or risk of progression. By type I interferons. Contains 2 dsRNA-binding domain (DRBM) (PubMed:9736623). The N- terminus contains the catalytic domain dimerization. The C-terminus binds EIF2S1/EIF2-alpha (PubMed:16179258). Autophosphorylated on several Ser, Thr and Tyr residues. Autophosphorylation of Thr-451 is dependent on Thr-446 and is stimulated by dsRNA binding and dimerization. Autophosphorylation apparently leads to the activation of the kinase. Tyrosine autophosphorylation is essential for efficient dsRNA-binding, dimerization, and kinase activation. Leukoencephalopathy, developmental delay, and episodic neurologic regression syndrome (LEUDEN) [MIM:618877]: An autosomal dominant disorder characterized by global developmental delay apparent in early childhood, cognitive impairment, ataxia, poor or absent speech with dysarthria, hypotonia, hypertonia, extrapyramidal signs, tremor, and abnormal involuntary movements. Affected individuals also exhibit neurological regression in the setting of febrile illness or infection. Many patients have seizures. Brain imaging shows diffuse white matter abnormalities with poor myelination. Note=The disease may be caused by variants affecting the gene represented in this entry. Dystonia 33 (DYT33) [MIM:619687]: A form of dystonia, a disorder defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT33 is a slowly progressive form characterized by onset of focal or generalized dystonia in the first decades of life. Disease manifestations are variable. Some patients show ambulation difficulties, dysarthria, or dysphagia. Some affected individuals may manifest motor delay, lower limb spasticity, and mild developmental delay with intellectual disability. DYT33 penetrance is incomplete. Inheritance can be autosomal dominant or recessive. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/prkr/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41866/EIF2AK2"; nucleotide binding activation of MAPKK activity positive regulation of cytokine production immune system process RNA binding double-stranded RNA binding protein kinase activity protein serine/threonine kinase activity eukaryotic translation initiation factor 2alpha kinase activity protein tyrosine kinase activity non-membrane spanning protein tyrosine kinase activity protein binding ATP binding nucleus cytoplasm cytosol ribosome translation protein phosphorylation negative regulation of cell proliferation response to virus regulation of translational initiation by eIF2 alpha phosphorylation membrane viral process kinase activity phosphorylation transferase activity negative regulation of translation peptidyl-tyrosine phosphorylation protein phosphatase regulator activity evasion or tolerance by virus of host immune response endoplasmic reticulum unfolded protein response positive regulation of chemokine production positive regulation of stress-activated MAPK cascade negative regulation of osteoblast proliferation cellular response to amino acid starvation response to interferon-alpha identical protein binding negative regulation of apoptotic process regulation of phosphoprotein phosphatase activity negative regulation of viral genome replication innate immune response protein autophosphorylation perinuclear region of cytoplasm positive regulation of NF-kappaB transcription factor activity defense response to virus regulation of NLRP3 inflammasome complex assembly positive regulation of NIK/NF-kappaB signaling regulation of hematopoietic progenitor cell differentiation regulation of hematopoietic stem cell proliferation regulation of hematopoietic stem cell differentiation uc010fac.1 uc010fac.2 uc010fac.3 uc010fac.4 uc010fac.5 
ENST00000233072.10 CPS1 ENST00000233072.10 carbamoyl-phosphate synthase 1, transcript variant 6 (from RefSeq NR_161225.1) B7Z818 CPSM_HUMAN ENST00000233072.1 ENST00000233072.2 ENST00000233072.3 ENST00000233072.4 ENST00000233072.5 ENST00000233072.6 ENST00000233072.7 ENST00000233072.8 ENST00000233072.9 J3KQL0 NR_161225 O43774 P31327 Q53TL5 Q59HF8 Q7Z5I5 uc002vee.1 uc002vee.2 uc002vee.3 uc002vee.4 uc002vee.5 uc002vee.6 The mitochondrial enzyme encoded by this gene catalyzes synthesis of carbamoyl phosphate from ammonia and bicarbonate. This reaction is the first committed step of the urea cycle, which is important in the removal of excess urea from cells. The encoded protein may also represent a core mitochondrial nucleoid protein. Three transcript variants encoding different isoforms have been found for this gene. The shortest isoform may not be localized to the mitochondrion. Mutations in this gene have been associated with carbamoyl phosphate synthetase deficiency, susceptibility to persistent pulmonary hypertension, and susceptibility to venoocclusive disease after bone marrow transplantation.[provided by RefSeq, May 2010]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta ##RefSeq-Attributes-END## Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence=; Requires N-acetyl-L-glutamate (NAG) as an allosteric activator. Activated by glycerol in the absence of NAG, whereas in the presence of NAG it is inhibited by increasing concentrations of glycerol. Kinetic parameters: KM=0.47 mM for ATP ; KM=4.0 mM for HCO(3)(-) ; KM=1.00 mM for NH(4)(+) ; Vmax=1.22 umol/min/mg enzyme for ATP ; Vmax=1.23 umol/min/mg enzyme for HCO(3)(-) ; Vmax=1.19 umol/min/mg enzyme for NH(4)(+) ; Can form homooligomers (monomers as predominant form and dimers). P31327; P10398: ARAF; NbExp=3; IntAct=EBI-536811, EBI-365961; P31327; P04049: RAF1; NbExp=4; IntAct=EBI-536811, EBI-365996; P31327; P63104: YWHAZ; NbExp=2; IntAct=EBI-536811, EBI-347088; Mitochondrion Nucleus, nucleolus Cell membrane ; Peripheral membrane protein ; Extracellular side Note=Localizes to the cell surface of hepatocytes. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P31327-1; Sequence=Displayed; Name=2; IsoId=P31327-2; Sequence=VSP_009332; Name=3; IsoId=P31327-3; Sequence=VSP_046685; Primarily in the liver and small intestine. The type-1 glutamine amidotransferase domain is defective. Undergoes proteolytic cleavage in the C-terminal region corresponding to the loss of approximately 12 AA residues from the C- terminus. Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation (By similarity). Glutarylated. Glutarylation levels increase during fasting. Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892, Lys-915, Lys-1360 and Lys-1486, leading to activation. Carbamoyl phosphate synthetase 1 deficiency (CPS1D) [MIM:237300]: An autosomal recessive disorder of the urea cycle causing hyperammonemia. It can present as a devastating metabolic disease dominated by severe hyperammonemia in neonates or as a more insidious late-onset condition, generally manifesting as life-threatening hyperammonemic crises under catabolic situations. Clinical features include protein intolerance, intermittent ataxia, seizures, lethargy, developmental delay and intellectual disability. te=The disease is caused by variants affecting the gene represented in this entry. Pulmonary hypertension, neonatal (PHN) [MIM:615371]: A disease characterized by elevated pulmonary artery pressure. Pulmonary hypertension in the neonate is associated with multiple underlying problems such as respiratory distress syndrome, meconium aspiration syndrome, congenital diaphragmatic hernia, bronchopulmonary dysplasia, sepsis, or congenital heart disease. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. CPS1 variants influence the availability of precursors for nitric oxide (NO) synthesis and play a role in clinical situations where endogenous NO production is critically important, such as neonatal pulmonary hypertension, increased pulmonary artery pressure following surgical repair of congenital heart defects or hepatovenocclusive disease following bone marrow transplantation. Infants with neonatal pulmonary hypertension homozygous for Thr-1406 have lower L-arginine concentrations than neonates homozygous for Asn-1406 (PubMed:11407344). Sequence=BAD92037.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Name=LOVD-Leiden Open Variation Database; Note=Carbamoyl- Phosphate Synthetase 1 (CPS1); URL="https://databases.lovd.nl/shared/genes/CPS1"; urea cycle nucleotide binding liver development catalytic activity carbamoyl-phosphate synthase (ammonia) activity carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity endopeptidase activity calcium ion binding protein binding ATP binding phospholipid binding nucleus nucleolus cytoplasm mitochondrion mitochondrial inner membrane mitochondrial matrix 'de novo' pyrimidine nucleobase biosynthetic process proteolysis glutamine metabolic process nitrogen compound metabolic process midgut development metabolic process response to toxic substance response to zinc ion response to amine glutamate binding ligase activity citrulline biosynthetic process triglyceride catabolic process response to food response to lipopolysaccharide macromolecular complex response to glucagon response to oleic acid vasodilation response to drug response to starvation mitochondrial nucleoid response to amino acid cellular response to fibroblast growth factor stimulus macromolecular complex binding nitric oxide metabolic process metal ion binding response to steroid hormone homocysteine metabolic process response to glucocorticoid response to cAMP anion homeostasis response to growth hormone hepatocyte differentiation carbamoyl phosphate biosynthetic process cellular response to cAMP cellular response to glucagon stimulus cellular response to oleic acid response to dexamethasone modified amino acid binding cellular response to ammonia uc002vee.1 uc002vee.2 uc002vee.3 uc002vee.4 uc002vee.5 uc002vee.6 
ENST00000233078.9 DAZAP1 ENST00000233078.9 DAZ associated protein 1, transcript variant 2 (from RefSeq NM_018959.4) DAZP1_HUMAN ENST00000233078.1 ENST00000233078.2 ENST00000233078.3 ENST00000233078.4 ENST00000233078.5 ENST00000233078.6 ENST00000233078.7 ENST00000233078.8 NM_018959 Q96EP5 Q96MJ3 Q9NRR9 uc002lsn.1 uc002lsn.2 uc002lsn.3 uc002lsn.4 uc002lsn.5 uc002lsn.6 In mammals, the Y chromosome directs the development of the testes and plays an important role in spermatogenesis. A high percentage of infertile men have deletions that map to regions of the Y chromosome. The DAZ (deleted in azoospermia) gene cluster maps to the AZFc region of the Y chromosome and is deleted in many azoospermic and severely oligospermic men. It is thought that the DAZ gene cluster arose from the transposition, amplification, and pruning of the ancestral autosomal gene DAZL also involved in germ cell development and gametogenesis. This gene encodes a RNA-binding protein with two RNP motifs that was originally identified by its interaction with the infertility factors DAZ and DAZL. Two isoforms are encoded by transcript variants of this gene. [provided by RefSeq, Jul 2008]. RNA-binding protein, which may be required during spermatogenesis. Interacts with DAZ and DAZL. Q96EP5; Q9NQZ3: DAZ1; NbExp=3; IntAct=EBI-2133162, EBI-997955; Q96EP5; P09012: SNRPA; NbExp=3; IntAct=EBI-2133162, EBI-607085; Cytoplasm Nucleus Note=Predominantly cytoplasmic (By similarity). Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles. In round spermatids, it localizes mainly in the nuclei, whereas in elongated spermatids, it localizes to the cytoplasm (By similarity). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96EP5-1; Sequence=Displayed; Name=2; IsoId=Q96EP5-2; Sequence=VSP_009441; Mainly expressed in testis. Expressed to a lower level in thymus. Weakly or not expressed in heart, liver, brain, placenta, lung, skeletal muscle, kidney and pancreas. Acetylation at Lys-150 is predominantly observed in the nuclear fraction, and may regulate nucleocytoplasmic transport. Sequence=BAB71295.1; Type=Erroneous initiation; Evidence=; maternal placenta development nucleic acid binding RNA binding mRNA binding mRNA 3'-UTR binding protein binding nucleus nucleoplasm cytoplasm cytosol multicellular organism development spermatogenesis poly(U) RNA binding cell proliferation cell differentiation macromolecular complex poly(G) binding RNA stem-loop binding positive regulation of mRNA splicing, via spliceosome ribonucleoprotein complex uc002lsn.1 uc002lsn.2 uc002lsn.3 uc002lsn.4 uc002lsn.5 uc002lsn.6 
ENST00000233084.8 DDX1 ENST00000233084.8 DEAD-box helicase 1 (from RefSeq NM_004939.3) B4DME8 B4DPN6 DDX1_HUMAN ENST00000233084.1 ENST00000233084.2 ENST00000233084.3 ENST00000233084.4 ENST00000233084.5 ENST00000233084.6 ENST00000233084.7 NM_004939 Q92499 uc002rce.1 uc002rce.2 uc002rce.3 uc002rce.4 uc002rce.5 uc002rce.6 DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein of unknown function. It shows high transcription levels in 2 retinoblastoma cell lines and in tissues of neuroectodermal origin. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X70649.1, SRR1803614.49929.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233084.8/ ENSP00000233084.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double- strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (PubMed:24870230). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1. Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By similarity). (Microbial infection) Required for HIV-1 Rev function as well as for HIV-1 and coronavirus IBV replication. Binds to the RRE sequence of HIV-1 mRNAs. (Microbial infection) Required for Coronavirus IBV replication. Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence=; Kinetic parameters: KM=0.120 mM for ATP (in the absence of nucleic acid) ; KM=0.090 mM for ATP (in the presence of RNA oligo(rU)20) ; KM=0.095 mM for ATP (in the presence of DNA oligo(dT)20) ; Note=kcat is 1.9 min(-1) for ATP hydrolysis in the absence of nucleic acid (PubMed:21589879). kcat is 3.8 min(-1) for ATP hydrolysis in the presence of RNA oligo(rU)20 (PubMed:21589879). kcat is 2.1 min(-1) for ATP hydrolysis in the presence of DNA oligo(dT)20 (PubMed:21589879). ; (Microbial infection) Interacts with Venezuelan equine encephalitis virus non-structural protein 3. Found in a multi-helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells with or without poly(I:C) RNA ligand stimulation. Interacts with DHX36. Interacts (via B30.2/SPRY domain) with DDX21 (via N-terminus); this interaction serves as bridges to TICAM1 (By similarity). Interacts with FAM98A (via N- and C-terminus) (PubMed:28040436). Interacts with MBNL1 (PubMed:18335541). Interacts with CSTF2 (PubMed:11598190). Interacts with HNRNPK (PubMed:12183465). Interacts with ATM (PubMed:18710941). Interacts with RELA (via C-terminus) (PubMed:19058135). Component of the tRNA-splicing ligase complex (PubMed:21311021, PubMed:24870230). Interacts with PQBP1 (PubMed:21933836). Interacts with PHF5A (via C- terminus) (By similarity). Interacts with ERCC6 (PubMed:26030138). (Microbial infection) Interacts with Rev of HIV-1. (Microbial infection) Interacts with Severe acute respiratory syndrome coronavirus (SARS-CoV) (via N-terminus) (PubMed:20573827). Interacts (via C-terminus) with the replicase polyprotein 1ab Nsp14 of the Avian infectious bronchitis virus (IBV). Q92499; Q8NCA5: FAM98A; NbExp=4; IntAct=EBI-358474, EBI-1210765; Q92499; Q9Y224: RTRAF; NbExp=3; IntAct=EBI-358474, EBI-1104547; Q92499; P0DTC9: N; Xeno; NbExp=3; IntAct=EBI-358474, EBI-25475856; Q92499; PRO_0000037415 [P0C6Y1]: rep; Xeno; NbExp=5; IntAct=EBI-358474, EBI-25826989; Q92499-1; P04618: rev; Xeno; NbExp=6; IntAct=EBI-15532186, EBI-6164309; Nucleus. Cytoplasm. Cytoplasmic granule. Cytoplasm, cytosol Mitochondrion Note=Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF) after IR treatment, a process that depends on the presence of chromosomal DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-dependent manner after IR treatment. Colocalized with RELA in the nucleus upon TNF-alpha induction. Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (PubMed:24608264). Colocalizes in the cytosol with DDX21, DHX36 and TICAM1. Colocalizes in the mitochondria with TICAM1 and poly(I:C) RNA ligand. The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) stimulation (By similarity). Cytoplasm Note=(Microbial infection) Relocalized to the cytoplasm with a perinuclear staining pattern in avian infectious bronchitis virus (IBV)-infected cells (PubMed:20573827). Required for proper localization of HIV-1 Rev (PubMed:15567440). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q92499-1; Sequence=Displayed; Name=2; IsoId=Q92499-2; Sequence=VSP_055454, VSP_055455; Name=3; IsoId=Q92499-3; Sequence=VSP_055453; Highest levels of transcription in 2 retinoblastoma cell lines and in tissues of neuroectodermal origin including the retina, brain, and spinal cord. The helicase domain is involved in the stimulation of RELA transcriptional activity. Phosphorylated by ATM kinase; phosphorylation is increased in response to ionizing radiation (IR). Belongs to the DEAD box helicase family. DDX1 subfamily. According to some authors the unwinding activity is ADP- dependent and not ATP-dependent. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40283/DDX1"; nucleotide binding spliceosomal complex assembly immune system process positive regulation of myeloid dendritic cell cytokine production nucleic acid binding DNA binding chromatin binding transcription cofactor activity RNA binding RNA helicase activity double-stranded RNA binding helicase activity nuclease activity exonuclease activity protein binding ATP binding nucleus nucleoplasm cytoplasm mitochondrion cytosol double-strand break repair tRNA splicing, via endonucleolytic cleavage and ligation mRNA processing regulation of translational initiation multicellular organism development tRNA processing poly(A) binding response to virus cytoplasmic stress granule membrane hydrolase activity DNA duplex unwinding DNA/RNA helicase activity positive regulation of I-kappaB kinase/NF-kappaB signaling response to exogenous dsRNA innate immune response defense response to virus cleavage body tRNA-splicing ligase complex nucleic acid phosphodiester bond hydrolysis regulation of nucleic acid-templated transcription protein localization to cytoplasmic stress granule ribonucleoprotein complex uc002rce.1 uc002rce.2 uc002rce.3 uc002rce.4 uc002rce.5 uc002rce.6 
ENST00000233099.6 HEATR5B ENST00000233099.6 HEAT repeat containing 5B (from RefSeq NM_019024.3) B5MDU8 ENST00000233099.1 ENST00000233099.2 ENST00000233099.3 ENST00000233099.4 ENST00000233099.5 HEATR5B HTR5B_HUMAN KIAA1414 NM_019024 Q7Z3B2 Q9NVL7 Q9P2D3 p200 p200a uc002rpp.1 uc002rpp.2 uc002rpp.3 Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). Self-associates (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, at least composed of AFTPH/aftiphilin, HEATR5B/p200a and SYNRG/gamma-synergin, which plays a role in the AP1G1/AP-1-mediated protein trafficking from early to recycling endosomes and between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). Within the complex interacts with AFTPH/aftiphilin and SYNRG/gamma-synergin; the interactions are direct (PubMed:15758025). Interacts with GGA1 (PubMed:15758025). Q9P2D3; Q12959: DLG1; NbExp=2; IntAct=EBI-2832021, EBI-357481; Cytoplasm, perinuclear region Cytoplasmic vesicle, clathrin-coated vesicle Note=Localization at clathrin- coated vesicles depends on AFTPH/aftiphilin. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9P2D3-1; Sequence=Displayed; Name=2; IsoId=Q9P2D3-2; Sequence=VSP_029690, VSP_029691; Name=3; IsoId=Q9P2D3-3; Sequence=VSP_029692; Belongs to the HEATR5 family. Sequence=BAA91733.1; Type=Erroneous initiation; Evidence=; protein binding cytosol endocytosis protein localization membrane endocytic vesicle retrograde transport, endosome to Golgi uc002rpp.1 uc002rpp.2 uc002rpp.3 
ENST00000233114.13 MDH1 ENST00000233114.13 malate dehydrogenase 1, transcript variant 1 (from RefSeq NM_005917.4) ENST00000233114.1 ENST00000233114.10 ENST00000233114.11 ENST00000233114.12 ENST00000233114.2 ENST00000233114.3 ENST00000233114.4 ENST00000233114.5 ENST00000233114.6 ENST00000233114.7 ENST00000233114.8 ENST00000233114.9 HEL-S-32 NM_005917 V9HWF2 V9HWF2_HUMAN uc002scj.1 uc002scj.2 uc002scj.3 uc002scj.4 This gene encodes an enzyme that catalyzes the NAD/NADH-dependent, reversible oxidation of malate to oxaloacetate in many metabolic pathways, including the citric acid cycle. Two main isozymes are known to exist in eukaryotic cells: one is found in the mitochondrial matrix and the other in the cytoplasm. This gene encodes the cytosolic isozyme, which plays a key role in the malate-aspartate shuttle that allows malate to pass through the mitochondrial membrane to be transformed into oxaloacetate for further cellular processes. Alternatively spliced transcript variants have been found for this gene. A recent study showed that a C-terminally extended isoform is produced by use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism, and that this isoform is localized in the peroxisomes. Pseudogenes have been identified on chromosomes X and 6. [provided by RefSeq, Feb 2016]. Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4- hydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:10780, ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.96; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10782; Evidence=; Reaction=(S)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH; Xref=Rhea:RHEA:57172, ChEBI:CHEBI:15378, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57174; Evidence=; Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21433; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21434; Evidence=; Belongs to the LDH/MDH superfamily. MDH type 2 family. catalytic activity carbohydrate metabolic process tricarboxylic acid cycle malate metabolic process oxidoreductase activity malate dehydrogenase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor carboxylic acid metabolic process L-malate dehydrogenase activity oxidation-reduction process uc002scj.1 uc002scj.2 uc002scj.3 uc002scj.4 
ENST00000233121.7 MAPRE3 ENST00000233121.7 microtubule associated protein RP/EB family member 3, transcript variant 1 (from RefSeq NM_012326.4) B7WPK5 ENST00000233121.1 ENST00000233121.2 ENST00000233121.3 ENST00000233121.4 ENST00000233121.5 ENST00000233121.6 MARE3_HUMAN NM_012326 O00265 Q6FHB0 Q6FI15 Q9BZP7 Q9BZP8 Q9UPY8 uc002rhw.1 uc002rhw.2 uc002rhw.3 uc002rhw.4 uc002rhw.5 The protein encoded by this gene is a member of the RP/EB family of genes. The protein localizes to the cytoplasmic microtubule network and binds APCL, a homolog of the adenomatous polyposis coli tumor suppressor gene. [provided by RefSeq, Jul 2008]. Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:28814570, PubMed:19255245). Promotes microtubule growth (PubMed:28814570, PubMed:19255245). May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes (PubMed:28814570, PubMed:19255245). Also acts as a regulator of minus- end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Homodimer (PubMed:19255245). Heterodimer with MAPRE1 (PubMed:19255245). Binds monomeric and polymerized GTP-bound tubulin (PubMed:10188731, PubMed:34996871). Interacts with APC2 (PubMed:10644998). Interacts with DCTN1 and SRCIN1 (PubMed:14514668, PubMed:19146815). Binds to the C-terminal domain of APC (PubMed:14514668). Interacts (via C-terminus) with CLIP1 (PubMed:17563362). Interacts with SLAIN2 and SLAIN1 (PubMed:21646404). Interacts with AKAP9 (PubMed:28814570). Interacts with PDE4DIP (PubMed:28814570). Interacts with PDE4DIP isoform 13/MMG8/SMYLE; this interaction is required for its recruitment to the Golgi apparatus (PubMed:25217626). Q9UPY8; Q15327: ANKRD1; NbExp=5; IntAct=EBI-726739, EBI-5653378; Q9UPY8; O95996: APC2; NbExp=7; IntAct=EBI-726739, EBI-1053045; Q9UPY8; Q8NEU8: APPL2; NbExp=3; IntAct=EBI-726739, EBI-741261; Q9UPY8; A1L168: C20orf202; NbExp=3; IntAct=EBI-726739, EBI-18396958; Q9UPY8; Q9C0I3-2: CCSER1; NbExp=3; IntAct=EBI-726739, EBI-17793327; Q9UPY8; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-726739, EBI-12593838; Q9UPY8; Q9NQ79: CRTAC1; NbExp=3; IntAct=EBI-726739, EBI-10205543; Q9UPY8; Q13561: DCTN2; NbExp=3; IntAct=EBI-726739, EBI-715074; Q9UPY8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-726739, EBI-742054; Q9UPY8; O60573: EIF4E2; NbExp=3; IntAct=EBI-726739, EBI-398610; Q9UPY8; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-726739, EBI-7225287; Q9UPY8; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-726739, EBI-11320806; Q9UPY8; Q8WXT5: FOXD4L4; NbExp=3; IntAct=EBI-726739, EBI-12911102; Q9UPY8; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-726739, EBI-7960826; Q9UPY8; P13984: GTF2F2; NbExp=3; IntAct=EBI-726739, EBI-1030560; Q9UPY8; Q8N3J3-3: HROB; NbExp=3; IntAct=EBI-726739, EBI-11061081; Q9UPY8; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-726739, EBI-11522367; Q9UPY8; P05412: JUN; NbExp=3; IntAct=EBI-726739, EBI-852823; Q9UPY8; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-726739, EBI-9478422; Q9UPY8; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-726739, EBI-373334; Q9UPY8; P28838: LAP3; NbExp=3; IntAct=EBI-726739, EBI-2339312; Q9UPY8; Q969G2: LHX4; NbExp=3; IntAct=EBI-726739, EBI-2865388; Q9UPY8; P25791: LMO2; NbExp=5; IntAct=EBI-726739, EBI-739696; Q9UPY8; P25791-3: LMO2; NbExp=6; IntAct=EBI-726739, EBI-11959475; Q9UPY8; Q15691: MAPRE1; NbExp=19; IntAct=EBI-726739, EBI-1004115; Q9UPY8; Q15555: MAPRE2; NbExp=7; IntAct=EBI-726739, EBI-739717; Q9UPY8; Q9UPY8: MAPRE3; NbExp=7; IntAct=EBI-726739, EBI-726739; Q9UPY8; P10636: MAPT; NbExp=3; IntAct=EBI-726739, EBI-366182; Q9UPY8; Q9H992: MARCHF7; NbExp=5; IntAct=EBI-726739, EBI-949983; Q9UPY8; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-726739, EBI-16439278; Q9UPY8; P52815: MRPL12; NbExp=3; IntAct=EBI-726739, EBI-358272; Q9UPY8; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-726739, EBI-9640281; Q9UPY8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-726739, EBI-79165; Q9UPY8; Q01851: POU4F1; NbExp=3; IntAct=EBI-726739, EBI-17480471; Q9UPY8; P25786: PSMA1; NbExp=4; IntAct=EBI-726739, EBI-359352; Q9UPY8; P20618: PSMB1; NbExp=3; IntAct=EBI-726739, EBI-372273; Q9UPY8; Q6PGN9: PSRC1; NbExp=3; IntAct=EBI-726739, EBI-7392664; Q9UPY8; Q04864-2: REL; NbExp=3; IntAct=EBI-726739, EBI-10829018; Q9UPY8; O00560: SDCBP; NbExp=6; IntAct=EBI-726739, EBI-727004; Q9UPY8; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-726739, EBI-11522811; Q9UPY8; P0CI01: SPDYE6; NbExp=3; IntAct=EBI-726739, EBI-11960469; Q9UPY8; Q6ZNM6: SPMIP10; NbExp=3; IntAct=EBI-726739, EBI-18115728; Q9UPY8; Q96LM5: SPMIP2; NbExp=3; IntAct=EBI-726739, EBI-12020542; Q9UPY8; Q9UL54: TAOK2; NbExp=3; IntAct=EBI-726739, EBI-352832; Q9UPY8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-726739, EBI-11741437; Q9UPY8; Q9BWF2: TRAIP; NbExp=3; IntAct=EBI-726739, EBI-1756205; Q9UPY8; Q14142: TRIM14; NbExp=3; IntAct=EBI-726739, EBI-2820256; Q9UPY8; Q12815: TROAP; NbExp=7; IntAct=EBI-726739, EBI-2349743; Q9UPY8; Q99757: TXN2; NbExp=6; IntAct=EBI-726739, EBI-2932492; Q9UPY8; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-726739, EBI-12111538; Q9UPY8; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-726739, EBI-5458880; Q9UPY8; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-726739, EBI-14104088; Q9UPY8; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-726739, EBI-11035148; Q9UPY8; Q8IVP9: ZNF547; NbExp=3; IntAct=EBI-726739, EBI-12895421; Q9UPY8; P14873: Map1b; Xeno; NbExp=4; IntAct=EBI-726739, EBI-764653; Q9UPY8; Q9QWI6-2: Srcin1; Xeno; NbExp=5; IntAct=EBI-726739, EBI-775607; Cytoplasm, cytoskeleton te=Associated with the microtubule network. Detected at the plus end of microtubules. Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=EBF3-L; IsoId=Q9UPY8-1; Sequence=Displayed; Name=2; Synonyms=EBF3-S; IsoId=Q9UPY8-2; Sequence=VSP_012947; Predominantly expressed in brain and muscle. Composed of two functionally independent domains. The N- terminal domain forms a hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1. Belongs to the MAPRE family. Sequence=AAK07556.1; Type=Erroneous initiation; Evidence=; Sequence=AAK07557.1; Type=Erroneous initiation; Evidence=; Sequence=CAA72060.1; Type=Frameshift; Evidence=; protein binding cytoplasm microtubule organizing center cytoskeleton microtubule cytoplasmic microtubule cell cycle microtubule binding protein C-terminus binding protein localization microtubule cytoskeleton protein kinase binding midbody regulation of microtubule polymerization or depolymerization regulation of microtubule polymerization microtubule plus-end protein localization to microtubule identical protein binding positive regulation of cyclin-dependent protein serine/threonine kinase activity positive regulation of protein kinase activity positive regulation of transcription, DNA-templated perinuclear region of cytoplasm microtubule plus-end binding spindle assembly spindle midzone cell division positive regulation of microtubule plus-end binding protein localization to microtubule plus-end mitotic spindle astral microtubule end uc002rhw.1 uc002rhw.2 uc002rhw.3 uc002rhw.4 uc002rhw.5 
ENST00000233143.6 TMSB10 ENST00000233143.6 thymosin beta 10 (from RefSeq NM_021103.4) ENST00000233143.1 ENST00000233143.2 ENST00000233143.3 ENST00000233143.4 ENST00000233143.5 NM_021103 P13472 P63313 PTMB10 Q596K9 THYB10 TYB10_HUMAN uc002sow.1 uc002sow.2 uc002sow.3 Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). P63313; P13196: ALAS1; NbExp=6; IntAct=EBI-2688673, EBI-3905054; P63313; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-2688673, EBI-1044640; P63313; Q9NUX5: POT1; NbExp=2; IntAct=EBI-2688673, EBI-752420; Cytoplasm, cytoskeleton. Found to decrease dramatically after birth. Belongs to the thymosin beta family. Sequence=AAA36746.1; Type=Erroneous initiation; Evidence=; Sequence=AAC41691.1; Type=Erroneous initiation; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42595/TMSB10"; actin binding actin monomer binding protein binding cytoplasm cytoskeleton actin filament organization regulation of cell migration sequestering of actin monomers uc002sow.1 uc002sow.2 uc002sow.3 
ENST00000233146.7 MSH2 ENST00000233146.7 mutS homolog 2, transcript variant 57 (from RefSeq NR_176249.1) B4E2Z2 ENST00000233146.1 ENST00000233146.2 ENST00000233146.3 ENST00000233146.4 ENST00000233146.5 ENST00000233146.6 MSH2_HUMAN NR_176249 O75488 P43246 uc002rvy.1 uc002rvy.2 uc002rvy.3 uc002rvy.4 Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containing DNA strand (PubMed:26300262). ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis. Component of the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). Heterodimer consisting of MSH2-MSH6 (MutS alpha) or MSH2-MSH3 (MutS beta) (PubMed:8942985). Both heterodimers form a ternary complex with MutL alpha (MLH1-PMS1) (PubMed:9788596, PubMed:10856833, PubMed:11427529, PubMed:11429708, PubMed:12414623, PubMed:14676842). Interacts with MCM9; the interaction recruits MCM9 to chromatin (PubMed:26300262). Interacts with MCM8 (PubMed:26300262). Interacts with EXO1 (PubMed:9788596, PubMed:10856833, PubMed:11427529, PubMed:11429708, PubMed:12414623, PubMed:14676842). Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex (PubMed:10783165). This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains (PubMed:10783165). Interacts with ATR (PubMed:14657349). Interacts with SLX4/BTBD12; this interaction is direct and links MutS beta to SLX4, a subunit of different structure-specific endonucleases (PubMed:19596235). Interacts with SMARCAD1 (PubMed:18675275). P43246; Q92624: APPBP2; NbExp=3; IntAct=EBI-355888, EBI-743771; P43246; Q9UQ84-1: EXO1; NbExp=3; IntAct=EBI-355888, EBI-944694; P43246; P09429: HMGB1; NbExp=2; IntAct=EBI-355888, EBI-389432; P43246; P20585: MSH3; NbExp=12; IntAct=EBI-355888, EBI-1164205; P43246; P52701: MSH6; NbExp=9; IntAct=EBI-355888, EBI-395529; P43246; Q8IY92: SLX4; NbExp=5; IntAct=EBI-355888, EBI-2370740; P43246; P39875: EXO1; Xeno; NbExp=2; IntAct=EBI-355888, EBI-6738; Nucleus Chromosome Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P43246-1; Sequence=Displayed; Name=2; IsoId=P43246-2; Sequence=VSP_045536; Ubiquitously expressed. Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway. Lynch syndrome 1 (LYNCH1) [MIM:120435]: A form of Lynch syndrome, an autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra- colonic tumors of the gastrointestinal, urological and female reproductive tracts. Lynch syndrome is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, it is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical Lynch syndrome is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected Lynch syndrome' or 'incomplete Lynch syndrome' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. te=The disease is caused by variants affecting the gene represented in this entry. Muir-Torre syndrome (MRTES) [MIM:158320]: Rare autosomal dominant disorder characterized by sebaceous neoplasms and visceral malignancy. Note=The disease is caused by variants affecting the gene represented in this entry. Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. te=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mismatch repair cancer syndrome 2 (MMRCS2) [MIM:619096]: An autosomal recessive form of mismatch repair cancer syndrome, a childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. te=The disease is caused by variants affecting the gene represented in this entry. Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. te=Disease susceptibility may be associated with variants affecting the gene represented in this entry. Belongs to the DNA mismatch repair MutS family. Sequence=AAC27930.1; Type=Frameshift; Note=The frameshift is caused by a single nucleotide deletion which is found in a HNPCC kindred.; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/340/MSH2"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/msh2/"; nucleotide binding double-strand/single-strand DNA junction binding nuclear chromosome, telomeric region in utero embryonic development somatic recombination of immunoglobulin genes involved in immune response DNA binding chromatin binding damaged DNA binding protein binding ATP binding nucleus nucleoplasm chromosome oxidative phosphorylation DNA repair mismatch repair postreplication repair double-strand break repair DNA recombination cellular response to DNA damage stimulus cell cycle arrest germ cell development protein C-terminus binding DNA-dependent ATPase activity determination of adult lifespan male gonad development intrinsic apoptotic signaling pathway in response to DNA damage response to X-ray response to UV-B membrane somatic hypermutation of immunoglobulin genes somatic recombination of immunoglobulin gene segments ATPase activity centromeric DNA binding B cell mediated immunity enzyme binding protein kinase binding B cell differentiation mismatched DNA binding intra-S DNA damage checkpoint guanine/thymine mispair binding mismatch repair complex MutSalpha complex MutSbeta complex intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator protein homodimerization activity negative regulation of neuron apoptotic process maintenance of DNA repeat elements isotype switching negative regulation of DNA recombination positive regulation of isotype switching to IgA isotypes positive regulation of isotype switching to IgG isotypes positive regulation of helicase activity protein localization to chromatin magnesium ion binding four-way junction DNA binding double-stranded DNA binding single-stranded DNA binding dinucleotide insertion or deletion binding single guanine insertion binding single thymine insertion binding dinucleotide repeat insertion binding oxidized purine DNA binding MutLalpha complex binding ADP binding uc002rvy.1 uc002rvy.2 uc002rvy.3 uc002rvy.4 
ENST00000233154.9 NCK2 ENST00000233154.9 NCK adaptor protein 2, transcript variant 1 (from RefSeq NM_003581.5) D3DVK1 ENST00000233154.1 ENST00000233154.2 ENST00000233154.3 ENST00000233154.4 ENST00000233154.5 ENST00000233154.6 ENST00000233154.7 ENST00000233154.8 GRB4 NCK2_HUMAN NM_003581 O43639 Q9BWN9 Q9UIC3 uc002tdg.1 uc002tdg.2 uc002tdg.3 uc002tdg.4 uc002tdg.5 This gene encodes a member of the NCK family of adaptor proteins. The protein contains three SH3 domains and one SH2 domain. The protein has no known catalytic function but has been shown to bind and recruit various proteins involved in the regulation of receptor protein tyrosine kinases. It is through these regulatory activities that this protein is believed to be involved in cytoskeletal reorganization. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008]. Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Interacts with DOCK1, LIMS1 and TGFB1I1. Part of a complex containing PPP1R15B, PP1 and NCK2. Interacts with FASLG (By similarity). Interacts with AXL. Interacts with PAK1, PKN2 and SOS1. Interacts (via SH2 domain) with EGFR. Interacts (via SH2 domain) with DDR1. O43639; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-713635, EBI-743598; O43639; Q9NYB9-2: ABI2; NbExp=10; IntAct=EBI-713635, EBI-11096309; O43639; Q9P2A4: ABI3; NbExp=6; IntAct=EBI-713635, EBI-742038; O43639; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-713635, EBI-14493093; O43639; Q7Z6G8-3: ANKS1B; NbExp=3; IntAct=EBI-713635, EBI-17714371; O43639; A7KAX9: ARHGAP32; NbExp=3; IntAct=EBI-713635, EBI-308663; O43639; P56945: BCAR1; NbExp=3; IntAct=EBI-713635, EBI-702093; O43639; Q9H165-2: BCL11A; NbExp=6; IntAct=EBI-713635, EBI-10183342; O43639; P62324: BTG1; NbExp=3; IntAct=EBI-713635, EBI-742279; O43639; Q53FE4: C4orf17; NbExp=3; IntAct=EBI-713635, EBI-715110; O43639; Q8N350-4: CBARP; NbExp=3; IntAct=EBI-713635, EBI-19051169; O43639; Q13191: CBLB; NbExp=8; IntAct=EBI-713635, EBI-744027; O43639; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-713635, EBI-744556; O43639; P07766: CD3E; NbExp=4; IntAct=EBI-713635, EBI-1211297; O43639; P15882: CHN1; NbExp=16; IntAct=EBI-713635, EBI-718947; O43639; P52757: CHN2; NbExp=6; IntAct=EBI-713635, EBI-714925; O43639; Q99828: CIB1; NbExp=3; IntAct=EBI-713635, EBI-372594; O43639; Q9C0C6: CIPC; NbExp=3; IntAct=EBI-713635, EBI-5654244; O43639; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-713635, EBI-11977093; O43639; Q16630-2: CPSF6; NbExp=3; IntAct=EBI-713635, EBI-11088043; O43639; Q8N684: CPSF7; NbExp=4; IntAct=EBI-713635, EBI-746909; O43639; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-713635, EBI-11523759; O43639; Q9NWM3: CUEDC1; NbExp=3; IntAct=EBI-713635, EBI-5838167; O43639; Q08345: DDR1; NbExp=3; IntAct=EBI-713635, EBI-711879; O43639; Q8NES8: DEFB124; NbExp=3; IntAct=EBI-713635, EBI-12843376; O43639; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-713635, EBI-11988027; O43639; Q9Y2H0-1: DLGAP4; NbExp=6; IntAct=EBI-713635, EBI-12000556; O43639; Q14919: DRAP1; NbExp=3; IntAct=EBI-713635, EBI-712941; O43639; Q8N9I9: DTX3; NbExp=5; IntAct=EBI-713635, EBI-2340258; O43639; Q86TH3: DVL1; NbExp=3; IntAct=EBI-713635, EBI-10185025; O43639; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-713635, EBI-2349927; O43639; P52799: EFNB2; NbExp=7; IntAct=EBI-713635, EBI-7532268; O43639; O15372: EIF3H; NbExp=6; IntAct=EBI-713635, EBI-709735; O43639; Q6IB98: EIF3S3; NbExp=3; IntAct=EBI-713635, EBI-10184995; O43639; P04626: ERBB2; NbExp=2; IntAct=EBI-713635, EBI-641062; O43639; P21860: ERBB3; NbExp=2; IntAct=EBI-713635, EBI-720706; O43639; Q86V42: FAM124A; NbExp=3; IntAct=EBI-713635, EBI-744506; O43639; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-713635, EBI-10220102; O43639; Q5JRC9: FAM47A; NbExp=3; IntAct=EBI-713635, EBI-34579660; O43639; Q9NYF3: FAM53C; NbExp=8; IntAct=EBI-713635, EBI-1644252; O43639; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-713635, EBI-1384254; O43639; P48023: FASLG; NbExp=4; IntAct=EBI-713635, EBI-495538; O43639; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-713635, EBI-11959077; O43639; Q96LA5: FCRL2; NbExp=3; IntAct=EBI-713635, EBI-10185081; O43639; P53539: FOSB; NbExp=3; IntAct=EBI-713635, EBI-2806743; O43639; O15117: FYB1; NbExp=3; IntAct=EBI-713635, EBI-1753267; O43639; Q13480: GAB1; NbExp=5; IntAct=EBI-713635, EBI-517684; O43639; Q9H706: GAREM1; NbExp=3; IntAct=EBI-713635, EBI-3440103; O43639; Q86UU5: GGN; NbExp=3; IntAct=EBI-713635, EBI-10259069; O43639; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-713635, EBI-10172004; O43639; P49639: HOXA1; NbExp=3; IntAct=EBI-713635, EBI-740785; O43639; P09017: HOXC4; NbExp=3; IntAct=EBI-713635, EBI-3923226; O43639; Q86TF7: HOXC4; NbExp=3; IntAct=EBI-713635, EBI-10185009; O43639; P13378: HOXD8; NbExp=3; IntAct=EBI-713635, EBI-7098661; O43639; O75031: HSF2BP; NbExp=3; IntAct=EBI-713635, EBI-7116203; O43639; Q0VD86: INCA1; NbExp=3; IntAct=EBI-713635, EBI-6509505; O43639; Q9H0H0: INTS2; NbExp=3; IntAct=EBI-713635, EBI-8471507; O43639; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-713635, EBI-743960; O43639; Q6ZU52: KIAA0408; NbExp=7; IntAct=EBI-713635, EBI-739493; O43639; P10721: KIT; NbExp=2; IntAct=EBI-713635, EBI-1379503; O43639; Q6TFL4: KLHL24; NbExp=3; IntAct=EBI-713635, EBI-2510117; O43639; Q6PF15: KLHL35; NbExp=3; IntAct=EBI-713635, EBI-9477654; O43639; Q5T749: KPRP; NbExp=3; IntAct=EBI-713635, EBI-10981970; O43639; Q13094: LCP2; NbExp=10; IntAct=EBI-713635, EBI-346946; O43639; P48059: LIMS1; NbExp=2; IntAct=EBI-713635, EBI-306928; O43639; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-713635, EBI-739832; O43639; A6PVS8: LRRIQ3; NbExp=6; IntAct=EBI-713635, EBI-10184751; O43639; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-713635, EBI-741037; O43639; P43360: MAGEA6; NbExp=6; IntAct=EBI-713635, EBI-1045155; O43639; Q96DN6: MBD6; NbExp=3; IntAct=EBI-713635, EBI-719591; O43639; P50222: MEOX2; NbExp=3; IntAct=EBI-713635, EBI-748397; O43639; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-713635, EBI-16439278; O43639; P08581: MET; NbExp=2; IntAct=EBI-713635, EBI-1039152; O43639; Q5JRA6: MIA3; NbExp=3; IntAct=EBI-713635, EBI-2291868; O43639; Q99583: MNT; NbExp=3; IntAct=EBI-713635, EBI-7959025; O43639; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-713635, EBI-2858213; O43639; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-713635, EBI-10963850; O43639; Q9H3P2: NELFA; NbExp=3; IntAct=EBI-713635, EBI-5461341; O43639; Q7Z628: NET1; NbExp=3; IntAct=EBI-713635, EBI-2511306; O43639; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-713635, EBI-10271199; O43639; Q5HYW2: NHSL2; NbExp=6; IntAct=EBI-713635, EBI-2859639; O43639; Q99743: NPAS2; NbExp=6; IntAct=EBI-713635, EBI-3932727; O43639; Q13285: NR5A1; NbExp=3; IntAct=EBI-713635, EBI-874629; O43639; O60422: ONECUT3; NbExp=3; IntAct=EBI-713635, EBI-17431136; O43639; Q13153: PAK1; NbExp=10; IntAct=EBI-713635, EBI-1307; O43639; Q13177: PAK2; NbExp=8; IntAct=EBI-713635, EBI-1045887; O43639; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-713635, EBI-10302990; O43639; Q8N4B1-4: PHETA1; NbExp=3; IntAct=EBI-713635, EBI-14131832; O43639; Q6ZUJ8-3: PIK3AP1; NbExp=7; IntAct=EBI-713635, EBI-11981743; O43639; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-713635, EBI-11320284; O43639; Q569H4: PRR16; NbExp=3; IntAct=EBI-713635, EBI-5564642; O43639; P86479: PRR20C; NbExp=3; IntAct=EBI-713635, EBI-10172814; O43639; P86480: PRR20D; NbExp=3; IntAct=EBI-713635, EBI-12754095; O43639; O75832: PSMD10; NbExp=2; IntAct=EBI-713635, EBI-752185; O43639; Q02833: RASSF7; NbExp=5; IntAct=EBI-713635, EBI-929013; O43639; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-713635, EBI-11322432; O43639; Q5T8P6: RBM26; NbExp=3; IntAct=EBI-713635, EBI-3232077; O43639; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-713635, EBI-7545592; O43639; Q04864: REL; NbExp=3; IntAct=EBI-713635, EBI-307352; O43639; Q04864-2: REL; NbExp=3; IntAct=EBI-713635, EBI-10829018; O43639; Q7L0Q8: RHOU; NbExp=6; IntAct=EBI-713635, EBI-1638043; O43639; Q96L33: RHOV; NbExp=4; IntAct=EBI-713635, EBI-8538631; O43639; Q9NQC3: RTN4; NbExp=2; IntAct=EBI-713635, EBI-715945; O43639; Q9UQR0: SCML2; NbExp=3; IntAct=EBI-713635, EBI-2513111; O43639; Q7RTU7: SCX; NbExp=3; IntAct=EBI-713635, EBI-17492262; O43639; Q15637-4: SF1; NbExp=3; IntAct=EBI-713635, EBI-12223157; O43639; Q15428: SF3A2; NbExp=3; IntAct=EBI-713635, EBI-2462271; O43639; Q15427: SF3B4; NbExp=7; IntAct=EBI-713635, EBI-348469; O43639; Q96IW2: SHD; NbExp=3; IntAct=EBI-713635, EBI-4402781; O43639; Q13573: SNW1; NbExp=3; IntAct=EBI-713635, EBI-632715; O43639; O14512: SOCS7; NbExp=3; IntAct=EBI-713635, EBI-1539606; O43639; O94875: SORBS2; NbExp=3; IntAct=EBI-713635, EBI-311323; O43639; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-713635, EBI-2510414; O43639; Q9H0A9-2: SPATC1L; NbExp=5; IntAct=EBI-713635, EBI-11995806; O43639; O43597: SPRY2; NbExp=3; IntAct=EBI-713635, EBI-742487; O43639; Q9H3Y6: SRMS; NbExp=3; IntAct=EBI-713635, EBI-8541270; O43639; Q8TE77: SSH3; NbExp=3; IntAct=EBI-713635, EBI-8743776; O43639; Q96PV0: SYNGAP1; NbExp=3; IntAct=EBI-713635, EBI-2682386; O43639; P15884: TCF4; NbExp=3; IntAct=EBI-713635, EBI-533224; O43639; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-713635, EBI-3923210; O43639; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-713635, EBI-12155101; O43639; A1L306: TNR; NbExp=3; IntAct=EBI-713635, EBI-10182881; O43639; P14373: TRIM27; NbExp=6; IntAct=EBI-713635, EBI-719493; O43639; Q8WV44: TRIM41; NbExp=8; IntAct=EBI-713635, EBI-725997; O43639; Q15654: TRIP6; NbExp=8; IntAct=EBI-713635, EBI-742327; O43639; P42681: TXK; NbExp=3; IntAct=EBI-713635, EBI-7877438; O43639; P0CG48: UBC; NbExp=2; IntAct=EBI-713635, EBI-3390054; O43639; Q8NFA0-2: USP32; NbExp=5; IntAct=EBI-713635, EBI-12220239; O43639; Q5ST30: VARS2; NbExp=3; IntAct=EBI-713635, EBI-2116622; O43639; Q5ST30-4: VARS2; NbExp=3; IntAct=EBI-713635, EBI-10244997; O43639; Q9H9H4: VPS37B; NbExp=6; IntAct=EBI-713635, EBI-4400866; O43639; P42768: WAS; NbExp=3; IntAct=EBI-713635, EBI-346375; O43639; Q92558: WASF1; NbExp=4; IntAct=EBI-713635, EBI-1548747; O43639; O00401: WASL; NbExp=7; IntAct=EBI-713635, EBI-957615; O43639; O43516-4: WIPF1; NbExp=3; IntAct=EBI-713635, EBI-12052927; O43639; Q9Y330: ZBTB12; NbExp=3; IntAct=EBI-713635, EBI-12377219; O43639; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-713635, EBI-12287587; O43639; O15156: ZBTB7B; NbExp=3; IntAct=EBI-713635, EBI-740434; O43639; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-713635, EBI-11522250; O43639; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-713635, EBI-5458880; O43639; Q5TFG8: ZC2HC1B; NbExp=3; IntAct=EBI-713635, EBI-12275374; O43639; Q9BYN7: ZNF341; NbExp=3; IntAct=EBI-713635, EBI-9089622; O43639; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-713635, EBI-11035148; O43639; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-713635, EBI-4395732; O43639; Q7VLE8: lspA1; Xeno; NbExp=2; IntAct=EBI-713635, EBI-26445163; O43639; Q63604: Ntrk2; Xeno; NbExp=2; IntAct=EBI-713635, EBI-7287667; Cytoplasm Endoplasmic reticulum Ubiquitous. Phosphorylated. immunological synapse formation phosphotyrosine binding SH3/SH2 adaptor activity protein binding cytoplasm endoplasmic reticulum cytosol regulation of translation actin filament organization signal transduction signal complex assembly epidermal growth factor receptor signaling pathway regulation of epidermal growth factor-activated receptor activity cytoskeletal adaptor activity negative regulation of cell proliferation vesicle membrane postsynaptic density cell migration lamellipodium assembly receptor signaling complex scaffold activity positive regulation of actin filament polymerization negative regulation of peptidyl-serine phosphorylation positive regulation of translation in response to endoplasmic reticulum stress positive regulation of T cell proliferation T cell activation macromolecular complex binding synapse positive regulation of transcription from RNA polymerase II promoter vascular endothelial growth factor receptor signaling pathway ephrin receptor signaling pathway dendritic spine development scaffold protein binding positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway negative regulation of PERK-mediated unfolded protein response negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress uc002tdg.1 uc002tdg.2 uc002tdg.3 uc002tdg.4 uc002tdg.5 
ENST00000233156.9 TFPI ENST00000233156.9 tissue factor pathway inhibitor, transcript variant 1 (from RefSeq NM_006287.6) ENST00000233156.1 ENST00000233156.2 ENST00000233156.3 ENST00000233156.4 ENST00000233156.5 ENST00000233156.6 ENST00000233156.7 ENST00000233156.8 LACI NM_006287 O95103 P10646 Q53TS4 TFPI1 TFPI1_HUMAN uc002upy.1 uc002upy.2 uc002upy.3 uc002upy.4 uc002upy.5 uc002upy.6 This gene encodes a Kunitz-type serine protease inhibitor that regulates the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process initiates with the formation of a factor VIIa-TF complex, which proteolytically activates additional proteases (factors IX and X) and ultimately leads to the formation of a fibrin clot. The product of this gene inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. Inhibition of the encoded protein restores hemostasis in animal models of hemophilia. This gene encodes multiple protein isoforms that differ in their inhibitory activity, specificity and cellular localization. [provided by RefSeq, Jul 2016]. Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma. [Isoform Alpha]: Secreted. [Isoform Beta]: Microsome membrane ; Lipid-anchor, GPI-anchor Event=Alternative splicing; Named isoforms=2; Name=Alpha; Synonyms=TFPIalpha; IsoId=P10646-1; Sequence=Displayed; Name=Beta; Synonyms=TFPIbeta; IsoId=P10646-2; Sequence=VSP_003030, VSP_003031; Mostly in endothelial cells. This inhibitor contains three inhibitory domains. The first domain interacts with VIIa and TF, the second one with Xa. O-glycosylated. [Isoform Beta]: GPI-anchored. Name=Wikipedia; Note=TFPI entry; URL="https://en.wikipedia.org/wiki/TFPI"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/tfpi/"; endopeptidase inhibitor activity serine-type endopeptidase inhibitor activity extracellular region extracellular space endoplasmic reticulum plasma membrane caveola blood coagulation blood coagulation, extrinsic pathway hemostasis cell surface negative regulation of peptidase activity negative regulation of endopeptidase activity membrane negative regulation of blood coagulation peptidase inhibitor activity organelle membrane anchored component of membrane response to estradiol response to lipopolysaccharide intracellular membrane-bounded organelle cellular response to lipopolysaccharide cellular response to interleukin-1 cellular response to steroid hormone stimulus uc002upy.1 uc002upy.2 uc002upy.3 uc002upy.4 uc002upy.5 uc002upy.6 
ENST00000233190.11 NDUFS1 ENST00000233190.11 NADH:ubiquinone oxidoreductase core subunit S1, transcript variant 1 (from RefSeq NM_005006.7) B4DIN9 B4DJA0 B4DPG1 B4DUC1 E7ENF3 ENST00000233190.1 ENST00000233190.10 ENST00000233190.2 ENST00000233190.3 ENST00000233190.4 ENST00000233190.5 ENST00000233190.6 ENST00000233190.7 ENST00000233190.8 ENST00000233190.9 NDUS1_HUMAN NM_005006 P28331 Q53TR8 Q8N1C4 Q8TCC9 uc002vbe.1 uc002vbe.2 uc002vbe.3 uc002vbe.4 uc002vbe.5 The protein encoded by this gene belongs to the complex I 75 kDa subunit family. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This protein is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. Mutations in this gene are associated with complex I deficiency. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2011]. Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:30879903, PubMed:31557978). Essential for catalysing the entry and efficient transfer of electrons within complex I (PubMed:31557978). Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (PubMed:30879903, PubMed:31557978). Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence=; Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence=; Note=Binds 1 [2Fe-2S] cluster per subunit. ; Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence=; Note=Binds 2 [4Fe-4S] clusters per subunit. ; Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits (PubMed:12611891). This is the largest subunit of complex I and it is a component of the iron- sulfur (IP) fragment of the enzyme (By similarity). Complex I associates with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (PubMed:30879903, PubMed:31557978). Interacts with MDM2 (PubMed:30879903). Interacts with AKAP1 (By similarity). P28331; Q99650: OSMR; NbExp=4; IntAct=EBI-1043922, EBI-2804080; P28331-2; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-6190702, EBI-741210; P28331-2; Q96MW5: COG8; NbExp=3; IntAct=EBI-6190702, EBI-720875; P28331-2; P24310: COX7A1; NbExp=3; IntAct=EBI-6190702, EBI-25876196; P28331-2; Q14154: DELE1; NbExp=3; IntAct=EBI-6190702, EBI-2805660; P28331-2; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-6190702, EBI-724653; P28331-2; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-6190702, EBI-25835236; P28331-2; Q99871: HAUS7; NbExp=3; IntAct=EBI-6190702, EBI-395719; P28331-2; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-6190702, EBI-739493; P28331-2; Q13887: KLF5; NbExp=3; IntAct=EBI-6190702, EBI-2696013; P28331-2; Q92615: LARP4B; NbExp=3; IntAct=EBI-6190702, EBI-1052558; P28331-2; Q9BV99: LRRC61; NbExp=3; IntAct=EBI-6190702, EBI-2350424; P28331-2; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-6190702, EBI-8487781; P28331-2; Q13562: NEUROD1; NbExp=3; IntAct=EBI-6190702, EBI-3908303; P28331-2; P22061-2: PCMT1; NbExp=3; IntAct=EBI-6190702, EBI-12386584; P28331-2; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-6190702, EBI-17438286; P28331-5; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-25876328, EBI-18924329; P28331-5; P42858: HTT; NbExp=6; IntAct=EBI-25876328, EBI-466029; P28331-5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25876328, EBI-10975473; P28331-5; O76024: WFS1; NbExp=3; IntAct=EBI-25876328, EBI-720609; Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=P28331-1; Sequence=Displayed; Name=2; IsoId=P28331-2; Sequence=VSP_042682; Name=3; IsoId=P28331-3; Sequence=VSP_043728, VSP_043729; Name=4; IsoId=P28331-4; Sequence=VSP_043727; Name=5; IsoId=P28331-5; Sequence=VSP_045864; Mitochondrial complex I deficiency, nuclear type 5 (MC1DN5) [MIM:618226]: A form of mitochondrial complex I deficiency, the most common biochemical signature of mitochondrial disorders, a group of highly heterogeneous conditions characterized by defective oxidative phosphorylation, which collectively affects 1 in 5-10000 live births. Clinical disorders have variable severity, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. MC1DN5 transmission pattern is consistent with autosomal recessive inheritance. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the complex I 75 kDa subunit family. NADH dehydrogenase activity protein binding mitochondrion mitochondrial inner membrane mitochondrial respiratory chain complex I mitochondrial intermembrane space mitochondrial matrix mitochondrial electron transport, NADH to ubiquinone NADH dehydrogenase (ubiquinone) activity apoptotic mitochondrial changes electron carrier activity membrane oxidoreductase activity oxidoreductase activity, acting on NAD(P)H mitochondrial respiratory chain complex I assembly ATP synthesis coupled electron transport cellular respiration ATP metabolic process metal ion binding iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding 4 iron, 4 sulfur cluster binding regulation of mitochondrial membrane potential oxidation-reduction process respiratory chain reactive oxygen species metabolic process uc002vbe.1 uc002vbe.2 uc002vbe.3 uc002vbe.4 uc002vbe.5 
ENST00000233202.11 SLC11A1 ENST00000233202.11 solute carrier family 11 member 1 (from RefSeq NM_000578.4) C0H5Y3 ENST00000233202.1 ENST00000233202.10 ENST00000233202.2 ENST00000233202.3 ENST00000233202.4 ENST00000233202.5 ENST00000233202.6 ENST00000233202.7 ENST00000233202.8 ENST00000233202.9 LSH NM_000578 NRAM1_HUMAN NRAMP NRAMP1 P49279 SLC11A1 uc002vhv.1 uc002vhv.2 uc002vhv.3 uc002vhv.4 This gene is a member of the solute carrier family 11 (proton-coupled divalent metal ion transporters) family and encodes a multi-pass membrane protein. The protein functions as a divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Mutations in this gene have been associated with susceptibility to infectious diseases such as tuberculosis and leprosy, and inflammatory diseases such as rheumatoid arthritis and Crohn disease. Alternatively spliced variants that encode different protein isoforms have been described but the full-length nature of only one has been determined. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803613.36007.1, D50402.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA2142363 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233202.11/ ENSP00000233202.6 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Macrophage-specific antiporter that fluxes metal ions in either direction against a proton gradient. Localized to late endosomal lysosomal membranes, delivers bivalent cations from the cytosol into these acidic compartments where they may directly affect antimicrobial activity (PubMed:11237855). Involved in iron metabolism and host natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes (Probable). Reaction=H(+)(out) + Zn(2+)(in) = H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:28839, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence=; Reaction=Fe(2+)(in) + H(+)(out) = Fe(2+)(out) + H(+)(in); Xref=Rhea:RHEA:29439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033; Evidence=; Reaction=H(+)(out) + Mn(2+)(in) = H(+)(in) + Mn(2+)(out); Xref=Rhea:RHEA:73063, ChEBI:CHEBI:15378, ChEBI:CHEBI:29035; Evidence=; Late endosome membrane ; Multi-pass membrane protein Lysosome membrane ; Multi- pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49279-1; Sequence=Displayed; Name=2; IsoId=P49279-2; Sequence=VSP_047875, VSP_047876; Macrophages; peripheral blood leukocytes, lung, spleen and liver. In response to lymphokine or bacterial products. Genetic variation in SLC11A1 is associated with susceptibility to infection with Mycobacterium ulcerans [MIM:610446]. Genetic variations in SLC11A1 determine Mycobacterium tuberculosis susceptibility [MIM:607948]. Belongs to the NRAMP family. negative regulation of cytokine production positive regulation of cytokine production T cell proliferation involved in immune response T cell cytokine production positive regulation of dendritic cell antigen processing and presentation positive regulation of T-helper 1 type immune response iron ion transmembrane transporter activity manganese ion transmembrane transporter activity lysosome late endosome plasma membrane integral component of plasma membrane ion transport iron ion transport manganese ion transport cellular cadmium ion homeostasis cellular iron ion homeostasis phagocytosis inflammatory response vacuolar acidification response to bacterium endosome membrane positive regulation of gene expression cadmium ion transmembrane transporter activity nitrite transport membrane integral component of membrane antimicrobial humoral response metal ion transport phagocytic vesicle membrane late endosome membrane activation of protein kinase activity response to lipopolysaccharide interleukin-2 production interleukin-3 production positive regulation of interferon-gamma production response to interferon-gamma iron ion transmembrane transport wound healing macrophage activation defense response to bacterium protein homodimerization activity defense response to protozoan neutrophil degranulation MHC class II biosynthetic process cell redox homeostasis respiratory burst positive regulation of transcription from RNA polymerase II promoter metal ion transmembrane transporter activity transition metal ion transmembrane transporter activity antigen processing and presentation of peptide antigen mRNA stabilization positive regulation of phagocytosis defense response to Gram-negative bacterium metal ion:proton antiporter activity iron ion homeostasis multicellular organismal iron ion homeostasis cadmium ion transmembrane transport tertiary granule membrane divalent metal ion export manganese ion transmembrane transport ficolin-1-rich granule membrane L-arginine transport uc002vhv.1 uc002vhv.2 uc002vhv.3 uc002vhv.4 
ENST00000233242.5 APOB ENST00000233242.5 apolipoprotein B (from RefSeq NM_000384.3) APOB_HUMAN ENST00000233242.1 ENST00000233242.2 ENST00000233242.3 ENST00000233242.4 NM_000384 O00502 P04114 P78479 P78480 P78481 Q13779 Q13785 Q13786 Q13787 Q13788 Q4ZG63 Q53QC8 Q7Z600 Q9UMN0 uc002red.1 uc002red.2 uc002red.3 This gene product is the main apolipoprotein of chylomicrons and low density lipoproteins (LDL), and is the ligand for the LDL receptor. It occurs in plasma as two main isoforms, apoB-48 and apoB-100: the former is synthesized exclusively in the gut and the latter in the liver. The intestinal and the hepatic forms of apoB are encoded by a single gene from a single, very long mRNA. The two isoforms share a common N-terminal sequence. The shorter apoB-48 protein is produced after RNA editing of the apoB-100 transcript at residue 2180 (CAA->UAA), resulting in the creation of a stop codon, and early translation termination. Mutations in this gene or its regulatory region cause hypobetalipoproteinemia, normotriglyceridemic hypobetalipoproteinemia, and hypercholesterolemia due to ligand-defective apoB, diseases affecting plasma cholesterol and apoB levels. [provided by RefSeq, Dec 2019]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X04506.1, HM487065.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN04284274 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233242.5/ ENSP00000233242.1 RefSeq Select criteria :: based on single protein-coding transcript undergoes RNA editing :: PMID: 16920700, 11727199 ##RefSeq-Attributes-END## Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B- 100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor. Interacts with PCSK9 (PubMed:22580899). Interacts with MTTP (PubMed:26224785, PubMed:27206948). Interacts with AUP1 (PubMed:28183703). Interacts with CIDEB (By similarity). P04114; P01130: LDLR; NbExp=4; IntAct=EBI-3926040, EBI-988319; P04114; P55157: MTTP; NbExp=4; IntAct=EBI-3926040, EBI-11614052; P04114; PRO_0000037946 [P29991]; Xeno; NbExp=3; IntAct=EBI-3926040, EBI-8826488; Cytoplasm Secreted Lipid droplet Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. Modified_positions=2180; Note=The stop codon (UAA) at position 2180 is created by an APOBEC1-containing mRNA editing complex. Apo B-48, derived from the fully edited RNA, is produced only in the intestine and is found in chylomicrons. Apo B-48 is a shortened form of apo B-100 which lacks the LDL-receptor region. The unedited version (apo B-100) is produced by the liver and is found in the VLDL and LDL. Genetic variations in APOB define the low density lipoprotein cholesterol level quantitative trait locus 4 (LDLCQ4) [MIM:615558]. Hypobetalipoproteinemia, familial, 1 (FHBL1) [MIM:615558]: A disorder of lipid metabolism characterized by less than 5th percentile age- and sex-specific levels of low density lipoproteins, and dietary fat malabsorption. Clinical presentation may vary from no symptoms to severe gastrointestinal and neurological dysfunction similar to abetalipoproteinemia. te=The disease is caused by variants affecting the gene represented in this entry. Most cases of FHBL1 result from nonsense mutations in the APOB gene that lead to a premature stop codon, which generate prematurely truncated apo B protein products (PubMed:21981844). Hypercholesterolemia, familial, 2 (FHCL2) [MIM:144010]: A form of hypercholesterolemia, a disorder of lipoprotein metabolism characterized by elevated serum low-density lipoprotein (LDL) cholesterol levels, which result in excess deposition of cholesterol in tissues and leads to xanthelasma, xanthomas, accelerated atherosclerosis and increased risk of premature coronary heart disease. FHCL2 inheritance is autosomal dominant. te=The disease is caused by variants affecting the gene represented in this entry. Note=Defects in APOB associated with defects in other genes (polygenic) can contribute to hypocholesterolemia. Sequence=AAA51752.1; Type=Frameshift; Evidence=; Name=Wikipedia; Note=Apolipoprotein B entry; URL="https://en.wikipedia.org/wiki/Apolipoprotein_B"; retinoid metabolic process in utero embryonic development toll-like receptor signaling pathway lipid transporter activity protein binding phospholipid binding extracellular region extracellular space cytoplasm early endosome endoplasmic reticulum endoplasmic reticulum lumen endoplasmic reticulum membrane smooth endoplasmic reticulum cytosol plasma membrane lipid metabolic process triglyceride mobilization lipid transport receptor-mediated endocytosis spermatogenesis nervous system development heparin binding steroid metabolic process cholesterol metabolic process fertilization response to virus response to carbohydrate post-embryonic development endosome membrane response to organic substance response to selenium ion positive regulation of gene expression positive regulation of macrophage derived foam cell differentiation positive regulation of lipid storage positive regulation of cholesterol storage vesicle membrane lipid catabolic process triglyceride catabolic process cholesterol transport flagellated sperm motility clathrin-coated endocytic vesicle membrane endosome lumen vesicle lumen response to estradiol response to lipopolysaccharide cholesterol efflux mature chylomicron chylomicron remnant very-low-density lipoprotein particle low-density lipoprotein particle intermediate-density lipoprotein particle high-density lipoprotein particle chylomicron remodeling low-density lipoprotein particle remodeling chylomicron assembly very-low-density lipoprotein particle assembly chylomicron remnant clearance low-density lipoprotein particle clearance very-low-density lipoprotein particle clearance lipase binding lipoprotein metabolic process lipoprotein biosynthetic process lipoprotein catabolic process chylomicron cholesterol homeostasis lipoprotein transport neuronal cell body lysosomal lumen intracellular membrane-bounded organelle post-translational protein modification cellular protein metabolic process regulation of cholesterol biosynthetic process artery morphogenesis low-density lipoprotein particle receptor binding leukocyte migration membrane organization extracellular exosome endoplasmic reticulum exit site cellular response to tumor necrosis factor cellular response to prostaglandin stimulus endocytic vesicle lumen uc002red.1 uc002red.2 uc002red.3 
ENST00000233331.12 INO80B ENST00000233331.12 INO80 complex subunit B (from RefSeq NM_031288.4) ENST00000233331.1 ENST00000233331.10 ENST00000233331.11 ENST00000233331.2 ENST00000233331.3 ENST00000233331.4 ENST00000233331.5 ENST00000233331.6 ENST00000233331.7 ENST00000233331.8 ENST00000233331.9 HMGA1L4 IN80B_HUMAN NM_031288 PAPA1 Q9C086 ZNHIT4 uc002slg.1 uc002slg.2 uc002slg.3 uc002slg.4 This gene encodes a subunit of an ATP-dependent chromatin remodeling complex, INO80, which plays a role in DNA and nucleosome-activated ATPase activity and ATP-dependent nucleosome sliding. Readthrough transcription of this gene into the neighboring downstream gene, which encodes WW domain-binding protein 1, generates a non-coding transcript. [provided by RefSeq, Feb 2011]. ##Evidence-Data-START## Transcript exon combination :: BC064425.1, ERR279845.3562.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233331.12/ ENSP00000233331.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Induces growth and cell cycle arrests at the G1 phase of the cell cycle. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP- binding and the helicase C-terminal domain of INO80. Interacts with RP9. Q9C086; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-715611, EBI-11096309; Q9C086; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-715611, EBI-11524452; Q9C086; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-715611, EBI-2548012; Q9C086; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-715611, EBI-11983447; Q9C086; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-715611, EBI-11530605; Q9C086; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-715611, EBI-2559016; Q9C086; Q15834: CCDC85B; NbExp=3; IntAct=EBI-715611, EBI-739674; Q9C086; Q01850: CDR2; NbExp=3; IntAct=EBI-715611, EBI-1181367; Q9C086; Q86X02: CDR2L; NbExp=3; IntAct=EBI-715611, EBI-11063830; Q9C086; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-715611, EBI-739624; Q9C086; P67870: CSNK2B; NbExp=3; IntAct=EBI-715611, EBI-348169; Q9C086; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-715611, EBI-3867333; Q9C086; Q7L190: DPPA4; NbExp=3; IntAct=EBI-715611, EBI-710457; Q9C086; Q92997: DVL3; NbExp=3; IntAct=EBI-715611, EBI-739789; Q9C086; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-715611, EBI-11533409; Q9C086; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-715611, EBI-5916454; Q9C086; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-715611, EBI-11519926; Q9C086; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-715611, EBI-2549423; Q9C086; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-715611, EBI-7261162; Q9C086; P49639: HOXA1; NbExp=5; IntAct=EBI-715611, EBI-740785; Q9C086; O75031: HSF2BP; NbExp=3; IntAct=EBI-715611, EBI-7116203; Q9C086; P18065: IGFBP2; NbExp=4; IntAct=EBI-715611, EBI-2504392; Q9C086; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-715611, EBI-2556193; Q9C086; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-715611, EBI-11954971; Q9C086; O76011: KRT34; NbExp=3; IntAct=EBI-715611, EBI-1047093; Q9C086; Q6A162: KRT40; NbExp=3; IntAct=EBI-715611, EBI-10171697; Q9C086; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-715611, EBI-10171774; Q9C086; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-715611, EBI-10176379; Q9C086; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-715611, EBI-12811111; Q9C086; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-715611, EBI-11962084; Q9C086; Q969G2: LHX4; NbExp=3; IntAct=EBI-715611, EBI-2865388; Q9C086; P48059-3: LIMS1; NbExp=3; IntAct=EBI-715611, EBI-12864460; Q9C086; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-715611, EBI-741037; Q9C086; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-715611, EBI-10172526; Q9C086; Q13064: MKRN3; NbExp=3; IntAct=EBI-715611, EBI-2340269; Q9C086; Q6PF18: MORN3; NbExp=3; IntAct=EBI-715611, EBI-9675802; Q9C086; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-715611, EBI-11522433; Q9C086; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-715611, EBI-6952711; Q9C086; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-715611, EBI-22310682; Q9C086; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-715611, EBI-79165; Q9C086; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-715611, EBI-11532361; Q9C086; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-715611, EBI-2876622; Q9C086; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-715611, EBI-302345; Q9C086; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-715611, EBI-302355; Q9C086; Q14498: RBM39; NbExp=3; IntAct=EBI-715611, EBI-395290; Q9C086; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-715611, EBI-10182375; Q9C086; Q9UN79: SOX13; NbExp=3; IntAct=EBI-715611, EBI-3928516; Q9C086; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-715611, EBI-2212028; Q9C086; Q96MF2: STAC3; NbExp=3; IntAct=EBI-715611, EBI-745680; Q9C086; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-715611, EBI-741515; Q9C086; Q08117-2: TLE5; NbExp=5; IntAct=EBI-715611, EBI-11741437; Q9C086; Q63HR2: TNS2; NbExp=3; IntAct=EBI-715611, EBI-949753; Q9C086; Q12933: TRAF2; NbExp=3; IntAct=EBI-715611, EBI-355744; Q9C086; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-715611, EBI-492476; Q9C086; P14373: TRIM27; NbExp=3; IntAct=EBI-715611, EBI-719493; Q9C086; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-715611, EBI-947459; Q9C086; P26368-2: U2AF2; NbExp=3; IntAct=EBI-715611, EBI-11097439; Q9C086; Q495M9: USH1G; NbExp=3; IntAct=EBI-715611, EBI-8601749; Q9C086; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-715611, EBI-12111538; Q9C086; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-715611, EBI-11035148; Q9C086; Q9H707: ZNF552; NbExp=3; IntAct=EBI-715611, EBI-2555731; Q9C086; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-715611, EBI-527853; Nucleus cleus, nucleolus Sequence=BAB21111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; protein binding nucleus nucleoplasm nucleolus DNA repair DNA recombination chromatin remodeling cellular response to DNA damage stimulus protein deubiquitination Ino80 complex metal ion binding uc002slg.1 uc002slg.2 uc002slg.3 uc002slg.4 
ENST00000233336.7 TTL ENST00000233336.7 tubulin tyrosine ligase, transcript variant 1 (from RefSeq NM_153712.5) ENST00000233336.1 ENST00000233336.2 ENST00000233336.3 ENST00000233336.4 ENST00000233336.5 ENST00000233336.6 NM_153712 Q585T3 Q7Z302 Q8N426 Q8NG68 TTL_HUMAN uc002thu.1 uc002thu.2 uc002thu.3 uc002thu.4 uc002thu.5 TTL is a cytosolic enzyme involved in the posttranslational modification of alpha-tubulin (see MIM 602529). Alpha-tubulin within assembled microtubules is detyrosinated over time at the C terminus. After microtubule disassembly, TTL restores the tyrosine residues and consequently participates in a cycle of tubulin detyrosination and tyrosination (Erck et al., 2003 [PubMed 14571137]).[supplied by OMIM, Mar 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1803616.85951.1, SRR1803616.219745.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233336.7/ ENSP00000233336.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin. Reaction=ATP + C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl- [tubulin] + L-tyrosine = ADP + C-terminal L-alpha-aminoacyl-L- glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H(+) + phosphate; Xref=Rhea:RHEA:17605, Rhea:RHEA-COMP:16434, Rhea:RHEA-COMP:16435, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58315, ChEBI:CHEBI:149554, ChEBI:CHEBI:149555, ChEBI:CHEBI:456216; EC=6.3.2.25; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence=; Monomer. Belongs to the tubulin--tyrosine ligase family. nucleotide binding microtubule cytoskeleton organization tubulin-tyrosine ligase activity ATP binding cell cellular protein modification process ligase activity C-terminal protein-tyrosinylation regulation of axon extension positive regulation of mitotic cell cycle regulation of metaphase plate congression uc002thu.1 uc002thu.2 uc002thu.3 uc002thu.4 uc002thu.5 
ENST00000233379.9 FAHD2A ENST00000233379.9 fumarylacetoacetate hydrolase domain containing 2A (from RefSeq NM_016044.3) CGI-105 ENST00000233379.1 ENST00000233379.2 ENST00000233379.3 ENST00000233379.4 ENST00000233379.5 ENST00000233379.6 ENST00000233379.7 ENST00000233379.8 FAH2A_HUMAN NM_016044 Q96GK7 Q9Y3B0 uc002sut.1 uc002sut.2 uc002sut.3 May have hydrolase activity. Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Q96GK7; P27797: CALR; NbExp=3; IntAct=EBI-21647872, EBI-1049597; Q96GK7; P36957: DLST; NbExp=3; IntAct=EBI-21647872, EBI-351007; Q96GK7; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-21647872, EBI-1055945; Belongs to the FAH family. catalytic activity hydrolase activity metal ion binding uc002sut.1 uc002sut.2 uc002sut.3 
ENST00000233468.5 SF3B6 ENST00000233468.5 splicing factor 3b subunit 6 (from RefSeq NM_016047.4) CGI-110 ENST00000233468.1 ENST00000233468.2 ENST00000233468.3 ENST00000233468.4 HSPC175 HT006 NM_016047 Q53TM1 Q9Y3B4 SAP14 SF3B14 SF3B14A SF3B6_HUMAN uc002rev.1 uc002rev.2 uc002rev.3 uc002rev.4 uc002rev.5 This gene encodes a 14 kDa protein subunit of the splicing factor 3b complex. Splicing factor 3b associates with both the U2 and U11/U12 small nuclear ribonucleoprotein complexes (U2 snRNP) of spliceosomes. This 14 kDa protein interacts directly with subunit 1 of the splicing factor 3b complex. This 14 kDa protein also interacts directly with the adenosine that carries out the first transesterification step of splicing at the pre-mRNA branch site. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.172119.1, SRR1163657.34312.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233468.5/ ENSP00000233468.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:27720643, PubMed:12234937, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B6 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:27720643). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). Within the 17S U2 SnRNP complex, SF3B6 directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing (PubMed:16432215). SF3B6 stabilizes the intron branch site-U2 snRNA duplex, thereby promoting- binding of introns with poor sequence complementarity (PubMed:34822310). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:12234937, PubMed:15146077, PubMed:32494006, PubMed:34822310). Part of the SF3B subcomplex of the 17S U2 SnRNP complex (PubMed:12234937, PubMed:12738865, PubMed:28541300, PubMed:16432215, PubMed:27720643). SF3B associates with the splicing subcomplex SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP) (PubMed:12234937). Within the SF3B complex interacts directly with SF3B1 (PubMed:16432215, PubMed:21062891, Ref.20). Component of the minor spliceosome, which splices U12-type introns (PubMed:15146077, PubMed:33509932). Q9Y3B4; O75533-1: SF3B1; NbExp=3; IntAct=EBI-1046261, EBI-15565798; Nucleus Belongs to the SF3B6 family. mRNA splicing, via spliceosome blastocyst formation nucleic acid binding RNA binding mRNA binding protein binding nucleus nucleoplasm spliceosomal complex U12-type spliceosomal complex mRNA processing RNA splicing uc002rev.1 uc002rev.2 uc002rev.3 uc002rev.4 uc002rev.5 
ENST00000233535.9 SLC30A3 ENST00000233535.9 solute carrier family 30 member 3, transcript variant 1 (from RefSeq NM_003459.5) ENST00000233535.1 ENST00000233535.2 ENST00000233535.3 ENST00000233535.4 ENST00000233535.5 ENST00000233535.6 ENST00000233535.7 ENST00000233535.8 NM_003459 Q8TC03 Q99726 SLC30A3 ZNT3 ZNT3_HUMAN uc002rjk.1 uc002rjk.2 uc002rjk.3 uc002rjk.4 uc002rjk.5 Probable proton-coupled zinc ion antiporter mediating the import of zinc from cytoplasm into synaptic vesicles and participating to cellular zinc ion homeostasis in the brain. Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence= Homodimer; dityrosine-linked. Homodimerization seems specific of the human protein and enhances the zinc transport efficiency. Interacts with TMEM163 (PubMed:36204728). Q99726; P25942: CD40; NbExp=3; IntAct=EBI-10294651, EBI-525714; Q99726; Q99675: CGRRF1; NbExp=3; IntAct=EBI-10294651, EBI-2130213; Q99726; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-10294651, EBI-18535450; Q99726; Q96P31-6: FCRL3; NbExp=3; IntAct=EBI-10294651, EBI-17443171; Q99726; P48165: GJA8; NbExp=3; IntAct=EBI-10294651, EBI-17458373; Q99726; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-10294651, EBI-712073; Q99726; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10294651, EBI-13345167; Q99726; O15529: GPR42; NbExp=3; IntAct=EBI-10294651, EBI-18076404; Q99726; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10294651, EBI-11721746; Q99726; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-10294651, EBI-18053395; Q99726; Q58DX5: NAALADL2; NbExp=3; IntAct=EBI-10294651, EBI-10178964; Q99726; Q9NX40: OCIAD1; NbExp=3; IntAct=EBI-10294651, EBI-2683029; Q99726; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-10294651, EBI-10192441; Q99726; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-10294651, EBI-2466594; Q99726; O95197-3: RTN3; NbExp=3; IntAct=EBI-10294651, EBI-11525735; Q99726; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-10294651, EBI-17247926; Q99726; O95470: SGPL1; NbExp=3; IntAct=EBI-10294651, EBI-1046170; Q99726; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-10294651, EBI-18159983; Q99726; Q6XR72: SLC30A10; NbExp=3; IntAct=EBI-10294651, EBI-13917996; Q99726; Q9BRI3: SLC30A2; NbExp=7; IntAct=EBI-10294651, EBI-8644112; Q99726; O14863: SLC30A4; NbExp=8; IntAct=EBI-10294651, EBI-13918058; Q99726; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-10294651, EBI-10262251; Q99726; O95436-2: SLC34A2; NbExp=5; IntAct=EBI-10294651, EBI-12811757; Q99726; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-10294651, EBI-17295964; Q99726; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10294651, EBI-8638294; Q99726; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-10294651, EBI-10315004; Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Multi-pass membrane protein Synapse, synaptosome Late endosome membrane ; Multi-pass membrane protein Lysosome membrane ; Multi- pass membrane protein Homodimerization through dityrosine bonds is stimulated by oxidative stress. Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily. zinc ion transmembrane transporter activity protein binding cytoplasm lysosome lysosomal membrane endosome late endosome plasma membrane integral component of plasma membrane ion transport cation transport zinc II ion transport synaptic vesicle cation transmembrane transporter activity response to zinc ion zinc-transporting ATPase activity membrane integral component of membrane cell junction integral component of synaptic vesicle membrane synaptic vesicle membrane cytoplasmic vesicle late endosome membrane neuron projection synapse positive regulation of transport transmembrane transport regulation of sequestering of zinc ion zinc II ion transmembrane transport glutamatergic synapse uc002rjk.1 uc002rjk.2 uc002rjk.3 uc002rjk.4 uc002rjk.5 
ENST00000233575.7 SNX17 ENST00000233575.7 sorting nexin 17, transcript variant 5 (from RefSeq NR_049782.2) B4DQM7 ENST00000233575.1 ENST00000233575.2 ENST00000233575.3 ENST00000233575.4 ENST00000233575.5 ENST00000233575.6 KIAA0064 NR_049782 Q15036 Q53HN7 Q6IAS3 SNX17_HUMAN uc002rkg.1 uc002rkg.2 uc002rkg.3 uc002rkg.4 This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein does not contain a coiled coil region, like some family members, but contains a B41 domain. This protein interacts with the cytoplasmic domain of P-selectin, and may function in the intracellular trafficking of P-selectin. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, May 2012]. Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels (PubMed:15121882, PubMed:15769472). Binds to NPxY sequences in the cytoplasmic tails of target cargos (PubMed:21512128). Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits (PubMed:28892079, PubMed:22492727). Also required for maintenance of normal cell surface levels of APP and LRP1 (PubMed:16712798, PubMed:19005208). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:16712798). Monomer (PubMed:21512128). Interacts with APP (via cytoplasmic YXNPXY motif) (By similarity). Interacts with KIF1B (By similarity). Interacts with the C-termini of P-selectin, PTC, LDLR, VLDLR, LRP1 and LRP8 (PubMed:11237770, PubMed:14739284, PubMed:15769472, PubMed:19005208). Interacts with KRIT1 (via N-terminus) (PubMed:16712798). Interacts with HRAS (PubMed:21512128). Interacts with ITGB1 and ITGB5 (via NPxY motif) (PubMed:22492727). Interacts with CCDC22, CCDC93, VPS26C and VPS35L; the interaction with VPS26C is direct and associates SNX17 with the retriever and CCC complexes (PubMed:28892079). Q15036; P05067: APP; NbExp=3; IntAct=EBI-1752620, EBI-77613; Q15036; P31273: HOXC8; NbExp=8; IntAct=EBI-1752620, EBI-1752118; Q15036; P16333: NCK1; NbExp=3; IntAct=EBI-1752620, EBI-389883; Q15036; P19174: PLCG1; NbExp=2; IntAct=EBI-1752620, EBI-79387; Q15036; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-1752620, EBI-712367; Q15036; Q13671: RIN1; NbExp=3; IntAct=EBI-1752620, EBI-366017; Q15036; Q8TEB7: RNF128; NbExp=3; IntAct=EBI-1752620, EBI-2341619; Cytoplasm rly endosome toplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q15036-1; Sequence=Displayed; Name=2; IsoId=Q15036-2; Sequence=VSP_044935; The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). Required for association with endosomes. The PTB-like F3 module within the FERM-like domain mediates cargo recognition via their NPxY sequences, while the F1 module (Ras- associating) is responsible for interaction with membrane-bound HRAS. Belongs to the sorting nexin family. Sequence=BAA06542.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; cardiac septum development receptor binding protein binding cytoplasm endosome early endosome Golgi apparatus cytosol cholesterol catabolic process intracellular protein transport receptor-mediated endocytosis signal transduction protein C-terminus binding lipid binding endosome membrane protein transport membrane endosomal transport regulation of endocytosis cytoplasmic vesicle membrane cytoplasmic vesicle endocytic recycling macromolecular complex phosphatidylinositol binding aorta development intracellular membrane-bounded organelle low-density lipoprotein particle receptor binding coronary vasculature development retrograde transport, endosome to plasma membrane uc002rkg.1 uc002rkg.2 uc002rkg.3 uc002rkg.4 
ENST00000233615.7 WBP1 ENST00000233615.7 WW domain binding protein 1 (from RefSeq NM_012477.4) B2RE02 ENST00000233615.1 ENST00000233615.2 ENST00000233615.3 ENST00000233615.4 ENST00000233615.5 ENST00000233615.6 NM_012477 O95637 Q96G27 WBP1_HUMAN uc002slj.1 uc002slj.2 uc002slj.3 uc002slj.4 The globular WW domain, named for the conserved tryptophan residues in the protein motif present in various structural and regulatory proteins, is known to play a role in the mediation of protein-protein interactions. This gene encodes a ligand of the WW domain of the Yes kinase-associated protein. Readthrough transcription of the neighboring upstream gene, which encodes INO80 complex subunit B, into this gene generates a non-coding transcript. [provided by RefSeq, Feb 2011]. ##Evidence-Data-START## Transcript exon combination :: BC071626.1, BC010012.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233615.7/ ENSP00000233615.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Interacts with NEDD4 (By similarity). Binds to the WW domain of YAP1, WWP1 and WWP2. Interacts with WWOX. Q96G27; O95208-2: EPN2; NbExp=3; IntAct=EBI-3867685, EBI-12135243; Q96G27; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-3867685, EBI-8640191; Q96G27; Q9NZC7: WWOX; NbExp=3; IntAct=EBI-3867685, EBI-4320739; Q96G27; P46937: YAP1; NbExp=4; IntAct=EBI-3867685, EBI-1044059; Q96G27; O75800: ZMYND10; NbExp=3; IntAct=EBI-3867685, EBI-747061; Expressed in most tissues but at significantly lower levels in placenta, lung, liver, and kidney. The PPxY motif 2 mediates interaction with WWOX. Both PPxY motifs mediate interaction with NEDD4 (By similarity). Sequence=AAD10950.1; Type=Erroneous initiation; Evidence=; protein binding cellular_component biological_process WW domain binding uc002slj.1 uc002slj.2 uc002slj.3 uc002slj.4 
ENST00000233623.11 TTC31 ENST00000233623.11 tetratricopeptide repeat domain 31, transcript variant 20 (from RefSeq NR_164773.1) ENST00000233623.1 ENST00000233623.10 ENST00000233623.2 ENST00000233623.3 ENST00000233623.4 ENST00000233623.5 ENST00000233623.6 ENST00000233623.7 ENST00000233623.8 ENST00000233623.9 NR_164773 Q49AM3 Q4KN40 Q53FD4 Q9H9F7 TTC31_HUMAN uc002slt.1 uc002slt.2 uc002slt.3 uc002slt.4 uc002slt.5 Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q49AM3-1; Sequence=Displayed; Name=2; IsoId=Q49AM3-2; Sequence=VSP_023990, VSP_023991; uc002slt.1 uc002slt.2 uc002slt.3 uc002slt.4 uc002slt.5 
ENST00000233627.14 NDUFS7 ENST00000233627.14 NADH:ubiquinone oxidoreductase core subunit S7, transcript variant 1 (from RefSeq NM_024407.5) ENST00000233627.1 ENST00000233627.10 ENST00000233627.11 ENST00000233627.12 ENST00000233627.13 ENST00000233627.2 ENST00000233627.3 ENST00000233627.4 ENST00000233627.5 ENST00000233627.6 ENST00000233627.7 ENST00000233627.8 ENST00000233627.9 NM_024407 Q7LD69 Q7LD69_HUMAN uc002lse.1 uc002lse.2 uc002lse.3 uc002lse.4 uc002lse.5 uc002lse.6 This gene encodes a protein that is a subunit of one of the complexes that forms the mitochondrial respiratory chain. This protein is one of over 40 subunits found in complex I, the nicotinamide adenine dinucleotide (NADH):ubiquinone oxidoreductase. This complex functions in the transfer of electrons from NADH to the respiratory chain, and ubiquinone is believed to be the immediate electron acceptor for the enzyme. Mutations in this gene cause Leigh syndrome due to mitochondrial complex I deficiency, a severe neurological disorder that results in bilaterally symmetrical necrotic lesions in subcortical brain regions. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK222738.1, SRR1163657.243667.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000233627.14/ ENSP00000233627.9 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence=; Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side Belongs to the complex I 20 kDa subunit family. protease binding NADH dehydrogenase (ubiquinone) activity neuron projection neuronal cell body metal ion binding quinone binding iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding oxidation-reduction process synaptic membrane uc002lse.1 uc002lse.2 uc002lse.3 uc002lse.4 uc002lse.5 uc002lse.6 
ENST00000233630.11 PCGF1 ENST00000233630.11 polycomb group ring finger 1 (from RefSeq NM_032673.3) ENST00000233630.1 ENST00000233630.10 ENST00000233630.2 ENST00000233630.3 ENST00000233630.4 ENST00000233630.5 ENST00000233630.6 ENST00000233630.7 ENST00000233630.8 ENST00000233630.9 NM_032673 NSPC1 PCGF1_HUMAN Q7Z506 Q9BSM1 RNF68 uc002slz.1 uc002slz.2 uc002slz.3 uc002slz.4 uc002slz.5 PCGF1 is a mammalian homolog of the Drosophila polycomb group genes, which act as transcriptional repressors to regulate anterior-posterior patterning in early embryonic development (Nunes et al., 2001 [PubMed 11287196]). See also PCGF2 (MIM 600346).[supplied by OMIM, Aug 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR5189667.331340.1, SRR1163655.595382.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233630.11/ ENSP00000233630.6 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Component of the Polycomb group (PcG) multiprotein BCOR complex, a complex required to maintain the transcriptionally repressive state of some genes, such as BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. Transcriptional repressor that may be targeted to the DNA by BCL6; this transcription repressor activity may be related to PKC signaling pathway. Represses CDKN1A expression by binding to its promoter, and this repression is dependent on the retinoic acid response element (RARE element). Promotes cell cycle progression and enhances cell proliferation as well. May have a positive role in tumor cell growth by down-regulating CDKN1A. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:26151332). Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (PubMed:26151332). Regulates the expression of DPPA4 and NANOG in the NT2 embryonic carcinoma cells (PubMed:26687479). Interacts with BCORL1, forming heterodimers (PubMed:23523425, PubMed:27568929). The PCGF1-BCORL1 heterodimeric complex interacts with the KDM2B-SKP1 heterodimeric complex to form a homotetrameric polycomb repression complex 1 (PRC1.1) (PubMed:27568929). Component of the repressive BCOR complex containing a Polycomb group subcomplex at least composed of RYBP, RING1 and RNF2/RING2 (PubMed:16943429). Specifically interacts with BCOR, RING1 and RNF2/RING2 (PubMed:16943429, PubMed:26687479, PubMed:23523425). Component of a PRC1-like complex (PubMed:21282530, PubMed:26151332). Interacts with CBX6, CBX7 and CBX8 (PubMed:21282530). Interacts with DPPA4, NANOG, POU5F1 and RYBP (PubMed:26687479). Q9BSM1; Q6W2J9: BCOR; NbExp=13; IntAct=EBI-749901, EBI-950027; Q9BSM1; O95931: CBX7; NbExp=2; IntAct=EBI-749901, EBI-3923843; Q9BSM1; Q9HC52: CBX8; NbExp=7; IntAct=EBI-749901, EBI-712912; Q9BSM1; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-749901, EBI-11977403; Q9BSM1; Q06587: RING1; NbExp=9; IntAct=EBI-749901, EBI-752313; Q9BSM1; Q99496: RNF2; NbExp=15; IntAct=EBI-749901, EBI-722416; Q9BSM1-1; Q6W2J9-1: BCOR; NbExp=7; IntAct=EBI-16041863, EBI-16028932; Q9BSM1-1; Q5H9F3-1: BCORL1; NbExp=6; IntAct=EBI-16041863, EBI-16041827; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BSM1-1; Sequence=Displayed; Name=2; IsoId=Q9BSM1-3; Sequence=VSP_036393; Ubiquitous. Sequence=AAH04952.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAP97183.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; negative regulation of transcription from RNA polymerase II promoter protein binding nucleus nucleoplasm chromatin silencing regulation of transcription, DNA-templated protein C-terminus binding PcG protein complex PRC1 complex histone H2A monoubiquitination histone H2A-K119 monoubiquitination metal ion binding promoter-specific chromatin binding uc002slz.1 uc002slz.2 uc002slz.3 uc002slz.4 uc002slz.5 
ENST00000233638.8 TLX2 ENST00000233638.8 T cell leukemia homeobox 2 (from RefSeq NM_016170.5) ENST00000233638.1 ENST00000233638.2 ENST00000233638.3 ENST00000233638.4 ENST00000233638.5 ENST00000233638.6 ENST00000233638.7 HOX11L1 NCX NM_016170 O43763 Q9UD56 Q9UQ48 TLX2_HUMAN uc002smb.1 uc002smb.2 uc002smb.3 uc002smb.4 This gene is a member of an orphan homeobox-containing transcription factor family. Studies of the mouse ortholog have shown that the encoded protein is crucial for the development of the enteric nervous system; in humans, loss-of-function may play a role in tumorigenesis of gastrointestinal stromal tumors. [provided by RefSeq, May 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC006356.2, AB008501.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2161674 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233638.8/ ENSP00000233638.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcription activator that binds DNA elements with the consensus sequence 5'-CGGTAATTGG-3'. Binds DNA via its homeobox. Required for normal cell death of enteric neurons in the gastrointestinal tract. Required for normal development of the enteric nervous system, and for proper development of normal motility of the gastrointestinal tract (By similarity). O43763; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-6101484, EBI-11962084; O43763; P78424: POU6F2; NbExp=3; IntAct=EBI-6101484, EBI-12029004; Nucleus nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding mesoderm formation DNA binding transcription factor activity, sequence-specific DNA binding cellular_component nucleus cytoplasm regulation of transcription, DNA-templated multicellular organism development sequence-specific DNA binding positive regulation of transcription from RNA polymerase II promoter enteric nervous system development negative regulation of dendrite morphogenesis uc002smb.1 uc002smb.2 uc002smb.3 uc002smb.4 
ENST00000233668.10 DOK1 ENST00000233668.10 docking protein 1, transcript variant 1 (from RefSeq NM_001381.5) DOK1_HUMAN ENST00000233668.1 ENST00000233668.2 ENST00000233668.3 ENST00000233668.4 ENST00000233668.5 ENST00000233668.6 ENST00000233668.7 ENST00000233668.8 ENST00000233668.9 NM_001381 O43204 Q53TY2 Q99704 Q9UHG6 uc002sms.1 uc002sms.2 uc002sms.3 uc002sms.4 uc002sms.5 The protein encoded by this gene is part of a signal transduction pathway downstream of receptor tyrosine kinases. The encoded protein is a scaffold protein that helps form a platform for the assembly of multiprotein signaling complexes. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK055944.1, SRR1163655.92502.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. Interacts with ABL1 (By similarity). Interacts with RasGAP and INPP5D/SHIP1. Interacts directly with phosphorylated ITGB3. Interacts with SRMS (via the SH2 and SH3 domains). Q99704; P04626: ERBB2; NbExp=2; IntAct=EBI-1384360, EBI-641062; Q99704; Q9H3Y6: SRMS; NbExp=7; IntAct=EBI-1384360, EBI-8541270; Q99704; Q9JIY2: Cbll1; Xeno; NbExp=2; IntAct=EBI-1384360, EBI-7644904; Q99704; Q9Q2G4: ORF; Xeno; NbExp=2; IntAct=EBI-1384360, EBI-6248094; [Isoform 1]: Cytoplasm. Nucleus. [Isoform 3]: Cytoplasm, perinuclear region. Event=Alternative splicing, Alternative initiation; Named isoforms=3; Name=1; Synonyms=p62Dok1; IsoId=Q99704-1; Sequence=Displayed; Name=2; Synonyms=p22Dokdel; IsoId=Q99704-2; Sequence=VSP_003852, VSP_003853; Name=3; Synonyms=p44Dok; IsoId=Q99704-3; Sequence=VSP_038224; Expressed in pancreas, heart, leukocyte and spleen. Expressed in both resting and activated peripheral blood T-cells. Expressed in breast cancer. The PTB domain mediates receptor interaction. Constitutively tyrosine-phosphorylated. Phosphorylated by TEC (By similarity). Phosphorylated by LYN (By similarity). Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway. Phosphorylated on tyrosine residues by SRMS. [Isoform 3]: Produced by alternative initiation at Met- 140 of isoform 1. Belongs to the DOK family. Type A subfamily. protein binding nucleus cytoplasm cytosol signal transduction cell surface receptor signaling pathway transmembrane receptor protein tyrosine kinase signaling pathway Ras protein signal transduction axon guidance intracellular signal transduction macrophage colony-stimulating factor signaling pathway positive regulation of epidermal growth factor receptor signaling pathway perinuclear region of cytoplasm uc002sms.1 uc002sms.2 uc002sms.3 uc002sms.4 uc002sms.5 
ENST00000233710.4 ACADL ENST00000233710.4 acyl-CoA dehydrogenase long chain (from RefSeq NM_001608.4) ACADL ACADL_HUMAN B2R8T3 ENST00000233710.1 ENST00000233710.2 ENST00000233710.3 NM_001608 P28330 Q8IUN8 uc002vdz.1 uc002vdz.2 uc002vdz.3 uc002vdz.4 uc002vdz.5 uc002vdz.6 The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803614.176300.1, SRR1803616.261303.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000233710.4/ ENSP00000233710.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl- CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase can act on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains (PubMed:8823175, PubMed:21237683). Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721, ChEBI:CHEBI:83727; EC=1.3.8.8; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17722; Evidence=; Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465; Evidence=; Reaction=H(+) + octanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62242; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181; Evidence=; Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177; Evidence=; Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297; Evidence=; Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron- transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; Evidence=; Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61526; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; Evidence=; Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:71412; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241; Evidence=; Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74691; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; Evidence=; Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA- COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65059, ChEBI:CHEBI:74692; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229; Evidence=; Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron- transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233; Evidence=; Reaction=(5E)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,5E)-tetradecadienoyl-CoA + reduced [electron- transfer flavoprotein]; Xref=Rhea:RHEA:49828, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:131943, ChEBI:CHEBI:131944; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49829; Evidence=; Reaction=(5Z)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron- transfer flavoprotein]; Xref=Rhea:RHEA:47448, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:84650, ChEBI:CHEBI:87701; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47449; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,9Z)-octadecadienoyl-CoA + reduced [electron- transfer flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77553; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301; Evidence=; Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence=; Kinetic parameters: KM=29 uM for hexanoyl-CoA ; KM=8 uM for octanoyl-CoA ; KM=10 uM for decanoyl-CoA ; KM=7 uM for dodecanoyl-CoA ; KM=10 uM for tetradecanoyl-CoA ; KM=14 uM for hexadecanoyl-CoA ; KM=8 uM for octadecanoyl-CoA ; Lipid metabolism; mitochondrial fatty acid beta-oxidation. Homotetramer. P28330; P22735: TGM1; NbExp=3; IntAct=EBI-12059321, EBI-2562368; Mitochondrion matrix Acetylation at Lys-318 and Lys-322 in proximity of the cofactor- binding sites strongly reduces catalytic activity. These sites are deacetylated by SIRT3. Belongs to the acyl-CoA dehydrogenase family. fatty-acyl-CoA binding temperature homeostasis acyl-CoA dehydrogenase activity long-chain-acyl-CoA dehydrogenase activity mitochondrion mitochondrial matrix lipid metabolic process fatty acid metabolic process fatty acid beta-oxidation palmitoyl-CoA oxidase activity oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors carnitine metabolic process, CoA-linked mitochondrial membrane fatty acid beta-oxidation using acyl-CoA dehydrogenase carnitine catabolic process long-chain fatty acid catabolic process cellular lipid catabolic process negative regulation of fatty acid biosynthetic process negative regulation of fatty acid oxidation flavin adenine dinucleotide binding protein homotetramerization oxidation-reduction process regulation of cholesterol metabolic process uc002vdz.1 uc002vdz.2 uc002vdz.3 uc002vdz.4 uc002vdz.5 uc002vdz.6 
ENST00000233735.2 REG1A ENST00000233735.2 regenerating family member 1 alpha (from RefSeq NM_002909.5) ENST00000233735.1 NM_002909 P05451 P11379 PSPS PSPS1 Q4ZG28 REG REG1A_HUMAN uc002snz.1 uc002snz.2 uc002snz.3 uc002snz.4 This gene is a type I subclass member of the Reg gene family. The Reg gene family is a multigene family grouped into four subclasses, types I, II, III and IV, based on the primary structures of the encoded proteins. This gene encodes a protein that is secreted by the exocrine pancreas. It is associated with islet cell regeneration and diabetogenesis and may be involved in pancreatic lithogenesis. Reg family members REG1B, REGL, PAP and this gene are tandemly clustered on chromosome 2p12 and may have arisen from the same ancestral gene by gene duplication. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: ERR279838.5622.1, AK291981.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968189 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233735.2/ ENSP00000233735.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration. Secreted. In pancreatic acinar cells and, in lower levels, in brain. Enhanced expression of PSP-related transcripts and intraneuronal accumulation of PSP-like proteins is found in brain from Alzheimer disease and Down syndrome patients. High expression levels in fetal and infant brains; much lower in adult brains. The composition of the O-linked carbohydrate on Thr-27 is complex and varied. In the crystallographic structure, the attached sugar appears to be N-acetylglucosamine, typical of an intracellular protein, rather than N-acetylgalactosamine. Name=Functional Glycomics Gateway - Glycan Binding; Note=Lithostathine A; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_254"; response to hypoxia transmembrane signaling receptor activity receptor binding extracellular region extracellular space cytosol signal transduction midgut development growth factor activity positive regulation of cell proliferation negative regulation of cell proliferation positive regulation of gene expression response to organic cyclic compound phosphatase binding protein phosphatase binding carbohydrate binding growth cone response to nutrient levels dendrite membrane neuronal cell body membrane macromolecular complex wound healing zymogen granule identical protein binding protein homodimerization activity peptidoglycan binding response to peptide hormone cell wall disruption in other organism basal part of cell perinuclear region of cytoplasm protein homooligomerization protein homotetramerization calcium ion homeostasis extracellular exosome oligosaccharide binding liver regeneration response to acetylsalicylate positive regulation of dendrite extension positive regulation of type B pancreatic cell proliferation positive regulation of acinar cell proliferation response to water-immersion restraint stress pancreas regeneration response to growth hormone-releasing hormone response to gastrin cellular response to chemokine cellular response to gastrin uc002snz.1 uc002snz.2 uc002snz.3 uc002snz.4 
ENST00000233741.9 FANCL ENST00000233741.9 FA complementation group L, transcript variant 2 (from RefSeq NM_018062.4) ENST00000233741.1 ENST00000233741.2 ENST00000233741.3 ENST00000233741.4 ENST00000233741.5 ENST00000233741.6 ENST00000233741.7 ENST00000233741.8 FANCL_HUMAN NM_018062 PHF9 Q6GU60 Q9NW38 uc002rzw.1 uc002rzw.2 uc002rzw.3 uc002rzw.4 uc002rzw.5 uc002rzw.6 This gene encodes a ubiquitin ligase that is a member of the Fanconi anemia complementation group (FANC). Members of this group are related by their assembly into a common nuclear protein complex rather than by sequence similarity. This gene encodes the protein for complementation group L that mediates monoubiquitination of FANCD2 as well as FANCI. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2018]. Ubiquitin ligase protein that mediates monoubiquitination of FANCD2 in the presence of UBE2T, a key step in the DNA damage pathway (PubMed:12973351, PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:24389026). Also mediates monoubiquitination of FANCI (PubMed:19589784). May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence= Protein modification; protein ubiquitination. Interacts with GGN (By similarity). Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM (PubMed:12973351, PubMed:15502827, PubMed:16116422, PubMed:22343915). The complex is not found in FA patients. In complex with FANCF, FANCA and FANCG, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins (PubMed:18550849). Interacts with FANCI (PubMed:21775430). Directly interacts (via the RING-type zinc finger) with UBE2T and UBE2W (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:21775430, PubMed:24389026). Q9NW38; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-2339898, EBI-11976299; Q9NW38; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-2339898, EBI-14493093; Q9NW38; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-2339898, EBI-713602; Q9NW38; O43307: ARHGEF9; NbExp=3; IntAct=EBI-2339898, EBI-3447299; Q9NW38; A2RRN7: CADPS; NbExp=3; IntAct=EBI-2339898, EBI-10179719; Q9NW38; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-2339898, EBI-12261896; Q9NW38; Q9NX63: CHCHD3; NbExp=6; IntAct=EBI-2339898, EBI-743375; Q9NW38; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-2339898, EBI-751587; Q9NW38; Q6BCY4-2: CYB5R2; NbExp=3; IntAct=EBI-2339898, EBI-12102608; Q9NW38; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2339898, EBI-3867333; Q9NW38; O95865: DDAH2; NbExp=3; IntAct=EBI-2339898, EBI-749139; Q9NW38; Q8NF50-2: DOCK8; NbExp=3; IntAct=EBI-2339898, EBI-10174653; Q9NW38; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-2339898, EBI-301024; Q9NW38; P15976-2: GATA1; NbExp=3; IntAct=EBI-2339898, EBI-9090198; Q9NW38; P28799: GRN; NbExp=3; IntAct=EBI-2339898, EBI-747754; Q9NW38; Q9BSH5: HDHD3; NbExp=3; IntAct=EBI-2339898, EBI-745201; Q9NW38; P09016: HOXD4; NbExp=3; IntAct=EBI-2339898, EBI-12822515; Q9NW38; Q02363: ID2; NbExp=3; IntAct=EBI-2339898, EBI-713450; Q9NW38; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-2339898, EBI-8638439; Q9NW38; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2339898, EBI-747204; Q9NW38; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-2339898, EBI-2125614; Q9NW38; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2339898, EBI-14069005; Q9NW38; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-2339898, EBI-1052037; Q9NW38; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-2339898, EBI-11953846; Q9NW38; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-2339898, EBI-12805508; Q9NW38; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2339898, EBI-741037; Q9NW38; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-2339898, EBI-10174029; Q9NW38; Q6PF18: MORN3; NbExp=3; IntAct=EBI-2339898, EBI-9675802; Q9NW38; P49720: PSMB3; NbExp=3; IntAct=EBI-2339898, EBI-603340; Q9NW38; Q8IUH3: RBM45; NbExp=3; IntAct=EBI-2339898, EBI-2512147; Q9NW38; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-2339898, EBI-10182375; Q9NW38; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2339898, EBI-396669; Q9NW38; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2339898, EBI-748391; Q9NW38; Q96H20: SNF8; NbExp=3; IntAct=EBI-2339898, EBI-747719; Q9NW38; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-2339898, EBI-18616594; Q9NW38; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-2339898, EBI-2212028; Q9NW38; Q12800: TFCP2; NbExp=3; IntAct=EBI-2339898, EBI-717422; Q9NW38; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-2339898, EBI-9090990; Q9NW38; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-2339898, EBI-12068150; Q9NW38; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-2339898, EBI-7850213; Q9NW38; Q9NZL3: ZNF224; NbExp=3; IntAct=EBI-2339898, EBI-12357267; Q9NW38; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-2339898, EBI-745520; Q9NW38; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-2339898, EBI-10251462; Q9NW38-1; Q9NPD8: UBE2T; NbExp=3; IntAct=EBI-16088720, EBI-2130165; Cytoplasm Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NW38-1; Sequence=Displayed; Name=2; IsoId=Q9NW38-2; Sequence=VSP_041727; The UBC-RWD region (URD) region mediates interaction with FANCI and FANCD2. The RING-type zinc finger domain is monoubiquitinated in the presence of UBE2T and UBE2W. Fanconi anemia complementation group L (FANCL) [MIM:614083]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Note=The disease is caused by variants affecting the gene represented in this entry. Although PubMed:12724401 reports that it contains a PHD-type zinc finger, it contains a RING-type zinc finger. Moreover, PHD-type zinc fingers do not have any ubiquitin ligase activity. Name=Fanconi Anemia Mutation Database; URL="https://www2.rockefeller.edu/fanconi/genes/jumpl"; ubiquitin-protein transferase activity protein binding nucleus nuclear envelope nucleoplasm cytoplasm DNA repair protein monoubiquitination cellular response to DNA damage stimulus gamete generation protein ubiquitination nuclear body transferase activity ubiquitin protein ligase binding interstrand cross-link repair regulation of cell proliferation intracellular membrane-bounded organelle Fanconi anaemia nuclear complex metal ion binding ubiquitin protein ligase activity uc002rzw.1 uc002rzw.2 uc002rzw.3 uc002rzw.4 uc002rzw.5 uc002rzw.6 
ENST00000233809.9 IGFBP2 ENST00000233809.9 insulin like growth factor binding protein 2, transcript variant 4 (from RefSeq NM_001313993.2) BP2 ENST00000233809.1 ENST00000233809.2 ENST00000233809.3 ENST00000233809.4 ENST00000233809.5 ENST00000233809.6 ENST00000233809.7 ENST00000233809.8 IBP2 IBP2_HUMAN NM_001313993 P18065 Q14619 Q9UCL3 uc061sgd.1 uc061sgd.2 The protein encoded by this gene is one of six similar proteins that bind insulin-like growth factors I and II (IGF-I and IGF-II). The encoded protein can be secreted into the bloodstream, where it binds IGF-I and IGF-II with high affinity, or it can remain intracellular, interacting with many different ligands. High expression levels of this protein promote the growth of several types of tumors and may be predictive of the chances of recovery of the patient. Several transcript variants, one encoding a secreted isoform and the others encoding nonsecreted isoforms, have been found for this gene. [provided by RefSeq, Sep 2015]. Inhibits IGF-mediated growth and developmental rates. IGF- binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Binds IGF2 more than IGF1. P18065; Q9C086: INO80B; NbExp=4; IntAct=EBI-2504392, EBI-715611; Secreted. The C-terminus is required for IGF-binding and growth inhibition. O-glycosylated. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/igfbp2/"; receptor binding protein binding insulin-like growth factor binding extracellular region extracellular space signal transduction female pregnancy aging response to nutrient response to mechanical stimulus response to lithium ion apical plasma membrane growth factor binding cytoplasmic vesicle insulin-like growth factor I binding insulin-like growth factor II binding response to estradiol response to retinoic acid cellular response to hormone stimulus regulation of growth positive regulation of activated T cell proliferation response to drug regulation of insulin-like growth factor receptor signaling pathway response to estrogen cellular protein metabolic process response to steroid hormone response to glucocorticoid extracellular exosome negative regulation of canonical Wnt signaling pathway uc061sgd.1 uc061sgd.2 
ENST00000233813.5 IGFBP5 ENST00000233813.5 insulin like growth factor binding protein 5 (from RefSeq NM_000599.4) ENST00000233813.1 ENST00000233813.2 ENST00000233813.3 ENST00000233813.4 IBP5 IBP5_HUMAN NM_000599 P24593 Q5U0A3 uc002vgj.1 uc002vgj.2 uc002vgj.3 uc002vgj.4 uc002vgj.5 uc002vgj.6 IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. P24593; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-720480, EBI-7131019; P24593; Q8IVF2-3: AHNAK2; NbExp=3; IntAct=EBI-720480, EBI-12078468; P24593; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-720480, EBI-19125216; P24593; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-720480, EBI-7054139; P24593; Q96BI3: APH1A; NbExp=3; IntAct=EBI-720480, EBI-2606935; P24593; P41181: AQP2; NbExp=3; IntAct=EBI-720480, EBI-12701138; P24593; Q13520: AQP6; NbExp=3; IntAct=EBI-720480, EBI-13059134; P24593; O43315: AQP9; NbExp=3; IntAct=EBI-720480, EBI-17444777; P24593; P07306: ASGR1; NbExp=3; IntAct=EBI-720480, EBI-1172335; P24593; Q8WZ55: BSND; NbExp=3; IntAct=EBI-720480, EBI-7996695; P24593; P19397: CD53; NbExp=3; IntAct=EBI-720480, EBI-6657396; P24593; Q9HA82: CERS4; NbExp=3; IntAct=EBI-720480, EBI-2622997; P24593; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-720480, EBI-17447707; P24593; P57739: CLDN2; NbExp=3; IntAct=EBI-720480, EBI-751440; P24593; P56880: CLDN20; NbExp=3; IntAct=EBI-720480, EBI-23801559; P24593; P56747: CLDN6; NbExp=3; IntAct=EBI-720480, EBI-12955011; P24593; O95471: CLDN7; NbExp=3; IntAct=EBI-720480, EBI-740744; P24593; O95484: CLDN9; NbExp=3; IntAct=EBI-720480, EBI-18341636; P24593; Q6ZS10: CLEC17A; NbExp=4; IntAct=EBI-720480, EBI-11977093; P24593; O43889-2: CREB3; NbExp=4; IntAct=EBI-720480, EBI-625022; P24593; P25024: CXCR1; NbExp=3; IntAct=EBI-720480, EBI-3905522; P24593; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-720480, EBI-11037623; P24593; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-720480, EBI-781551; P24593; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-720480, EBI-18304435; P24593; Q96P31-6: FCRL3; NbExp=3; IntAct=EBI-720480, EBI-17443171; P24593; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-720480, EBI-12142257; P24593; P36382: GJA5; NbExp=3; IntAct=EBI-720480, EBI-750433; P24593; P48165: GJA8; NbExp=3; IntAct=EBI-720480, EBI-17458373; P24593; O75712: GJB3; NbExp=3; IntAct=EBI-720480, EBI-3908586; P24593; O95377: GJB5; NbExp=3; IntAct=EBI-720480, EBI-3909454; P24593; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-720480, EBI-712073; P24593; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-720480, EBI-11955647; P24593; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-720480, EBI-13345167; P24593; O60883: GPR37L1; NbExp=3; IntAct=EBI-720480, EBI-2927498; P24593; O15529: GPR42; NbExp=3; IntAct=EBI-720480, EBI-18076404; P24593; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-720480, EBI-13067820; P24593; Q8TED1: GPX8; NbExp=3; IntAct=EBI-720480, EBI-11721746; P24593; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-720480, EBI-18053395; P24593; O95279: KCNK5; NbExp=3; IntAct=EBI-720480, EBI-3934936; P24593; Q8IYS2: KIAA2013; NbExp=3; IntAct=EBI-720480, EBI-2866116; P24593; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-720480, EBI-3267258; P24593; Q6UX15-2: LAYN; NbExp=3; IntAct=EBI-720480, EBI-19944128; P24593; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-720480, EBI-10173166; P24593; Q86WI0: LHFPL1; NbExp=3; IntAct=EBI-720480, EBI-18268016; P24593; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-720480, EBI-11956541; P24593; Q6N075: MFSD5; NbExp=3; IntAct=EBI-720480, EBI-3920969; P24593; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-720480, EBI-750085; P24593; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-720480, EBI-12806656; P24593; Q9GZW8: MS4A7; NbExp=3; IntAct=EBI-720480, EBI-721391; P24593; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-720480, EBI-10247000; P24593; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-720480, EBI-716063; P24593; Q8NFJ6: PROKR2; NbExp=3; IntAct=EBI-720480, EBI-12902928; P24593; Q9UBD6: RHCG; NbExp=3; IntAct=EBI-720480, EBI-15853497; P24593; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-720480, EBI-18159983; P24593; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-720480, EBI-12808018; P24593; Q9H2H9: SLC38A1; NbExp=4; IntAct=EBI-720480, EBI-9978441; P24593; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-720480, EBI-10290130; P24593; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-720480, EBI-7225508; P24593; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-720480, EBI-10819434; P24593; Q8N205-2: SYNE4; NbExp=3; IntAct=EBI-720480, EBI-12099160; P24593; Q8WY91: THAP4; NbExp=3; IntAct=EBI-720480, EBI-726691; P24593; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-720480, EBI-12947623; P24593; Q96A25: TMEM106A; NbExp=3; IntAct=EBI-720480, EBI-3915978; P24593; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-720480, EBI-2821497; P24593; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-720480, EBI-11724423; P24593; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-720480, EBI-10982110; P24593; Q9NWC5: TMEM45A; NbExp=3; IntAct=EBI-720480, EBI-10823938; P24593; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-720480, EBI-18178701; P24593; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-720480, EBI-12345267; P24593; Q9Y320: TMX2; NbExp=3; IntAct=EBI-720480, EBI-6447886; P24593; O95859: TSPAN12; NbExp=3; IntAct=EBI-720480, EBI-2466403; P24593; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-720480, EBI-12195249; Secreted. Osteosarcoma, and at lower levels in liver, kidney and brain. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/igfbp5/"; regulation of cell growth osteoblast differentiation fibronectin binding protein binding insulin-like growth factor binding extracellular region extracellular space endoplasmic reticulum lumen signal transduction female pregnancy aging negative regulation of smooth muscle cell migration insulin-like growth factor binding protein complex negative regulation of translation growth factor binding negative regulation of cell migration hair follicle morphogenesis insulin-like growth factor I binding insulin-like growth factor II binding intracellular signal transduction regulation of growth insulin-like growth factor ternary complex glucose homeostasis regulation of insulin-like growth factor receptor signaling pathway positive regulation of insulin-like growth factor receptor signaling pathway negative regulation of insulin-like growth factor receptor signaling pathway post-translational protein modification cellular protein metabolic process type B pancreatic cell proliferation negative regulation of osteoblast differentiation negative regulation of growth lung alveolus development negative regulation of smooth muscle cell proliferation striated muscle cell differentiation positive regulation of protein kinase B signaling mammary gland involution response to growth hormone cellular response to cAMP cellular response to organic cyclic compound negative regulation of muscle tissue development negative regulation of skeletal muscle hypertrophy positive regulation of vascular smooth muscle cell proliferation positive regulation of vascular associated smooth muscle cell migration uc002vgj.1 uc002vgj.2 uc002vgj.3 uc002vgj.4 uc002vgj.5 uc002vgj.6 
ENST00000233826.4 KCNJ13 ENST00000233826.4 potassium inwardly rectifying channel subfamily J member 13, transcript variant 1 (from RefSeq NM_002242.4) A0PGH1 ENST00000233826.1 ENST00000233826.2 ENST00000233826.3 KCJ13_HUMAN NM_002242 O60928 O76023 Q53SA1 Q8N3Y4 uc002vtp.1 uc002vtp.2 uc002vtp.3 uc002vtp.4 uc002vtp.5 This gene encodes a member of the inwardly rectifying potassium channel family of proteins. Members of this family form ion channel pores that allow potassium ions to pass into a cell. The encoded protein belongs to a subfamily of low signal channel conductance proteins that have a low dependence on potassium concentration. Mutations in this gene are associated with snowflake vitreoretinal degeneration. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Feb 2010]. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium. Membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O60928-1; Sequence=Displayed; Name=2; Synonyms=Kir7.1S; IsoId=O60928-2; Sequence=VSP_042627, VSP_042628; Predominantly expressed in small intestine. Expression is also detected in stomach, kidney, and all central nervous system regions tested with the exception of spinal cord. Phosphorylation at Ser-201 by PKC strongly inhibits ionic currents, while phosphorylation at Ser-287 by PKA increases them. Snowflake vitreoretinal degeneration (SVD) [MIM:193230]: Developmental and progressive hereditary eye disorder that affects multiple tissues within the eye. Diagnostic features of SVD include fibrillar degeneration of the vitreous humor, early-onset cataract, minute crystalline deposits in the neurosensory retina, and retinal detachment. Note=The disease is caused by variants affecting the gene represented in this entry. Leber congenital amaurosis 16 (LCA16) [MIM:614186]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ13 subfamily. inward rectifier potassium channel activity voltage-gated ion channel activity ion transport potassium ion transport membrane integral component of membrane regulation of ion transmembrane transport potassium ion import across plasma membrane uc002vtp.1 uc002vtp.2 uc002vtp.3 uc002vtp.4 uc002vtp.5 
ENST00000233838.9 GGCX ENST00000233838.9 gamma-glutamyl carboxylase, transcript variant 1 (from RefSeq NM_000821.7) B4DMC5 E9PEE1 ENST00000233838.1 ENST00000233838.2 ENST00000233838.3 ENST00000233838.4 ENST00000233838.5 ENST00000233838.6 ENST00000233838.7 ENST00000233838.8 GC NM_000821 P38435 Q14415 Q6GU45 VKGC_HUMAN uc002sps.1 uc002sps.2 uc002sps.3 uc002sps.4 uc002sps.5 This gene encodes an integral membrane protein of the rough endoplasmic reticulum that carboxylates glutamate residues of vitamin K-dependent proteins to gamma carboxyl glutamate, a modification that is required for their activity. The vitamin K-dependent protein substrates have a propeptide that binds the enzyme, with carbon dioxide, dioxide, and reduced vitamin K acting as co-substrates. Vitamin K-dependent proteins affect a number of physiologic processes including blood coagulation, prevention of vascular calcification, and inflammation. Allelic variants of this gene have been associated with pseudoxanthoma elasticum-like disorder with associated multiple coagulation factor deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2015]. Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide (PubMed:17073445). Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP) (PubMed:17073445). Reaction=2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol; Xref=Rhea:RHEA:45140, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:11094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15759, ChEBI:CHEBI:16526, ChEBI:CHEBI:28433, ChEBI:CHEBI:29973, ChEBI:CHEBI:84990; EC=4.1.1.90; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45142; Evidence=; pH dependence: Optimum pH is 7. ; Monomer (PubMed:11570873). May interact with CALU (By similarity). Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P38435-1; Sequence=Displayed; Name=2; IsoId=P38435-2; Sequence=VSP_046179; Combined deficiency of vitamin K-dependent clotting factors 1 (VKCFD1) [MIM:277450]: VKCFD leads to a bleeding tendency that is usually reversed by oral administration of vitamin K. te=The disease is caused by variants affecting the gene represented in this entry. Pseudoxanthoma elasticum-like disorder with multiple coagulation factor deficiency (PXEL-MCFD) [MIM:610842]: Characterized by hyperlaxity of the skin involving the entire body. Important phenotypic differences with classical PXE include much more severe skin laxity with spreading toward the trunk and limbs with thick, leathery skin folds rather than confinement to flexural areas, and no decrease in visual acuity. Moreover, detailed electron microscopic analyses revealed that alterations of elastic fibers as well as their mineralization are slightly different from those in classic PXE. Note=The disease is caused by variants affecting the gene represented in this entry. The vitamin K-dependent protein substrates of carboxylase have usually a propeptide that binds to a high-affinity site on the carboxylase. CO(2), O(2) and reduced vitamin K are cosubstrates. Belongs to the vitamin K-dependent gamma-carboxylase family. endoplasmic reticulum endoplasmic reticulum membrane cellular protein modification process blood coagulation gamma-glutamyl carboxylase activity membrane integral component of membrane lyase activity peptidyl-glutamic acid carboxylation uc002sps.1 uc002sps.2 uc002sps.3 uc002sps.4 uc002sps.5 
ENST00000233840.3 NEU2 ENST00000233840.3 neuraminidase 2 (from RefSeq NM_005383.2) ENST00000233840.1 ENST00000233840.2 NEUR2_HUMAN NM_005383 Q3KNW4 Q6NTB4 Q9Y3R4 uc010zmn.1 uc010zmn.2 This gene belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. Expression studies in COS7 cells confirmed that this gene encodes a functional sialidase. Its cytosolic localization was demonstrated by cell fractionation experiments. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC069151.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145743, SAMEA2145893 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233840.3/ ENSP00000233840.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides (PubMed:14613940, PubMed:22228546). Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate. Displays preference for alpha- (2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)- sialylated GD1b, in both monomeric forms and micelles. Hydrolyzes monomeric GM1 ganglioside, but has no activity toward the miscellar form (PubMed:14613940). Has lower sialidase activity for glycoproteins such as fetuin and TF/transferrin that carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages. Cleaves milk oligosaccharide alpha- (2->3)-sialyllactose, but is inactive toward alpha-(2->6)-sialyllactose isomer. Has no activity toward colominic acid, a homomer of alpha- (2->8)-linked Neu5Ac residues (PubMed:14613940). Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- (2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence=; Reaction=a ganglioside GD1a + H2O = a ganglioside GM1 + N- acetylneuraminate; Xref=Rhea:RHEA:47832, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82637, ChEBI:CHEBI:82639; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47833; Evidence=; Reaction=a ganglioside GM1 + H2O = a ganglioside GA1 + N- acetylneuraminate; Xref=Rhea:RHEA:47872, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82639, ChEBI:CHEBI:88069; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47873; Evidence=; Reaction=a ganglioside GT1b + H2O = a ganglioside GD1b + N- acetylneuraminate; Xref=Rhea:RHEA:47828, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82939, ChEBI:CHEBI:82940; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47829; Evidence=; Reaction=a ganglioside GD1b + H2O = a ganglioside GM1 + N- acetylneuraminate; Xref=Rhea:RHEA:47876, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:82639, ChEBI:CHEBI:82939; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47877; Evidence=; Reaction=a ganglioside GD3 + H2O = a ganglioside GM3 + N- acetylneuraminate; Xref=Rhea:RHEA:48120, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:79210, ChEBI:CHEBI:79214; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48121; Evidence=; Reaction=a ganglioside GM3 + H2O = a beta-D-galactosyl-(1->4)-beta-D- glucosyl-(1<->1)-ceramide + N-acetylneuraminate; Xref=Rhea:RHEA:48136, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:79208, ChEBI:CHEBI:79210; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48137; Evidence=; Reaction=a ganglioside GM2 + H2O = a ganglioside GA2 + N- acetylneuraminate; Xref=Rhea:RHEA:48172, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418, ChEBI:CHEBI:79218, ChEBI:CHEBI:90085; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48173; Evidence=; Reaction=a neolactoside IV(3)-alpha-NeuAc-nLc4Cer(d18:1(4E)) + H2O = a neolactoside nLc4Cer(d18:1(4E)) + N-acetylneuraminate; Xref=Rhea:RHEA:47852, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006, ChEBI:CHEBI:35418, ChEBI:CHEBI:58665; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47853; Evidence=; Reaction=H2O + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl- (1->4)-D-glucose = lactose + N-acetylneuraminate; Xref=Rhea:RHEA:64640, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:35418, ChEBI:CHEBI:156068; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64641; Evidence=; Kinetic parameters: KM=0.24 mM for ganglioside GM3 (in the presence of Triton X-100) ; KM=0.14 mM for ganglioside GD1a (in the presence of Triton X-100) ; KM=0.51 mM for ganglioside GD1b (in the presence of Triton X-100) ; KM=0.38 mM for ganglioside GT1b (in the presence of Triton X-100) ; KM=0.28 mM for neolactoside IV(3)-alpha-NeuAc-nLc4Cer(d18:1(4E)) (in the presence of Triton X-100) ; KM=0.31 mM for alpha(2->3)-sialyllactose ; Vmax=67 umol/min/mg enzyme toward ganglioside GM3 (in the presence of Triton X-100) ; Vmax=322 umol/min/mg enzyme toward ganglioside GD1a (in the presence of Triton X-100) ; Vmax=5.45 umol/min/mg enzyme toward ganglioside GD1b (in the presence of Triton X-100) ; Vmax=190 umol/min/mg enzyme toward ganglioside GT1b (in the presence of Triton X-100) ; Vmax=253 umol/min/mg enzyme toward ganglioside neolactoside IV(3)- alpha-NeuAc-nLc4Cer(d18:1(4E)) (in the presence of Triton X-100) ; Vmax=10 umol/min/mg enzyme toward alpha(2->3)-sialyllactose ; Vmax=12.7 umol/min/mg enzyme toward fetuin ; Vmax=0.75 umol/min/mg enzyme toward TF/transferrin ; Vmax=0.70 umol/min/mg enzyme toward alpha-1-acid glycoprotein ; pH dependence: Optimum pH is 5.6. ; Q9Y3R4; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10327976, EBI-3867333; Q9Y3R4; Q7Z3S9: NOTCH2NLA; NbExp=6; IntAct=EBI-10327976, EBI-945833; Cytoplasm, cytosol Expressed in skeletal muscle, fetal liver and embryonic carcinoma cell line NT2-D1. Belongs to the glycosyl hydrolase 33 family. exo-alpha-sialidase activity protein binding cytoplasm lysosome cytosol carbohydrate metabolic process lipid metabolic process glycosphingolipid metabolic process ganglioside catabolic process metabolic process oligosaccharide catabolic process membrane lipid catabolic process hydrolase activity hydrolase activity, acting on glycosyl bonds intracellular membrane-bounded organelle cellular oligosaccharide catabolic process exo-alpha-(2->3)-sialidase activity exo-alpha-(2->6)-sialidase activity exo-alpha-(2->8)-sialidase activity catalytic complex uc010zmn.1 uc010zmn.2 
ENST00000233893.10 HSPE1 ENST00000233893.10 heat shock protein family E (Hsp10) member 1 (from RefSeq NM_002157.3) CH10_HUMAN ENST00000233893.1 ENST00000233893.2 ENST00000233893.3 ENST00000233893.4 ENST00000233893.5 ENST00000233893.6 ENST00000233893.7 ENST00000233893.8 ENST00000233893.9 NM_002157 O95421 P61604 Q04984 Q53X54 Q9UDH0 uc002uul.1 uc002uul.2 uc002uul.3 uc002uul.4 uc002uul.5 This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.[provided by RefSeq, Feb 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.102397.1, SRR1163655.433354.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: inferred from homology MANE Ensembl match :: ENST00000233893.10/ ENSP00000233893.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:7912672, PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). Homoheptamer arranged in a ring structure (PubMed:25918392). 2 heptameric Hsp10 rings interact with a Hsp60 tetradecamer in the structure of a back-to-back double heptameric ring to form the symmetrical football complex (PubMed:25918392). P61604; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-711483, EBI-741158; P61604; Q8WWX9: SELENOM; NbExp=3; IntAct=EBI-711483, EBI-10277687; Mitochondrion matrix. By stress. Mass=10843.5; Mass_error=0.2; Method=Electrospray; Evidence=; Belongs to the GroES chaperonin family. osteoblast differentiation RNA binding protein binding ATP binding mitochondrion mitochondrial matrix protein folding activation of cysteine-type endopeptidase activity involved in apoptotic process response to unfolded protein membrane metal ion binding unfolded protein binding chaperone mediated protein folding requiring cofactor chaperone binding extracellular exosome uc002uul.1 uc002uul.2 uc002uul.3 uc002uul.4 uc002uul.5 
ENST00000233948.4 WNT6 ENST00000233948.4 Wnt family member 6 (from RefSeq NM_006522.4) ENST00000233948.1 ENST00000233948.2 ENST00000233948.3 NM_006522 Q9H1J6 Q9H238 Q9Y6F9 WNT6_HUMAN uc002vjc.1 uc002vjc.2 uc002vjc.3 The WNT gene family consists of structurally related genes which encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It is overexpressed in cervical cancer cell line and strongly coexpressed with another family member, WNT10A, in colorectal cancer cell line. The gene overexpression may play key roles in carcinogenesis. This gene and the WNT10A gene are clustered in the chromosome 2q35 region. The protein encoded by this gene is 97% identical to the mouse Wnt6 protein at the amino acid level. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY009401.1, AK075522.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142853 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233948.4/ ENSP00000233948.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. Together with CAV1 may promote chemoresistance of gastric cancer cells to DNA- damaging anthracycline drugs through the activation of the canonical Wnt receptor signaling pathway. Interacts with PORCN. Secreted, extracellular space, extracellular matrix. Expressed in gastric cancer cell lines and gastric cancer tissues (at protein level). Detected in the apical gland region of the gastric foveolar epithelium (at protein level). Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. Belongs to the Wnt family. branching involved in ureteric bud morphogenesis receptor binding frizzled binding extracellular region extracellular space endoplasmic reticulum lumen Golgi lumen plasma membrane multicellular organism development axis specification cell surface positive regulation of gene expression Wnt signaling pathway neuron differentiation endocytic vesicle membrane extracellular matrix odontogenesis of dentin-containing tooth cell fate commitment positive regulation of transcription, DNA-templated epithelial-mesenchymal cell signaling cornea development in camera-type eye extracellular exosome positive regulation of tooth mineralization cellular response to retinoic acid nephron tubule formation nephron tubule development uc002vjc.1 uc002vjc.2 uc002vjc.3 
ENST00000233954.6 IL1RL1 ENST00000233954.6 interleukin 1 receptor like 1, transcript variant 1 (from RefSeq NM_016232.5) A8K6B3 B4E0I3 DER4 ENST00000233954.1 ENST00000233954.2 ENST00000233954.3 ENST00000233954.4 ENST00000233954.5 ILRL1_HUMAN NM_016232 Q01638 Q53TU7 Q8NEJ3 Q9ULV7 Q9UQ44 ST2 T1 uc002tbu.1 uc002tbu.2 The protein encoded by this gene is a member of the interleukin 1 receptor family. Studies of the similar gene in mouse suggested that this receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells. This gene, interleukin 1 receptor, type I (IL1R1), interleukin 1 receptor, type II (IL1R2) and interleukin 1 receptor-like 2 (IL1RL2) form a cytokine receptor gene cluster in a region mapped to chromosome 2q12. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jul 2008]. Receptor for interleukin-33 (IL-33) which plays crucial roles in innate and adaptive immunity, contributing to tissue homeostasis and responses to environmental stresses together with coreceptor IL1RAP (PubMed:35238669). Its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function (PubMed:16286016) (Probable). Upon tissue injury, induces UCP2- dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3- dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity). [Isoform B]: Inhibits IL-33 signaling. Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence=; Interacts with MYD88, IRAK1, IRAK4, and TRAF6. Bound to its ligand IL-33, interacts with IL1RAP to form the minimal interleukin-33 signaling complex with a 1:1:1 stoichiometry. Interacts with KIT (bound to KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88. Interacts with TMED1 (PubMed:23319592). Q01638; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-993762, EBI-3939278; Q01638; O95760: IL33; NbExp=2; IntAct=EBI-993762, EBI-724057; Q01638-2; P07307-3: ASGR2; NbExp=3; IntAct=EBI-12838366, EBI-12808270; Q01638-2; Q2HXU8-2: CLEC12B; NbExp=3; IntAct=EBI-12838366, EBI-12811991; Q01638-2; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-12838366, EBI-11749983; Q01638-2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12838366, EBI-6942903; Q01638-2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12838366, EBI-13345167; Q01638-2; O15529: GPR42; NbExp=3; IntAct=EBI-12838366, EBI-18076404; Q01638-2; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-12838366, EBI-2689785; Q01638-2; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-12838366, EBI-17640454; Q01638-2; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-12838366, EBI-9978441; Q01638-2; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-12838366, EBI-17670824; Q01638-2; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-12838366, EBI-751210; [Isoform C]: Cell membrane. [Isoform B]: Secreted. Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=4; Name=A; Synonyms=ST2L; IsoId=Q01638-1; Sequence=Displayed; Name=B; Synonyms=ST2S; IsoId=Q01638-2; Sequence=VSP_002666, VSP_002667; Name=C; Synonyms=ST2V; IsoId=Q01638-3; Sequence=VSP_002664, VSP_002665; Name=4; IsoId=Q01638-4; Sequence=VSP_054933, VSP_002666, VSP_002667; Highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine. Isoform A is prevalently expressed in the lung, testis, placenta, stomach and colon. Isoform B is more abundant in the brain, kidney and the liver. Isoform C is not detected in brain, heart, liver, kidney and skeletal muscle. Expressed on T-cells in fibrotic liver; at protein level. Overexpressed in fibrotic and cirrhotic liver. The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity. Ubiquitinated at Lys-321 in a FBXL19-mediated manner; leading to proteasomal degradation. Ubiquitination by TRAF6 via 'Lys-27'-linked polyubiquitination and deubiquitination by USP38 serves as a critical regulatory mechanism for fine-tuning IL1RL1-mediated inflammatory response (PubMed:35238669). [Isoform C]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the interleukin-1 receptor family. interleukin-33 binding interleukin-33 receptor activity negative regulation of T-helper 1 type immune response cytokine receptor activity interleukin-1 receptor activity protein binding extracellular region plasma membrane immune response signal transduction external side of plasma membrane membrane integral component of membrane negative regulation of interferon-gamma production positive regulation of interleukin-5 production interleukin-33-mediated signaling pathway positive regulation of macrophage activation positive regulation of inflammatory response positive regulation of chemokine secretion uc002tbu.1 uc002tbu.2 
ENST00000233957.7 IL18R1 ENST00000233957.7 interleukin 18 receptor 1, transcript variant 1 (from RefSeq NM_003855.5) B2R9Y5 ENST00000233957.1 ENST00000233957.2 ENST00000233957.3 ENST00000233957.4 ENST00000233957.5 ENST00000233957.6 IL18R1 IL18R_HUMAN IL1RRP NM_003855 Q13478 Q52LC9 uc010fiy.1 uc010fiy.2 uc010fiy.3 uc010fiy.4 uc010fiy.5 uc010fiy.6 The protein encoded by this gene is a cytokine receptor that belongs to the interleukin 1 receptor family. This receptor specifically binds interleukin 18 (IL18), and is essential for IL18 mediated signal transduction. IFN-alpha and IL12 are reported to induce the expression of this receptor in NK and T cells. This gene along with four other members of the interleukin 1 receptor family, including IL1R2, IL1R1, ILRL2 (IL-1Rrp2), and IL1RL1 (T1/ST2), form a gene cluster on chromosome 2q. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2013]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DRR138517.888460.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Within the IL18 receptor complex, responsible for the binding of the pro-inflammatory cytokine IL18, but not IL1A nor IL1B (PubMed:8626725, PubMed:14528293, PubMed:25261253, PubMed:25500532). Involved in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850). Contributes to IL18-induced cytokine production, either independently of SLC12A3, or as a complex with SLC12A3 (By similarity). Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence=; Forms a ternary complex with IL18 and IL18RAP (PubMed:14528293, PubMed:25500532). Within this complex, IL18R1 is involved in ligand-binding and IL18RAP in signaling leading to NF- kappa-B and JNK activation (Probable). Interacts with SLC12A3 in peritoneal macrophages; this interaction is increased by IL18 treatment (By similarity). Q13478; Q14116: IL18; NbExp=2; IntAct=EBI-9817499, EBI-3910835; Membrane ; Single- pass type I membrane protein Highly expressed in leukocytes, spleen, lung. Also expressed, but at lower levels, in liver, small intestine, colon, prostate, thymus, placenta, and heart. Specifically coexpressed with IL18R1 in Th1 cells (PubMed:10925275, PubMed:11046021, PubMed:10653850). Induced by IL12/interleukin-12 in T-cells. Proposed to be a phenotypic marker for T-helper 1 (Th1) cells. The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity. N-glycosylated. N-linked glycosyl chains contribute to ligand recognition and intra-receptor interactions required for formation of an active ternary receptor complex. Belongs to the interleukin-1 receptor family. interleukin-1 receptor activity protein binding plasma membrane inflammatory response immune response signal transduction membrane integral component of membrane natural killer cell activation positive regulation of interferon-gamma production interleukin-18-mediated signaling pathway signaling receptor activity interleukin-18 binding interleukin-18 receptor activity T-helper 1 cell differentiation interleukin-18 receptor complex positive regulation of NF-kappaB transcription factor activity cellular response to cytokine stimulus positive regulation of NIK/NF-kappaB signaling positive regulation of T-helper 1 cell cytokine production uc010fiy.1 uc010fiy.2 uc010fiy.3 uc010fiy.4 uc010fiy.5 uc010fiy.6 
ENST00000233969.3 SLC9A2 ENST00000233969.3 solute carrier family 9 member A2 (from RefSeq NM_003048.6) B2RMS2 ENST00000233969.1 ENST00000233969.2 NHE2 NM_003048 Q9UBY0 SL9A2_HUMAN SLC9A2 uc002tca.1 uc002tca.2 uc002tca.3 uc002tca.4 uc002tca.5 This gene encodes a member of the sodium-hydrogen exchanger (NHE) protein family. These proteins are involved in sodium-ion transport by exchanging intracellular hydrogen ions to external sodium ions and help in the regulation of cell pH and volume. The encoded protein is localized to the apical membrane and is involved in apical absorption of sodium. [provided by RefSeq, Jun 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.84593.1, SRR1803614.213018.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968832 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233969.3/ ENSP00000233969.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Plasma membrane Na(+)/H(+) antiporter. Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) (PubMed:10444453). Major apical Na(+)/H(+) exchanger in the base of the colonic crypt. Controls in the colonic crypt intracellular pH (pHi) to direct colonic epithelial cell differentiation into the absorptive enterocyte lineage at the expense of the secretory lineage (By similarity). Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence=; Interacts with CHP1 and CHP2. Apical cell membrane ; Multi-pass membrane protein Expressed in skeletal muscle, colon and kidney. Lower levels in the testis, prostate, ovary, and small intestine (PubMed:10444453, PubMed:8843774). In the distal colon, expressed along the cryptal axis (PubMed:8843774). Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. The number, localization and denomination of hydrophobic domains in the Na(+)/H(+) exchangers vary among authors. plasma membrane ion transport cation transport sodium ion transport regulation of pH protein localization antiporter activity solute:proton antiporter activity sodium:proton antiporter activity potassium:proton antiporter activity membrane integral component of membrane regulation of intracellular pH transmembrane transport potassium ion transmembrane transport anion transmembrane transport sodium ion import across plasma membrane hydrogen ion transmembrane transport uc002tca.1 uc002tca.2 uc002tca.3 uc002tca.4 uc002tca.5 
ENST00000233997.4 AZU1 ENST00000233997.4 azurocidin 1 (from RefSeq NM_001700.5) AZU1 CAP7_HUMAN ENST00000233997.1 ENST00000233997.2 ENST00000233997.3 NM_001700 P20160 P80014 Q52LG4 Q9UCM1 Q9UCT5 uc002lpz.1 uc002lpz.2 uc002lpz.3 Azurophil granules, specialized lysosomes of the neutrophil, contain at least 10 proteins implicated in the killing of microorganisms. This gene encodes a preproprotein that is proteolytically processed to generate a mature azurophil granule antibiotic protein, with monocyte chemotactic and antimicrobial activity. It is also an important multifunctional inflammatory mediator. This encoded protein is a member of the serine protease gene family but it is not a serine proteinase, because the active site serine and histidine residues are replaced. The genes encoding this protein, neutrophil elastase 2, and proteinase 3 are in a cluster located at chromosome 19pter. All 3 genes are expressed coordinately and their protein products are packaged together into azurophil granules during neutrophil differentiation. [provided by RefSeq, Nov 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X58794.1, ERR279847.7758.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145893, SAMEA2146236 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000233997.4/ ENSP00000233997.1 Protein has antimicrobial activity :: PMID: 11994286 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram- negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G. Cytoplasmic granule membrane ; Peripheral membrane protein ; Cytoplasmic side Note=Localizes to azurophil granules of neutrophil granulocytes. Also called primary granules, these specialized lysosomes of the neutrophil formed early during promyelocyte development store antibacterial proteins and peptides. Cleavage of the N-terminal propeptide which is composed of 7 amino acids occurs in two steps. The initial cleavage of 5 amino acids is followed by the cleavage of a dipeptide to produce the mature form. Belongs to the peptidase S1 family. Elastase subfamily. microglial cell activation serine-type endopeptidase activity protein binding extracellular region extracellular space proteolysis chemotaxis inflammatory response protein kinase C-activating G-protein coupled receptor signaling pathway heparin binding peptidase activity glial cell migration positive regulation of gene expression positive regulation of peptidyl-threonine phosphorylation toxic substance binding membrane antimicrobial humoral response extrinsic component of membrane azurophil granule membrane azurophil granule lumen calcium-mediated signaling using intracellular calcium source monocyte activation positive regulation of tumor necrosis factor biosynthetic process azurophil granule defense response to bacterium negative regulation of apoptotic process regulation of vascular permeability neutrophil degranulation heparan sulfate proteoglycan binding cellular extravasation positive regulation of MHC class II biosynthetic process positive regulation of cell adhesion positive regulation of protein kinase activity macrophage chemotaxis positive regulation of interleukin-1 beta biosynthetic process positive regulation of fractalkine biosynthetic process positive regulation of phagocytosis defense response to Gram-negative bacterium induction of positive chemotaxis defense response to virus cell chemotaxis extracellular exosome protein kinase C signaling neutrophil mediated killing of bacterium uc002lpz.1 uc002lpz.2 uc002lpz.3 
ENST00000234038.11 PPP1R7 ENST00000234038.11 protein phosphatase 1 regulatory subunit 7, transcript variant 1 (from RefSeq NM_002712.3) B4DFD4 B5MCY6 ENST00000234038.1 ENST00000234038.10 ENST00000234038.2 ENST00000234038.3 ENST00000234038.4 ENST00000234038.5 ENST00000234038.6 ENST00000234038.7 ENST00000234038.8 ENST00000234038.9 NM_002712 PP1R7_HUMAN Q15435 Q9UQE5 Q9UQE6 Q9Y6K4 SDS22 uc002wat.1 uc002wat.2 uc002wat.3 uc002wat.4 This gene encodes a protein subunit that regulates the activity of the serine/threonine phosphatase, protein phosphatase-1. The encoded protein is required for completion of the mitotic cycle and for targeting protein phosphatase-1 to mitotic kinetochores. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]. Regulatory subunit of protein phosphatase 1. Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G isoform 1. Q15435; P62136: PPP1CA; NbExp=7; IntAct=EBI-1024281, EBI-357253; Q15435; P62140: PPP1CB; NbExp=10; IntAct=EBI-1024281, EBI-352350; Q15435; P36873: PPP1CC; NbExp=5; IntAct=EBI-1024281, EBI-356283; Q15435; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1024281, EBI-739895; Q15435-3; P01112: HRAS; NbExp=3; IntAct=EBI-10695066, EBI-350145; Nucleus Event=Alternative splicing; Named isoforms=5; Name=1; Synonyms=sds22alpha1; IsoId=Q15435-1; Sequence=Displayed; Name=2; Synonyms=sds22alpha2; IsoId=Q15435-2; Sequence=VSP_019244; Name=3; Synonyms=sds22beta1; IsoId=Q15435-3; Sequence=VSP_019245, VSP_019246; Name=4; Synonyms=sds22beta2; IsoId=Q15435-4; Sequence=VSP_019244, VSP_019245, VSP_019246; Name=5; IsoId=Q15435-5; Sequence=VSP_055672, VSP_019245, VSP_019246; Widely expressed. Belongs to the SDS22 family. protein binding nucleus chromosome cytoplasm protein phosphatase regulator activity enzyme regulator activity positive regulation of protein dephosphorylation regulation of phosphoprotein phosphatase activity regulation of catalytic activity extracellular exosome uc002wat.1 uc002wat.2 uc002wat.3 uc002wat.4 
ENST00000234040.9 PASK ENST00000234040.9 PAS domain containing serine/threonine kinase, transcript variant 2 (from RefSeq NM_015148.4) ENST00000234040.1 ENST00000234040.2 ENST00000234040.3 ENST00000234040.4 ENST00000234040.5 ENST00000234040.6 ENST00000234040.7 ENST00000234040.8 G5E9F1 KIAA0135 NM_015148 PASK_HUMAN Q05BE4 Q68DY3 Q6GSJ5 Q86XH6 Q96RG2 Q99763 Q9UFR7 uc002wao.1 uc002wao.2 uc002wao.3 This gene encodes a member of the serine/threonine kinase family that contains two PAS domains. Expression of this gene is regulated by glucose, and the encoded protein plays a role in the regulation of insulin gene expression. Downregulation of this gene may play a role in type 2 diabetes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Nov 2011]. Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Protein kinase activity is inhibited by the first PAS domain: binding of an unidentified ligand desinhibits the protein kinase activity. May be activated by autophosphorylation on Thr-1161 and Thr-1165 (PubMed:11459942). The activating role of autophosphorylation at Thr-1161 is unclear: according to a report, autophosphorylation at Thr-1161 does not play a major role in activation (PubMed:20943661). Autophosphorylation is enhanced upon phosphatidylinositol monophosphate (phosphatidylinositol 4-phosphate) binding and inhibited upon phosphatidylinositol bi- and tri-phosphate binding. In contrast, phosphorylation of target proteins is inhibited upon all phosphatidylinositol-binding (phosphatidylinositol mono- bi- and tri-phosphate). Q96RG2; P16220: CREB1; NbExp=2; IntAct=EBI-1042651, EBI-711855; Q96RG2; P02545: LMNA; NbExp=2; IntAct=EBI-1042651, EBI-351935; Q96RG2; Q93100: PHKB; NbExp=2; IntAct=EBI-1042651, EBI-740559; Q96RG2; P62753: RPS6; NbExp=3; IntAct=EBI-1042651, EBI-356625; Q96RG2; P07293: CACNA1S; Xeno; NbExp=2; IntAct=EBI-1042651, EBI-8613624; Q96RG2; P02542: DES; Xeno; NbExp=2; IntAct=EBI-1042651, EBI-8614455; Q96RG2; Q28115: GFAP; Xeno; NbExp=2; IntAct=EBI-1042651, EBI-907866; Q96RG2; P02646: TNNI3; Xeno; NbExp=2; IntAct=EBI-1042651, EBI-8614386; Q96RG2; P20152: Vim; Xeno; NbExp=2; IntAct=EBI-1042651, EBI-299269; Cytoplasm Nucleus Note=Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q96RG2-1; Sequence=Displayed; Name=2; IsoId=Q96RG2-2; Sequence=VSP_009302; Name=3; IsoId=Q96RG2-4; Sequence=VSP_045543, VSP_045544; Ubiquitously expressed, with slightly higher expression in brain, prostate and testis. Reduced expression was found in placenta. Present in germ cells of testis and in the midpiece of sperm tails (at protein level). The protein kinase domain mediates binding to phosphatidylinositol. Autophosphorylated on Thr-1161 and Thr-1165. Autophosphorylation is activated by phospholipids. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Sequence=BAA09484.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding nucleus cytoplasm cytosol protein phosphorylation lipid binding kinase activity phosphorylation transferase activity phosphatidylinositol binding intracellular signal transduction regulation of respiratory gaseous exchange negative regulation of glycogen biosynthetic process positive regulation of translation protein autophosphorylation regulation of glucagon secretion energy homeostasis uc002wao.1 uc002wao.2 uc002wao.3 
ENST00000234071.8 PROC ENST00000234071.8 protein C, inactivator of coagulation factors Va and VIIIa, transcript variant 12 (from RefSeq NM_001375613.1) B4DPQ7 ENST00000234071.1 ENST00000234071.2 ENST00000234071.3 ENST00000234071.4 ENST00000234071.5 ENST00000234071.6 ENST00000234071.7 NM_001375613 P04070 PROC_HUMAN Q15189 Q15190 Q16001 Q53S74 Q9UC55 uc002tok.1 uc002tok.2 uc002tok.3 uc002tok.4 uc002tok.5 This gene encodes a vitamin K-dependent plasma glycoprotein. The encoded protein is cleaved to its activated form by the thrombin-thrombomodulin complex. This activated form contains a serine protease domain and functions in degradation of the activated forms of coagulation factors V and VIII. Mutations in this gene have been associated with thrombophilia due to protein C deficiency, neonatal purpura fulminans, and recurrent venous thrombosis.[provided by RefSeq, Dec 2009]. Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts a protective effect on the endothelial cell barrier function (PubMed:25651845). Reaction=Degradation of blood coagulation factors Va and VIIIa.; EC=3.4.21.69; Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin. P04070; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1383018, EBI-3867333; P04070; P51511: MMP15; NbExp=2; IntAct=EBI-1383018, EBI-1383043; Secreted Golgi apparatus Endoplasmic reticulum Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P04070-1; Sequence=Displayed; Name=2; IsoId=P04070-2; Sequence=VSP_054393, VSP_054394; Plasma; synthesized in the liver. The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium. N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not N- glycosylated at Asn-371, is beta. O-glycosylated with core 1 or possibly core 8 glycans. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. May be phosphorylated on a Ser or Thr in a region (AA 25-30) of the propeptide. Thrombophilia due to protein C deficiency, autosomal dominant (THPH3) [MIM:176860]: A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. Individuals with decreased amounts of protein C are classically referred to as having type I protein C deficiency and those with normal amounts of a functionally defective protein as having type II deficiency. te=The disease is caused by variants affecting the gene represented in this entry. Thrombophilia due to protein C deficiency, autosomal recessive (THPH4) [MIM:612304]: A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. It results in a thrombotic condition that can manifest as a severe neonatal disorder or as a milder disorder with late-onset thrombophilia. The severe form leads to neonatal death through massive neonatal venous thrombosis. Often associated with ecchymotic skin lesions which can turn necrotic called purpura fulminans, this disorder is very rare. te=The disease is caused by variants affecting the gene represented in this entry. Calcium also binds, with stronger affinity to another site, beyond the GLA domain. This GLA-independent binding site is necessary for the recognition of the thrombin-thrombomodulin complex. Belongs to the peptidase S1 family. Sequence=S76088; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence=; Name=Wikipedia; Note=Protein C entry; URL="https://en.wikipedia.org/wiki/Protein_C"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/proc/"; serine-type endopeptidase activity calcium ion binding protein binding extracellular region extracellular space endoplasmic reticulum endoplasmic reticulum lumen Golgi apparatus Golgi lumen proteolysis ER to Golgi vesicle-mediated transport blood coagulation hemostasis peptidase activity serine-type peptidase activity hydrolase activity negative regulation of blood coagulation negative regulation of apoptotic process post-translational protein modification cellular protein metabolic process negative regulation of inflammatory response negative regulation of coagulation positive regulation of establishment of endothelial barrier uc002tok.1 uc002tok.2 uc002tok.3 uc002tok.4 uc002tok.5 
ENST00000234111.9 ODC1 ENST00000234111.9 ornithine decarboxylase 1, transcript variant 1 (from RefSeq NM_002539.3) DCOR_HUMAN ENST00000234111.1 ENST00000234111.2 ENST00000234111.3 ENST00000234111.4 ENST00000234111.5 ENST00000234111.6 ENST00000234111.7 ENST00000234111.8 NM_002539 P11926 Q53TU3 Q6LDS9 uc002rao.1 uc002rao.2 uc002rao.3 uc002rao.4 This gene encodes the rate-limiting enzyme of the polyamine biosynthesis pathway which catalyzes ornithine to putrescine. The activity level for the enzyme varies in response to growth-promoting stimuli and exhibits a high turnover rate in comparison to other mammalian proteins. Originally localized to both chromosomes 2 and 7, the gene encoding this enzyme has been determined to be located on 2p25, with a pseudogene located on 7q31-qter. Multiple alternatively spliced transcript variants encoding distinct isoforms have been identified. [provided by RefSeq, Dec 2013]. Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence=; Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence=; Inhibited by S-nitrosylation (PubMed:10462479, PubMed:11461922). Inhibited by antizymes (AZs) OAZ1, OAZ2 and OAZ3 in response to polyamine levels. AZs inhibit the assembly of the functional homodimer by binding to ODC monomers. Additionally, OAZ1 targets ODC monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:17900240). Inhibited by 1-amino-oxy-3- aminopropane (APA, an isosteric analog of putrescine) (PubMed:17407445). Irreversibly inhibited by alpha- difluoromethylornithine (DFMO) (PubMed:17407445). Kinetic parameters: KM=0.08 mM for L-ornithine ; Note=kcat is 3.3 sec(-1) with L-ornithine as substrate. ; Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (Probable). Does not form a heterodimer with AZIN2 (By similarity). P11926; Q9H8Y8: GORASP2; NbExp=11; IntAct=EBI-1044287, EBI-739467; P11926; Q92993: KAT5; NbExp=6; IntAct=EBI-1044287, EBI-399080; P11926; Q9UMX2: OAZ3; NbExp=5; IntAct=EBI-1044287, EBI-10281601; P11926; Q9UMX2-2: OAZ3; NbExp=3; IntAct=EBI-1044287, EBI-12049527; Down-regulated in response to enterovirus 71 (EV71) infection (at protein level). S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues. Bachmann-Bupp syndrome (BABS) [MIM:619075]: An autosomal dominant disorder characterized by global developmental delay, alopecia, absolute or relative macrocephaly, and facial dysmorphism. Neuroimaging shows white matter abnormalities, prominent Virchow-Robin spaces, periventricular cysts, and abnormalities of the corpus callosum. Note=The disease is caused by variants affecting the gene represented in this entry. BABS is due to truncating variants that lead to a gain of function. This phenomenon apparently results from truncation proximal to or involving the C-terminal region of ODC1 protein, distal enough to allow escape from nonsense-mediated decay. A gain of function is corroborated by elevated plasma levels of N-acetylputrescine, with otherwise normal polyamine levels, in affected individuals. Belongs to the Orn/Lys/Arg decarboxylase class-II family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/odc1/"; Name=Wikipedia; Note=Ornithine decarboxylase entry; URL="https://en.wikipedia.org/wiki/Ornithine_decarboxylase"; kidney development catalytic activity ornithine decarboxylase activity protein binding cellular_component cytoplasm cytosol regulation of cellular amino acid metabolic process polyamine metabolic process polyamine biosynthetic process positive regulation of cell proliferation putrescine biosynthetic process response to virus lyase activity carboxy-lyase activity putrescine biosynthetic process from ornithine regulation of protein catabolic process protein homodimerization activity perinuclear region of cytoplasm uc002rao.1 uc002rao.2 uc002rao.3 uc002rao.4 
ENST00000234160.5 GORASP2 ENST00000234160.5 golgi reassembly stacking protein 2, transcript variant 1 (from RefSeq NM_015530.5) B4DKT0 ENST00000234160.1 ENST00000234160.2 ENST00000234160.3 ENST00000234160.4 GOLPH6 GORS2_HUMAN NM_015530 Q53TE3 Q96I74 Q96K84 Q9H8Y8 Q9H946 Q9UFW4 uc002ugk.1 uc002ugk.2 uc002ugk.3 uc002ugk.4 uc002ugk.5 This gene encodes a member of the Golgi reassembly stacking protein family. These proteins may play a role in the stacking of Golgi cisternae and Golgi ribbon formation, as well as Golgi fragmentation during apoptosis or mitosis. The encoded protein also plays a role in the intracellular transport of transforming growth factor alpha and may function as a molecular chaperone. A pseudogene of this gene is located on the short arm of chromosome 2. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jan 2011]. Key structural protein of the Golgi apparatus (PubMed:33301566). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (PubMed:33301566). Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (PubMed:33301566). However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis (PubMed:10487747, PubMed:21515684, PubMed:22523075). May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (PubMed:11101516). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936, PubMed:27062250, PubMed:28067262). Homodimer. Homooligomer. ER stress induces phosphorylation- dependent monomerization (PubMed:27062250). Interacts with BLZF1/Golgin 45 (PubMed:11739401). Identified in a complex with RAB2 and GORASP2 (PubMed:11739401). Interacts with JAM2 and JAM3 (By similarity). Interacts with members of the p24 cargo receptors (PubMed:11739402). Interacts with CNIH1 and the cytoplasmic domain of transmembrane TGFA, prior its transit in the trans-Golgi (PubMed:11101516, PubMed:17607000). Interacts with KCTD5 (PubMed:19361449). Interacts with TMED2 and TMED3 (By similarity). Interacts with SEC16A in response to ER stress (PubMed:28067262). Interacts (via PDZ GRASP-type 1 domain) with core-glycosylated CFTR in response to ER stress (PubMed:21884936). Q9H8Y8; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-739467, EBI-10308705; Q9H8Y8; Q96HD9: ACY3; NbExp=15; IntAct=EBI-739467, EBI-3916242; Q9H8Y8; Q9NXW9: ALKBH4; NbExp=3; IntAct=EBI-739467, EBI-8637516; Q9H8Y8; Q96GX9: APIP; NbExp=3; IntAct=EBI-739467, EBI-359248; Q9H8Y8; O94989: ARHGEF15; NbExp=3; IntAct=EBI-739467, EBI-740691; Q9H8Y8; Q15041: ARL6IP1; NbExp=4; IntAct=EBI-739467, EBI-714543; Q9H8Y8; O95671: ASMTL; NbExp=3; IntAct=EBI-739467, EBI-743231; Q9H8Y8; O75348: ATP6V1G1; NbExp=5; IntAct=EBI-739467, EBI-711802; Q9H8Y8; P54253: ATXN1; NbExp=3; IntAct=EBI-739467, EBI-930964; Q9H8Y8; P54252: ATXN3; NbExp=3; IntAct=EBI-739467, EBI-946046; Q9H8Y8; Q7L4P6: BEND5; NbExp=4; IntAct=EBI-739467, EBI-724373; Q9H8Y8; Q9Y2F9: BTBD3; NbExp=3; IntAct=EBI-739467, EBI-311155; Q9H8Y8; Q6P1W5: C1orf94; NbExp=7; IntAct=EBI-739467, EBI-946029; Q9H8Y8; Q9Y2V2: CARHSP1; NbExp=3; IntAct=EBI-739467, EBI-718719; Q9H8Y8; Q13191: CBLB; NbExp=8; IntAct=EBI-739467, EBI-744027; Q9H8Y8; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-739467, EBI-947308; Q9H8Y8; Q494R4: CCDC153; NbExp=4; IntAct=EBI-739467, EBI-10241443; Q9H8Y8; Q9GZT6: CCDC90B; NbExp=3; IntAct=EBI-739467, EBI-713148; Q9H8Y8; P32320: CDA; NbExp=3; IntAct=EBI-739467, EBI-9250559; Q9H8Y8; Q9UJX2: CDC23; NbExp=9; IntAct=EBI-739467, EBI-396137; Q9H8Y8; Q07002: CDK18; NbExp=3; IntAct=EBI-739467, EBI-746238; Q9H8Y8; P55273: CDKN2D; NbExp=3; IntAct=EBI-739467, EBI-745859; Q9H8Y8; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-739467, EBI-742887; Q9H8Y8; P13569: CFTR; NbExp=6; IntAct=EBI-739467, EBI-349854; Q9H8Y8; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-739467, EBI-723153; Q9H8Y8; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-739467, EBI-1057156; Q9H8Y8; Q9UHC6: CNTNAP2; NbExp=3; IntAct=EBI-739467, EBI-310892; Q9H8Y8; P02489: CRYAA; NbExp=12; IntAct=EBI-739467, EBI-6875961; Q9H8Y8; P02511: CRYAB; NbExp=3; IntAct=EBI-739467, EBI-739060; Q9H8Y8; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-739467, EBI-9087876; Q9H8Y8; P32321: DCTD; NbExp=7; IntAct=EBI-739467, EBI-739870; Q9H8Y8; Q14565: DMC1; NbExp=8; IntAct=EBI-739467, EBI-930865; Q9H8Y8; P59910: DNAJB13; NbExp=3; IntAct=EBI-739467, EBI-11514233; Q9H8Y8; Q16555: DPYSL2; NbExp=15; IntAct=EBI-739467, EBI-1104711; Q9H8Y8; Q9H596: DUSP21; NbExp=7; IntAct=EBI-739467, EBI-7357329; Q9H8Y8; Q13115: DUSP4; NbExp=3; IntAct=EBI-739467, EBI-6591081; Q9H8Y8; O43781-2: DYRK3; NbExp=5; IntAct=EBI-739467, EBI-13332019; Q9H8Y8; Q9NTX5: ECHDC1; NbExp=3; IntAct=EBI-739467, EBI-2807146; Q9H8Y8; Q14232: EIF2B1; NbExp=8; IntAct=EBI-739467, EBI-491065; Q9H8Y8; Q9NT22: EMILIN3; NbExp=5; IntAct=EBI-739467, EBI-3197883; Q9H8Y8; Q8TC92: ENOX1; NbExp=3; IntAct=EBI-739467, EBI-713221; Q9H8Y8; O95571: ETHE1; NbExp=3; IntAct=EBI-739467, EBI-715318; Q9H8Y8; Q9NYK6-3: EURL; NbExp=5; IntAct=EBI-739467, EBI-13371226; Q9H8Y8; Q92562: FIG4; NbExp=3; IntAct=EBI-739467, EBI-4290773; Q9H8Y8; Q8TAK5: GABPB2; NbExp=6; IntAct=EBI-739467, EBI-8468945; Q9H8Y8; O60262: GNG7; NbExp=6; IntAct=EBI-739467, EBI-717760; Q9H8Y8; P63211: GNGT1; NbExp=5; IntAct=EBI-739467, EBI-10220715; Q9H8Y8; Q08379: GOLGA2; NbExp=7; IntAct=EBI-739467, EBI-618309; Q9H8Y8; Q8N9W4-2: GOLGA6L2; NbExp=3; IntAct=EBI-739467, EBI-10268729; Q9H8Y8; O43708: GSTZ1; NbExp=3; IntAct=EBI-739467, EBI-748043; Q9H8Y8; Q9UHL9: GTF2IRD1; NbExp=3; IntAct=EBI-739467, EBI-372530; Q9H8Y8; Q00444: HOXC5; NbExp=3; IntAct=EBI-739467, EBI-11955357; Q9H8Y8; O75506: HSBP1; NbExp=3; IntAct=EBI-739467, EBI-748664; Q9H8Y8; Q9Y547: IFT25; NbExp=3; IntAct=EBI-739467, EBI-747101; Q9H8Y8; Q9NQC1-2: JADE2; NbExp=3; IntAct=EBI-739467, EBI-10311936; Q9H8Y8; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-739467, EBI-742916; Q9H8Y8; Q96MP8-2: KCTD7; NbExp=5; IntAct=EBI-739467, EBI-11954971; Q9H8Y8; Q7L273: KCTD9; NbExp=7; IntAct=EBI-739467, EBI-4397613; Q9H8Y8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-739467, EBI-2125614; Q9H8Y8; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-739467, EBI-14069005; Q9H8Y8; Q6L8G4: KRTAP5-11; NbExp=5; IntAct=EBI-739467, EBI-11993296; Q9H8Y8; Q17RB8: LONRF1; NbExp=10; IntAct=EBI-739467, EBI-2341787; Q9H8Y8; Q9GZQ8: MAP1LC3B; NbExp=6; IntAct=EBI-739467, EBI-373144; Q9H8Y8; O95460-2: MATN4; NbExp=3; IntAct=EBI-739467, EBI-12072296; Q9H8Y8; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-739467, EBI-10172526; Q9H8Y8; Q9BRT3: MIEN1; NbExp=3; IntAct=EBI-739467, EBI-6137472; Q9H8Y8; Q502X0: MORN2; NbExp=3; IntAct=EBI-739467, EBI-725982; Q9H8Y8; Q8TAP9: MPLKIP; NbExp=5; IntAct=EBI-739467, EBI-11603426; Q9H8Y8; O60682: MSC; NbExp=5; IntAct=EBI-739467, EBI-740310; Q9H8Y8; Q5VTT5-2: MYOM3; NbExp=3; IntAct=EBI-739467, EBI-12247808; Q9H8Y8; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-739467, EBI-2859639; Q9H8Y8; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-739467, EBI-3917542; Q9H8Y8; P16083: NQO2; NbExp=5; IntAct=EBI-739467, EBI-358466; Q9H8Y8; Q9UKK9: NUDT5; NbExp=3; IntAct=EBI-739467, EBI-721623; Q9H8Y8; P11926: ODC1; NbExp=11; IntAct=EBI-739467, EBI-1044287; Q9H8Y8; P61457: PCBD1; NbExp=6; IntAct=EBI-739467, EBI-740475; Q9H8Y8; O76083: PDE9A; NbExp=4; IntAct=EBI-739467, EBI-742764; Q9H8Y8; Q96PV4: PNMA5; NbExp=7; IntAct=EBI-739467, EBI-10171633; Q9H8Y8; P30048: PRDX3; NbExp=6; IntAct=EBI-739467, EBI-748336; Q9H8Y8; O43741: PRKAB2; NbExp=3; IntAct=EBI-739467, EBI-1053424; Q9H8Y8; P60891: PRPS1; NbExp=6; IntAct=EBI-739467, EBI-749195; Q9H8Y8; P25788: PSMA3; NbExp=3; IntAct=EBI-739467, EBI-348380; Q9H8Y8; Q13200: PSMD2; NbExp=3; IntAct=EBI-739467, EBI-357648; Q9H8Y8; Q15008: PSMD6; NbExp=5; IntAct=EBI-739467, EBI-359701; Q9H8Y8; O00194: RAB27B; NbExp=3; IntAct=EBI-739467, EBI-10179046; Q9H8Y8; Q14964: RAB39A; NbExp=3; IntAct=EBI-739467, EBI-3048577; Q9H8Y8; Q8TBY0: RBM46; NbExp=3; IntAct=EBI-739467, EBI-12068216; Q9H8Y8; O15211: RGL2; NbExp=3; IntAct=EBI-739467, EBI-712355; Q9H8Y8; P49796-8: RGS3; NbExp=3; IntAct=EBI-739467, EBI-10211517; Q9H8Y8; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-739467, EBI-17589229; Q9H8Y8; P49247: RPIA; NbExp=8; IntAct=EBI-739467, EBI-744831; Q9H8Y8; P57086: SCAND1; NbExp=6; IntAct=EBI-739467, EBI-745846; Q9H8Y8; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-739467, EBI-693002; Q9H8Y8; Q6ZU15: SEPTIN14; NbExp=3; IntAct=EBI-739467, EBI-2009297; Q9H8Y8; P34896: SHMT1; NbExp=3; IntAct=EBI-739467, EBI-715117; Q9H8Y8; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-739467, EBI-12938570; Q9H8Y8; Q6ZVD7: STOX1; NbExp=4; IntAct=EBI-739467, EBI-3923644; Q9H8Y8; Q01995: TAGLN; NbExp=6; IntAct=EBI-739467, EBI-1054248; Q9H8Y8; P15884: TCF4; NbExp=4; IntAct=EBI-739467, EBI-533224; Q9H8Y8; Q9BXF9: TEKT3; NbExp=4; IntAct=EBI-739467, EBI-8644516; Q9H8Y8; Q08117: TLE5; NbExp=4; IntAct=EBI-739467, EBI-717810; Q9H8Y8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-739467, EBI-11741437; Q9H8Y8; Q96S44: TP53RK; NbExp=3; IntAct=EBI-739467, EBI-739588; Q9H8Y8; P17752: TPH1; NbExp=5; IntAct=EBI-739467, EBI-3956833; Q9H8Y8; Q13077: TRAF1; NbExp=7; IntAct=EBI-739467, EBI-359224; Q9H8Y8; Q12933: TRAF2; NbExp=8; IntAct=EBI-739467, EBI-355744; Q9H8Y8; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-739467, EBI-3650647; Q9H8Y8; O00463: TRAF5; NbExp=3; IntAct=EBI-739467, EBI-523498; Q9H8Y8; O75865-2: TRAPPC6A; NbExp=5; IntAct=EBI-739467, EBI-8451480; Q9H8Y8; O00635: TRIM38; NbExp=6; IntAct=EBI-739467, EBI-2130415; Q9H8Y8; Q86TN4-2: TRPT1; NbExp=3; IntAct=EBI-739467, EBI-12403619; Q9H8Y8; Q15714-2: TSC22D1; NbExp=8; IntAct=EBI-739467, EBI-12034704; Q9H8Y8; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-739467, EBI-372432; Q9H8Y8; Q15631: TSN; NbExp=6; IntAct=EBI-739467, EBI-1044160; Q9H8Y8; Q6DKK2: TTC19; NbExp=5; IntAct=EBI-739467, EBI-948354; Q9H8Y8; P40222: TXLNA; NbExp=7; IntAct=EBI-739467, EBI-359793; Q9H8Y8; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-739467, EBI-720977; Q9H8Y8; O95164: UBL3; NbExp=3; IntAct=EBI-739467, EBI-12876508; Q9H8Y8; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-739467, EBI-4400866; Q9H8Y8; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-739467, EBI-2799833; Q9H8Y8; Q9NQW7-3: XPNPEP1; NbExp=3; IntAct=EBI-739467, EBI-12079490; Q9H8Y8; O96006: ZBED1; NbExp=3; IntAct=EBI-739467, EBI-740037; Q9H8Y8; O43829: ZBTB14; NbExp=4; IntAct=EBI-739467, EBI-10176632; Q9H8Y8; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-739467, EBI-746595; Q9H8Y8; Q9UQR1: ZNF148; NbExp=3; IntAct=EBI-739467, EBI-2688184; Q9H8Y8; Q9UQR1-2: ZNF148; NbExp=5; IntAct=EBI-739467, EBI-11742222; Q9H8Y8; PRO_0000045603 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-739467, EBI-6927928; Golgi apparatus membrane ipid-anchor Endoplasmic reticulum membrane Golgi apparatus Note=Detected in the intermediate Golgi, membrane-associated (By similarity). ER stress triggers its relocalization from Golgi to ER membrane (PubMed:27062250, PubMed:28067262). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9H8Y8-1; Sequence=Displayed; Name=2; IsoId=Q9H8Y8-2; Sequence=VSP_011300; Name=3; IsoId=Q9H8Y8-3; Sequence=VSP_054364; Myristoylated (PubMed:11101516). Myristoylation is essential for the Golgi targeting (By similarity). Palmitoylated. Phosphorylated in mitotic cells (PubMed:11408587). ER stress- induced phosphorylation at Ser-441 induces monomerization and subsequent relocalization from Golgi to ER which is essential for mediating unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane (PubMed:21884936, PubMed:27062250). Belongs to the GORASP family. Golgi membrane protein binding endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus organelle organization Golgi organization spermatogenesis membrane cell differentiation response to endoplasmic reticulum stress organelle assembly uc002ugk.1 uc002ugk.2 uc002ugk.3 uc002ugk.4 uc002ugk.5 
ENST00000234170.10 CEBPZ ENST00000234170.10 CCAAT enhancer binding protein zeta (from RefSeq NM_005760.3) CBF2 CEBPZ_HUMAN ENST00000234170.1 ENST00000234170.2 ENST00000234170.3 ENST00000234170.4 ENST00000234170.5 ENST00000234170.6 ENST00000234170.7 ENST00000234170.8 ENST00000234170.9 NM_005760 Q03701 Q8NE75 uc002rpz.1 uc002rpz.2 uc002rpz.3 uc002rpz.4 uc002rpz.5 uc002rpz.6 This gene belongs to the CEBP family. The encoded protein plays a role in cellular response to environmental stimuli through a transcriptional process that involves heat shock factors, conserved DNA elements (heat shock elements or HSEs) and CCAAT boxes. The protein acts as a DNA-binding transcriptional activator and regulates the heat-shock protein 70 (HSP70) promoter in a CCAAT-dependent manner. The protein is also involved in cell growth and differentiation, particularly, hematopoietic differentiation. Methylation of the promoter of this gene or mutations within the gene may be correlated with occurance of acute myeloid leukemia (AML). [provided by RefSeq, Jun 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660807.201620.1, SRR1660803.53522.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234170.10/ ENSP00000234170.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Stimulates transcription from the HSP70 promoter. Nucleus. Belongs to the CBF/MAK21 family. Sequence=AAA51924.1; Type=Frameshift; Evidence=; RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding RNA binding nucleus transcription from RNA polymerase II promoter ribosome biogenesis positive regulation of transcription from RNA polymerase II promoter uc002rpz.1 uc002rpz.2 uc002rpz.3 uc002rpz.4 uc002rpz.5 uc002rpz.6 
ENST00000234179.8 PRKD3 ENST00000234179.8 protein kinase D3 (from RefSeq NM_005813.6) D6W587 ENST00000234179.1 ENST00000234179.2 ENST00000234179.3 ENST00000234179.4 ENST00000234179.5 ENST00000234179.6 ENST00000234179.7 EPK2 KPCD3_HUMAN NM_005813 O94806 PRKCN Q53TR7 Q8NEL8 uc061iee.1 uc061iee.2 uc061iee.3 This gene belongs to the multigene protein kinase D family of serine/threonine kinases, which bind diacylglycerol and phorbol esters. Members of this family are characterized by an N-terminal regulatory domain comprised of a tandem repeat of cysteine-rich zinc-finger motifs and a pleckstrin domain. The C-terminal region contains the catalytic domain and is distantly related to calcium-regulated kinases. Catalytic activity of this enzyme promotes its nuclear localization. This protein has been implicated in a variety of functions including negative regulation of human airway epithelial barrier formation, growth regulation of breast and prostate cancer cells, and vesicle trafficking. [provided by RefSeq, Jan 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.77122.1, SRR1803615.162147.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Activated by DAG and phorbol esters. Phorbol- ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester with high affinity and mediate translocation to the cell membrane. Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC relieves auto-inhibition by the PH domain. O94806; P63027: VAMP2; NbExp=7; IntAct=EBI-1255366, EBI-520113; O94806-2; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-13337369, EBI-10320765; Cytoplasm Membrane Note=Translocation to the cell membrane is required for kinase activation. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O94806-1; Sequence=Displayed; Name=2; IsoId=O94806-2; Sequence=VSP_029405, VSP_029406; Ubiquitous. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily. nucleotide binding protein kinase activity protein serine/threonine kinase activity protein kinase C activity protein binding ATP binding nucleoplasm cytoplasm cytosol protein phosphorylation protein kinase C-activating G-protein coupled receptor signaling pathway membrane kinase activity phosphorylation transferase activity sphingolipid biosynthetic process intracellular signal transduction metal ion binding protein kinase D signaling uc061iee.1 uc061iee.2 uc061iee.3 
ENST00000234198.9 DLX2 ENST00000234198.9 distal-less homeobox 2 (from RefSeq NM_004405.4) DLX2 ENST00000234198.1 ENST00000234198.2 ENST00000234198.3 ENST00000234198.4 ENST00000234198.5 ENST00000234198.6 ENST00000234198.7 ENST00000234198.8 NM_004405 X5D7D8 X5D7D8_HUMAN uc002uhn.1 uc002uhn.2 uc002uhn.3 uc002uhn.4 uc002uhn.5 Many vertebrate homeo box-containing genes have been identified on the basis of their sequence similarity with Drosophila developmental genes. Members of the Dlx gene family contain a homeobox that is related to that of Distal-less (Dll), a gene expressed in the head and limbs of the developing fruit fly. The Distal-less (Dlx) family of genes comprises at least 6 different members, DLX1-DLX6. The DLX proteins are postulated to play a role in forebrain and craniofacial development. This gene is located in a tail-to-tail configuration with another member of the gene family on the long arm of chromosome 2. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK291367.1, BC032558.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2144120, SAMEA2145743 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234198.9/ ENSP00000234198.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Nucleus Belongs to the distal-less homeobox family. negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding chromatin binding single-stranded RNA binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter proximal/distal pattern formation subpallium development hippocampus development olfactory bulb development forebrain neuron differentiation regulation of transcription from RNA polymerase II promoter involved in forebrain neuron fate commitment cerebral cortex GABAergic interneuron differentiation cerebral cortex GABAergic interneuron fate commitment cell differentiation odontogenesis of dentin-containing tooth sequence-specific DNA binding positive regulation of cell differentiation negative regulation of Notch signaling pathway positive regulation of transcription from RNA polymerase II promoter negative regulation of photoreceptor cell differentiation embryonic cranial skeleton morphogenesis embryonic skeletal system development negative regulation of oligodendrocyte differentiation branching morphogenesis of a nerve cartilage development positive regulation of amacrine cell differentiation uc002uhn.1 uc002uhn.2 uc002uhn.3 uc002uhn.4 uc002uhn.5 
ENST00000234256.4 SLC1A4 ENST00000234256.4 solute carrier family 1 member 4, transcript variant 1 (from RefSeq NM_003038.5) ASCT1 B7Z3C0 D6W5F0 ENST00000234256.1 ENST00000234256.2 ENST00000234256.3 NM_003038 P43007 SATT SATT_HUMAN SLC1A4 uc010yqa.1 uc010yqa.2 uc010yqa.3 uc010yqa.4 The protein encoded by this gene is a sodium-dependent neutral amino acid transporter for alanine, serine, cysteine, and threonine. Defects in this gene have been associated with developmental delay, microcephaly, and intellectual disability. [provided by RefSeq, Jan 2017]. Sodium-dependent neutral amino-acid transporter that mediates transport of alanine, serine, cysteine, proline, hydroxyproline and threonine. Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out); Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926; Evidence=; Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out); Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; Evidence=; Reaction=L-cysteine(in) + Na(+)(in) = L-cysteine(out) + Na(+)(out); Xref=Rhea:RHEA:68232, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235; Evidence=; Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out); Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; Evidence= Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out); Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039; Evidence=; Reaction=4-hydroxy-L-proline(in) + Na(+)(in) = 4-hydroxy-L-proline(out) + Na(+)(out); Xref=Rhea:RHEA:70023, ChEBI:CHEBI:29101, ChEBI:CHEBI:58419; Evidence=; Membrane ; Multi- pass membrane protein Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P43007-1; Sequence=Displayed; Name=2; IsoId=P43007-2; Sequence=VSP_042880, VSP_042881; Expressed mostly in brain, muscle, and pancreas but detected in all tissues examined. Spastic tetraplegia, thin corpus callosum, and progressive microcephaly (SPATCCM) [MIM:616657]: A neurodevelopmental disorder characterized by thin corpus callosum, severe progressive microcephaly, severe intellectual disability, seizures, spasticity, and global developmental delay. Most patients are unable to achieve independent walking or speech. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. SLC1A4 subfamily. amino acid transmembrane transport chloride channel activity centrosome microtubule organizing center intermediate filament plasma membrane integral component of plasma membrane amino acid transport glutamine transport cell surface amino acid transmembrane transporter activity neutral amino acid transmembrane transporter activity L-alanine transmembrane transporter activity L-cystine transmembrane transporter activity L-glutamine transmembrane transporter activity L-proline transmembrane transporter activity L-serine transmembrane transporter activity L-threonine transmembrane transporter activity symporter activity L-alanine transport L-cystine transport proline transport L-serine transport threonine transport membrane integral component of membrane dendrite hydroxyproline transport L-hydroxyproline transmembrane transporter activity synaptic transmission, glutamatergic proline transmembrane transport melanosome neuronal cell body cognition transmembrane transport extracellular exosome chloride transmembrane transport uc010yqa.1 uc010yqa.2 uc010yqa.3 uc010yqa.4 
ENST00000234296.7 ORC2 ENST00000234296.7 origin recognition complex subunit 2, transcript variant 2 (from RefSeq NR_033915.2) ENST00000234296.1 ENST00000234296.2 ENST00000234296.3 ENST00000234296.4 ENST00000234296.5 ENST00000234296.6 NR_033915 ORC2L ORC2_HUMAN Q13204 Q13416 Q53TX5 uc002uwr.1 uc002uwr.2 uc002uwr.3 uc002uwr.4 uc002uwr.5 The origin recognition complex (ORC) is a highly conserved six subunits protein complex essential for the initiation of the DNA replication in eukaryotic cells. Studies in yeast demonstrated that ORC binds specifically to origins of replication and serves as a platform for the assembly of additional initiation factors such as Cdc6 and Mcm proteins. The protein encoded by this gene is a subunit of the ORC complex. This protein forms a core complex with ORC3, -4, and -5. It also interacts with CDC45 and MCM10, which are proteins known to be important for the initiation of DNA replication. This protein has been demonstrated to specifically associate with the origin of replication of Epstein-Barr virus in human cells, and is thought to be required for DNA replication from viral origin of replication. Alternatively spliced transcript variants have been found, one of which is a nonsense-mediated mRNA decay candidate. [provided by RefSeq, Oct 2010]. Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3. Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase (PubMed:12909626, PubMed:17716973). Interacts with DBF4 (By similarity). Interacts with MCM10 (PubMed:11095689). Interacts with LRWD1 throughout the cell cycle; this interaction, wich occurs only with non-ubiquitinated form of LRWD1, prevents LRWD1 ubiquitination and hence stabilizes the protein (PubMed:22645314). Interacts with POLQ (PubMed:24989122). Q13416; Q99459: CDC5L; NbExp=2; IntAct=EBI-374957, EBI-374880; Q13416; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-374957, EBI-11962928; Q13416; Q08050: FOXM1; NbExp=2; IntAct=EBI-374957, EBI-866480; Q13416; Q7L590: MCM10; NbExp=5; IntAct=EBI-374957, EBI-374912; Q13416; P25205: MCM3; NbExp=2; IntAct=EBI-374957, EBI-355153; Q13416; Q13415: ORC1; NbExp=14; IntAct=EBI-374957, EBI-374847; Q13416; Q9UBD5: ORC3; NbExp=28; IntAct=EBI-374957, EBI-374916; Q13416; O43929: ORC4; NbExp=12; IntAct=EBI-374957, EBI-374889; Q13416; O43913: ORC5; NbExp=15; IntAct=EBI-374957, EBI-374928; Q13416; Q9NS91: RAD18; NbExp=3; IntAct=EBI-374957, EBI-2339393; Q13416; P57055: RIPPLY3; NbExp=3; IntAct=EBI-374957, EBI-12092053; Q13416; Q15554: TERF2; NbExp=3; IntAct=EBI-374957, EBI-706637; Q13416; P03211: EBNA1; Xeno; NbExp=6; IntAct=EBI-374957, EBI-996522; Nucleus. Belongs to the ORC2 family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/orc2l/"; G1/S transition of mitotic cell cycle negative regulation of transcription from RNA polymerase II promoter nuclear chromosome, telomeric region chromatin heterochromatin origin recognition complex condensed chromosome inner kinetochore DNA replication origin binding protein binding nucleus nucleoplasm nuclear origin of replication recognition complex centrosome DNA replication DNA replication initiation membrane uc002uwr.1 uc002uwr.2 uc002uwr.3 uc002uwr.4 uc002uwr.5 
ENST00000234301.3 COX7A2L ENST00000234301.3 cytochrome c oxidase subunit 7A2 like, transcript variant 6 (from RefSeq NR_134947.2) COX7A2L D6W5A1 ENST00000234301.1 ENST00000234301.2 NR_134947 Q6FGA0 Q6FGA0_HUMAN hCG_1783904 uc002rsk.1 uc002rsk.2 uc002rsk.3 uc002rsk.4 uc002rsk.5 Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein similar to polypeptides 1 and 2 of subunit VIIa in the C-terminal region, and also highly similar to the mouse Sig81 protein sequence. This gene is expressed in all tissues, and upregulated in a breast cancer cell line after estrogen treatment. It is possible that this gene represents a regulatory subunit of COX and mediates the higher level of energy production in target cells by estrogen. Several transcript variants, some protein-coding and others non-protein coding, have been found for this gene. [provided by RefSeq, Jan 2016]. Belongs to the cytochrome c oxidase VIIa family. cytochrome-c oxidase activity nucleolus mitochondrion mitochondrial respiratory chain electron carrier activity membrane integral component of membrane electron transport chain hydrogen ion transmembrane transport uc002rsk.1 uc002rsk.2 uc002rsk.3 uc002rsk.4 uc002rsk.5 
ENST00000234310.8 PPP3R1 ENST00000234310.8 protein phosphatase 3 regulatory subunit B, alpha (from RefSeq NM_000945.4) B2RC10 B5MDU4 CANB1_HUMAN CNA2 CNB ENST00000234310.1 ENST00000234310.2 ENST00000234310.3 ENST00000234310.4 ENST00000234310.5 ENST00000234310.6 ENST00000234310.7 NM_000945 P06705 P15117 P63098 Q08044 Q53SL0 uc002sei.1 uc002sei.2 uc002sei.3 Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity. Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B) (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:26794871, PubMed:27974827). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). Interacts with catalytic subunit PPP3CA/calcineurin A (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:27974827, PubMed:31375679). Interacts with catalytic subunit PPP3CB/calcineurin A (PubMed:26794871). Interacts with CIB1 (via C-terminal region); the interaction increases upon cardiomyocyte hypertrophy (By similarity). Interacts with RCAN1 (PubMed:12809556). Interacts with SPATA33 (via PQIIIT motif) (PubMed:34446558). P63098; Q99683: MAP3K5; NbExp=2; IntAct=EBI-915984, EBI-476263; P63098; Q08209: PPP3CA; NbExp=6; IntAct=EBI-915984, EBI-352922; P63098; Q08209-1: PPP3CA; NbExp=7; IntAct=EBI-915984, EBI-15637215; P63098; Q08209-2: PPP3CA; NbExp=13; IntAct=EBI-915984, EBI-11959013; P63098; P48454: PPP3CC; NbExp=4; IntAct=EBI-915984, EBI-2827192; Cytoplasm, cytosol Cell membrane Cell membrane, sarcolemma Cell membrane ; Lipid-anchor Note=Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocyte hypertrophy. This protein has four functional calcium-binding sites (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:26794871, PubMed:27974827). Although African swine fever virus infects pigs and not humans, human PPP3R1 and PPP3CA have been used for the crystallization. PPP3CA and PPP3R1 interact with African swine fever virus Mal-047/A238L (via PKIIIT and FLCVK motifs); the interaction does not block catalytic activity per se but inhibits PPP3CA function by blocking the access to the two substrate recognition (PubMed:23468591). Belongs to the calcineurin regulatory subunit family. calcium-dependent protein serine/threonine phosphatase activity calcium ion binding protein binding calmodulin binding nucleoplasm cytoplasm mitochondrion cytosol plasma membrane calcineurin complex protein dephosphorylation Wnt signaling pathway, calcium modulating pathway cyclosporin A binding membrane phosphatase binding protein domain specific binding calcineurin-NFAT signaling cascade Fc-epsilon receptor signaling pathway sarcolemma positive regulation of transcription from RNA polymerase II promoter metal ion binding positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway uc002sei.1 uc002sei.2 uc002sei.3 
ENST00000234313.8 PLEK ENST00000234313.8 pleckstrin (from RefSeq NM_002664.3) B2R9E8 ENST00000234313.1 ENST00000234313.2 ENST00000234313.3 ENST00000234313.4 ENST00000234313.5 ENST00000234313.6 ENST00000234313.7 NM_002664 P08567 P47 PLEK_HUMAN Q53SU8 Q6FGM8 Q6FGQ1 Q8WV81 uc002sen.1 uc002sen.2 uc002sen.3 uc002sen.4 uc002sen.5 uc002sen.6 Major protein kinase C substrate of platelets. P08567; O95810: CAVIN2; NbExp=4; IntAct=EBI-2565501, EBI-742141; P08567; Q14642: INPP5A; NbExp=4; IntAct=EBI-2565501, EBI-8670520; hematopoietic progenitor cell differentiation platelet degranulation protein kinase C binding protein binding extracellular region cytoplasm cytosol plasma membrane vesicle docking involved in exocytosis integrin-mediated signaling pathway positive regulation of platelet activation negative regulation of inositol phosphate biosynthetic process positive regulation of inositol-polyphosphate 5-phosphatase activity membrane cell projection organization positive regulation of actin filament depolymerization phospholipase C-inhibiting G-protein coupled receptor signaling pathway cortical actin cytoskeleton organization ruffle organization actin cytoskeleton reorganization positive regulation of actin filament bundle assembly ruffle membrane positive regulation of integrin activation intracellular signal transduction protein homodimerization activity phosphatidylinositol-3,4-bisphosphate binding negative regulation of G-protein coupled receptor protein signaling pathway phosphatidylinositol metabolic process negative regulation of calcium-mediated signaling regulation of cell diameter thrombin-activated receptor signaling pathway platelet aggregation protein kinase C signaling protein secretion by platelet uc002sen.1 uc002sen.2 uc002sen.3 uc002sen.4 uc002sen.5 uc002sen.6 
ENST00000234347.10 PRTN3 ENST00000234347.10 proteinase 3 (from RefSeq NM_002777.4) ENST00000234347.1 ENST00000234347.2 ENST00000234347.3 ENST00000234347.4 ENST00000234347.5 ENST00000234347.6 ENST00000234347.7 ENST00000234347.8 ENST00000234347.9 MBN NM_002777 P15637 P18078 P24158 PRTN3_HUMAN Q4VB08 Q4VB09 Q6LBM7 Q6LBN2 Q9UD25 Q9UQD8 uc002lqa.1 uc002lqa.2 uc002lqa.3 Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) (PubMed:3198760, PubMed:2033050, PubMed:28240246). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration (PubMed:23202369). May play a role in neutrophil transendothelial migration, probably when associated with CD177 (PubMed:22266279). Reaction=Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.; EC=3.4.21.76; Evidence= Inhibited by phenylmethanesulfonyl fluoride (PMSF) and diisopropyl fluorophosphate (DFP). pH dependence: Optimum pH is 7.4. ; May form dimers (PubMed:28240246). Interacts with CD177; the interaction tethers PRTN3 to the cell surface; the interaction is direct (PubMed:17244676, PubMed:28240246). Interacts with SERPINB1 (PubMed:30692621). P24158; P24001-4: IL32; NbExp=3; IntAct=EBI-465028, EBI-15570379; Cytoplasmic granule creted Cell membrane eripheral membrane protein xtracellular side mbrane raft ; Peripheral membrane protein ; Extracellular side Note=Localizes predominantly to azurophil granules (primary secretory granules) in neutrophils (PubMed:2033050, PubMed:3198760, PubMed:7897245, PubMed:18462208). Secreted upon neutrophil stimulation by TNF-alpha, lipopolysaccharide (LPS), fMLP and CXCL8/IL8 or during neutrophil transmigration (PubMed:22266279, PubMed:28240246). Following secretion tethered to the cell membrane by CD177 (PubMed:18462208, PubMed:22266279). Expressed in polymorphonuclear leukocytes (at protein level) (PubMed:2033050, PubMed:7897245, PubMed:3198760). Expressed in neutrophils (at protein level) (PubMed:28240246, PubMed:18462208, PubMed:21193407, PubMed:22266279, PubMed:17244676). Expressed in differentiating neutrophils (PubMed:18462208). Induced during CSF3/G-CSF-mediated neutrophil differentiation. Note=Is the major autoantigen in anti-neutrophil cytoplasmic autoantibody (ANCA)-associated vasculitis (Wegener's granulomatosis) (PubMed:2377228, PubMed:2679910). This complex, systemic disease is characterized by granulomatous inflammation with necrotizing lesions in the respiratory tract, glomerulonephritis, vasculitis, and anti- neutrophil cytoplasmatic autoantibodies detected in patient sera (PubMed:2377228, PubMed:2679910). PRTN3 causes emphysema when administered by tracheal insufflation to hamsters (PubMed:3198760). Belongs to the peptidase S1 family. Elastase subfamily. Sequence=AAA36342.1; Type=Frameshift; Evidence=; Sequence=CAA39598.1; Type=Erroneous initiation; Evidence=; Name=Wikipedia; Note=Proteinase 3 entry; URL="https://en.wikipedia.org/wiki/Proteinase_3"; serine-type endopeptidase activity receptor binding protein binding extracellular region extracellular space cytosol plasma membrane proteolysis membrane protein ectodomain proteolysis phagocytosis blood coagulation peptidase activity serine-type peptidase activity positive regulation of cell proliferation membrane hydrolase activity cytokine-mediated signaling pathway antimicrobial humoral response enzyme binding collagen catabolic process azurophil granule lumen neutrophil degranulation positive regulation of GTPase activity plasma membrane raft membrane raft cell-cell junction maintenance negative regulation of phagocytosis extracellular exosome neutrophil extravasation mature conventional dendritic cell differentiation uc002lqa.1 uc002lqa.2 uc002lqa.3 
ENST00000234371.10 KISS1R ENST00000234371.10 KISS1 receptor (from RefSeq NM_032551.5) A5D8U2 AXOR12 B2RTV1 ENST00000234371.1 ENST00000234371.2 ENST00000234371.3 ENST00000234371.4 ENST00000234371.5 ENST00000234371.6 ENST00000234371.7 ENST00000234371.8 ENST00000234371.9 GPR54 KISSR_HUMAN NM_032551 Q969F8 Q96QG0 uc002lqk.1 uc002lqk.2 uc002lqk.3 uc002lqk.4 uc002lqk.5 The protein encoded by this gene is a galanin-like G protein-coupled receptor that binds metastin, a peptide encoded by the metastasis suppressor gene KISS1. The tissue distribution of the expressed gene suggests that it is involved in the regulation of endocrine function, and this is supported by the finding that this gene appears to play a role in the onset of puberty. Mutations in this gene have been associated with hypogonadotropic hypogonadism and central precocious puberty. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC141812.1, AY253982.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN01820689, SAMN01820701 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234371.10/ ENSP00000234371.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Receptor for metastin (kisspeptin-54 or kp-54), a C- terminally amidated peptide of KiSS1. KiSS1 is a metastasis suppressor protein that suppresses metastases in malignant melanomas and in some breast carcinomas without affecting tumorigenicity. The metastasis suppressor properties may be mediated in part by cell cycle arrest and induction of apoptosis in malignant cells. The receptor is essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/KISS1R system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. The receptor is also probably involved in the regulation and fine-tuning of trophoblast invasion generated by the trophoblast itself. Analysis of the transduction pathways activated by the receptor identifies coupling to phospholipase C and intracellular calcium release through pertussis toxin-insensitive G(q) proteins. Q969F8; P50148: GNAQ; NbExp=2; IntAct=EBI-8481408, EBI-3909604; Q969F8; P67775: PPP2CA; NbExp=3; IntAct=EBI-8481408, EBI-712311; Cell membrane; Multi-pass membrane protein. Most highly expressed in the pancreas, placenta and spinal cord, with lower-level of expression in peripheral blood leukocytes, kidney, lung, fetal liver, stomach, small intestine, testes, spleen, thymus, adrenal glands and lymph nodes. In the adult brain, expressed in the superior frontal gyrus, putamen, caudate nucleus, cingulate gyrus, nucleus accumbens, hippocampus, pons and amygdala, as well as the hypothalamus and pituitary. Expression levels are higher in early (7-9 weeks) than term placentas. Expression levels were increased in both early placentas and molar pregnancies and were reduced in choriocarcinoma cells. Expressed at higher levels in first trimester trophoblasts than at term of gestation. Also found in the extravillous trophoblast suggesting endocrine/paracrine activation mechanism. Expressed at higher levels in first trimester trophoblasts than at term of gestation. Hypogonadotropic hypogonadism 8 with or without anosmia (HH8) [MIM:614837]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. In some cases, it is associated with non-reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). te=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in KISS1R as well as in other HH-associated genes including FGFR1 and IL17RD (PubMed:23643382). Precocious puberty, central 1 (CPPB1) [MIM:176400]: A condition defined as the development of secondary sexual characteristics in boys and girls at a chronological age that is 2.5 standard deviations below the mean age at onset of puberty in the population. Central precocious puberty results from premature activation of the hypothalamic-pituitary-gonadal axis. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the G-protein coupled receptor 1 family. Name=Protein Spotlight; Note=Tintin's blight - Issue 58 of May 2005; URL="https://web.expasy.org/spotlight/back_issues/058"; G-protein coupled receptor activity protein binding plasma membrane integral component of plasma membrane cilium signal transduction G-protein coupled receptor signaling pathway neuropeptide signaling pathway neuropeptide receptor activity G-protein coupled peptide receptor activity cell surface membrane integral component of membrane intracellular membrane-bounded organelle uc002lqk.1 uc002lqk.2 uc002lqk.3 uc002lqk.4 uc002lqk.5 
ENST00000234389.3 GRIN3B ENST00000234389.3 glutamate ionotropic receptor NMDA type subunit 3B (from RefSeq NM_138690.3) ENST00000234389.1 ENST00000234389.2 NMD3B_HUMAN NM_138690 O60391 Q5EAK7 Q7RTW9 uc002lqo.1 uc002lqo.2 The protein encoded by this gene is a subunit of an N-methyl-D-aspartate (NMDA) receptor. The encoded protein is found primarily in motor neurons, where it forms a heterotetramer with GRIN1 to create an excitatory glycine receptor. Variations in this gene have been proposed to be linked to schizophrenia. [provided by RefSeq, Nov 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY507106.1, AY507107.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158569, SAMN01820689 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234389.3/ ENSP00000234389.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B). Does not form functional homomeric channels. Found in a complex containing GRIN1 and GRIN2A (By similarity). Cell membrane ; Multi-pass membrane protein Postsynaptic cell membrane Note=Requires the presence of GRIN1 to be targeted at the plasma membrane. Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR3B/GRIN3B subfamily. Sequence=AAC12680.1; Type=Erroneous gene model prediction; Evidence=; ionotropic glutamate receptor activity ion channel activity cation channel activity calcium channel activity plasma membrane ion transport glutamate receptor activity ligand-gated ion channel activity membrane integral component of membrane glycine binding NMDA selective glutamate receptor complex cell junction neurotransmitter receptor activity ion transmembrane transport ionotropic glutamate receptor signaling pathway synaptic transmission, glutamatergic signaling receptor activity neurotransmitter binding neuronal cell body synapse postsynaptic membrane modulation of synaptic transmission protein insertion into membrane regulation of calcium ion transport regulation of postsynaptic membrane potential calcium ion transmembrane transport cation transmembrane transport postsynaptic density membrane transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential uc002lqo.1 uc002lqo.2 
ENST00000234392.3 VAX2 ENST00000234392.3 ventral anterior homeobox 2 (from RefSeq NM_012476.3) ENST00000234392.1 ENST00000234392.2 NM_012476 Q53Y33 Q9UIW0 VAX2_HUMAN uc002shh.1 uc002shh.2 uc002shh.3 uc002shh.4 uc002shh.5 This gene encodes a homeobox protein and is almost exclusively expressed in the ventral portion of the retina during development. In mouse studies, this gene was found to be required for the correct formation of the optic fissure and other aspects of retinal development. [provided by RefSeq, Sep 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: Y17791.1, SRR3476690.1009352.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142853, SAMEA2145743 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234392.3/ ENSP00000234392.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Transcription factor that may function in dorsoventral specification of the forebrain. Regulates the expression of Wnt signaling antagonists including the expression of a truncated TCF7L2 isoform that cannot bind CTNNB1 and acts therefore as a potent dominant-negative Wnt antagonist. Plays a crucial role in eye development and, in particular, in the specification of the ventral optic vesicle (By similarity). May be a regulator of axial polarization in the retina. Q9UIW0; Q99471: PFDN5; NbExp=3; IntAct=EBI-12090999, EBI-357275; Q9UIW0; P78424: POU6F2; NbExp=3; IntAct=EBI-12090999, EBI-12029004; Q9UIW0; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-12090999, EBI-12068150; Nucleus Expressed in the ventral part of the optic vesicles at 7 week dpc. Belongs to the EMX homeobox family. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus cytoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development ectoderm development axonogenesis central nervous system development visual perception dorsal/ventral axis specification Wnt signaling pathway neuron differentiation forebrain development chromatin DNA binding camera-type eye development sequence-specific DNA binding embryonic eye morphogenesis retina development in camera-type eye uc002shh.1 uc002shh.2 uc002shh.3 uc002shh.4 uc002shh.5 
ENST00000234396.10 ATP6V1B1 ENST00000234396.10 ATPase H+ transporting V1 subunit B1 (from RefSeq NM_001692.4) ATP6B1 ENST00000234396.1 ENST00000234396.2 ENST00000234396.3 ENST00000234396.4 ENST00000234396.5 ENST00000234396.6 ENST00000234396.7 ENST00000234396.8 ENST00000234396.9 NM_001692 P15313 Q53FY0 Q6P4H6 VATB VATB1_HUMAN VPP3 uc002shj.1 uc002shj.2 uc002shj.3 uc002shj.4 uc002shj.5 uc002shj.6 This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC063411.1, AK291121.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968832, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234396.10/ ENSP00000234396.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Non-catalytic subunit of the V1 complex of vacuolar(H+)- ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:16769747). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32001091). Essential for the proper assembly and activity of V- ATPase (PubMed:16769747). In renal intercalated cells, mediates secretion of protons (H+) into the urine thereby ensuring correct urinary acidification (PubMed:16769747). Required for optimal olfactory function by mediating the acidification of the nasal olfactory epithelium (By similarity). V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (By similarity). The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity). The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By similarity). Forms a complex with NHERF1 and SCL4A7 (PubMed:12444018). P15313; P54253: ATXN1; NbExp=6; IntAct=EBI-2891281, EBI-930964; P15313; P46379-2: BAG6; NbExp=3; IntAct=EBI-2891281, EBI-10988864; P15313; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-2891281, EBI-12593112; P15313; O14645: DNALI1; NbExp=3; IntAct=EBI-2891281, EBI-395638; P15313; P04792: HSPB1; NbExp=3; IntAct=EBI-2891281, EBI-352682; P15313; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2891281, EBI-10975473; P15313; O14901: KLF11; NbExp=3; IntAct=EBI-2891281, EBI-948266; P15313; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2891281, EBI-396669; P15313; Q13148: TARDBP; NbExp=6; IntAct=EBI-2891281, EBI-372899; P15313; P02766: TTR; NbExp=3; IntAct=EBI-2891281, EBI-711909; P15313; O76024: WFS1; NbExp=3; IntAct=EBI-2891281, EBI-720609; Apical cell membrane Basolateral cell membrane Kidney; localizes to early distal nephron, encompassing thick ascending limbs and distal convoluted tubules (at protein level) (PubMed:29993276, PubMed:16769747). Expressed in the cochlea and endolymphatic sac (PubMed:9916796). The PDZ-binding motif mediates interactions with NHERF1 and SCL4A7. Renal tubular acidosis, distal, 2, with progressive sensorineural hearing loss (DRTA2) [MIM:267300]: An autosomal recessive disease characterized by the association of renal distal tubular acidosis with sensorineural hearing loss. Distal renal tubular acidosis is characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha-intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the ATPase alpha/beta chains family. Sequence=AAA36498.1; Type=Erroneous initiation; Evidence=; ossification renal water homeostasis renal sodium ion transport ATP binding cytoplasm cytosol microvillus prostaglandin metabolic process ion transport regulation of pH excretion sensory perception of sound synaptic vesicle insulin receptor signaling pathway regulation of gene expression endomembrane system hydrogen ion transmembrane transporter activity membrane regulation of macroautophagy basolateral plasma membrane apical plasma membrane lateral plasma membrane vacuolar proton-transporting V-type ATPase complex hydrolase activity adult behavior proton-transporting V-type ATPase, V1 domain transferrin transport ion transmembrane transport renal sodium excretion olfactory behavior inner ear morphogenesis macromolecular complex binding pH reduction ATP metabolic process chloride ion homeostasis calcium ion homeostasis potassium ion homeostasis extracellular exosome phagosome acidification extrinsic component of synaptic vesicle membrane hydrogen ion transmembrane transport uc002shj.1 uc002shj.2 uc002shj.3 uc002shj.4 uc002shj.5 uc002shj.6 
ENST00000234420.11 MSH6 ENST00000234420.11 mutS homolog 6, transcript variant 42 (from RefSeq NR_176261.1) B4DF41 B4E3I4 ENST00000234420.1 ENST00000234420.10 ENST00000234420.2 ENST00000234420.3 ENST00000234420.4 ENST00000234420.5 ENST00000234420.6 ENST00000234420.7 ENST00000234420.8 ENST00000234420.9 F5H2F9 GTBP MSH6 MSH6_HUMAN NR_176261 O43706 O43917 P52701 Q8TCX4 Q9BTB5 uc002rwd.1 uc002rwd.2 uc002rwd.3 uc002rwd.4 uc002rwd.5 uc002rwd.6 Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. Component of the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). Heterodimer consisting of MSH2-MSH6 (MutS alpha) (PubMed:8942985, PubMed:7604264). Forms a ternary complex with MutL alpha (MLH1-PMS1). Interacts with MCM9 (PubMed:26300262). Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex (PubMed:10783165). This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains (PubMed:10783165). (Microbial infection) Interacts with herpes simplex virus 1 protein UL12. P52701; Q9NXL9: MCM9; NbExp=2; IntAct=EBI-395529, EBI-2804985; P52701; P43246: MSH2; NbExp=9; IntAct=EBI-395529, EBI-355888; Nucleus Chromosome Note=Associates with H3K36me3 via its PWWP domain. Event=Alternative splicing; Named isoforms=4; Name=GTBP-N; IsoId=P52701-1; Sequence=Displayed; Name=GTBP-alt; IsoId=P52701-2; Sequence=VSP_003291, VSP_003292; Name=3; IsoId=P52701-3; Sequence=VSP_054419; Name=4; IsoId=P52701-4; Sequence=VSP_055020; The PWWP domain specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). The N-terminus is blocked. Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway. Lynch syndrome 5 (LYNCH5) [MIM:614350]: A form of Lynch syndrome, an autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra- colonic tumors of the gastrointestinal, urological and female reproductive tracts. Lynch syndrome is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, it is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical Lynch syndrome is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected Lynch syndrome' or 'incomplete Lynch syndrome' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. te=The disease is caused by variants affecting the gene represented in this entry. Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. te=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mismatch repair cancer syndrome 3 (MMRCS3) [MIM:619097]: An autosomal recessive form of mismatch repair cancer syndrome, a childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. Note=The disease is caused by variants affecting the gene represented in this entry. Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. te=Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the DNA mismatch repair MutS family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/344/MSH6"; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/msh6/"; nucleotide binding four-way junction DNA binding meiotic mismatch repair nuclear chromatin DNA binding chromatin binding damaged DNA binding protein binding ATP binding nucleus nucleoplasm chromosome Golgi apparatus cytosol DNA repair pyrimidine dimer repair mismatch repair cellular response to DNA damage stimulus DNA-dependent ATPase activity determination of adult lifespan intrinsic apoptotic signaling pathway in response to DNA damage response to UV viral process somatic hypermutation of immunoglobulin genes somatic recombination of immunoglobulin gene segments enzyme binding mismatched DNA binding guanine/thymine mispair binding mismatch repair complex MutSalpha complex methylated histone binding interstrand cross-link repair intracellular membrane-bounded organelle maintenance of DNA repeat elements isotype switching negative regulation of DNA recombination positive regulation of helicase activity intrinsic apoptotic signaling pathway magnesium ion binding double-stranded DNA binding ATPase activity single guanine insertion binding single thymine insertion binding oxidized purine DNA binding MutLalpha complex binding ADP binding protein homodimerization activity uc002rwd.1 uc002rwd.2 uc002rwd.3 uc002rwd.4 uc002rwd.5 uc002rwd.6 
ENST00000234453.10 PLEKHA3 ENST00000234453.10 pleckstrin homology domain containing A3 (from RefSeq NM_019091.4) ENST00000234453.1 ENST00000234453.2 ENST00000234453.3 ENST00000234453.4 ENST00000234453.5 ENST00000234453.6 ENST00000234453.7 ENST00000234453.8 ENST00000234453.9 FAPP1 NM_019091 PKHA3_HUMAN Q4ZG69 Q86TQ1 Q9HB20 Q9NXT3 uc002umn.1 uc002umn.2 uc002umn.3 uc002umn.4 uc002umn.5 Plays a role in regulation of vesicular cargo transport from the trans-Golgi network (TGN) to the plasma membrane (PubMed:15107860). Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels and activates the PtdIns(4)P phosphatase activity of SACM1L when it binds PtdIns(4)P in 'trans' configuration (PubMed:30659099). Binds preferentially to PtdIns(4)P (PubMed:11001876, PubMed:15107860). Negatively regulates APOB secretion from hepatocytes (PubMed:30659099). Interacts with GTP-bound ARF1 (PubMed:15107860, PubMed:21454700). Interacts with SACM1L and VAPA and/or VAPB to form a ternary complex (PubMed:30659099). Q9HB20; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-11079894, EBI-10694655; Q9HB20; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-11079894, EBI-14103818; Q9HB20; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-11079894, EBI-10288852; Q9HB20; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-11079894, EBI-2514313; Q9HB20; Q9HB20: PLEKHA3; NbExp=6; IntAct=EBI-11079894, EBI-11079894; Q9HB20; O43148: RNMT; NbExp=3; IntAct=EBI-11079894, EBI-877832; Q9HB20; O14492-2: SH2B2; NbExp=3; IntAct=EBI-11079894, EBI-19952306; Q9HB20; O95988: TCL1B; NbExp=3; IntAct=EBI-11079894, EBI-727338; Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein Note=Localizes to ER-trans Golgi network (TGN) contacts sites. Widely expressed. The PH domain binds the small GTPase ARF1 and phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and is required for its recruitment to the trans-Golgi network (TGN). Sequence=BAA90927.1; Type=Erroneous initiation; Evidence=; Golgi membrane Golgi apparatus cytosol phosphatidylinositol biosynthetic process biological_process lipid binding membrane ER to Golgi ceramide transport ceramide transport phosphatidylinositol-4-phosphate binding ceramide 1-phosphate binding ceramide 1-phosphate transporter activity ceramide 1-phosphate transport uc002umn.1 uc002umn.2 uc002umn.3 uc002umn.4 uc002umn.5 
ENST00000234454.6 SPR ENST00000234454.6 sepiapterin reductase (from RefSeq NM_003124.5) A8K741 D6W5H2 ENST00000234454.1 ENST00000234454.2 ENST00000234454.3 ENST00000234454.4 ENST00000234454.5 NM_003124 P35270 Q53GI9 Q9UBB1 SPRE_HUMAN uc002sik.1 uc002sik.2 uc002sik.3 uc002sik.4 This gene encodes an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is important in the biosynthesis of tetrahydrobiopterin (BH4). Mutations in this gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency. A pseudogene has been identified on chromosome 1. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163658.467140.1, AK222942.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234454.6/ ENSP00000234454.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. Reaction=L-erythro-7,8-dihydrobiopterin + NADP(+) = H(+) + NADPH + sepiapterin; Xref=Rhea:RHEA:18953, ChEBI:CHEBI:15378, ChEBI:CHEBI:16095, ChEBI:CHEBI:43029, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.153; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18955; Evidence=; Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = 6- pyruvoyl-5,6,7,8-tetrahydropterin + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:32627, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59560, ChEBI:CHEBI:136564; EC=1.1.1.153; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32629; Evidence=; Kinetic parameters: KM=14.3 uM for sepiapterin KM=10 uM for NADPH Note=kcat is 1.1 sec(-1) with sepiapterin as substrate (PubMed:10350607). kcat is 1.1 sec(-1) with NADPH as substrate (PubMed:10350607). ; Homodimer. Cytoplasm. In vitro phosphorylation of Ser-213 by CaMK2 does not change kinetic parameters. Dystonia, DOPA-responsive, due to sepiapterin reductase deficiency (DRDSPRD) [MIM:612716]: A form of DOPA-responsive dystonia. In the majority of cases, patients manifest progressive psychomotor retardation, dystonia and spasticity. Cognitive anomalies are also often present. The disease is due to severe dopamine and serotonin deficiencies in the central nervous system caused by a defect in BH4 synthesis. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the sepiapterin reductase family. aldo-keto reductase (NADP) activity sepiapterin reductase activity nucleoplasm cytoplasm cytosol tetrahydrobiopterin biosynthetic process nitric oxide biosynthetic process oxidoreductase activity NADP binding regulation of nitric-oxide synthase activity cofactor metabolic process oxidation-reduction process extracellular exosome uc002sik.1 uc002sik.2 uc002sik.3 uc002sik.4 
ENST00000234590.10 ENO1 ENST00000234590.10 enolase 1, transcript variant 1 (from RefSeq NM_001428.5) B2RD59 ENO1L1 ENOA_HUMAN ENST00000234590.1 ENST00000234590.2 ENST00000234590.3 ENST00000234590.4 ENST00000234590.5 ENST00000234590.6 ENST00000234590.7 ENST00000234590.8 ENST00000234590.9 MBPB1 MPB1 NM_001428 P06733 P22712 Q16704 Q4TUS4 Q53FT9 Q53HR3 Q658M5 Q6GMP2 Q71V37 Q7Z3V6 Q8WU71 Q96GV1 Q9BT62 Q9UCH6 Q9UM55 uc001apj.1 uc001apj.2 uc001apj.3 uc001apj.4 This gene encodes alpha-enolase, one of three enolase isoenzymes found in mammals. Each isoenzyme is a homodimer composed of 2 alpha, 2 gamma, or 2 beta subunits, and functions as a glycolytic enzyme. Alpha-enolase in addition, functions as a structural lens protein (tau-crystallin) in the monomeric form. Alternative splicing of this gene results in a shorter isoform that has been shown to bind to the c-myc promoter and function as a tumor suppressor. Several pseudogenes have been identified, including one on the long arm of chromosome 1. Alpha-enolase has also been identified as an autoantigen in Hashimoto encephalopathy. [provided by RefSeq, Jan 2011]. Glycolytic enzyme the catalyzes the conversion of 2- phosphoglycerate to phosphoenolpyruvate (PubMed:29775581, PubMed:1369209). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:2005901, PubMed:10802057, PubMed:12666133, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209). [Isoform MBP-1]: Binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Binds two Mg(2+) per subunit. Required for catalysis and for stabilizing the dimer. ; pH dependence: Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0. ; Carbohydrate degradation; glycolysis; pyruvate from D- glyceraldehyde 3-phosphate: step 4/5. Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific (PubMed:18560153). ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (PubMed:9308760). Isoform MBP-1 interacts with TRAPPC2B (PubMed:11134351). Interacts with ENO4 and PGAM2 (By similarity). Interacts with CMTM6 (PubMed:28813417). P06733; P22303: ACHE; NbExp=2; IntAct=EBI-353877, EBI-1637793; P06733; P42858: HTT; NbExp=13; IntAct=EBI-353877, EBI-466029; P06733; P12004: PCNA; NbExp=3; IntAct=EBI-353877, EBI-358311; P06733; Q8WZ42: TTN; NbExp=3; IntAct=EBI-353877, EBI-681210; P06733; P63104: YWHAZ; NbExp=2; IntAct=EBI-353877, EBI-347088; Cytoplasm Cell membrane Cytoplasm, myofibril, sarcomere, M line Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line. [Isoform MBP-1]: Nucleus. Event=Alternative initiation; Named isoforms=2; Name=alpha-enolase; IsoId=P06733-1; Sequence=Displayed; Name=MBP-1; IsoId=P06733-2; Sequence=VSP_018725; The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. Induced in diffuse large cell lymphoma (DLCL) after treatment with the natural biological agent, Bryo1. Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). ISGylated. Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the phosphopyruvate hydratase activity. Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis. Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies. Is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism. [Isoform MBP-1]: It is uncertain whether the alternative initiation site is at Met-94 or at Met-97. Belongs to the enolase family. Sequence=AAA35698.1; Type=Frameshift; Evidence=; Sequence=AAA35698.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/eno1/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40453/ENO1"; phosphopyruvate hydratase complex negative regulation of transcription from RNA polymerase II promoter magnesium ion binding RNA polymerase II regulatory region sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding RNA binding phosphopyruvate hydratase activity protein binding extracellular space nucleus cytoplasm cytosol plasma membrane gluconeogenesis glycolytic process response to virus cell surface positive regulation of plasminogen activation membrane lyase activity negative regulation of cell growth M band protein homodimerization activity cadherin binding negative regulation of transcription, DNA-templated positive regulation of muscle contraction metal ion binding GTPase binding canonical glycolysis extracellular exosome cell cortex region negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway positive regulation of ATP biosynthetic process uc001apj.1 uc001apj.2 uc001apj.3 uc001apj.4 
ENST00000234626.11 CDC7 ENST00000234626.11 cell division cycle 7, transcript variant 1 (from RefSeq NM_003503.4) CDC7 CDC7L1 CDC7_HUMAN D3DT31 ENST00000234626.1 ENST00000234626.10 ENST00000234626.2 ENST00000234626.3 ENST00000234626.4 ENST00000234626.5 ENST00000234626.6 ENST00000234626.7 ENST00000234626.8 ENST00000234626.9 NM_003503 O00311 O00558 Q5T5U5 uc001doe.1 uc001doe.2 uc001doe.3 uc001doe.4 uc001doe.5 This gene encodes a cell division cycle protein with kinase activity that is critical for the G1/S transition. The yeast homolog is also essential for initiation of DNA replication as cell division occurs. Overexpression of this gene product may be associated with neoplastic transformation for some tumors. Multiple alternatively spliced transcript variants that encode the same protein have been detected. [provided by RefSeq, Aug 2008]. Kinase involved in initiation of DNA replication. Phosphorylates critical substrates that regulate the G1/S phase transition and initiation of DNA replication, such as MCM proteins and CLASPIN. Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Forms a complex with either DBF4/DBF4A or DBF4B, leading to the activation of the kinase activity (PubMed:10373557, PubMed:12065429, PubMed:15668232, PubMed:17062569). Interacts with CLASPIN (via the acidic patch); the interaction is required for phosphorylation of MCM proteins and CLASPIN (PubMed:27401717). O00311; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-374980, EBI-11524452; O00311; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-374980, EBI-739580; O00311; Q9UBU7: DBF4; NbExp=8; IntAct=EBI-374980, EBI-372690; O00311; Q9UBU7-1: DBF4; NbExp=3; IntAct=EBI-374980, EBI-16017435; O00311; P51114-2: FXR1; NbExp=3; IntAct=EBI-374980, EBI-11022345; O00311; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-374980, EBI-948296; O00311; Q08379: GOLGA2; NbExp=3; IntAct=EBI-374980, EBI-618309; O00311; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-374980, EBI-11163335; O00311; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-374980, EBI-2549423; O00311; P42858: HTT; NbExp=3; IntAct=EBI-374980, EBI-466029; O00311; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-374980, EBI-11522367; O00311; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-374980, EBI-747204; O00311; Q9H2S9: IKZF4; NbExp=3; IntAct=EBI-374980, EBI-1640423; O00311; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-374980, EBI-1216080; O00311; Q9BTE3: MCMBP; NbExp=2; IntAct=EBI-374980, EBI-749378; O00311; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-374980, EBI-16439278; O00311; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-374980, EBI-11522433; O00311; Q14140: SERTAD2; NbExp=3; IntAct=EBI-374980, EBI-2822051; O00311; O75886: STAM2; NbExp=3; IntAct=EBI-374980, EBI-373258; O00311; P55061: TMBIM6; NbExp=3; IntAct=EBI-374980, EBI-1045825; O00311; P14373: TRIM27; NbExp=3; IntAct=EBI-374980, EBI-719493; O00311; O94972: TRIM37; NbExp=3; IntAct=EBI-374980, EBI-741602; O00311; Q2TAA8: TSNAXIP1; NbExp=3; IntAct=EBI-374980, EBI-6872498; O00311; P0CW01: TSPY10; NbExp=3; IntAct=EBI-374980, EBI-19697726; O00311; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=3; IntAct=EBI-374980, EBI-12369705; O00311; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-374980, EBI-12017160; O00311; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-374980, EBI-3918996; O00311; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-374980, EBI-17494306; Nucleus Event=Alternative splicing; Named isoforms=1; Comment=A number of isoforms may be produced.; Name=1; IsoId=O00311-1; Sequence=Displayed; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc7/"; G1/S transition of mitotic cell cycle nucleotide binding double-strand break repair via break-induced replication protein kinase activity protein serine/threonine kinase activity protein binding ATP binding nucleus nucleoplasm cytoplasm DNA replication protein phosphorylation cell cycle positive regulation of cell proliferation positive regulation of nuclear cell cycle DNA replication positive regulation of G2/M transition of mitotic cell cycle kinase activity phosphorylation transferase activity peptidyl-serine phosphorylation cell cycle phase transition intercellular bridge metal ion binding cell division negative regulation of G0 to G1 transition mitotic spindle uc001doe.1 uc001doe.2 uc001doe.3 uc001doe.4 uc001doe.5 
ENST00000234677.7 SARS1 ENST00000234677.7 seryl-tRNA synthetase 1, transcript variant 1 (from RefSeq NM_006513.4) B2R6Y9 ENST00000234677.1 ENST00000234677.2 ENST00000234677.3 ENST00000234677.4 ENST00000234677.5 ENST00000234677.6 NM_006513 P49591 Q5T5C8 Q9NSE3 SARS SARS1 SERS SYSC_HUMAN uc001dwu.1 uc001dwu.2 uc001dwu.3 uc001dwu.4 This gene belongs to the class II amino-acyl tRNA family. The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts. Multiple alternatively spliced transcript variants have been described but the biological validity of all variants is unknown. [provided by RefSeq, Jul 2010]. Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser) (PubMed:22353712, PubMed:24095058, PubMed:9431993, PubMed:26433229, PubMed:28236339, PubMed:34570399, PubMed:36041817). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec) (PubMed:9431993, PubMed:26433229, PubMed:28236339, PubMed:34570399). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC (PubMed:24940000). Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). Thereby, inhibits the production of VEGFA and sprouting angiogenesis mediated by VEGFA (PubMed:19423848, PubMed:19423847, PubMed:24940000). Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L- seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evidence= Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L- seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evidence= Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. Homodimer (PubMed:22353712, PubMed:26433229). The tRNA molecule may bind across the dimer (PubMed:26433229). Interacts with SIRT2 (PubMed:24940000). Interacts with METTL6; interaction is required for the tRNA N(3)-methylcytidine methyltransferase activity of METTL6 (PubMed:28655767, PubMed:34268557). P49591; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-1053431, EBI-18899653; P49591; P09525: ANXA4; NbExp=3; IntAct=EBI-1053431, EBI-2556852; P49591; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-1053431, EBI-9089489; P49591; A0A024R9H7: CCDC26; NbExp=3; IntAct=EBI-1053431, EBI-10271580; P49591; P38936: CDKN1A; NbExp=3; IntAct=EBI-1053431, EBI-375077; P49591; Q9Y4F5-3: CEP170B; NbExp=3; IntAct=EBI-1053431, EBI-12950757; P49591; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-1053431, EBI-25847826; P49591; O43504: LAMTOR5; NbExp=3; IntAct=EBI-1053431, EBI-713382; P49591; Q92615: LARP4B; NbExp=3; IntAct=EBI-1053431, EBI-1052558; P49591; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-1053431, EBI-10174029; P49591; Q8N2H9-4: PELI3; NbExp=3; IntAct=EBI-1053431, EBI-25852006; P49591; O15534: PER1; NbExp=3; IntAct=EBI-1053431, EBI-2557276; P49591; Q14181: POLA2; NbExp=3; IntAct=EBI-1053431, EBI-712752; P49591; P79522: PRR3; NbExp=3; IntAct=EBI-1053431, EBI-2803328; P49591; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-1053431, EBI-438710; P49591; Q9NUC0: SERTAD4; NbExp=3; IntAct=EBI-1053431, EBI-1773811; P49591; O14544: SOCS6; NbExp=3; IntAct=EBI-1053431, EBI-3929549; P49591; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-1053431, EBI-10696971; P49591; Q496A3: SPATS1; NbExp=3; IntAct=EBI-1053431, EBI-3923692; P49591; Q9UH65: SWAP70; NbExp=3; IntAct=EBI-1053431, EBI-310749; P49591; Q7Z7C8-2: TAF8; NbExp=3; IntAct=EBI-1053431, EBI-9089028; P49591; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-1053431, EBI-25830583; P49591; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-1053431, EBI-10316321; P49591; Q9BRR0: ZKSCAN3; NbExp=3; IntAct=EBI-1053431, EBI-1965777; P49591; Q9BYN7-2: ZNF341; NbExp=3; IntAct=EBI-1053431, EBI-16435478; Cytoplasm cleus Note=Predominantly cytoplasmic, but a minor proportion is also found in the nucleus. Brain. Consists of two distinct domains, a catalytic core and a N- terminal extension that is involved in tRNA binding. Neurodevelopmental disorder with microcephaly, ataxia, and seizures (NEDMAS) [MIM:617709]: An autosomal recessive disorder characterized by delayed psychomotor development, intellectual disability, seizures apparent in infancy, impaired speech, and aggressive behavior. Additional features include microcephaly, ataxia, and muscle weakness. te=The disease is caused by variants affecting the gene represented in this entry. Note=A splice site deletion resulting in a five amino acid in- frame insertion in SARS1, is associated with autosomal dominant complex spastic paraplegia with ataxia, intellectual disability, developmental delay and seizures, but without microcephaly. Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily. negative regulation of transcription from RNA polymerase II promoter nucleotide binding RNA polymerase II core promoter proximal region sequence-specific DNA binding DNA binding RNA binding aminoacyl-tRNA ligase activity serine-tRNA ligase activity protein binding ATP binding nucleus cytoplasm cytosol translation tRNA aminoacylation for protein translation seryl-tRNA aminoacylation tRNA processing selenocysteine metabolic process negative regulation of angiogenesis ligase activity protein homodimerization activity extracellular exosome selenocysteinyl-tRNA(Sec) biosynthetic process negative regulation of vascular endothelial growth factor production uc001dwu.1 uc001dwu.2 uc001dwu.3 uc001dwu.4 
ENST00000234739.8 BCL9 ENST00000234739.8 BCL9 transcription coactivator (from RefSeq NM_004326.4) BCL9_HUMAN ENST00000234739.1 ENST00000234739.2 ENST00000234739.3 ENST00000234739.4 ENST00000234739.5 ENST00000234739.6 ENST00000234739.7 NM_004326 O00512 Q5T489 uc031uul.1 uc031uul.2 uc031uul.3 BCL9 is associated with B-cell acute lymphoblastic leukemia. It may be a target of translocation in B-cell malignancies with abnormalities of 1q21. Its function is unknown. The overexpression of BCL9 may be of pathogenic significance in B-cell malignancies. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: Y13620.1, SRR1803617.62371.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234739.8/ ENSP00000234739.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'. O00512; Q6P1J9: CDC73; NbExp=2; IntAct=EBI-533127, EBI-930143; O00512; P35222: CTNNB1; NbExp=5; IntAct=EBI-533127, EBI-491549; O00512; Q9Y3Y4: PYGO1; NbExp=8; IntAct=EBI-533127, EBI-3397474; O00512; Q9BRQ0: PYGO2; NbExp=3; IntAct=EBI-533127, EBI-932471; O00512; P18824: arm; Xeno; NbExp=3; IntAct=EBI-533127, EBI-216128; O00512; Q9V9W8: pygo; Xeno; NbExp=3; IntAct=EBI-533127, EBI-152653; Nucleus Detected at low levels in thymus, prostate, testis, ovary and small intestine, and at lower levels in spleen, colon and blood. Note=A chromosomal aberration involving BCL9 is found in a patient with precursor B-cell acute lymphoblastic leukemia (ALL). Translocation t(1;14)(q21;q32). This translocation leaves the coding region intact, but may have pathogenic effects due to alterations in the expression level of BCL9. Several cases of translocations within the 3'-UTR of BCL9 have been found in B-cell malignancies. Belongs to the BCL9 family. It is uncertain whether Met-1 or Met-27 is the initiator. Sequence=CAA73942.1; Type=Frameshift; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/466/BCL9"; transcription coactivator activity protein binding nucleus nucleoplasm cytoplasm Golgi apparatus cis-Golgi network beta-catenin binding myotube differentiation involved in skeletal muscle regeneration Wnt signaling pathway somatic stem cell population maintenance skeletal muscle cell differentiation positive regulation of transcription from RNA polymerase II promoter canonical Wnt signaling pathway beta-catenin-TCF complex assembly beta-catenin-TCF complex regulation of transforming growth factor beta receptor signaling pathway uc031uul.1 uc031uul.2 uc031uul.3 
ENST00000234798.5 TPSG1 ENST00000234798.5 tryptase gamma 1 (from RefSeq NM_012467.4) ENST00000234798.1 ENST00000234798.2 ENST00000234798.3 ENST00000234798.4 NM_012467 PRSS31 Q96RZ8 Q9C015 Q9NRQ8 Q9NRR2 Q9UBB2 TMT TPSG1 TRYG1_HUMAN uc002ckw.1 uc002ckw.2 uc002ckw.3 uc002ckw.4 Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3. There is uncertainty regarding the number of genes in this cluster. Currently four functional genes - alpha I, beta I, beta II and gamma I - have been identified. And beta I has an allelic variant named alpha II, beta II has an allelic variant beta III, also gamma I has an allelic variant gamma II. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha-tryptases predominant. This gene differs from other members of the tryptase gene family in that it has C-terminal hydrophobic domain, which may serve as a membrane anchor. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## RNAseq introns :: single sample supports all introns SAMEA2153946 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Q9NRR2; P37235: HPCAL1; NbExp=3; IntAct=EBI-17210651, EBI-749311; Q9NRR2; P61601: NCALD; NbExp=3; IntAct=EBI-17210651, EBI-749635; Membrane ; Single-pass membrane protein Expressed in many tissues. There are two alleles; gamma-I and gamma-II which differ by 5 residues. Belongs to the peptidase S1 family. Tryptase subfamily. serine-type endopeptidase activity extracellular space integral component of plasma membrane proteolysis peptidase activity serine-type peptidase activity membrane integral component of membrane hydrolase activity uc002ckw.1 uc002ckw.2 uc002ckw.3 uc002ckw.4 
ENST00000234816.7 ANGPTL1 ENST00000234816.7 angiopoietin like 1, transcript variant 1 (from RefSeq NM_004673.4) ANG3 ANGL1_HUMAN ANGPT3 ARP1 ENST00000234816.1 ENST00000234816.2 ENST00000234816.3 ENST00000234816.4 ENST00000234816.5 ENST00000234816.6 NM_004673 O95841 PSEC0154 Q5T5Z5 UNQ162/PRO188 uc001gma.1 uc001gma.2 uc001gma.3 uc001gma.4 uc001gma.5 Angiopoietins are members of the vascular endothelial growth factor family and the only known growth factors largely specific for vascular endothelium. Angiopoietin-1, angiopoietin-2, and angiopoietin-4 participate in the formation of blood vessels. The protein encoded by this gene is another member of the angiopoietin family that is widely expressed in adult tissues with mRNA levels highest in highly vascularized tissues. This protein was found to be a secretory protein that does not act as an endothelial cell mitogen in vitro. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803613.47398.1, AY358278.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA2142348 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234816.7/ ENSP00000234816.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Secreted Highly expressed in adrenal gland, placenta, thyroid gland, heart, skeletal muscle and small intestine. Weakly expressed in testis, ovary, colon, pancreas, kidney and stomach. receptor binding extracellular region extracellular space transmembrane receptor protein tyrosine kinase signaling pathway extracellular exosome uc001gma.1 uc001gma.2 uc001gma.3 uc001gma.4 uc001gma.5 
ENST00000234827.6 TCEANC2 ENST00000234827.6 transcription elongation factor A N-terminal and central domain containing 2, transcript variant 1 (from RefSeq NM_153035.3) C1orf83 ENST00000234827.1 ENST00000234827.2 ENST00000234827.3 ENST00000234827.4 ENST00000234827.5 NM_153035 Q5T702 Q8N8N2 Q96MN5 TEAN2_HUMAN uc001cwt.1 uc001cwt.2 uc001cwt.3 Q96MN5; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-5462748, EBI-741181; Q96MN5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5462748, EBI-79165; Q96MN5; Q15025: TNIP1; NbExp=4; IntAct=EBI-5462748, EBI-357849; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96MN5-1; Sequence=Displayed; Name=2; IsoId=Q96MN5-2; Sequence=VSP_025096; Belongs to the TCEANC2 family. protein binding nucleus transcription, DNA-templated uc001cwt.1 uc001cwt.2 uc001cwt.3 
ENST00000234831.10 TMEM59 ENST00000234831.10 transmembrane protein 59, transcript variant 2 (from RefSeq NM_004872.5) B3KQL7 C1orf8 ENST00000234831.1 ENST00000234831.2 ENST00000234831.3 ENST00000234831.4 ENST00000234831.5 ENST00000234831.6 ENST00000234831.7 ENST00000234831.8 ENST00000234831.9 HSPC001 NM_004872 O75393 Q4VBP9 Q5T705 Q96KX7 Q9BXS4 TMM59_HUMAN UNQ169/PRO195 uc001cwp.1 uc001cwp.2 uc001cwp.3 uc001cwp.4 uc001cwp.5 This gene encodes a protein shown to regulate autophagy in response to bacterial infection. This protein may also regulate the retention of amyloid precursor protein (APP) in the Golgi apparatus through its control of APP glycosylation. Overexpression of this protein has been found to promote apoptosis in a glioma cell line. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2015]. Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy (PubMed:27273576, PubMed:23376921). Modulates the O-glycosylation and complex N- glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP (PubMed:20427278). Inhibits APP transport to the cell surface and further shedding (PubMed:20427278). Interacts with ATG16L1 (via WD repeats). Q9BXS4; Q676U5: ATG16L1; NbExp=6; IntAct=EBI-7054441, EBI-535909; Late endosome membrane ; Single-pass type I membrane protein Lysosome membrane ; Single-pass type I membrane protein Cell membrane ; Single-pass type I membrane protein Golgi apparatus membrane ; Single-pass type I membrane protein Note=Mainly localizes to late endosomes/lysosomes. Probably first exported to the cell surface and then actively endocytosed to transiently localize in early endosomes on its way to the late endosomal/lysosomal compartment where it becomes quickly degraded. The ATG16L1-binding motif mediates interaction with ATG16L1 and promotes autophagy. N-glycosylated. Belongs to the TMEM59 family. Sequence=AAC39890.1; Type=Frameshift; Evidence=; Sequence=AAH03106.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Golgi cis cisterna Golgi trans cisterna Golgi membrane endopeptidase activity protein binding lysosome lysosomal membrane endosome late endosome Golgi apparatus Golgi medial cisterna plasma membrane proteolysis autophagy positive regulation of autophagy negative regulation of protein processing membrane integral component of membrane late endosome membrane extracellular exosome negative regulation of protein glycosylation in Golgi negative regulation of protein localization to plasma membrane uc001cwp.1 uc001cwp.2 uc001cwp.3 uc001cwp.4 uc001cwp.5 
ENST00000234875.9 RPL22 ENST00000234875.9 ribosomal protein L22 (from RefSeq NM_000983.4) B2R495 ENST00000234875.1 ENST00000234875.2 ENST00000234875.3 ENST00000234875.4 ENST00000234875.5 ENST00000234875.6 ENST00000234875.7 ENST00000234875.8 NM_000983 P35268 Q6IBD1 RL22_HUMAN uc001amd.1 uc001amd.2 uc001amd.3 uc001amd.4 uc001amd.5 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a cytoplasmic ribosomal protein that is a component of the 60S subunit. The protein belongs to the L22E family of ribosomal proteins. Its initiating methionine residue is post-translationally removed. The protein can bind specifically to Epstein-Barr virus-encoded RNAs (EBERs) 1 and 2. The mouse protein has been shown to be capable of binding to heparin. Transcript variants utilizing alternative polyA signals exist. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. It was previously thought that this gene mapped to 3q26 and that it was fused to the acute myeloid leukemia 1 (AML1) gene located at 21q22 in some therapy-related myelodysplastic syndrome patients with 3;21 translocations; however, these fusions actually involve a ribosomal protein L22 pseudogene located at 3q26, and this gene actually maps to 1p36.3-p36.2. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.436838.1, SRR3476690.1039763.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000234875.9/ ENSP00000346088.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:32669547). Component of the large ribosomal subunit. P35268; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-354533, EBI-297683; P35268; P54253: ATXN1; NbExp=3; IntAct=EBI-354533, EBI-930964; P35268; Q8N7W2-2: BEND7; NbExp=5; IntAct=EBI-354533, EBI-10181188; P35268; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-354533, EBI-12051833; P35268; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-354533, EBI-742054; P35268; Q92914: FGF11; NbExp=3; IntAct=EBI-354533, EBI-11987787; P35268; U3KQK0: H2BC15; NbExp=3; IntAct=EBI-354533, EBI-12142839; P35268; P42858: HTT; NbExp=3; IntAct=EBI-354533, EBI-466029; P35268; P35268: RPL22; NbExp=3; IntAct=EBI-354533, EBI-354533; P35268; O00560: SDCBP; NbExp=5; IntAct=EBI-354533, EBI-727004; P35268; Q9H190: SDCBP2; NbExp=5; IntAct=EBI-354533, EBI-742426; P35268; Q96MF2: STAC3; NbExp=3; IntAct=EBI-354533, EBI-745680; P35268; O75683: SURF6; NbExp=3; IntAct=EBI-354533, EBI-2691252; P35268; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-354533, EBI-741515; P35268; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-354533, EBI-597063; P35268; P17473: IE; Xeno; NbExp=2; IntAct=EBI-354533, EBI-11702772; Cytoplasm Binds to Epstein-Barr virus small RNAs and to heparin. Belongs to the eukaryotic ribosomal protein eL22 family. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay cytoplasmic translation RNA binding structural constituent of ribosome protein binding nucleus cytoplasm cytosol ribosome focal adhesion translation translational initiation SRP-dependent cotranslational protein targeting to membrane heparin binding viral transcription cytosolic large ribosomal subunit translation regulator activity alpha-beta T cell differentiation extracellular exosome presynapse glutamatergic synapse regulation of translation at presynapse, modulating synaptic transmission ribonucleoprotein complex uc001amd.1 uc001amd.2 uc001amd.3 uc001amd.4 uc001amd.5 
ENST00000234961.7 OPRD1 ENST00000234961.7 opioid receptor delta 1 (from RefSeq NM_000911.4) B5B0B8 ENST00000234961.1 ENST00000234961.2 ENST00000234961.3 ENST00000234961.4 ENST00000234961.5 ENST00000234961.6 NM_000911 OPRD OPRD_HUMAN P41143 uc001brf.1 uc001brf.2 uc001brf.3 G-protein coupled receptor that functions as a receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine. May form homooligomers. Forms a heterodimer with OPRM1 (By similarity). Interacts with GPRASP1 (PubMed:12142540, PubMed:15086532). Interacts with RTP4; the interaction promotes cell surface localization of the OPRD1-OPRM1 heterodimer (By similarity). P41143; P16615: ATP2A2; NbExp=3; IntAct=EBI-2624456, EBI-358933; P41143; P27824: CANX; NbExp=2; IntAct=EBI-2624456, EBI-355947; P41143; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-2624456, EBI-12019274; P41143; Q5JY77: GPRASP1; NbExp=2; IntAct=EBI-2624456, EBI-2514717; P41143; Q9NS64: RPRM; NbExp=3; IntAct=EBI-2624456, EBI-1052363; P41143; Q9Y666-2: SLC12A7; NbExp=3; IntAct=EBI-2624456, EBI-12854384; P41143; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-2624456, EBI-12808018; P41143; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-2624456, EBI-10226799; P41143; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-2624456, EBI-10982110; P41143; P11607: ATP2A2; Xeno; NbExp=2; IntAct=EBI-2624456, EBI-8004986; Cell membrane ulti-pass membrane protein Detected in oocytes (at protein level). Detected in brain cortex, hypothalamus, hippocampus and olfactory bulb. Detected in oocytes. N-glycosylated. Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation; the ubiquitination is diminished by RTP4. Belongs to the G-protein coupled receptor 1 family. Name=Wikipedia; Note=Delta opioid receptor entry; URL="https://en.wikipedia.org/wiki/Delta_opioid_receptor"; G-protein coupled receptor activity opioid receptor activity protein binding cytoplasm plasma membrane integral component of plasma membrane immune response signal transduction G-protein coupled receptor signaling pathway G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway phospholipase C-activating G-protein coupled receptor signaling pathway neuropeptide signaling pathway adult locomotory behavior negative regulation of gene expression membrane integral component of membrane cytokine-mediated signaling pathway integral component of synaptic vesicle membrane intrinsic component of plasma membrane negative regulation of protein complex assembly vesicle dendrite membrane positive regulation of CREB transcription factor activity positive regulation of peptidyl-serine phosphorylation receptor serine/threonine kinase binding opioid receptor signaling pathway enkephalin receptor activity peptide binding eating behavior neuropeptide binding axon terminus membrane raft postsynaptic membrane regulation of mitochondrial membrane potential regulation of calcium ion transport regulation of sensory perception of pain cellular response to growth factor stimulus cellular response to hypoxia cellular response to toxic substance spine apparatus neuronal dense core vesicle integral component of presynaptic membrane integral component of postsynaptic density membrane uc001brf.1 uc001brf.2 uc001brf.3 
ENST00000235090.10 WDR77 ENST00000235090.10 WD repeat domain 77, transcript variant 5 (from RefSeq NR_133654.2) B3KMW6 B4DP38 ENST00000235090.1 ENST00000235090.2 ENST00000235090.3 ENST00000235090.4 ENST00000235090.5 ENST00000235090.6 ENST00000235090.7 ENST00000235090.8 ENST00000235090.9 HKMT1069 MEP50 MEP50_HUMAN NR_133654 Nbla10071 Q3LID2 Q53FU2 Q6JZZ5 Q96GK4 Q9BQA1 Q9BWY3 WD45 WDR77 uc001ebb.1 uc001ebb.2 uc001ebb.3 uc001ebb.4 uc001ebb.5 The protein encoded by this gene is an androgen receptor coactivator that forms a complex with protein arginine methyltransferase 5, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins. The encoded protein may be involved in the early stages of prostate cancer, with most of the protein being nuclear-localized in benign cells but cytoplasmic in cancer cells. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015]. Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones (PubMed:11756452). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:23071334). Component of the methylosome complex composed of PRMT5, WDR77 and CLNS1A (PubMed:21081503, PubMed:18984161). Found in a complex composed of PRMT5, WDR77 and RIOK1 (PubMed:21081503). RIOK1 and CLNS1A bound directly to PRMT5 at the same binding site, in a mutually exclusive manner, which allows the recruitment of distinct methylation substrates, such as nucleolin/NCL and Sm proteins, respectively (PubMed:21081503). Found in a complex with the component of the methylosome, PRMT5, CLNS1A, WDR77, PRMT1 and ERH (PubMed:25284789). Directly interacts with PRMT5, as well as with several Sm proteins, including SNRPB and SNRPD2 and, more weakly, SNRPD3 and SNRPE (PubMed:11756452, PubMed:33376131). Forms a compact hetero-octamer with PRMT5, decorating the outer surface of a PRMT5 tetramer. Interacts with SUZ12 and histone H2A/H2AC20, but not with histones H2B, H3 nor H4 (PubMed:16712789). Interacts with CTDP1 and LSM11 (PubMed:12560496, PubMed:16087681). Interacts with APEX1, AR and NKX3-1 (PubMed:19188445, PubMed:12972618). Interacts with CHTOP (PubMed:25284789). Interacts with FAM47E. Interacts with TSC22D2 (PubMed:27337956). Q9BQA1; P55212: CASP6; NbExp=3; IntAct=EBI-1237307, EBI-718729; Q9BQA1; P04792: HSPB1; NbExp=3; IntAct=EBI-1237307, EBI-352682; Q9BQA1; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1237307, EBI-10975473; Q9BQA1; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1237307, EBI-21591415; Q9BQA1; O14744: PRMT5; NbExp=17; IntAct=EBI-1237307, EBI-351098; Q9BQA1; P62826: RAN; NbExp=3; IntAct=EBI-1237307, EBI-286642; Q9BQA1; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1237307, EBI-396669; Q9BQA1; O76024: WFS1; NbExp=3; IntAct=EBI-1237307, EBI-720609; Q9BQA1; P03418: N; Xeno; NbExp=3; IntAct=EBI-1237307, EBI-6930799; Nucleus toplasm te=Nuclear in Leydig cells and cytoplasmic in germ cells during fetal testicular development. In adult testis, predominantly nuclear. Subcellular location varies from nuclear to cytoplasmic in various tumors (PubMed:17437848). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BQA1-1; Sequence=Displayed; Name=2; IsoId=Q9BQA1-2; Sequence=VSP_056166; Highly expressed in heart, skeletal muscle, spleen, testis, uterus, prostate and thymus. In testis, expressed in germ cells and Leydig cells, but not in peritubular myocytes, nor in Sertoli cells. Expressed in prostate cancers, in seminomas and in Leydig cell tumors. Expressed in Leydig cells during fetal testicular development, especially during the second semester. Germ cells expression is detected as early as 10 weeks of gestation. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44142/WDR77"; spliceosomal snRNP assembly protein binding nucleus nucleoplasm cytoplasm Golgi apparatus cytosol regulation of transcription from RNA polymerase II promoter positive regulation of cell proliferation negative regulation of cell proliferation methyl-CpG binding ligand-dependent nuclear receptor transcription coactivator activity methylosome secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development negative regulation of epithelial cell proliferation involved in prostate gland development positive regulation of nucleic acid-templated transcription uc001ebb.1 uc001ebb.2 uc001ebb.3 uc001ebb.4 uc001ebb.5 
ENST00000235150.5 RNF19B ENST00000235150.5 ring finger protein 19B, transcript variant 3 (from RefSeq NM_001300826.2) B7ZLB2 E9PAW6 ENST00000235150.1 ENST00000235150.2 ENST00000235150.3 ENST00000235150.4 G3XA82 IBRDC3 NKLAM NM_001300826 Q0VG77 Q5TH44 Q5TH45 Q6P6A4 Q6ZMZ0 Q8N2S8 Q8WUF3 RN19B_HUMAN uc010ohp.1 uc010ohp.2 uc010ohp.3 uc010ohp.4 This gene encodes a multi-pass membrane protein containing two RING-type and one IBR-type zinc finger motifs. The encoded protin is an E3 ubiquitin-protein ligase that plays a role in the cytotoxic effects of natural killer (NK) cells. Alternative splicing results in multiple transcript variants. There are pseudogenes for this gene on chromosomes X and Y in a possible pseudoautosomal region. [provided by RefSeq, Jul 2014]. E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1 (PubMed:16709802, PubMed:27485036). Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells (PubMed:10438909). Protects against staurosporin-induced cell death (PubMed:27485036). Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence=; Protein modification; protein ubiquitination. Interacts with UBE2L3, UBE2L6 and UCKL1. Q6ZMZ0; Q9BXS5: AP1M1; NbExp=4; IntAct=EBI-2466594, EBI-541426; Q6ZMZ0; O95236-2: APOL3; NbExp=3; IntAct=EBI-2466594, EBI-11976321; Q6ZMZ0; P07306: ASGR1; NbExp=3; IntAct=EBI-2466594, EBI-1172335; Q6ZMZ0; O14735: CDIPT; NbExp=3; IntAct=EBI-2466594, EBI-358858; Q6ZMZ0; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-2466594, EBI-11996768; Q6ZMZ0; Q02127: DHODH; NbExp=3; IntAct=EBI-2466594, EBI-3928775; Q6ZMZ0; P14324: FDPS; NbExp=3; IntAct=EBI-2466594, EBI-948245; Q6ZMZ0; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-2466594, EBI-6166686; Q6ZMZ0; O14653: GOSR2; NbExp=3; IntAct=EBI-2466594, EBI-4401517; Q6ZMZ0; O60725: ICMT; NbExp=3; IntAct=EBI-2466594, EBI-11721771; Q6ZMZ0; Q5EB52: MEST; NbExp=3; IntAct=EBI-2466594, EBI-1050204; Q6ZMZ0; Q6N075: MFSD5; NbExp=3; IntAct=EBI-2466594, EBI-3920969; Q6ZMZ0; P11836: MS4A1; NbExp=3; IntAct=EBI-2466594, EBI-2808234; Q6ZMZ0; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-2466594, EBI-9550165; Q6ZMZ0; P52306-5: RAP1GDS1; NbExp=3; IntAct=EBI-2466594, EBI-12832744; Q6ZMZ0; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-2466594, EBI-3917235; Q6ZMZ0; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2466594, EBI-8652744; Q6ZMZ0; Q15436: SEC23A; NbExp=3; IntAct=EBI-2466594, EBI-81088; Q6ZMZ0; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-2466594, EBI-9679163; Q6ZMZ0; Q99726: SLC30A3; NbExp=3; IntAct=EBI-2466594, EBI-10294651; Q6ZMZ0; Q03518: TAP1; NbExp=3; IntAct=EBI-2466594, EBI-747259; Q6ZMZ0; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-2466594, EBI-8644968; Q6ZMZ0; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-2466594, EBI-10171534; Q6ZMZ0; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-2466594, EBI-12876824; Q6ZMZ0; P01375: TNF; NbExp=3; IntAct=EBI-2466594, EBI-359977; Q6ZMZ0; O60636: TSPAN2; NbExp=3; IntAct=EBI-2466594, EBI-3914288; Q6ZMZ0; P68036: UBE2L3; NbExp=2; IntAct=EBI-2466594, EBI-711173; Q6ZMZ0; O14933: UBE2L6; NbExp=3; IntAct=EBI-2466594, EBI-2129974; Q6ZMZ0; Q9NWZ5: UCKL1; NbExp=4; IntAct=EBI-2466594, EBI-2466660; Cytoplasmic granule membrane ; Multi-pass membrane protein Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q6ZMZ0-1; Sequence=Displayed; Name=2; IsoId=Q6ZMZ0-2; Sequence=VSP_028635, VSP_028633, VSP_028634; Name=3; IsoId=Q6ZMZ0-3; Sequence=VSP_028632, VSP_028635, VSP_028633, VSP_028634; Name=4; IsoId=Q6ZMZ0-4; Sequence=VSP_028635; Expressed specifically in natural killer cells, activated macrophages and cytotoxic T-cells (PubMed:10438909). Present in natural killer cells (at protein level) (PubMed:10912506). Ubiquitously expressed with high expression in testis (PubMed:27485036). In natural killer cells, by IFNB1/IFN-beta and IL2/interleukin-2 (at protein level) (PubMed:10438909). Up-regulated by endoplasmic reticulum (ER) stress triggered by thapsigargin or tunicamycin (PubMed:27485036). The first IBR-type zinc finger is the most crucial for interaction with UBE2L3, UBE2L6 and UCKL1. Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT- type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. Belongs to the RBR family. RNF19 subfamily. Sequence=AAI13561.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAI43688.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=EAX07490.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; ubiquitin ligase complex protein polyubiquitination adaptive immune response immune system process ubiquitin-protein transferase activity protein binding cytoplasm endoplasmic reticulum endoplasmic reticulum membrane cytosol ubiquitin-dependent protein catabolic process membrane integral component of membrane protein ubiquitination transferase activity ubiquitin conjugating enzyme binding positive regulation of proteasomal ubiquitin-dependent protein catabolic process ubiquitin binding cytolytic granule metal ion binding protein autoubiquitination ubiquitin protein ligase activity uc010ohp.1 uc010ohp.2 uc010ohp.3 uc010ohp.4 
ENST00000235307.7 C1orf21 ENST00000235307.7 chromosome 1 open reading frame 21 (from RefSeq NM_030806.4) B2R551 CA021_HUMAN ENST00000235307.1 ENST00000235307.2 ENST00000235307.3 ENST00000235307.4 ENST00000235307.5 ENST00000235307.6 NM_030806 PIG13 Q9H246 uc001gqv.1 uc001gqv.2 uc001gqv.3 Q9H246; Q8N682: DRAM1; NbExp=3; IntAct=EBI-10305393, EBI-10305400; Q9H246; Q15172: PPP2R5A; NbExp=5; IntAct=EBI-10305393, EBI-641666; Expressed in spleen, prostate, testis and uterus. protein binding uc001gqv.1 uc001gqv.2 uc001gqv.3 
ENST00000235329.10 MFN2 ENST00000235329.10 mitofusin 2, transcript variant 1 (from RefSeq NM_014874.4) A8K1B3 CPRP1 ENST00000235329.1 ENST00000235329.2 ENST00000235329.3 ENST00000235329.4 ENST00000235329.5 ENST00000235329.6 ENST00000235329.7 ENST00000235329.8 ENST00000235329.9 KIAA0214 MFN2 MFN2_HUMAN NM_014874 O95140 O95572 Q5JXC3 Q5JXC4 Q9H131 Q9NSX8 uc001atn.1 uc001atn.2 uc001atn.3 uc001atn.4 uc001atn.5 uc001atn.6 This gene encodes a mitochondrial membrane protein that participates in mitochondrial fusion and contributes to the maintenance and operation of the mitochondrial network. This protein is involved in the regulation of vascular smooth muscle cell proliferation, and it may play a role in the pathophysiology of obesity. Mutations in this gene cause Charcot-Marie-Tooth disease type 2A2, and hereditary motor and sensory neuropathy VI, which are both disorders of the peripheral nervous system. Defects in this gene have also been associated with early-onset stroke. Two transcript variants encoding the same protein have been identified. [provided by RefSeq, Jul 2008]. Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:28114303). Overexpression induces the formation of mitochondrial networks (PubMed:28114303). Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (By similarity). Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) (PubMed:23620051). Is required for PRKN recruitment to dysfunctional mitochondria (PubMed:23620051). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity). Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence=; Forms homomultimers and heteromultimers with MFN1 (PubMed:26085578). Oligomerization is essential for mitochondrion fusion (Probable). Interacts with VAT1 (By similarity). Interacts with STOML2; may form heterooligomers (PubMed:17121834). Interacts (phosphorylated) with PRKN (PubMed:23620051). Interacts with EIF2AK3 (By similarity). Interacts with THG1L; THG1L probably functions as a guanyl-nucleotide exchange factor/GEF, activating MFN2. O95140; Q5S007: LRRK2; NbExp=3; IntAct=EBI-3324756, EBI-5323863; O95140; Q9NX47: MARCHF5; NbExp=2; IntAct=EBI-3324756, EBI-2341610; O95140; Q8IWA4: MFN1; NbExp=2; IntAct=EBI-3324756, EBI-1048197; O95140; O60260: PRKN; NbExp=4; IntAct=EBI-3324756, EBI-716346; O95140; Q9Y512: SAMM50; NbExp=2; IntAct=EBI-3324756, EBI-748409; Mitochondrion outer membrane ulti-pass membrane protein Note=Colocalizes with BAX during apoptosis. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95140-1; Sequence=Displayed; Name=2; IsoId=O95140-2; Sequence=VSP_015159, VSP_015160, VSP_015161; Ubiquitous; expressed at low level. Highly expressed in heart and kidney. A helix bundle is formed by helices from the N-terminal and the C-terminal part of the protein. The GTPase domain cannot be expressed by itself, without the helix bundle. Rearrangement of the helix bundle and/or of the coiled coil domains may bring membranes from adjacent mitochondria into close contact, and thereby play a role in mitochondrial fusion. Phosphorylated by PINK1. Ubiquitinated by non-degradative ubiquitin by PRKN, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion (PubMed:23620051). Ubiquitinated by HUWE1 when dietary stearate (C18:0) levels are low; ubiquitination inhibits mitochondrial fusion (PubMed:26214738, PubMed:30217973). Charcot-Marie-Tooth disease, axonal, 2A2B (CMT2A2B) [MIM:617087]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2A2B is a severe form with autosomal recessive inheritance. te=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, axonal, 2A2A (CMT2A2A) [MIM:609260]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. te=The disease is caused by variants affecting the gene represented in this entry. Neuropathy, hereditary motor and sensory, 6A, with optic atrophy (HMSN6A) [MIM:601152]: An autosomal dominant neurologic disorder characterized by optic atrophy and peripheral sensorimotor neuropathy manifesting as axonal Charcot-Marie-Tooth disease. Charcot- Marie-Tooth disease is a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. It is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies and primary peripheral axonal neuropathies. Peripheral axonal neuropathies are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, and normal or slightly reduced nerve conduction velocities. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily. Sequence=BAA34389.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=CAB70866.2; Type=Frameshift; Evidence=; Name=Inherited peripheral neuropathies mutation db; URL="https://uantwerpen.vib.be/CMTMutations"; nucleotide binding blastocyst formation GTPase activity protein binding GTP binding mitochondrion mitochondrial outer membrane cytosol protein targeting to mitochondrion autophagy apoptotic process response to unfolded protein mitochondrial membrane organization blood coagulation mitochondrial fusion microtubule cytoskeleton membrane integral component of membrane macroautophagy hydrolase activity intrinsic component of mitochondrial outer membrane ubiquitin protein ligase binding protein localization to pre-autophagosomal structure negative regulation of Ras protein signal transduction camera-type eye morphogenesis negative regulation of smooth muscle cell proliferation mitochondrion localization parkin-mediated mitophagy in response to mitochondrial depolarization positive regulation of vascular smooth muscle cell proliferation positive regulation of vascular associated smooth muscle cell apoptotic process cell cycle arrest uc001atn.1 uc001atn.2 uc001atn.3 uc001atn.4 uc001atn.5 uc001atn.6 
ENST00000235332.6 MIIP ENST00000235332.6 migration and invasion inhibitory protein (from RefSeq NM_021933.4) C0KL22 ENST00000235332.1 ENST00000235332.2 ENST00000235332.3 ENST00000235332.4 ENST00000235332.5 IIP45 MIIP_HUMAN NM_021933 Q5JXC2 Q96HU6 Q9H839 Q9HA00 uc001ato.1 uc001ato.2 uc001ato.3 uc001ato.4 This gene encodes a protein that interacts with the oncogene protein insulin-like growth factor binding protein 2 and may function as an inhibitor of cell migration and invasion. This protein also interacts with the cell division protein 20 and may be involved in regulating mitotic progression. This protein may function as a tumor suppressor by inhibiting the growth or certain cancers. [provided by RefSeq, Sep 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.769016.1, FJ618905.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000235332.6/ ENSP00000235332.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Inhibits glioma cells invasion and down-regulates adhesion- and motility-associated genes such as NFKB2 and ICAM1. Exhibits opposing effects to IGFBP2 on cell invasion. Interacts with IGFBP2. Q5JXC2; O75934: BCAS2; NbExp=3; IntAct=EBI-2801965, EBI-1050106; Q5JXC2; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-2801965, EBI-744556; Q5JXC2; P28329-3: CHAT; NbExp=3; IntAct=EBI-2801965, EBI-25837549; Q5JXC2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2801965, EBI-3867333; Q5JXC2; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-2801965, EBI-743105; Q5JXC2; P60228: EIF3E; NbExp=3; IntAct=EBI-2801965, EBI-347740; Q5JXC2; P22607: FGFR3; NbExp=3; IntAct=EBI-2801965, EBI-348399; Q5JXC2; O43559: FRS3; NbExp=3; IntAct=EBI-2801965, EBI-725515; Q5JXC2; P06396: GSN; NbExp=3; IntAct=EBI-2801965, EBI-351506; Q5JXC2; P01112: HRAS; NbExp=3; IntAct=EBI-2801965, EBI-350145; Q5JXC2; Q7L273: KCTD9; NbExp=3; IntAct=EBI-2801965, EBI-4397613; Q5JXC2; Q5T749: KPRP; NbExp=3; IntAct=EBI-2801965, EBI-10981970; Q5JXC2; O76011: KRT34; NbExp=3; IntAct=EBI-2801965, EBI-1047093; Q5JXC2; Q9H204: MED28; NbExp=3; IntAct=EBI-2801965, EBI-514199; Q5JXC2; P42568: MLLT3; NbExp=3; IntAct=EBI-2801965, EBI-716132; Q5JXC2; Q70IA6: MOB2; NbExp=3; IntAct=EBI-2801965, EBI-2558739; Q5JXC2; O43482: OIP5; NbExp=3; IntAct=EBI-2801965, EBI-536879; Q5JXC2; P32242: OTX1; NbExp=3; IntAct=EBI-2801965, EBI-740446; Q5JXC2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2801965, EBI-5235340; Q5JXC2; O75716: STK16; NbExp=4; IntAct=EBI-2801965, EBI-749295; Q5JXC2; Q9BT92: TCHP; NbExp=3; IntAct=EBI-2801965, EBI-740781; Q5JXC2; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-2801965, EBI-750487; Q5JXC2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2801965, EBI-11741437; Q5JXC2; Q15654: TRIP6; NbExp=3; IntAct=EBI-2801965, EBI-742327; Q5JXC2; Q8N6Y0: USHBP1; NbExp=5; IntAct=EBI-2801965, EBI-739895; Q5JXC2; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2801965, EBI-740727; Q5JXC2; Q9Y649; NbExp=3; IntAct=EBI-2801965, EBI-25900580; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q5JXC2-1; Sequence=Displayed; Name=2; Synonyms=IIP45S; IsoId=Q5JXC2-2; Sequence=VSP_032214; Ubiquitous. Isoform 1 is expressed in brain but underexpressed in glioma tissues, at protein level. Isoform 2 is not detected in normal organs, but is expressed in gliomas with increasing levels with glioma progression. On the contrary, at protein level, isoform 2 is not detected in gliomas, suggesting that this isoform is unstable in glioma cells. Up-regulated by IGFBP2. Isoform 2 is degraded by the ubiquitin-proteasome pathway. protein binding negative regulation of G2/M transition of mitotic cell cycle negative regulation of cell migration uc001ato.1 uc001ato.2 uc001ato.3 uc001ato.4 
ENST00000235345.6 SLC35D1 ENST00000235345.6 solute carrier family 35 member D1 (from RefSeq NM_015139.3) A8K185 B7Z3X2 ENST00000235345.1 ENST00000235345.2 ENST00000235345.3 ENST00000235345.4 ENST00000235345.5 KIAA0260 NM_015139 Q52LU5 Q92548 Q9NTN3 S35D1_HUMAN SLC35D1 UGTREL7 uc001ddk.1 uc001ddk.2 uc001ddk.3 uc001ddk.4 Glycosylation of cellular glycoconjugates occurs in the endoplasmic reticulum (ER) and Golgi compartment, and requires transport of nucleotide sugars from the cytosol into the lumen of the ER and Golgi by specific transporters. The protein encoded by this gene resides in the ER, and transports both UDP-glucuronic acid (UDP-GlcA) and UDP-N-acetylgalactosamine (UDP-GalNAc) from the cytoplasm to the ER lumen. It may participate in glucuronidation and/or chondroitin sulfate biosynthesis. Mutations in this gene are associated with Schneckenbecken dysplasia.[provided by RefSeq, Sep 2009]. ##Evidence-Data-START## Transcript exon combination :: SRR1660805.12470.1, SRR1660809.38849.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000235345.6/ ENSP00000235345.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar (PubMed:16965264, PubMed:17599910, PubMed:31423530). Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) and UDP-alpha-D- glucuronate (UDP-GlcA), which are used by ER glucosyltransferases as sugar donors for the synthesis of sugar chains of glycoproteins, glycolipids and oligosaccharides (PubMed:11322953, PubMed:16965264, PubMed:17599910, PubMed:31423530, PubMed:17952091). May couple UDP- GlcNAc or UDP-GalNAc efflux to UDP-GlcA influx into the ER lumen that in turn stimulates glucuronidation and subsequent excretion of endobiotics and xenobiotics (PubMed:16965264, PubMed:17599910). Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development (By similarity). Reaction=UDP-alpha-D-glucuronate(out) + UDP-N-acetyl-alpha-D- glucosamine(in) = UDP-alpha-D-glucuronate(in) + UDP-N-acetyl-alpha-D- glucosamine(out); Xref=Rhea:RHEA:73703, ChEBI:CHEBI:57705, ChEBI:CHEBI:58052; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73704; Evidence= Reaction=UDP-alpha-D-glucuronate(out) + UDP-N-acetyl-alpha-D- galactosamine(in) = UDP-alpha-D-glucuronate(in) + UDP-N-acetyl-alpha- D-galactosamine(out); Xref=Rhea:RHEA:74835, ChEBI:CHEBI:58052, ChEBI:CHEBI:67138; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74836; Evidence=; Reaction=UDP-N-acetyl-alpha-D-glucosamine(in) + UMP(out) = UDP-N- acetyl-alpha-D-glucosamine(out) + UMP(in); Xref=Rhea:RHEA:72695, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865; Evidence=; Reaction=UDP-N-acetyl-alpha-D-galactosamine(in) + UMP(out) = UDP-N- acetyl-alpha-D-galactosamine(out) + UMP(in); Xref=Rhea:RHEA:72735, ChEBI:CHEBI:57865, ChEBI:CHEBI:67138; Evidence=; Reaction=UDP-alpha-D-glucuronate(in) + UMP(out) = UDP-alpha-D- glucuronate(out) + UMP(in); Xref=Rhea:RHEA:72727, ChEBI:CHEBI:57865, ChEBI:CHEBI:58052; Evidence=; Reaction=UDP-alpha-D-galactose(in) + UMP(out) = UDP-alpha-D- galactose(out) + UMP(in); Xref=Rhea:RHEA:72703, ChEBI:CHEBI:57865, ChEBI:CHEBI:66914; Evidence=; Reaction=UDP-alpha-D-glucose(in) + UMP(out) = UDP-alpha-D-glucose(out) + UMP(in); Xref=Rhea:RHEA:72731, ChEBI:CHEBI:57865, ChEBI:CHEBI:58885; Evidence=; Reaction=UDP-alpha-D-xylose(in) + UMP(out) = UDP-alpha-D-xylose(out) + UMP(in); Xref=Rhea:RHEA:72723, ChEBI:CHEBI:57632, ChEBI:CHEBI:57865; Evidence=; Reaction=UDP-beta-L-arabinopyranose(in) + UMP(out) = UDP-beta-L- arabinopyranose(out) + UMP(in); Xref=Rhea:RHEA:74671, ChEBI:CHEBI:57865, ChEBI:CHEBI:61457; Evidence=; Reaction=UDP-beta-L-arabinofuranose(in) + UMP(out) = UDP-beta-L- arabinofuranose(out) + UMP(in); Xref=Rhea:RHEA:74679, ChEBI:CHEBI:57865, ChEBI:CHEBI:61463; Evidence=; Kinetic parameters: KM=6 uM for UDP-alpha-D-glucuronate ; KM=37 uM for UDP-N-acetyl-alpha-D-glucosamine ; KM=27 uM for UDP-N-acetyl-alpha-D-galactosamine ; KM=36 uM for UDP-alpha-D-xylose ; KM=106 uM for UDP-beta-L-arabinopyranose ; KM=108 uM for UDP-alpha-D-glucose ; KM=126 uM for UDP-alpha-D-galactose ; Note=kcat is 0.1 sec(-1) with UDP-alpha-D-glucuronate as substrate. kcat is 0.4 sec(-1) with UDP-N-acetyl-alpha-D-glucosamine as substrate. kcat is 0.3 sec(-1) with UDP-N-acetyl-alpha-D- galactosamine as substrate. kcat is 0.2 sec(-1) with UDP-alpha-D- xylose as substrate. kcat is 0.1 sec(-1) with UDP-beta-L- arabinopyranose as substrate. kcat is 0.2 sec(-1) with UDP-alpha-D- glucose as substrate. kcat is 0.2 sec(-1) with UDP-alpha-D-galactose as substrate. ; Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NTN3-1; Sequence=Displayed; Name=2; IsoId=Q9NTN3-2; Sequence=VSP_056860, VSP_056861; Ubiquitous. Schneckenbecken dysplasia (SHNKND) [MIM:269250]: A rare, lethal autosomal recessive skeletal dysplasia characterized by snail- like configuration of the hypoplastic iliac bone, short-limbed dwarfism, short ribs, and flattened, hypoplastic vertebral bodies. SHNKND is lethal in the neonatal period. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TPT transporter family. SLC35D subfamily. The use of uridine 5'-monophosphate (UMP) as a counter-anion is disputed and needs further investigation. Sequence=BAA13390.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; UDP-glucuronic acid transmembrane transporter activity UDP-N-acetylglucosamine transmembrane transporter activity UDP-N-acetylgalactosamine transmembrane transporter activity endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus UDP-glucuronate biosynthetic process carbohydrate transport pyrimidine nucleotide-sugar transmembrane transporter activity antiporter activity UDP-glucuronic acid transport UDP-N-acetylgalactosamine transport membrane integral component of membrane transmembrane transporter activity chondroitin sulfate biosynthetic process embryonic skeletal system development pyrimidine nucleotide-sugar transmembrane transport UDP-N-acetylglucosamine transmembrane transport uc001ddk.1 uc001ddk.2 uc001ddk.3 uc001ddk.4 
ENST00000235347.4 PRAMEF10 ENST00000235347.4 PRAME family member 10 (from RefSeq NM_001039361.4) ENST00000235347.1 ENST00000235347.2 ENST00000235347.3 NM_001039361 O60809 PRA10_HUMAN PRAMEF10 Q2M1V2 uc031tpi.1 uc031tpi.2 Belongs to the PRAME family. cytoplasm positive regulation of cell proliferation negative regulation of apoptotic process negative regulation of cell differentiation negative regulation of transcription, DNA-templated uc031tpi.1 uc031tpi.2 
ENST00000235349.6 PRAMEF4 ENST00000235349.6 PRAME family member 4 (from RefSeq NM_001009611.4) ENST00000235349.1 ENST00000235349.2 ENST00000235349.3 ENST00000235349.4 ENST00000235349.5 NM_001009611 O60810 PRAM4_HUMAN PRAMEF4 Q5LJB5 uc001aun.1 uc001aun.2 uc001aun.3 uc001aun.4 Belongs to the PRAME family. Sequence=CAB41253.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; cytoplasm positive regulation of cell proliferation negative regulation of apoptotic process negative regulation of cell differentiation negative regulation of transcription, DNA-templated uc001aun.1 uc001aun.2 uc001aun.3 uc001aun.4 
ENST00000235382.7 RGS2 ENST00000235382.7 regulator of G protein signaling 2 (from RefSeq NM_002923.4) ENST00000235382.1 ENST00000235382.2 ENST00000235382.3 ENST00000235382.4 ENST00000235382.5 ENST00000235382.6 G0S8 GIG31 NM_002923 P41220 Q6I9U5 RGS2_HUMAN uc001gsl.1 uc001gsl.2 uc001gsl.3 uc001gsl.4 uc001gsl.5 Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 2 belongs to this family. The protein acts as a mediator of myeloid differentiation and may play a role in leukemogenesis. [provided by RefSeq, Aug 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1095256.1, SRR3476690.817888.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000235382.7/ ENSP00000235382.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP- bound form (PubMed:11063746, PubMed:19478087). It is involved in the negative regulation of the angiotensin-activated signaling pathway (PubMed:28784619). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (By similarity). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (PubMed:19736320). Interacts with GNAQ (PubMed:18434541, PubMed:19478087, PubMed:28784619). Does not interact with GNAI1 and GNAI3 (PubMed:18434541, PubMed:19478087). Interacts with EIF2B5 (PubMed:19736320). Interacts with PRKG1 (isoform alpha) (PubMed:14608379). P41220; O76071: CIAO1; NbExp=3; IntAct=EBI-712388, EBI-725145; P41220; Q5S007: LRRK2; NbExp=6; IntAct=EBI-712388, EBI-5323863; P41220; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-712388, EBI-742948; P41220; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-712388, EBI-11522433; P41220; Q9ULJ8: PPP1R9A; NbExp=3; IntAct=EBI-712388, EBI-2515561; P41220; O60260-5: PRKN; NbExp=6; IntAct=EBI-712388, EBI-21251460; P41220-1; O60337: MARCHF6; NbExp=3; IntAct=EBI-16037474, EBI-2684600; P41220-1; P21279: Gnaq; Xeno; NbExp=3; IntAct=EBI-16037474, EBI-771975; [Isoform 1]: Cell membrane toplasm cleus, nucleolus [Isoform 2]: Cell membrane Cytoplasm Nucleus, nucleolus [Isoform 3]: Cell membrane Cytoplasm Nucleus, nucleolus [Isoform 4]: Cell membrane Mitochondrion Event=Alternative initiation; Named isoforms=4; Name=1; IsoId=P41220-1; Sequence=Displayed; Name=2; IsoId=P41220-2; Sequence=VSP_041296; Name=3; IsoId=P41220-3; Sequence=VSP_041297; Name=4; IsoId=P41220-4; Sequence=VSP_041298; Expressed in acute myelogenous leukemia (AML) and in acute lymphoblastic leukemia (ALL). Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity. [Isoform 3]: Lacks type V adenylyl cyclase (AC) inhibitory function. [Isoform 4]: Lacks type V adenylyl cyclase (AC) inhibitory function. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42102/RGS2"; G-protein alpha-subunit binding response to amphetamine GTPase activity GTPase activator activity protein binding calmodulin binding nucleus nucleolus cytoplasm mitochondrion cytosol plasma membrane regulation of translation cell cycle G-protein coupled receptor signaling pathway spermatogenesis brain development regulation of G-protein coupled receptor protein signaling pathway cytoplasmic side of plasma membrane negative regulation of signal transduction negative regulation of phospholipase activity negative regulation of cardiac muscle hypertrophy positive regulation of neuron projection development membrane negative regulation of translation ovulation neuron projection negative regulation of MAP kinase activity positive regulation of GTPase activity negative regulation of cAMP-mediated signaling response to ethanol negative regulation of G-protein coupled receptor protein signaling pathway beta-tubulin binding brown fat cell differentiation relaxation of cardiac muscle relaxation of vascular smooth muscle maternal process involved in female pregnancy positive regulation of cardiac muscle contraction negative regulation of cell growth involved in cardiac muscle cell development negative regulation of glycine import uc001gsl.1 uc001gsl.2 uc001gsl.3 uc001gsl.4 uc001gsl.5 
ENST00000235521.5 WARS2 ENST00000235521.5 tryptophanyl tRNA synthetase 2, mitochondrial, transcript variant 1 (from RefSeq NM_015836.4) B1ALR1 B2R9D4 ENST00000235521.1 ENST00000235521.2 ENST00000235521.3 ENST00000235521.4 NM_015836 Q53FT4 Q5VUD2 Q86TQ0 Q9UGM6 SYWM_HUMAN uc001ehn.1 uc001ehn.2 uc001ehn.3 uc001ehn.4 uc001ehn.5 Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Two forms of tryptophanyl-tRNA synthetase exist, a cytoplasmic form, named WARS, and a mitochondrial form, named WARS2. This gene encodes the mitochondrial tryptophanyl-tRNA synthetase. Two alternative transcripts encoding different isoforms have been described. [provided by RefSeq, Jul 2008]. Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of tRNA(Trp). Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L- tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence=; Kinetic parameters: KM=27 uM for tryptophan ; KM=401 uM for ATP ; Mitochondrion matrix Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UGM6-1; Sequence=Displayed; Name=2; IsoId=Q9UGM6-2; Sequence=VSP_041414, VSP_041415; Brain. Neurodevelopmental disorder, mitochondrial, with abnormal movements and lactic acidosis, with or without seizures (NEMMLAS) [MIM:617710]: An autosomal recessive, mitochondrial disorder with a broad phenotypic spectrum ranging from severe neonatal lactic acidosis, encephalomyopathy and early death to an attenuated course with milder manifestations. Clinical features include delayed psychomotor development, intellectual disability, hypotonia, dystonia, ataxia, and spasticity. Severe combined respiratory chain deficiency may be found in severely affected individuals. te=The disease is caused by variants affecting the gene represented in this entry. Parkinsonism-dystonia 3, childhood-onset (PKDYS3) [MIM:619738]: An autosomal recessive neurodegenerative disorder with onset in infancy or early childhood. Affected individuals present with progressive movement abnormalities, including parkinsonism with tremor, dystonia, myoclonus ataxia, and hyperkinetic movements such as ballismus. The parkinsonism features may be responsive to treatment with levodopa, although many patients develop levodopa-induced dyskinesia. Some patients may have mild cognitive impairment or psychiatric disturbances. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the class-I aminoacyl-tRNA synthetase family. nucleotide binding vasculogenesis aminoacyl-tRNA ligase activity tryptophan-tRNA ligase activity ATP binding mitochondrion mitochondrial matrix cytosol plasma membrane translation tRNA aminoacylation for protein translation tryptophanyl-tRNA aminoacylation ligase activity mitochondrial tryptophanyl-tRNA aminoacylation uc001ehn.1 uc001ehn.2 uc001ehn.3 uc001ehn.4 uc001ehn.5 
ENST00000235532.9 OSCP1 ENST00000235532.9 organic solute carrier partner 1, transcript variant 1 (from RefSeq NM_145047.5) A6NHM5 A6NHS9 A6NIN9 C1orf102 ENST00000235532.1 ENST00000235532.2 ENST00000235532.3 ENST00000235532.4 ENST00000235532.5 ENST00000235532.6 ENST00000235532.7 ENST00000235532.8 NM_145047 NOR1 OSCP1_HUMAN Q4AEJ0 Q8N7G2 Q8TDF1 Q8WVF1 uc001caq.1 uc001caq.2 uc001caq.3 uc001caq.4 May be involved in drug clearance in the placenta. Kinetic parameters: KM=35.0 uM for p-aminohippurate (PAH) ; KM=62.3 uM for tetraethylammonium ; Note=In Xenopus laevis oocytes, in a sodium-independent manner.; Basal cell membrane. Note=Syncytiotrophoblast in placenta. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q8WVF1-1; Sequence=Displayed; Name=2; IsoId=Q8WVF1-2; Sequence=VSP_020826; Name=3; IsoId=Q8WVF1-3; Sequence=VSP_039475; Name=4; IsoId=Q8WVF1-4; Sequence=VSP_039475, VSP_039476, VSP_039477; Expressed predominantly in testis, also found in placenta and to a lesser extent in thymus and small intestine; abundantly expressed in tumor-derived cell lines (PubMed:16006562). Ubiquitously expressed (PubMed:12819961). May be involved in the development and/or progression of nosopharyngeal carcinoma. The polymorphism 'Glu58Gly' (described in PubMed:12819961) is in fact an error, the G to A change described representing a synonymous mutation that does not induce any amino acid change in Gly-32. Sequence=AAL89738.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; cytoplasm plasma membrane basal plasma membrane membrane transmembrane transporter activity drug transmembrane export uc001caq.1 uc001caq.2 uc001caq.3 uc001caq.4 
ENST00000235628.2 NT5C1A ENST00000235628.2 5'-nucleotidase, cytosolic IA (from RefSeq NM_032526.3) 5NT1A_HUMAN ENST00000235628.1 NM_032526 Q3SYB9 Q5TG98 Q9BWT8 Q9BXI3 uc001cdq.1 uc001cdq.2 Cytosolic nucleotidases, such as NT5C1A, dephosphorylate nucleoside monophosphates (Hunsucker et al., 2001 [PubMed 11133996]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC103879.1, AF331801.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145544, SAMEA2145743 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the hydrolysis of ribonucleotide and deoxyribonucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside (PubMed:11133996, PubMed:7599155, PubMed:8967393, PubMed:34814800). AMP is the major substrate but can also hydrolyze dCMP and IMP (PubMed:11133996, PubMed:7599155, PubMed:8967393, PubMed:34814800). Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence= Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'- deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167, ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474, ChEBI:CHEBI:65317; EC=3.1.3.89; Evidence=; Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence=; Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence= Reaction=dCMP + H2O = 2'-deoxycytidine + phosphate; Xref=Rhea:RHEA:29363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15698, ChEBI:CHEBI:43474, ChEBI:CHEBI:57566; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Activated by ADP. Kinetic parameters: KM=2.96 mM for AMP ; KM=5320 uM for AMP ; KM=1.46 mM for AMP ; KM=0.193 mM for dCMP ; KM=12.11 mM for IMP ; Vmax=7.7 umol/min/mg enzyme for AMP ; Vmax=18.1 umol/min/mg enzyme for dCMP ; Vmax=33.2 umol/min/mg enzyme for IMP ; pH dependence: Optimum pH is 7.0. ; Q9BXI3; Q16543: CDC37; NbExp=3; IntAct=EBI-10441581, EBI-295634; Q9BXI3; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-10441581, EBI-741158; Cytoplasm Highly expressed in skeletal muscle. Detected at intermediate levels in heart, brain, kidney and pancreas. Belongs to the 5'-nucleotidase type 3 family. nucleotide binding magnesium ion binding protein binding cytoplasm cytosol purine nucleotide catabolic process 5'-nucleotidase activity nucleoside metabolic process nucleotide metabolic process purine nucleoside monophosphate catabolic process dephosphorylation hydrolase activity adenosine metabolic process pyrimidine nucleoside catabolic process uc001cdq.1 uc001cdq.2 
ENST00000235835.8 AKR7A2 ENST00000235835.8 aldo-keto reductase family 7 member A2, transcript variant 1 (from RefSeq NM_003689.4) AKR7A2 ENST00000235835.1 ENST00000235835.2 ENST00000235835.3 ENST00000235835.4 ENST00000235835.5 ENST00000235835.6 ENST00000235835.7 HEL-S-166mP NM_003689 V9HWA2 V9HWA2_HUMAN hCG_40469 uc001bbw.1 uc001bbw.2 uc001bbw.3 uc001bbw.4 uc001bbw.5 The protein encoded by this gene belongs to the aldo/keto reductase (AKR) superfamily and AKR7 family, which are involved in the detoxification of aldehydes and ketones. The AKR7 family consists of 3 genes that are present in a cluster on the p arm of chromosome 1. This protein, thought to be localized in the golgi, catalyzes the NADPH-dependent reduction of succinic semialdehyde to the endogenous neuromodulator, gamma-hydroxybutyrate. It may also function as a detoxication enzyme in the reduction of aflatoxin B1 and 2-carboxybenzaldehyde. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2016]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: EU794591.1, BK000395.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on manual assertion, conservation, expression, longest protein ##RefSeq-Attributes-END## cytosol uc001bbw.1 uc001bbw.2 uc001bbw.3 uc001bbw.4 uc001bbw.5 
ENST00000236051.3 EBNA1BP2 ENST00000236051.3 EBNA1 binding protein 2, transcript variant 2 (from RefSeq NM_006824.3) EBP2 EBP2_HUMAN ENST00000236051.1 ENST00000236051.2 NM_006824 Q96A66 Q99848 uc001cin.1 uc001cin.2 uc001cin.3 uc001cin.4 uc001cin.5 Required for the processing of the 27S pre-rRNA. Specifically interacts with EBV EBNA1. The EBNA1-EBP2 interaction is important for the stable segregation of EBV episomes during cell division (PubMed:10074103). Interacts with WDR46. Q99848; Q8TDN6: BRIX1; NbExp=4; IntAct=EBI-1048111, EBI-1052326; Q99848; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-1048111, EBI-739624; Q99848; Q8IZU0: FAM9B; NbExp=5; IntAct=EBI-1048111, EBI-10175124; Nucleus, nucleolus te=Associated with the nucleolus in an RNA-dependent manner. Ubiquitous. Belongs to the EBP2 family. RNA binding protein binding nucleus nucleolus rRNA processing preribosome, large subunit precursor nuclear periphery ribosome biogenesis ribosomal large subunit biogenesis uc001cin.1 uc001cin.2 uc001cin.3 uc001cin.4 uc001cin.5 
ENST00000236137.10 SLC19A2 ENST00000236137.10 solute carrier family 19 member 2, transcript variant 1 (from RefSeq NM_006996.3) B2R9H0 B4E1X4 ENST00000236137.1 ENST00000236137.2 ENST00000236137.3 ENST00000236137.4 ENST00000236137.5 ENST00000236137.6 ENST00000236137.7 ENST00000236137.8 ENST00000236137.9 NM_006996 O60779 Q8WV87 Q9UBL7 Q9UKJ2 Q9UN31 Q9UN43 S19A2_HUMAN THT1 TRMA uc001gge.1 uc001gge.2 uc001gge.3 uc001gge.4 uc001gge.5 uc001gge.6 This gene encodes the thiamin transporter protein. Mutations in this gene cause thiamin-responsive megaloblastic anemia syndrome (TRMA), which is an autosomal recessive disorder characterized by diabetes mellitus, megaloblastic anemia and sensorineural deafness. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2016]. High-affinity transporter for the intake of thiamine (PubMed:10542220, PubMed:10391222, PubMed:33008889, PubMed:35512554, PubMed:35724964). Mediates H(+)-dependent pyridoxine transport (PubMed:33008889, PubMed:35512554, PubMed:35724964). Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in); Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385; Evidence= Reaction=n H(+)(out) + pyridoxine(out) = n H(+)(in) + pyridoxine(in); Xref=Rhea:RHEA:76203, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709; Evidence= Pyridoxine transport is inhibited by carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP) and carbonyl cyanide m-chlorophenylhydrazone (CCCP). Kinetic parameters: KM=37.8 uM for pyridoxine (at pH 5.5) ; KM=3.66 uM for thiamine (at pH 5.5) ; KM=2.83 uM for thiamine (at pH 7.4) ; KM=2.5 uM for thiamine ; Vmax=332 pmol/min/mg enzyme for pyridoxine (at pH 5.5) ; Vmax=100 pmol/min/mg enzyme for thiamine (at pH 5.5) ; Vmax=106 pmol/min/mg enzyme for thiamine (at pH 7.4) ; pH dependence: Optimum pH is 8-8.5. ; O60779; O60635: TSPAN1; NbExp=5; IntAct=EBI-3941998, EBI-3914312; Cell membrane ulti-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O60779-1; Sequence=Displayed; Name=2; IsoId=O60779-2; Sequence=VSP_036467; Ubiquitous; most abundant in skeletal and cardiac muscle. Medium expression in placenta, heart, liver and kidney, low in lung. Thiamine-responsive megaloblastic anemia syndrome (TRMA) [MIM:249270]: An autosomal recessive disease characterized by megaloblastic anemia, diabetes mellitus, and sensorineural deafness. Onset is typically between infancy and adolescence, but all of the cardinal findings are often not present initially. The anemia, and sometimes the diabetes, improves with high doses of thiamine. Other more variable features include optic atrophy, congenital heart defects, short stature, and stroke. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the reduced folate carrier (RFC) transporter (TC 2.A.48) family. Sequence=AAD51280.1; Type=Frameshift; Evidence=; Sequence=AAD51283.1; Type=Frameshift; Evidence=; Sequence=BAG64936.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; protein binding plasma membrane folic acid transporter activity thiamine transmembrane transporter activity folic acid transport thiamine transport membrane integral component of membrane thiamine-containing compound metabolic process vitamin transport transmembrane transport thiamine transmembrane transport vitamin transmembrane transporter activity uc001gge.1 uc001gge.2 uc001gge.3 uc001gge.4 uc001gge.5 uc001gge.6 
ENST00000236147.6 SELL ENST00000236147.6 selectin L, transcript variant 2 (from RefSeq NR_029467.2) A0A024R8Z0 B2R6Q8 ENST00000236147.1 ENST00000236147.2 ENST00000236147.3 ENST00000236147.4 ENST00000236147.5 LNHR LYAM1 LYAM1_HUMAN NR_029467 P14151 P15023 Q9UJ43 uc001ggk.1 uc001ggk.2 uc001ggk.3 uc001ggk.4 uc001ggk.5 This gene encodes a cell surface adhesion molecule that belongs to a family of adhesion/homing receptors. The encoded protein contains a C-type lectin-like domain, a calcium-binding epidermal growth factor-like domain, and two short complement-like repeats. The gene product is required for binding and subsequent rolling of leucocytes on endothelial cells, facilitating their migration into secondary lymphoid organs and inflammation sites. Single-nucleotide polymorphisms in this gene have been associated with various diseases including immunoglobulin A nephropathy. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Oct 2009]. Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells (PubMed:12403782, PubMed:28489325, PubMed:28011641). Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia (PubMed:12403782, PubMed:28011641). Interaction with SELPLG/PSGL1 and PODXL2 is required for promoting recruitment and rolling of leukocytes. This interaction is dependent on the sialyl Lewis X glycan modification of SELPLG and PODXL2, and tyrosine sulfation modifications of SELPLG. Sulfation on 'Tyr-51' of SELPLG is important for L-selectin binding. P14151-2; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-17865914, EBI-8644112; Cell membrane ingle-pass type I membrane protein Event=Alternative initiation; Named isoforms=2; Comment=The start of isoform 1 corresponds to the N-terminus of mammalian orthologs. The start codon for isoform 2 is in the same exon and reading frame as that for isoform 1, suggesting alternative initiation. ; Name=1; IsoId=P14151-1; Sequence=Displayed; Name=2; IsoId=P14151-2; Sequence=VSP_042650; Expressed in B-cell lines and T-lymphocytes. N-glycosylated. Belongs to the selectin/LECAM family. Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/sell/"; Name=Functional Glycomics Gateway - Glycan Binding; Note=L-selectin; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_234"; protease binding calcium ion binding protein binding plasma membrane integral component of plasma membrane cell adhesion heparin binding membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules carbohydrate binding secretory granule membrane glycosphingolipid binding neutrophil degranulation metal ion binding regulation of immune response leukocyte migration leukocyte tethering or rolling oligosaccharide binding uc001ggk.1 uc001ggk.2 uc001ggk.3 uc001ggk.4 uc001ggk.5 
ENST00000236192.12 VAMP4 ENST00000236192.12 vesicle associated membrane protein 4, transcript variant 1 (from RefSeq NM_003762.5) A0A024R8Z6 ENST00000236192.1 ENST00000236192.10 ENST00000236192.11 ENST00000236192.2 ENST00000236192.3 ENST00000236192.4 ENST00000236192.5 ENST00000236192.6 ENST00000236192.7 ENST00000236192.8 ENST00000236192.9 NM_003762 Q6IAZ3 Q6IAZ3_HUMAN VAMP4 hCG_37824 uc001ghx.1 uc001ghx.2 uc001ghx.3 uc001ghx.4 Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. This protein may play a role in trans-Golgi network-to-endosome transport. [provided by RefSeq, Jul 2008]. Membrane ; Single- pass type IV membrane protein Belongs to the synaptobrevin family. synaptic vesicle membrane integral component of membrane synaptic vesicle to endosome fusion vesicle-mediated transport integral component of synaptic vesicle membrane regulation of synaptic vesicle endocytosis uc001ghx.1 uc001ghx.2 uc001ghx.3 uc001ghx.4 
ENST00000236273.9 SYF2 ENST00000236273.9 SYF2 pre-mRNA splicing factor, transcript variant 1 (from RefSeq NM_015484.5) CBPIN ENST00000236273.1 ENST00000236273.2 ENST00000236273.3 ENST00000236273.4 ENST00000236273.5 ENST00000236273.6 ENST00000236273.7 ENST00000236273.8 GCIPIP NM_015484 O95926 Q5TH73 SYF2_HUMAN uc001bjt.1 uc001bjt.2 uc001bjt.3 This gene encodes a nuclear protein that interacts with cyclin D-type binding-protein 1, which is thought to be a cell cycle regulator at the G1/S transition. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008]. Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28502770, PubMed:28076346). Identified in the spliceosome C complex (PubMed:11991638, PubMed:28502770, PubMed:28076346). Interacts with CCNDBP1 (PubMed:11118353). O95926; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-2557644, EBI-742909; O95926; O95273: CCNDBP1; NbExp=3; IntAct=EBI-2557644, EBI-748961; O95926; P40692: MLH1; NbExp=3; IntAct=EBI-2557644, EBI-744248; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95926-1; Sequence=Displayed; Name=2; IsoId=O95926-2; Sequence=VSP_054802; Abundantly expressed in the heart, skeletal muscle and kidney. Expressed at lower level other tissues. Belongs to the SYF2 family. mRNA splicing, via spliceosome Prp19 complex in utero embryonic development RNA binding protein binding nucleus nucleoplasm spliceosomal complex mRNA processing mitotic G2 DNA damage checkpoint gastrulation positive regulation of cell proliferation RNA splicing nuclear speck embryonic organ development U2-type catalytic step 2 spliceosome catalytic step 2 spliceosome post-mRNA release spliceosomal complex uc001bjt.1 uc001bjt.2 uc001bjt.3 
ENST00000236342.12 DHDDS ENST00000236342.12 dehydrodolichyl diphosphate synthase subunit, transcript variant 1 (from RefSeq NM_205861.3) B7Z4B9 B7ZB20 D3DPK7 D3DPK8 D3DPK9 DHDDS DHDDS_HUMAN E9KL43 ENST00000236342.1 ENST00000236342.10 ENST00000236342.11 ENST00000236342.2 ENST00000236342.3 ENST00000236342.4 ENST00000236342.5 ENST00000236342.6 ENST00000236342.7 ENST00000236342.8 ENST00000236342.9 HDS NM_205861 Q5T0A4 Q86SQ9 Q8NE90 Q9BTG5 Q9BTK3 Q9H905 uc001bml.1 uc001bml.2 uc001bml.3 uc001bml.4 uc001bml.5 The protein encoded by this gene catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier lipid required for the biosynthesis of several classes of glycoproteins. Mutations in this gene are associated with retinitis pigmentosa type 59. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Aug 2011]. With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER) (PubMed:25066056, PubMed:28842490, PubMed:32817466). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length (PubMed:32817466). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol (PubMed:21572394). Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di- trans,poly-cis-polyprenyl diphosphate + n diphosphate; Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019, ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763; EC=2.5.1.87; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Note=Binds 1 magnesium ion per subunit. ; Activated by phospholipids including cardiolipin, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol and phosphatidylserine. Kinetic parameters: KM=11.1 uM for isopentenyl diphosphate ; KM=0.68 uM for (2E,6E)-farnesyl diphosphate ; Note=Values were measured with the heterodimer. kcat is 0.58 sec(-1) with (2E,6E)-farnesyl diphosphate and isopentenyl diphosphate as substrate. ; pH dependence: Optimum pH is 8-9. Active from pH 5.5 to 9.3. ; Protein modification; protein glycosylation. Lipid metabolism. Forms an active dehydrodolichyl diphosphate synthase complex with NUS1 (PubMed:25066056, PubMed:28842490, PubMed:32817466). Interacts with NPC2 (PubMed:21572394). Q86SQ9; Q96E22: NUS1; NbExp=3; IntAct=EBI-26942900, EBI-6949352; Endoplasmic reticulum membrane ; Peripheral membrane protein Note=colocalizes with calnexin. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q86SQ9-1; Sequence=Displayed; Name=2; IsoId=Q86SQ9-2; Sequence=VSP_010031; Name=3; IsoId=Q86SQ9-3; Sequence=VSP_010030; Name=4; IsoId=Q86SQ9-4; Sequence=VSP_045007; Expressed at high levels in testis and kidney. Expressed in epididymis (at protein level). Slightly expressed in heart, spleen and thymus. The catalytic site at NUS1-DHDDS interface accomodates both the allylic and the homoallylic IPP substrates to the S1 and S2 pockets respectively. The beta-phosphate groups of IPP substrates form hydrogen bonds with the RXG motif of NUS1 and four conserved residues of DHDDS (Arg-85, Arg-205, Arg-211 and Ser-213), while the allylic isopentenyl group is pointed toward the hydrophobic tunnel of the S1 pocket where the product elongation occurs. Retinitis pigmentosa 59 (RP59) [MIM:613861]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note=The disease is caused by variants affecting the gene represented in this entry. Developmental delay and seizures with or without movement abnormalities (DEDSM) [MIM:617836]: An autosomal dominant neurodevelopmental disorder characterized by global developmental delay, variable intellectual disability, and early-onset seizures with a myoclonic component. Most patients have delayed motor development and show abnormal movements, including ataxia, dystonia, and tremor. Note=The disease may be caused by variants affecting the gene represented in this entry. [Isoform 3]: May be due to exon skipping. Belongs to the UPP synthase family. polyprenyltransferase activity protein binding endoplasmic reticulum endoplasmic reticulum membrane protein glycosylation dolichyl diphosphate biosynthetic process lipid metabolic process membrane polyprenol biosynthetic process transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups dehydrodolichyl diphosphate synthase activity dehydrodolichyl diphosphate synthase complex uc001bml.1 uc001bml.2 uc001bml.3 uc001bml.4 uc001bml.5 
ENST00000236671.7 CTSD ENST00000236671.7 cathepsin D (from RefSeq NM_001909.5) CTSD ENST00000236671.1 ENST00000236671.2 ENST00000236671.3 ENST00000236671.4 ENST00000236671.5 ENST00000236671.6 HEL-S-130P NM_001909 V9HWI3 V9HWI3_HUMAN hCG_49857 uc001luc.1 uc001luc.2 uc001luc.3 This gene encodes a member of the A1 family of peptidases. The encoded preproprotein is proteolytically processed to generate multiple protein products. These products include the cathepsin D light and heavy chains, which heterodimerize to form the mature enzyme. This enzyme exhibits pepsin-like activity and plays a role in protein turnover and in the proteolytic activation of hormones and growth factors. Mutations in this gene play a causal role in neuronal ceroid lipofuscinosis-10 and may be involved in the pathogenesis of several other diseases, including breast cancer and possibly Alzheimer's disease. [provided by RefSeq, Nov 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.350777.1, SRR3476690.959075.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000236671.7/ ENSP00000236671.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Reaction=Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.; EC=3.4.23.5; Evidence=; Lysosome Belongs to the peptidase A1 family. aspartic-type endopeptidase activity lysosome proteolysis peptidase activity hydrolase activity uc001luc.1 uc001luc.2 uc001luc.3 
ENST00000236709.4 A4GNT ENST00000236709.4 alpha-1,4-N-acetylglucosaminyltransferase (from RefSeq NM_016161.3) A4GCT_HUMAN ENST00000236709.1 ENST00000236709.2 ENST00000236709.3 NM_016161 Q0VDK1 Q0VDK2 Q9UNA3 uc003ers.1 uc003ers.2 uc003ers.3 This gene encodes a protein from the glycosyltransferase 32 family. The enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. It forms a unique glycan, GlcNAcalpha1-->4Galbeta-->R and is largely associated with the Golgi apparatus membrane. [provided by RefSeq, Jul 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. ##Evidence-Data-START## Transcript exon combination :: AK225668.1, AF141315.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142586, SAMEA2146982 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000236709.4/ ENSP00000236709.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans (PubMed:10430883). Necessary for the synthesis of type III mucin which is specifically produced in the stomach, duodenum, and pancreatic duct (PubMed:10430883). May protect against inflammation-associated gastric adenocarcinomas (By similarity). Protein modification; protein glycosylation. Golgi apparatus membrane ; Single- pass type II membrane protein Detected in stomach and pancreas. The conserved DXD motif is involved in enzyme activity. Belongs to the glycosyltransferase 32 family. Name=Functional Glycomics Gateway - GTase; Note=Alpha- 1,4-N-acetylglucosaminyltransferase; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_532"; Golgi membrane Golgi apparatus carbohydrate metabolic process protein glycosylation protein O-linked glycosylation acetylglucosaminyltransferase activity glycoprotein biosynthetic process membrane integral component of membrane O-glycan processing transferase activity transferase activity, transferring glycosyl groups negative regulation of epithelial cell proliferation uc003ers.1 uc003ers.2 uc003ers.3 
ENST00000236826.8 MMP8 ENST00000236826.8 matrix metallopeptidase 8, transcript variant 1 (from RefSeq NM_002424.3) CLG1 ENST00000236826.1 ENST00000236826.2 ENST00000236826.3 ENST00000236826.4 ENST00000236826.5 ENST00000236826.6 ENST00000236826.7 MMP8_HUMAN NM_002424 P22894 Q45F99 uc001phe.1 uc001phe.2 uc001phe.3 This gene encodes a member of the matrix metalloproteinase (MMP) family of proteins. These proteins are involved in the breakdown of extracellular matrix in embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Proteolysis at different sites on this protein results in multiple active forms of the enzyme with distinct N-termini. This protein functions in the degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2015]. Can degrade fibrillar type I, II, and III collagens. Reaction=Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.; EC=3.4.24.34; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 3 Ca(2+) ions per subunit.; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; Cannot be activated without removal of the activation peptide. Cytoplasmic granule. Secreted, extracellular space, extracellular matrix Note=Stored in intracellular granules. Neutrophils. The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation- peptide release activates the enzyme. Belongs to the peptidase M10A family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp8/"; endopeptidase activity metalloendopeptidase activity serine-type endopeptidase activity extracellular region extracellular space proteolysis peptidase activity metallopeptidase activity zinc ion binding positive regulation of gene expression negative regulation of gene expression hydrolase activity extracellular matrix disassembly extracellular matrix organization collagen catabolic process extracellular matrix negative regulation of interleukin-10 production positive regulation of interleukin-6 production specific granule lumen endodermal cell differentiation neutrophil degranulation positive regulation of DNA binding positive regulation of MAPK cascade positive regulation of nitric oxide biosynthetic process positive regulation of JNK cascade metal ion binding positive regulation of NIK/NF-kappaB signaling positive regulation of reactive oxygen species biosynthetic process regulation of microglial cell activation positive regulation of microglial cell activation positive regulation of tumor necrosis factor secretion tertiary granule lumen uc001phe.1 uc001phe.2 uc001phe.3 
ENST00000236850.5 APOA1 ENST00000236850.5 apolipoprotein A1, transcript variant 4 (from RefSeq NM_001318021.1) A8K866 APOA1 APOA1_HUMAN ENST00000236850.1 ENST00000236850.2 ENST00000236850.3 ENST00000236850.4 NM_001318021 P02647 Q6LDN9 Q6Q785 Q9UCS8 Q9UCT8 uc001ppv.1 uc001ppv.2 uc001ppv.3 This gene encodes apolipoprotein A-I, which is the major protein component of high density lipoprotein (HDL) in plasma. The encoded preproprotein is proteolytically processed to generate the mature protein, which promotes cholesterol efflux from tissues to the liver for excretion, and is a cofactor for lecithin cholesterolacyltransferase (LCAT), an enzyme responsible for the formation of most plasma cholesteryl esters. This gene is closely linked with two other apolipoprotein genes on chromosome 11. Defects in this gene are associated with HDL deficiencies, including Tangier disease, and with systemic non-neuropathic amyloidosis. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein. [provided by RefSeq, Dec 2015]. Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. Homodimer (By similarity). Interacts with NAXE and CLU (PubMed:1742316, PubMed:11991719). Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin (PubMed:1909888). Interacts with NDRG1 (PubMed:15922294). Interacts with SCGB3A2 (PubMed:12847263). Interacts with NAXE and YJEFN3 (PubMed:23719382). P02647; O95477: ABCA1; NbExp=8; IntAct=EBI-701692, EBI-784112; P02647; P02647: APOA1; NbExp=28; IntAct=EBI-701692, EBI-701692; P02647; P05067: APP; NbExp=8; IntAct=EBI-701692, EBI-77613; P02647; Q07021: C1QBP; NbExp=2; IntAct=EBI-701692, EBI-347528; P02647; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-701692, EBI-2548702; P02647; Q96DZ9-2: CMTM5; NbExp=6; IntAct=EBI-701692, EBI-11522780; P02647; P00738: HP; NbExp=3; IntAct=EBI-701692, EBI-1220767; P02647; P13473-2: LAMP2; NbExp=3; IntAct=EBI-701692, EBI-21591415; P02647; P04180: LCAT; NbExp=2; IntAct=EBI-701692, EBI-9104464; P02647; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-701692, EBI-2623095; P02647; P37840: SNCA; NbExp=3; IntAct=EBI-701692, EBI-985879; Secreted. Major protein of plasma HDL, also found in chylomicrons. Synthesized in the liver and small intestine. The oxidized form at Met-110 and Met-136 is increased in individuals with increased risk for coronary artery disease, such as in carrier of the eNOSa/b genotype and exposure to cigarette smoking. It is also present in increased levels in aortic lesions relative to native ApoA-I and increased levels are seen with increasing severity of disease. Glycosylated. Palmitoylated. Phosphorylation sites are present in the extracellular medium. [Apolipoprotein A-I]: Mass=28081; Method=Electrospray; Note=Without methionine sulfoxide.; Evidence=; [Apolipoprotein A-I]: Mass=28098; Method=Electrospray; Note=With 1 methionine sulfoxide, oxidation at Met-110.; Evidence=; [Apolipoprotein A-I]: Mass=28095; Method=Electrospray; Note=With 1 methionine sulfoxide, oxidation at Met-136.; Evidence=; [Apolipoprotein A-I]: Mass=28114; Method=Electrospray; Note=With 2 methionine sulfoxides, oxidation at Met-110 and Met-136.; Evidence=; Genetic variations in APOA1 can result in APOA1 deficiency and are associated with low levels of HDL cholesterol [MIM:107680]. Hypoalphalipoproteinemia, primary, 2 (FHA2) [MIM:618463]: An autosomal recessive disorder of lipoprotein metabolism, biochemically characterized by severe apoA-I deficiency and severely reduced serum high-density lipoprotein cholesterol (HDL-C). Affected individuals have undetectable serum levels of apoA-I, and develop xanthomas and corneal opacities. The disease is generally associated with atherosclerosis and markedly increased cardiovascular risk. te=The disease is caused by variants affecting the gene represented in this entry. Hypoalphalipoproteinemia, primary, 2, intermediate (FHA2I) [MIM:619836]: An autosomal dominant disorder of lipoprotein metabolism, biochemically characterized by partial apoA-I deficiency and reduced serum high-density lipoprotein cholesterol (HDL-C). Affected individuals have half the normal plasma apoA-I and HDL-C levels, and may develop xanthomas and corneal opacities. Most patients do not have increased cardiovascular risk. Note=The disease is caused by variants affecting the gene represented in this entry. Note=APOA1 mutations may be involved in the pathogenesis of amyloid polyneuropathy-nephropathy Iowa type, also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III (PubMed:3142462, PubMed:2123470). The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Amyloidosis 8 (AMYL8) [MIM:105200]: A form of hereditary generalized amyloidosis. Clinical features include extensive visceral amyloid deposits, renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. There is no involvement of the nervous system. te=The disease is caused by variants affecting the gene represented in this entry. Familial apolipoprotein gene cluster deletion syndrome (FAPLDS) [MIM:620058]: An autosomal dominant disorder of lipoprotein metabolism. Affected individuals do not produce ApoA-I, ApoC-III and ApoA-IV lipoproteins, have marked plasma high density lipoprotein (HDL) deficiency, and manifest premature atherosclerosis and coronary artery disease. Note=The gene represented in this entry is involved in disease pathogenesis. Belongs to the apolipoprotein A1/A4/E family. retinoid metabolic process beta-amyloid binding regulation of protein phosphorylation endothelial cell proliferation platelet degranulation negative regulation of cytokine secretion involved in immune response receptor binding lipid transporter activity protein binding phospholipid binding phospholipid transporter activity extracellular region extracellular space nucleus early endosome endoplasmic reticulum lumen cytosol plasma membrane lipid metabolic process phospholipid metabolic process phosphatidylcholine biosynthetic process cholesterol biosynthetic process lipid transport receptor-mediated endocytosis G-protein coupled receptor signaling pathway integrin-mediated signaling pathway response to nutrient high-density lipoprotein particle binding steroid metabolic process cholesterol metabolic process glucocorticoid metabolic process lipid binding cell surface negative regulation of tumor necrosis factor-mediated signaling pathway positive regulation of cholesterol esterification positive regulation of cholesterol efflux positive regulation of triglyceride catabolic process negative regulation of very-low-density lipoprotein particle remodeling peripheral nervous system axon regeneration cholesterol binding phospholipid transport protein oxidation peptidyl-methionine modification regulation of lipid metabolic process enzyme binding lipid storage endocytic vesicle regulation of intestinal cholesterol absorption cholesterol transport adrenal gland development heat shock protein binding animal organ regeneration phosphatidylcholine binding cytoplasmic vesicle regulation of Cdc42 protein signal transduction cholesterol efflux phospholipid efflux negative regulation of heterotypic cell-cell adhesion apolipoprotein receptor binding apolipoprotein A-I receptor binding very-low-density lipoprotein particle low-density lipoprotein particle intermediate-density lipoprotein particle high-density lipoprotein particle discoidal high-density lipoprotein particle spherical high-density lipoprotein particle chylomicron remodeling very-low-density lipoprotein particle remodeling high-density lipoprotein particle remodeling chylomicron assembly high-density lipoprotein particle assembly high-density lipoprotein particle clearance secretory granule lumen positive regulation of Rho protein signal transduction lipoprotein metabolic process lipoprotein biosynthetic process response to drug chylomicron cholesterol homeostasis identical protein binding blood vessel endothelial cell migration response to estrogen post-translational protein modification reverse cholesterol transport cellular protein metabolic process chemorepellent activity positive regulation of fatty acid biosynthetic process phosphatidylcholine metabolic process negative regulation of interleukin-1 beta secretion negative regulation of inflammatory response positive regulation of phagocytosis protein stabilization negative chemotaxis positive regulation of lipoprotein lipase activity vitamin transport positive regulation of hydrolase activity negative regulation of hydrolase activity positive regulation of stress fiber assembly transmembrane transport phospholipid homeostasis lipase inhibitor activity negative regulation of lipase activity phosphatidylcholine-sterol O-acyltransferase activator activity negative regulation of cell adhesion molecule production negative regulation of response to cytokine stimulus extracellular exosome triglyceride homeostasis cholesterol import high-density lipoprotein particle receptor binding endocytic vesicle lumen lipoprotein particle binding blood microparticle positive regulation of substrate adhesion-dependent cell spreading positive regulation of phospholipid efflux extracellular vesicle transforming growth factor beta receptor signaling pathway ERK1 and ERK2 cascade uc001ppv.1 uc001ppv.2 uc001ppv.3 
ENST00000236877.11 SLC8A2 ENST00000236877.11 solute carrier family 8 member A2 (from RefSeq NM_015063.3) B4DYQ9 ENST00000236877.1 ENST00000236877.10 ENST00000236877.2 ENST00000236877.3 ENST00000236877.4 ENST00000236877.5 ENST00000236877.6 ENST00000236877.7 ENST00000236877.8 ENST00000236877.9 KIAA1087 NAC2_HUMAN NCX2 NM_015063 Q9UPR5 uc002pgx.1 uc002pgx.2 uc002pgx.3 uc002pgx.4 uc002pgx.5 Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory. Plays a role in regulating urinary Ca(2+) and Na(+) excretion. Reaction=Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in); Xref=Rhea:RHEA:69955, ChEBI:CHEBI:29101, ChEBI:CHEBI:29108; Evidence=; Calcium transport is down-regulated by Na(+) and stimulated by Ca(2+). Cell membrane ; Multi-pass membrane protein Basolateral cell membrane ; Multi-pass membrane protein Perikaryon Cell projection, dendrite Cell projection, dendritic spine The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). The first Calx-beta domain can bind up to four Ca(2+) ions. The second domain can bind another two Ca(2+) ions that are essential for calcium- regulated ion exchange. Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC8 subfamily. Sequence=BAA83039.1; Type=Erroneous initiation; Evidence=; calcium:sodium antiporter activity calmodulin binding plasma membrane integral component of plasma membrane ion transport sodium ion transport calcium ion transport cellular calcium ion homeostasis cell communication learning memory antiporter activity membrane integral component of membrane basolateral plasma membrane dendrite sodium ion transmembrane transport cell projection dendritic spine perikaryon metal ion binding regulation of short-term neuronal synaptic plasticity transmembrane transport long-term synaptic potentiation calcium ion transmembrane transport regulation of cardiac conduction uc002pgx.1 uc002pgx.2 uc002pgx.3 uc002pgx.4 uc002pgx.5 
ENST00000236938.12 FCRLA ENST00000236938.12 Fc receptor like A, transcript variant 2 (from RefSeq NM_032738.4) A0N0M1 A6NC03 A6NL20 ENST00000236938.1 ENST00000236938.10 ENST00000236938.11 ENST00000236938.2 ENST00000236938.3 ENST00000236938.4 ENST00000236938.5 ENST00000236938.6 ENST00000236938.7 ENST00000236938.8 ENST00000236938.9 F5H720 F8W743 FCRL FCRL1 FCRLA_HUMAN FCRLM1 FCRX FREB G3V1J2 NM_032738 Q5VXA1 Q5VXA2 Q5VXA3 Q5VXA4 Q5VXB0 Q5VXB1 Q7L513 Q8NEW4 Q8WXH3 Q96PC6 Q96PJ0 Q96PJ1 Q96PJ2 Q96PJ4 Q9BR57 UNQ291/PRO329 uc001gbd.1 uc001gbd.2 uc001gbd.3 uc001gbd.4 uc001gbd.5 This gene encodes a protein similar to receptors for the Fc fragment of gamma immunoglobulin (IgG). These receptors, referred to as FCGRs, mediate the destruction of IgG-coated antigens and of cells induced by antibodies. This encoded protein is selectively expressed in B cells, and may be involved in their development. This protein may also be involved in the development of lymphomas. Multiple alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [provided by RefSeq, Aug 2011]. May be implicated in B-cell differentiation and lymphomagenesis. Monomer or homodimer; disulfide-linked. Cytoplasm te=Seems not to be secreted. Event=Alternative splicing; Named isoforms=15; Name=1; Synonyms=FCRLa; IsoId=Q7L513-1; Sequence=Displayed; Name=2; Synonyms=FCRLa1; IsoId=Q7L513-2; Sequence=VSP_017605; Name=3; Synonyms=FCRLb; IsoId=Q7L513-3; Sequence=VSP_017608; Name=4; Synonyms=FCRLc1; IsoId=Q7L513-4; Sequence=VSP_017606; Name=5; Synonyms=FCRLc2; IsoId=Q7L513-5; Sequence=VSP_017604; Name=6; Synonyms=FCRLd; IsoId=Q7L513-6; Sequence=VSP_017607; Name=7; Synonyms=FCRLe; IsoId=Q7L513-7; Sequence=VSP_017603; Name=8; Synonyms=FCRLf; IsoId=Q7L513-8; Sequence=VSP_017609; Name=9; IsoId=Q7L513-9; Sequence=VSP_038297; Name=10; IsoId=Q7L513-10; Sequence=VSP_038297, VSP_017605; Name=11; IsoId=Q7L513-11; Sequence=VSP_038297, VSP_017606; Name=12; IsoId=Q7L513-12; Sequence=VSP_038297, VSP_017608; Name=13; IsoId=Q7L513-13; Sequence=VSP_038297, VSP_017607; Name=14; IsoId=Q7L513-14; Sequence=VSP_038297, VSP_017604; Name=15; IsoId=Q7L513-15; Sequence=VSP_038297, VSP_017603; Expressed specifically in primary and secondary lymphoid tissues like lymph node, spleen and tonsil. Specifically expressed in B-cells with a high level in normal germinal center B- cells, centroblasts and in a subset of diffuse large B-cell lymphomas. Highly expressed in bone marrow B-cells and weakly in earlier B lineage cells. Expressed in pre-germinal and germinal center B-cells in secondary lymphoid tissues. Also expressed in melanoma and melanocytes. It is uncertain whether Met-1 or Met-8 is the initiator. cytoplasm cell differentiation uc001gbd.1 uc001gbd.2 uc001gbd.3 uc001gbd.4 uc001gbd.5 
ENST00000236959.14 ATIC ENST00000236959.14 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (from RefSeq NM_004044.7) ENST00000236959.1 ENST00000236959.10 ENST00000236959.11 ENST00000236959.12 ENST00000236959.13 ENST00000236959.2 ENST00000236959.3 ENST00000236959.4 ENST00000236959.5 ENST00000236959.6 ENST00000236959.7 ENST00000236959.8 ENST00000236959.9 HEL-S-70p NM_004044 V9HWH7 V9HWH7_HUMAN uc002vex.1 uc002vex.2 uc002vex.3 uc002vex.4 uc002vex.5 uc002vex.6 This gene encodes a bifunctional protein that catalyzes the last two steps of the de novo purine biosynthetic pathway. The N-terminal domain has phosphoribosylaminoimidazolecarboxamide formyltransferase activity, and the C-terminal domain has IMP cyclohydrolase activity. A mutation in this gene results in AICA-ribosiduria. [provided by RefSeq, Sep 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.22572.1, SRR1803613.156414.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000236959.14/ ENSP00000236959.9 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5- formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193; Evidence=; Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate; Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145; Evidence=; Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447; Evidence=; Purine metabolism; IMP biosynthesis via de novo pathway; 5- formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino- 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1. Cytoplasm, cytosol Belongs to the PurH family. brainstem development catalytic activity IMP cyclohydrolase activity phosphoribosylaminoimidazolecarboxamide formyltransferase activity cytosol plasma membrane purine nucleotide biosynthetic process 'de novo' IMP biosynthetic process nucleoside metabolic process ribonucleotide metabolic process response to inorganic substance cerebellum development cerebral cortex development animal organ regeneration dihydrofolate metabolic process tetrahydrofolate biosynthetic process cellular response to interleukin-7 uc002vex.1 uc002vex.2 uc002vex.3 uc002vex.4 uc002vex.5 uc002vex.6 
ENST00000236979.2 TNP1 ENST00000236979.2 transition protein 1 (from RefSeq NM_003284.4) ENST00000236979.1 NM_003284 Q4ZG82 Q4ZG82_HUMAN TNP1 hCG_16381 uc002vgk.1 uc002vgk.2 uc002vgk.3 uc002vgk.4 Transition protein-1 is a spermatid-specific product of the haploid genome which replaces histone and is itself replaced in the mature sperm by the protamines (see PRM1, MIM 182880; PRM2, MIM 182890) (Luerssen et al., 1990 [PubMed 2249851]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BU569792.1, BP371302.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000236979.2/ ENSP00000236979.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Chromosome Nucleus Belongs to the nuclear transition protein 1 family. nucleosome nuclear nucleosome male germ cell nucleus DNA binding nucleus spermatogenesis positive regulation of protein processing spermatogenesis, exchange of chromosomal proteins uc002vgk.1 uc002vgk.2 uc002vgk.3 uc002vgk.4 
ENST00000237014.8 TTR ENST00000237014.8 transthyretin (from RefSeq NM_000371.4) ENST00000237014.1 ENST00000237014.2 ENST00000237014.3 ENST00000237014.4 ENST00000237014.5 ENST00000237014.6 ENST00000237014.7 NM_000371 P02766 PALB Q549C7 Q6IB96 Q9UBZ6 Q9UCM9 TTHY_HUMAN uc002kwx.1 uc002kwx.2 uc002kwx.3 uc002kwx.4 uc002kwx.5 uc002kwx.6 This gene encodes one of the three prealbumins, which include alpha-1-antitrypsin, transthyretin and orosomucoid. The encoded protein, transthyretin, is a homo-tetrameric carrier protein, which transports thyroid hormones in the plasma and cerebrospinal fluid. It is also involved in the transport of retinol (vitamin A) in the plasma by associating with retinol-binding protein. The protein may also be involved in other intracellular processes including proteolysis, nerve regeneration, autophagy and glucose homeostasis. Mutations in this gene are associated with amyloid deposition, predominantly affecting peripheral nerves or the heart, while a small percentage of the gene mutations are non-amyloidogenic. The mutations are implicated in the etiology of several diseases, including amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis and carpal tunnel syndrome. [provided by RefSeq, Aug 2017]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BG699033.1, BG562535.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000237014.8/ ENSP00000237014.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules. Interacts with RBP4. P02766; Q15109: AGER; NbExp=2; IntAct=EBI-711909, EBI-1646426; P02766; P05067: APP; NbExp=3; IntAct=EBI-711909, EBI-77613; P02766; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-711909, EBI-821758; P02766; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-711909, EBI-2875816; P02766; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-711909, EBI-14199987; P02766; P18848: ATF4; NbExp=3; IntAct=EBI-711909, EBI-492498; P02766; Q9Y2D1: ATF5; NbExp=3; IntAct=EBI-711909, EBI-492509; P02766; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-711909, EBI-2891281; P02766; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-711909, EBI-741210; P02766; Q8N163: CCAR2; NbExp=3; IntAct=EBI-711909, EBI-355410; P02766; Q01850: CDR2; NbExp=3; IntAct=EBI-711909, EBI-1181367; P02766; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-711909, EBI-11953200; P02766; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-711909, EBI-744045; P02766; Q9Y240: CLEC11A; NbExp=3; IntAct=EBI-711909, EBI-3957044; P02766; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-711909, EBI-25836090; P02766; Q96MW5: COG8; NbExp=3; IntAct=EBI-711909, EBI-720875; P02766; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-711909, EBI-350590; P02766; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-711909, EBI-10213520; P02766; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-711909, EBI-25835236; P02766; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-711909, EBI-396453; P02766; Q7Z602: GPR141; NbExp=3; IntAct=EBI-711909, EBI-21649723; P02766; P68431: H3C12; NbExp=3; IntAct=EBI-711909, EBI-79722; P02766; Q86U28: ISCA2; NbExp=3; IntAct=EBI-711909, EBI-10258659; P02766; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-711909, EBI-12382297; P02766; Q06136: KDSR; NbExp=3; IntAct=EBI-711909, EBI-3909166; P02766; Q12756: KIF1A; NbExp=3; IntAct=EBI-711909, EBI-2679809; P02766; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-711909, EBI-714379; P02766; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-711909, EBI-8487781; P02766; P41218: MNDA; NbExp=3; IntAct=EBI-711909, EBI-2829677; P02766; P25713: MT3; NbExp=3; IntAct=EBI-711909, EBI-8084264; P02766; Q16718: NDUFA5; NbExp=3; IntAct=EBI-711909, EBI-746417; P02766; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-711909, EBI-10172876; P02766; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-711909, EBI-1059321; P02766; Q96FW1: OTUB1; NbExp=4; IntAct=EBI-711909, EBI-1058491; P02766; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-711909, EBI-25830200; P02766; O75781-2: PALM; NbExp=3; IntAct=EBI-711909, EBI-16399860; P02766; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-711909, EBI-2513978; P02766; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-711909, EBI-9090282; P02766; P11908: PRPS2; NbExp=3; IntAct=EBI-711909, EBI-4290895; P02766; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-711909, EBI-743880; P02766; P02753: RBP4; NbExp=4; IntAct=EBI-711909, EBI-2116134; P02766; Q96D59: RNF183; NbExp=3; IntAct=EBI-711909, EBI-743938; P02766; Q9C004: SPRY4; NbExp=3; IntAct=EBI-711909, EBI-354861; P02766; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-711909, EBI-18616594; P02766; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-711909, EBI-723091; P02766; Q8WUA7-2: TBC1D22A; NbExp=3; IntAct=EBI-711909, EBI-21575846; P02766; Q13569: TDG; NbExp=3; IntAct=EBI-711909, EBI-348333; P02766; P21980-2: TGM2; NbExp=3; IntAct=EBI-711909, EBI-25842075; P02766; A0AVI4-2: TMEM129; NbExp=3; IntAct=EBI-711909, EBI-25871541; P02766; P02766: TTR; NbExp=11; IntAct=EBI-711909, EBI-711909; P02766; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-711909, EBI-348496; P02766; O95164: UBL3; NbExp=3; IntAct=EBI-711909, EBI-12876508; P02766; Q8IWV7: UBR1; NbExp=3; IntAct=EBI-711909, EBI-711736; P02766; P45880: VDAC2; NbExp=3; IntAct=EBI-711909, EBI-354022; P02766; P58304: VSX2; NbExp=3; IntAct=EBI-711909, EBI-6427899; P02766; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-711909, EBI-7705033; P02766; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-711909, EBI-1538838; P02766; Q86V28; NbExp=3; IntAct=EBI-711909, EBI-10259496; Secreted. Cytoplasm. Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver. Each monomer has two 4-stranded beta sheets and the shape of a prolate ellipsoid. Antiparallel beta-sheet interactions link monomers into dimers. A short loop from each monomer forms the main dimer-dimer interaction. These two pairs of loops separate the opposed, convex beta-sheets of the dimers to form an internal channel. Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway. Sulfonation of the reactive cysteine Cys-30 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation. Amyloidosis, transthyretin-related (AMYL-TTR) [MIM:105210]: A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor. te=The disease is caused by variants affecting the gene represented in this entry. Hyperthyroxinemia, dystransthyretinemic (DTTRH) [MIM:145680]: A condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities. Note=The disease is caused by variants affecting the gene represented in this entry. Carpal tunnel syndrome 1 (CTS1) [MIM:115430]: A condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. Note=The disease is caused by variants affecting the gene represented in this entry. Tetramer dissociation and partial unfolding leads to the formation of aggregates and amyloid fibrils. Small molecules that occupy at least one of the thyroid hormone binding sites stabilize the tetramer, and thereby stabilize the native state and protect against misfolding and the formation of amyloid fibrils. Two binding sites for thyroxine are located in the channel. Less than 1% of plasma prealbumin molecules are normally involved in thyroxine transport. L-thyroxine binds to the transthyretin by an order of magnitude stronger than does the triiodo-L-thyronine. Thyroxine-binding globulin is the major carrier protein for thyroid hormones in man. About 40% of plasma transthyretin circulates in a tight protein-protein complex with the plasma retinol-binding protein (RBP). The formation of the complex with RBP stabilizes the binding of retinol to RBP and decreases the glomerular filtration and renal catabolism of the relatively small RBP molecule. There is evidence for 2 binding sites for RBP, one possibly being a region that includes Ile-104, located on the outer surface of the transthyretin molecule. Belongs to the transthyretin family. Name=Wikipedia; Note=Transthyretin entry; URL="https://en.wikipedia.org/wiki/Transthyretin"; retinoid metabolic process hormone activity protein binding extracellular region extracellular space cytoplasm purine nucleobase metabolic process signal transduction extracellular matrix organization macromolecular complex azurophil granule lumen hormone binding retinol metabolic process identical protein binding neutrophil degranulation cellular protein metabolic process protein heterodimerization activity extracellular exosome thyroid hormone binding thyroid hormone transport uc002kwx.1 uc002kwx.2 uc002kwx.3 uc002kwx.4 uc002kwx.5 uc002kwx.6 
ENST00000237172.12 FILIP1 ENST00000237172.12 filamin A interacting protein 1, transcript variant 2 (from RefSeq NM_015687.5) B2RMU6 ENST00000237172.1 ENST00000237172.10 ENST00000237172.11 ENST00000237172.2 ENST00000237172.3 ENST00000237172.4 ENST00000237172.5 ENST00000237172.6 ENST00000237172.7 ENST00000237172.8 ENST00000237172.9 FLIP1_HUMAN KIAA1275 NM_015687 Q5VUL6 Q7Z7B0 Q86TC3 Q8N8B9 Q96SK6 Q9NVI8 Q9ULE5 uc003pia.1 uc003pia.2 uc003pia.3 uc003pia.4 uc003pia.5 This gene encodes a filamin A binding protein. The encoded protein promotes the degradation of filamin A and may regulate cortical neuron migration and dendritic spine morphology. Mice lacking a functional copy of this gene exhibit reduced dendritic spine length and altered excitatory signaling. [provided by RefSeq, Oct 2016]. By acting through a filamin-A/F-actin axis, it controls the start of neocortical cell migration from the ventricular zone. May be able to induce the degradation of filamin-A. Interacts with FLNA. Interacts with RHOD (in GTP-bound form). Cytoplasm, cytoskeleton Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=L-FILIP; IsoId=Q7Z7B0-1; Sequence=Displayed; Name=2; IsoId=Q7Z7B0-2; Sequence=VSP_018345; Name=3; Synonyms=S-FILIP; IsoId=Q7Z7B0-3; Sequence=VSP_018344; Moderately expressed in adult heart and brain. Weakly expressed in lung, skeletal muscle, ovary, testis, kidney, and fetal brain, and hardly detectable in liver, pancreas, spleen, and fetal liver. Within brain, moderate expression is found in amygdala and caudate nucleus. Belongs to the FILIP1 family. Sequence=BAA91763.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleolus cytoplasm cytoskeleton plasma membrane actin cytoskeleton uc003pia.1 uc003pia.2 uc003pia.3 uc003pia.4 uc003pia.5 
ENST00000237201.2 SPACA1 ENST00000237201.2 sperm acrosome associated 1 (from RefSeq NM_030960.3) ENST00000237201.1 NM_030960 Q9HBV2 SACA1_HUMAN SAMP32 uc003pmn.1 uc003pmn.2 uc003pmn.3 uc003pmn.4 The correlation of anti-sperm antibodies with cases of unexplained infertility implicates a role for these antibodies in blocking fertilization. Improved diagnosis and treatment of immunologic infertility, as well as identification of proteins for targeted contraception, are dependent on the identification and characterization of relevant sperm antigens. The protein expressed by this gene is recognized by anti-sperm antibodies from infertile males. Furthermore, antibodies generated against the recombinant protein block in vitro fertilization. This protein localizes to the acrosomal membrane of spermatids and mature spermatozoa where it is thought to play a role in acrosomal morphogenesis and in sperm-egg binding and fusion, respectively. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: AF203447.1, BC029488.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968968, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000237201.2/ ENSP00000237201.1 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Plays a role in acrosome expansion and establishment of normal sperm morphology during spermatogenesis (By similarity). Important for male fertility (PubMed:11870081). Q9HBV2; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-17498703, EBI-1754287; Q9HBV2; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-17498703, EBI-3904417; Q9HBV2; P27449: ATP6V0C; NbExp=3; IntAct=EBI-17498703, EBI-721179; Q9HBV2; Q12983: BNIP3; NbExp=3; IntAct=EBI-17498703, EBI-749464; Q9HBV2; P62955: CACNG7; NbExp=3; IntAct=EBI-17498703, EBI-17499011; Q9HBV2; P21854: CD72; NbExp=3; IntAct=EBI-17498703, EBI-307924; Q9HBV2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-17498703, EBI-12256978; Q9HBV2; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-17498703, EBI-12019274; Q9HBV2; P54849: EMP1; NbExp=3; IntAct=EBI-17498703, EBI-4319440; Q9HBV2; P54852: EMP3; NbExp=3; IntAct=EBI-17498703, EBI-3907816; Q9HBV2; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-17498703, EBI-6166686; Q9HBV2; Q8N112: LSMEM2; NbExp=3; IntAct=EBI-17498703, EBI-10264855; Q9HBV2; Q8IZ57: NRSN1; NbExp=3; IntAct=EBI-17498703, EBI-10264528; Q9HBV2; P42857: NSG1; NbExp=3; IntAct=EBI-17498703, EBI-6380741; Q9HBV2; P26678: PLN; NbExp=3; IntAct=EBI-17498703, EBI-692836; Q9HBV2; Q01453: PMP22; NbExp=3; IntAct=EBI-17498703, EBI-2845982; Q9HBV2; Q9NS64: RPRM; NbExp=3; IntAct=EBI-17498703, EBI-1052363; Q9HBV2; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-17498703, EBI-749270; Q9HBV2; A2A2V5: SERTM1; NbExp=3; IntAct=EBI-17498703, EBI-17284533; Q9HBV2; Q13326: SGCG; NbExp=3; IntAct=EBI-17498703, EBI-5357343; Q9HBV2; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-17498703, EBI-10226799; Q9HBV2; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-17498703, EBI-741850; Q9HBV2; Q9C0I4: THSD7B; NbExp=3; IntAct=EBI-17498703, EBI-311394; Q9HBV2; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-17498703, EBI-2844246; Q9HBV2; Q9BQJ4: TMEM47; NbExp=3; IntAct=EBI-17498703, EBI-13370320; Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane ; Single-pass type I membrane protein Note=Primarily found in the equatorial segment of the acrosome (PubMed:11870081). The tyrosine phosphorylated protein localizes to a smaller region within the equatorial segment (By similarity). Also expressed weakly in the principal segment (PubMed:11870081). Testis specific. N-glycosylated. acrosome assembly inner acrosomal membrane acrosomal membrane spermatogenesis membrane integral component of membrane cytoplasmic vesicle uc003pmn.1 uc003pmn.2 uc003pmn.3 uc003pmn.4 
ENST00000237264.9 TBPL1 ENST00000237264.9 TATA-box binding protein like 1, transcript variant 2 (from RefSeq NM_004865.4) A8K8F5 ENST00000237264.1 ENST00000237264.2 ENST00000237264.3 ENST00000237264.4 ENST00000237264.5 ENST00000237264.6 ENST00000237264.7 ENST00000237264.8 NM_004865 O95753 P62380 Q9BWD5 Q9Z2Z0 TBPL1_HUMAN TLF TLP TLP21 TRF2 TRP uc003qel.1 uc003qel.2 uc003qel.3 uc003qel.4 uc003qel.5 This gene encodes a member of the TATA box-binding protein family. TATA box-binding proteins play a critical role in transcription by RNA polymerase II as components of the transcription factor IID (TFIID) complex. The encoded protein does not bind to the TATA box and initiates transcription from TATA-less promoters. This gene plays a critical role in spermatogenesis, and single nucleotide polymorphisms in this gene may be associated with male infertility. Alternatively spliced transcript variants have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 3. [provided by RefSeq, Nov 2011]. Part of a specialized transcription system that mediates the transcription of most ribosomal proteins through the 5'-TCT-3' motif which is a core promoter element at these genes. Seems to also mediate the transcription of NF1. Does not bind the TATA box. Binds TFIIA and TFIIB. P62380; Q92997: DVL3; NbExp=3; IntAct=EBI-716225, EBI-739789; P62380; P28799: GRN; NbExp=3; IntAct=EBI-716225, EBI-747754; P62380; P52655: GTF2A1; NbExp=5; IntAct=EBI-716225, EBI-389518; P62380; Q9Y4Y9: LSM5; NbExp=3; IntAct=EBI-716225, EBI-373007; P62380; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-716225, EBI-396669; P62380; P13805: TNNT1; NbExp=3; IntAct=EBI-716225, EBI-726527; P62380; O76024: WFS1; NbExp=3; IntAct=EBI-716225, EBI-720609; Cytoplasm Nucleus Ubiquitously expressed, with highest levels in the testis and ovary. Belongs to the TBP family. RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding acrosome assembly DNA binding transcription factor activity, sequence-specific DNA binding transcription coactivator activity protein binding nucleus transcription factor complex transcription factor TFIIA complex cytoplasm dTTP biosynthetic process DNA-templated transcription, initiation transcription from RNA polymerase II promoter spermatogenesis spermatid nucleus differentiation transcription factor binding positive regulation of transcription from RNA polymerase II promoter uc003qel.1 uc003qel.2 uc003qel.3 uc003qel.4 uc003qel.5 
ENST00000237275.9 ZC2HC1B ENST00000237275.9 zinc finger C2HC-type containing 1B (from RefSeq NM_001013623.3) B2RUZ7 C6orf94 ENST00000237275.1 ENST00000237275.2 ENST00000237275.3 ENST00000237275.4 ENST00000237275.5 ENST00000237275.6 ENST00000237275.7 ENST00000237275.8 FAM164B NM_001013623 Q5TFG8 Q5TFG9 ZC21B_HUMAN uc010khk.1 uc010khk.2 uc010khk.3 uc010khk.4 uc010khk.5 Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Q5TFG8; Q8WTX7: CASTOR1; NbExp=3; IntAct=EBI-12275374, EBI-10276168; Q5TFG8; Q06546: GABPA; NbExp=3; IntAct=EBI-12275374, EBI-638925; Q5TFG8; O43639: NCK2; NbExp=3; IntAct=EBI-12275374, EBI-713635; Q5TFG8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-12275374, EBI-10271199; Q5TFG8; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-12275374, EBI-10183064; Belongs to the ZC2HC1 family. metal ion binding uc010khk.1 uc010khk.2 uc010khk.3 uc010khk.4 uc010khk.5 
ENST00000237281.5 FBXO30 ENST00000237281.5 F-box protein 30, transcript variant 1 (from RefSeq NM_032145.5) ENST00000237281.1 ENST00000237281.2 ENST00000237281.3 ENST00000237281.4 FBX30 FBX30_HUMAN NM_032145 Q8TB52 Q9BXZ7 uc003qla.1 uc003qla.2 uc003qla.3 uc003qla.4 uc003qla.5 This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class and it is upregulated in nasopharyngeal carcinoma. [provided by RefSeq, Jul 2008]. Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Required for muscle atrophy following denervation. Protein modification; protein ubiquitination. Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with SKP1, CUL1 and RBX1/ROC1 (By similarity). Auto-ubiquitinated. May be neddylated. Neddylation may be required for E3 ligase activity (By similarity). Sequence=AAK30299.1; Type=Erroneous initiation; Evidence=; Sequence=AAK30299.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence=; protein polyubiquitination cytosol zinc ion binding protein ubiquitination post-translational protein modification metal ion binding ubiquitin protein ligase activity uc003qla.1 uc003qla.2 uc003qla.3 uc003qla.4 uc003qla.5 
ENST00000237283.9 ADAT2 ENST00000237283.9 adenosine deaminase tRNA specific 2, transcript variant 1 (from RefSeq NM_182503.3) A6NL12 ADAT2_HUMAN B3KWY3 DEADC1 ENST00000237283.1 ENST00000237283.2 ENST00000237283.3 ENST00000237283.4 ENST00000237283.5 ENST00000237283.6 ENST00000237283.7 ENST00000237283.8 NM_182503 Q7Z327 Q7Z6V5 Q8IY39 uc003qjj.1 uc003qjj.2 uc003qjj.3 uc003qjj.4 uc003qjj.5 Probably participates in deamination of adenosine-34 to inosine in many tRNAs. Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA- COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33; Evidence=; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Q7Z6V5; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-2809203, EBI-741200; Q7Z6V5; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2809203, EBI-744081; Q7Z6V5; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2809203, EBI-358489; Q7Z6V5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2809203, EBI-5235340; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q7Z6V5-1; Sequence=Displayed; Name=2; IsoId=Q7Z6V5-2; Sequence=VSP_025582; Belongs to the cytidine and deoxycytidylate deaminase family. ADAT2 subfamily. Sequence=AAH37955.2; Type=Erroneous initiation; Evidence=; tRNA wobble adenosine to inosine editing catalytic activity protein binding nucleoplasm tRNA modification tRNA processing tRNA-specific adenosine deaminase activity zinc ion binding hydrolase activity metal ion binding tRNA-specific adenosine-34 deaminase activity tRNA-specific adenosine-34 deaminase complex uc003qjj.1 uc003qjj.2 uc003qjj.3 uc003qjj.4 uc003qjj.5 
ENST00000237353.15 PMFBP1 ENST00000237353.15 polyamine modulated factor 1 binding protein 1, transcript variant 1 (from RefSeq NM_031293.3) B3KVI9 ENST00000237353.1 ENST00000237353.10 ENST00000237353.11 ENST00000237353.12 ENST00000237353.13 ENST00000237353.14 ENST00000237353.2 ENST00000237353.3 ENST00000237353.4 ENST00000237353.5 ENST00000237353.6 ENST00000237353.7 ENST00000237353.8 ENST00000237353.9 G3V1Q7 H7BY07 NM_031293 PMFBP_HUMAN Q8NA09 Q8TBY8 Q9BY16 Q9H0H4 uc002fcd.1 uc002fcd.2 uc002fcd.3 uc002fcd.4 uc002fcd.5 Required for normal spermatogenesis (PubMed:1770140, PubMed:30032984, PubMed:30298696). It functions as a scaffold protein that attaches the sperm head-tail connecting piece to the nuclear envelope, thus maintaining sperm head and tail integrity (PubMed:30032984). May also be involved in the general organization of cellular cytoskeleton (By similarity). Cell projection, cilium, flagellum Note=Localized at the sperm head-tail connecting piece (PubMed:30032984, PubMed:30298696). During spermatogenesis, it is first observed in the cytoplasm of round spermatids, it later appears in the implantation fossa region of the sperm nucleus during sperm head elongation and differentiation, and finally it localizes to the head- tail connecting piece (By similarity). Event=Alternative splicing; Named isoforms=4; Name=2; IsoId=Q8TBY8-2; Sequence=Displayed; Name=1; IsoId=Q8TBY8-1; Sequence=VSP_060105, VSP_060108; Name=3; IsoId=Q8TBY8-3; Sequence=VSP_060106; Name=4; IsoId=Q8TBY8-4; Sequence=VSP_060104, VSP_060107; Spermatogenic failure 31 (SPGF31) [MIM:618112]: An autosomal recessive infertility disorder caused by spermatogenesis defects that result in oligozoospermia with a high proportion of acephalic sperm. Note=The disease is caused by variants affecting the gene represented in this entry. Sequence=AAK15456.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; molecular_function cytoplasm cilium spermatogenesis motile cilium cell projection sperm connecting piece uc002fcd.1 uc002fcd.2 uc002fcd.3 uc002fcd.4 uc002fcd.5 
ENST00000237380.12 MED28 ENST00000237380.12 mediator complex subunit 28 (from RefSeq NM_025205.5) EG1 ENST00000237380.1 ENST00000237380.10 ENST00000237380.11 ENST00000237380.2 ENST00000237380.3 ENST00000237380.4 ENST00000237380.5 ENST00000237380.6 ENST00000237380.7 ENST00000237380.8 ENST00000237380.9 FKSG20 MED28_HUMAN NM_025205 Q9BZJ5 Q9H204 uc003gpk.1 uc003gpk.2 uc003gpk.3 Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May be part of a complex containing NF2/merlin that participates in cellular signaling to the actin cytoskeleton downstream of tyrosine kinase signaling pathways. Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Forms a ternary complex with NF2/merlin and GRB2. Binds to actin. Q9H204; Q8NA61: CBY2; NbExp=3; IntAct=EBI-514199, EBI-741724; Q9H204; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-514199, EBI-11524851; Q9H204; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-514199, EBI-21603100; Q9H204; P06241: FYN; NbExp=6; IntAct=EBI-514199, EBI-515315; Q9H204; P62993: GRB2; NbExp=3; IntAct=EBI-514199, EBI-401755; Q9H204; P42858: HTT; NbExp=9; IntAct=EBI-514199, EBI-466029; Q9H204; P06239: LCK; NbExp=4; IntAct=EBI-514199, EBI-1348; Q9H204; Q5TCQ9: MAGI3; NbExp=2; IntAct=EBI-514199, EBI-310506; Q9H204; Q9NVC6: MED17; NbExp=2; IntAct=EBI-514199, EBI-394562; Q9H204; Q15528: MED22; NbExp=2; IntAct=EBI-514199, EBI-394687; Q9H204; Q9NX70: MED29; NbExp=3; IntAct=EBI-514199, EBI-394656; Q9H204; Q96HR3: MED30; NbExp=6; IntAct=EBI-514199, EBI-394659; Q9H204; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-514199, EBI-2801965; Q9H204; Q92597: NDRG1; NbExp=3; IntAct=EBI-514199, EBI-716486; Q9H204; P35240: NF2; NbExp=4; IntAct=EBI-514199, EBI-1014472; Q9H204; P35240-1: NF2; NbExp=2; IntAct=EBI-514199, EBI-1014500; Q9H204; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-514199, EBI-912440; Q9H204; Q9UHX1: PUF60; NbExp=6; IntAct=EBI-514199, EBI-1053259; Q9H204; P12931: SRC; NbExp=3; IntAct=EBI-514199, EBI-621482; Q9H204; P51687: SUOX; NbExp=3; IntAct=EBI-514199, EBI-3921347; Q9H204; Q8WWU5-7: TCP11; NbExp=3; IntAct=EBI-514199, EBI-17721485; Q9H204; P07947: YES1; NbExp=2; IntAct=EBI-514199, EBI-515331; Q9H204; Q9D8C6: Med11; Xeno; NbExp=2; IntAct=EBI-514199, EBI-6260909; Q9H204; Q9CQI9: Med30; Xeno; NbExp=2; IntAct=EBI-514199, EBI-309220; Q9H204; Q9D7W5: Med8; Xeno; NbExp=2; IntAct=EBI-514199, EBI-7990252; Q9H204; P03255; Xeno; NbExp=2; IntAct=EBI-514199, EBI-2603114; Nucleus Cytoplasm Membrane ; Peripheral membrane protein Note=According to PubMed:15467741, it is cytoplasmic and mainly membrane-associated. Widely expressed. Highly expressed in vascular tissues such as placenta, testis and liver. Up-regulated by endothelial cells when exposed to tumor conditional media. Belongs to the Mediator complex subunit 28 family. Sequence=AAK11563.1; Type=Frameshift; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/50131/MED28"; actin binding protein binding nucleus nucleoplasm cytoplasm cytoskeleton membrane mediator complex stem cell population maintenance cortical actin cytoskeleton negative regulation of smooth muscle cell differentiation uc003gpk.1 uc003gpk.2 uc003gpk.3 
ENST00000237455.5 RNF103 ENST00000237455.5 ring finger protein 103, transcript variant 1 (from RefSeq NM_005667.4) A6NFV6 B2RAG4 ENST00000237455.1 ENST00000237455.2 ENST00000237455.3 ENST00000237455.4 NM_005667 O00237 Q53SU6 Q8IVB9 RN103_HUMAN ZFP103 uc002srn.1 uc002srn.2 uc002srn.3 uc002srn.4 uc002srn.5 The protein encoded by this gene contains a RING-H2 finger, a motif known to be involved in protein-protein and protein-DNA interactions. This gene is highly expressed in normal cerebellum, but not in the cerebral cortex. The expression of the rat counterpart in the frontal cortex and hippocampus was shown to be induced by elctroconvulsive treatment (ECT) as well as chronic antidepressant treatment, suggesting that this gene may be a molecular target for ECT and antidepressants. The protein is a ubiquitin ligase that functions in the endoplasmic reticulum-associated degradation pathway. Alternative splicing of this gene results in multiple transcript variants. Read-through transcription also exists between this gene and the downstream CHMP3 (charged multivesicular body protein 3) gene. [provided by RefSeq, Oct 2011]. Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway. Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Protein modification; protein ubiquitination. Interacts with DERL1 and VCP. Endoplasmic reticulum membrane ; Multi-pass membrane protein Highly expressed in the normal cerebellum but not in the cerebral cortex. ubiquitin-protein transferase activity protein binding endoplasmic reticulum endoplasmic reticulum membrane central nervous system development membrane integral component of membrane protein ubiquitination transferase activity ER-associated ubiquitin-dependent protein catabolic process endoplasmic reticulum quality control compartment metal ion binding ubiquitin protein ligase activity endoplasmic reticulum mannose trimming uc002srn.1 uc002srn.2 uc002srn.3 uc002srn.4 uc002srn.5 
ENST00000237500.10 MYL12B ENST00000237500.10 myosin light chain 12B, transcript variant 2 (from RefSeq NM_033546.4) D3DUH6 ENST00000237500.1 ENST00000237500.2 ENST00000237500.3 ENST00000237500.4 ENST00000237500.5 ENST00000237500.6 ENST00000237500.7 ENST00000237500.8 ENST00000237500.9 ML12B_HUMAN MRLC2 MYLC2B NM_033546 O14950 Q13182 Q7Z5Z4 uc002klt.1 uc002klt.2 uc002klt.3 uc002klt.4 uc002klt.5 uc002klt.6 The activity of nonmuscle myosin II (see MYH9; MIM 160775) is regulated by phosphorylation of a regulatory light chain, such as MRLC2. This phosphorylation results in higher MgATPase activity and the assembly of myosin II filaments (Iwasaki et al., 2001 [PubMed 11942626]).[supplied by OMIM, Mar 2008]. Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin heavy chain MYO19. O14950; P60709: ACTB; NbExp=3; IntAct=EBI-1642165, EBI-353944; O14950; P35749: MYH11; NbExp=2; IntAct=EBI-1642165, EBI-1052928; O14950; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-1642165, EBI-12028784; Ubiquitously expressed in various hematopoietic cells. Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. This chain binds calcium. Sequence=AAP73808.1; Type=Frameshift; Evidence=; calcium ion binding protein binding cytosol muscle contraction myosin complex metal ion binding extracellular exosome cell cortex region uc002klt.1 uc002klt.2 uc002klt.3 uc002klt.4 uc002klt.5 uc002klt.6 
ENST00000237530.11 RPN2 ENST00000237530.11 ribophorin II, transcript variant 1 (from RefSeq NM_002951.5) ENST00000237530.1 ENST00000237530.10 ENST00000237530.2 ENST00000237530.3 ENST00000237530.4 ENST00000237530.5 ENST00000237530.6 ENST00000237530.7 ENST00000237530.8 ENST00000237530.9 NM_002951 P04844 Q5JYR6 Q6IBA5 Q96E21 Q9BUQ3 Q9UBE1 RPN2 RPN2_HUMAN uc002xgp.1 uc002xgp.2 uc002xgp.3 uc002xgp.4 uc002xgp.5 This gene encodes a type I integral membrane protein found only in the rough endoplasmic reticulum. The encoded protein is part of an N-oligosaccharyl transferase complex that links high mannose oligosaccharides to asparagine residues found in the Asn-X-Ser/Thr consensus motif of nascent polypeptide chains. This protein is similar in sequence to the yeast oligosaccharyl transferase subunit SWP1. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2008]. Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Protein modification; protein glycosylation. Component of the oligosaccharyltransferase (OST) complex (PubMed:31831667). OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits (PubMed:23606741, PubMed:25135935, PubMed:31831667). STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity). Interacts with DDI2 (PubMed:29290612). Interacts with TMEM35A/NACHO (By similarity). P04844; Q9H5K3: POMK; NbExp=2; IntAct=EBI-719731, EBI-11337900; Endoplasmic reticulum Endoplasmic reticulum membrane; Multi- pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P04844-1; Sequence=Displayed; Name=2; IsoId=P04844-2; Sequence=VSP_043051, VSP_043052; Expressed in all tissues tested. Belongs to the SWP1 family. autophagosome membrane protein binding endoplasmic reticulum endoplasmic reticulum membrane rough endoplasmic reticulum cellular protein modification process protein glycosylation protein N-linked glycosylation aging oligosaccharyltransferase complex membrane integral component of membrane protein N-linked glycosylation via asparagine response to drug ribosome binding dolichyl-diphosphooligosaccharide-protein glycotransferase activity uc002xgp.1 uc002xgp.2 uc002xgp.3 uc002xgp.4 uc002xgp.5 
ENST00000237536.9 MTCL2 ENST00000237536.9 microtubule crosslinking factor 2, transcript variant 1 (from RefSeq NM_080627.4) A6NK10 C20orf117 ENST00000237536.1 ENST00000237536.2 ENST00000237536.3 ENST00000237536.4 ENST00000237536.5 ENST00000237536.6 ENST00000237536.7 ENST00000237536.8 KIAA0889 MTCL2 MTCL2_HUMAN NM_080627 O94964 Q14DB2 Q5JW51 Q6ZTG8 SOGA SOGA1 uc021wcx.1 uc021wcx.2 uc021wcx.3 Microtubule-associated factor that enables integration of the centrosomal and Golgi-associated microtubules on the Golgi membrane, supporting directional migration. Preferentially acts on the perinuclear microtubules accumulated around the Golgi. Associates with the Golgi membrane through the N-terminal coiled-coil region and directly binds microtubules through the C-terminal domain (By similarity). Required for faithful chromosome segregation during mitosis (PubMed:33587225). Regulates autophagy by playing a role in the reduction of glucose production in an adiponectin- and insulin- dependent manner (By similarity). Interacts with CLASP1 and CLASP2 (PubMed:33587225). The C- terminal 25 kDa form occurs as a monomer (By similarity). O94964-4; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-14083835, EBI-746752; O94964-4; O14503: BHLHE40; NbExp=3; IntAct=EBI-14083835, EBI-711810; O94964-4; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-14083835, EBI-2349927; O94964-4; Q3B820: FAM161A; NbExp=3; IntAct=EBI-14083835, EBI-719941; O94964-4; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-14083835, EBI-12094670; O94964-4; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-14083835, EBI-1216080; O94964-4; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-14083835, EBI-10172876; O94964-4; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-14083835, EBI-1105153; O94964-4; Q92753-1: RORB; NbExp=3; IntAct=EBI-14083835, EBI-18560266; O94964-4; O75558: STX11; NbExp=3; IntAct=EBI-14083835, EBI-714135; O94964-4; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-14083835, EBI-1105213; O94964-4; Q99598: TSNAX; NbExp=3; IntAct=EBI-14083835, EBI-742638; O94964-4; P17024: ZNF20; NbExp=3; IntAct=EBI-14083835, EBI-717634; Cytoplasm, cytoskeleton Golgi apparatus membrane Midbody Note=Associates with microtubules during late mitosis and interphase. [C-terminal 80 kDa form]: Secreted Note=Secreted in primary hepatocyte- conditioned media. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=O94964-2; Sequence=Displayed; Name=2; IsoId=O94964-1; Sequence=VSP_062223; Name=3; IsoId=O94964-3; Sequence=VSP_062222, VSP_062225, VSP_062226; Name=4; IsoId=O94964-4; Sequence=VSP_062223, VSP_062224; Up-regulated in the plasma by adiponectin in healthy fasting female. Associates with the Golgi membrane through the N-terminal coiled-coil region and directly binds microtubules through the C- terminal domain. Proteolytically cleaved in primary hepatocytes into a C-terminal 80 kDa form (By similarity). Proteolytically cleaved into a C-terminal SOGA 25 kDa form that is detected in plasma. Phosphorylated during mitosis in a CDK1-dependent manner. Belongs to the MTCL family. Sequence=BAA74912.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; molecular_function extracellular region extracellular space insulin receptor signaling pathway regulation of autophagy negative regulation of gluconeogenesis extracellular exosome uc021wcx.1 uc021wcx.2 uc021wcx.3 
ENST00000237596.7 PKD2 ENST00000237596.7 polycystin 2, transient receptor potential cation channel, transcript variant 2 (from RefSeq NR_156488.2) ENST00000237596.1 ENST00000237596.2 ENST00000237596.3 ENST00000237596.4 ENST00000237596.5 ENST00000237596.6 NR_156488 O60441 PKD2 PKD2_HUMAN Q13563 Q15764 Q2M1Q3 Q2M1Q5 TRPP2 uc003hre.1 uc003hre.2 uc003hre.3 uc003hre.4 uc003hre.5 This gene encodes a member of the polycystin protein family. The encoded protein is a multi-pass membrane protein that functions as a calcium permeable cation channel, and is involved in calcium transport and calcium signaling in renal epithelial cells. This protein interacts with polycystin 1, and they may be partners in a common signaling cascade involved in tubular morphogenesis. Mutations in this gene are associated with autosomal dominant polycystic kidney disease type 2. [provided by RefSeq, Mar 2011]. Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B (PubMed:27214281). Can also form a functional, homotetrameric ion channel (PubMed:29899465). Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:18695040). Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+) (PubMed:11854751, PubMed:15692563, PubMed:27071085, PubMed:27991905). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum (PubMed:11854751, PubMed:20881056). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left- right patterning. Detection of asymmetric nodal flow gives rise to a Ca(2+) signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (By similarity). Channel activity is regulated by phosphorylation (PubMed:16551655, PubMed:20881056, PubMed:26269590). Channel activity is regulated by intracellular Ca(2+) (PubMed:11854751). Component of the heterotetrameric polycystin channel complex with PKD1; the tetramer contains one PKD1 chain and three PKD2 chains (PubMed:20881056, PubMed:19556541, PubMed:27214281, PubMed:30093605). Interaction with PKD1 is required for ciliary localization (By similarity). Homotetramer (PubMed:20881056, PubMed:27768895, PubMed:27991905, PubMed:28092368, PubMed:29899465). Isoform 1 interacts with PKD1 while isoform 3 does not (By similarity). Interacts with PKD1L1. Interacts with CD2AP (PubMed:10913159). Interacts with HAX1 (PubMed:10760273). Interacts with NEK8 (By similarity). Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C (By similarity). Interacts (via C-terminus) with TRPV4 (via C-terminus) (PubMed:18695040). Interacts (via C-terminal acidic region) with PACS1 and PACS2; these interactions retain the protein in the endoplasmic reticulum and prevent trafficking to the cell membrane (PubMed:15692563). Interacts with TMEM33 (By similarity). Q13563; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7813714, EBI-3867333; Q13563; O75031: HSF2BP; NbExp=3; IntAct=EBI-7813714, EBI-7116203; Q13563; Q02363: ID2; NbExp=7; IntAct=EBI-7813714, EBI-713450; Q13563; Q6A162: KRT40; NbExp=3; IntAct=EBI-7813714, EBI-10171697; Q13563; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-7813714, EBI-10171774; Q13563; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-7813714, EBI-11962084; Q13563; P43361: MAGEA8; NbExp=4; IntAct=EBI-7813714, EBI-10182930; Q13563; Q99750: MDFI; NbExp=3; IntAct=EBI-7813714, EBI-724076; Q13563; P98161: PKD1; NbExp=8; IntAct=EBI-7813714, EBI-1752013; Q13563; P98161-1: PKD1; NbExp=4; IntAct=EBI-7813714, EBI-1951183; Q13563; Q13563: PKD2; NbExp=11; IntAct=EBI-7813714, EBI-7813714; Q13563; O15162: PLSCR1; NbExp=3; IntAct=EBI-7813714, EBI-740019; Q13563; P48995: TRPC1; NbExp=12; IntAct=EBI-7813714, EBI-929665; Q13563; P48995-2: TRPC1; NbExp=4; IntAct=EBI-7813714, EBI-9830970; Q13563; O35387: Hax1; Xeno; NbExp=3; IntAct=EBI-7813714, EBI-642449; Q13563; Q91908: itpr1.S; Xeno; NbExp=2; IntAct=EBI-7813714, EBI-9633447; Q13563; Q9QZC1: Trpc3; Xeno; NbExp=3; IntAct=EBI-7813714, EBI-10051366; Q13563; Q9EPK8: Trpv4; Xeno; NbExp=11; IntAct=EBI-7813714, EBI-7091763; Q13563-1; P98161: PKD1; NbExp=5; IntAct=EBI-9837017, EBI-1752013; Q13563-1; P98161-3: PKD1; NbExp=4; IntAct=EBI-9837017, EBI-15930070; Q13563-1; Q13563-1: PKD2; NbExp=12; IntAct=EBI-9837017, EBI-9837017; Q13563-1; O08852: Pkd1; Xeno; NbExp=2; IntAct=EBI-9837017, EBI-6666305; Cell projection, cilium membrane ulti-pass membrane protein doplasmic reticulum membrane ulti-pass membrane protein ll membrane ulti-pass membrane protein solateral cell membrane Cytoplasmic vesicle membrane Golgi apparatus Vesicle Secreted, extracellular exosome Note=PKD2 localization to the plasma and ciliary membranes requires PKD1. PKD1:PKD2 interaction is required to reach the Golgi apparatus form endoplasmic reticulum and then traffic to the cilia (By similarity). Retained in the endoplasmic reticulum by interaction with PACS1 and PACS2 (PubMed:15692563). Detected on kidney tubule basolateral membranes and basal cytoplasmic vesicles (PubMed:10770959). Cell surface and cilium localization requires GANAB (PubMed:27259053). Detected on migrasomes and on extracellular exosomes in urine (PubMed:21406692). Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q13563-1; Sequence=Displayed; Name=2; Synonyms=delta6; IsoId=Q13563-2; Sequence=VSP_042479, VSP_042480; Name=3; Synonyms=delta7; IsoId=Q13563-3; Sequence=VSP_042481; Name=4; Synonyms=delta9; IsoId=Q13563-4; Sequence=VSP_042482, VSP_042483; Name=5; Synonyms=delta12/13; IsoId=Q13563-5; Sequence=VSP_042484; Detected in fetal and adult kidney (PubMed:10770959). Detected at the thick ascending limb of the loop of Henle, at distal tubules, including the distal convoluted tubule and cortical collecting tubules, with weak staining of the collecting duct (PubMed:10770959). Detected on placenta syncytiotrophoblasts (at protein level) (PubMed:26269590). Strongly expressed in ovary, fetal and adult kidney, testis, and small intestine. Not detected in peripheral leukocytes. The C-terminal coiled-coil domain is involved in oligomerization and the interaction with PKD1 (PubMed:18694932, PubMed:19556541). The isolated coiled-coil domain forms a homotrimer in vitro; the homotrimer interacts with a single PKD1 chain (PubMed:19556541). The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro) (PubMed:18694932). Phosphorylated. Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant (PubMed:16551655). PKD- mediated phosphorylation at the C-terminus regulates its function in the release of Ca(2+) stores from the endoplasmic reticulum (PubMed:20881056). PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance (PubMed:26269590). N-glycosylated. The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance. Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328; only one of these two residues is glycosylated at a given time. Polycystic kidney disease 2 with or without polycystic liver disease (PKD2) [MIM:613095]: An autosomal dominant disorder characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occurs in the liver and other organs. It represents approximately 15% of the cases of autosomal dominant polycystic kidney disease. PKD2 is clinically milder than PKD1 but it has a deleterious impact on overall life expectancy. te=The disease is caused by variants affecting the gene represented in this entry. The mechanisms that govern channel opening are complex and still under debate; heterologous expression of PKD2 by itself or together with PKD1 gives rise to very low or undetectable spontaneous ion channel activity, in spite of its presence at the cell membrane. [Isoform 5]: Minor isoform. Belongs to the polycystin family. Name=Functional Glycomics Gateway - Glycan Binding; Note=Polycystin 2 - Not a C-type lectin; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_205"; branching involved in ureteric bud morphogenesis kidney development liver development embryonic placenta development heart looping polycystin complex detection of nodal flow receptor binding voltage-gated ion channel activity voltage-gated calcium channel activity voltage-gated sodium channel activity voltage-gated potassium channel activity cation channel activity calcium channel activity potassium channel activity calcium ion binding protein binding cytoplasm endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus plasma membrane integral component of plasma membrane cell-cell junction cilium ion transport potassium ion transport calcium ion transport cellular calcium ion homeostasis cell cycle arrest positive regulation of cytosolic calcium ion concentration JAK-STAT cascade determination of left/right symmetry heart development cytoskeletal protein binding negative regulation of cell proliferation basal plasma membrane positive regulation of gene expression channel activity outward rectifier potassium channel activity membrane integral component of membrane Wnt signaling pathway basolateral plasma membrane spinal cord development neural tube development voltage-gated cation channel activity lamellipodium cytoplasmic vesicle membrane cytoplasmic vesicle motile cilium positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity cellular response to reactive oxygen species cation channel complex regulation of ion transmembrane transport metanephric part of ureteric bud development sodium ion transmembrane transport aorta development ciliary basal body regulation of cell proliferation identical protein binding protein homodimerization activity actinin binding cytoplasmic sequestering of transcription factor cell projection HLH domain binding ion channel binding cilium organization basal cortex positive regulation of nitric oxide biosynthetic process positive regulation of cyclin-dependent protein serine/threonine kinase activity positive regulation of transcription from RNA polymerase II promoter metal ion binding calcium-induced calcium release activity detection of mechanical stimulus ATPase binding release of sequestered calcium ion into cytosol phosphoprotein binding protein tetramerization protein homotetramerization protein heterotetramerization centrosome duplication muscle alpha-actinin binding alpha-actinin binding ciliary membrane negative regulation of ryanodine-sensitive calcium-release channel activity placenta blood vessel development renal tubule morphogenesis renal artery morphogenesis extracellular exosome calcium ion transmembrane transport positive regulation of cell cycle arrest cellular response to calcium ion cellular response to cAMP integral component of cytoplasmic side of endoplasmic reticulum membrane cellular response to hydrostatic pressure cellular response to osmotic stress cellular response to fluid shear stress integral component of lumenal side of endoplasmic reticulum membrane potassium ion transmembrane transport determination of liver left/right asymmetry metanephric mesenchyme development mesonephric tubule development mesonephric duct development metanephric smooth muscle tissue development metanephric cortex development metanephric ascending thin limb development metanephric cortical collecting duct development metanephric distal tubule development metanephric S-shaped body morphogenesis mitotic spindle regulation of calcium ion import non-motile cilium inorganic cation transmembrane transport cell-cell signaling by wnt negative regulation of G1/S transition of mitotic cell cycle filamentous actin uc003hre.1 uc003hre.2 uc003hre.3 uc003hre.4 uc003hre.5 
ENST00000237612.8 ABCG2 ENST00000237612.8 ATP binding cassette subfamily G member 2 (Junior blood group), transcript variant 1 (from RefSeq NM_004827.3) A0A1W3 A8K1T5 ABCG2_HUMAN ABCP BCRP BCRP1 ENST00000237612.1 ENST00000237612.2 ENST00000237612.3 ENST00000237612.4 ENST00000237612.5 ENST00000237612.6 ENST00000237612.7 MXR NM_004827 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 Q9UNQ0 uc003hrg.1 uc003hrg.2 uc003hrg.3 uc003hrg.4 uc003hrg.5 The membrane-associated protein encoded by this gene is included in the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. Alternatively referred to as a breast cancer resistance protein, this protein functions as a xenobiotic transporter which may play a major role in multi-drug resistance. It likely serves as a cellular defense mechanism in response to mitoxantrone and anthracycline exposure. Significant expression of this protein has been observed in the placenta, which may suggest a potential role for this molecule in placenta tissue. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2012]. Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells (PubMed:11306452, PubMed:12958161, PubMed:19506252, PubMed:20705604, PubMed:28554189, PubMed:30405239, PubMed:31003562). Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme (PubMed:20705604, PubMed:23189181). Also mediates the efflux of sphingosine-1-P from cells (PubMed:20110355). Acts as a urate exporter functioning in both renal and extrarenal urate excretion (PubMed:19506252, PubMed:20368174, PubMed:22132962, PubMed:31003562, PubMed:36749388). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (PubMed:12682043, PubMed:28554189, PubMed:30405239). Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (PubMed:11306452, PubMed:12477054, PubMed:15670731, PubMed:18056989, PubMed:31254042). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity). Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence= Reaction=ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out); Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462; Evidence=; Reaction=ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate; Xref=Rhea:RHEA:61332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144643, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61333; Evidence=; Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952; Evidence=; Reaction=ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3- sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61348, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61349; Evidence=; Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; Evidence=; Reaction=4-methylumbelliferone sulfate(in) + ATP + H2O = 4- methylumbelliferone sulfate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144581, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61369; Evidence=; Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3- benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl- 2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D- glucuronate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144584, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61385; Evidence=; Reaction=4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4- methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144582, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61373; Evidence=; Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3- benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2- methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144583, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61377; Evidence=; Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; Evidence=; Reaction=ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate; Xref=Rhea:RHEA:61356, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:50681, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61357; Evidence=; Reaction=ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57986, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61353; Evidence=; Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58687, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361; Evidence=; Specifically inhibited by the fungal toxin fumitremorgin C and Ko143. Kinetic parameters: KM=16.6 uM for estrone 3-sulfate ; KM=1.23 mM for ATP ; KM=12.9 uM for 4-methylumbelliferone sulfate ; KM=26.9 uM for 6-hydroxy-5,7-dimethyl-2-methylamino-4-(3- pyridylmethyl)benzothiazole sulfate ; KM=8.24 mM for urate ; Vmax=2.34 nmol/min/mg enzyme for estrone 3-sulfate transport ; Vmax=6.96 nmol/min/mg enzyme for urate transport ; Homodimer; disulfide-linked (PubMed:15001581, PubMed:17686774, PubMed:18056989, PubMed:28554189). The minimal functional unit is a homodimer, but the major oligomeric form in plasma membrane is a homotetramer with possibility of higher order oligomerization up to homododecamers (PubMed:15001581). Q9UNQ0; Q9UNQ0: ABCG2; NbExp=5; IntAct=EBI-1569435, EBI-1569435; Q9UNQ0; P22413: ENPP1; NbExp=4; IntAct=EBI-1569435, EBI-3197846; Q9UNQ0; P11309-2: PIM1; NbExp=5; IntAct=EBI-1569435, EBI-1018633; Q9UNQ0; P0CG48: UBC; NbExp=2; IntAct=EBI-1569435, EBI-3390054; Q9UNQ0-1; Q9UNQ0-1: ABCG2; NbExp=3; IntAct=EBI-20717342, EBI-20717342; Cell membrane ulti-pass membrane protein Apical cell membrane ; Multi-pass membrane protein Mitochondrion membrane ; Multi-pass membrane protein Note=Enriched in membrane lipid rafts. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UNQ0-1; Sequence=Displayed; Name=2; IsoId=Q9UNQ0-2; Sequence=VSP_014232, VSP_014233; Highly expressed in placenta (PubMed:9850061). Low expression in small intestine, liver and colon (PubMed:9861027). Expressed in brain (at protein level) (PubMed:12958161). The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. N-glycosylated (PubMed:15807535, PubMed:23189181). Glycosylation- deficient ABCG2 is normally expressed and functional. Phosphorylated. Phosphorylation at Thr-362 by PIM1 is induced by drugs like mitoxantrone and is associated with cells increased drug resistance. It regulates the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. Genetic variations in ABCG2 define the blood group Junior system (JR) [MIM:614490]. Individuals with Jr(a-) blood group lack the Jr(a) antigen on their red blood cells. These individuals may have anti-Jr(a) antibodies in their serum, which can cause transfusion reactions or hemolytic disease of the fetus or newborn. Although the clinical significance of the Jr(a-) blood group has been controversial, severe fatal hemolytic disease of the newborn has been reported. The Jr(a-) phenotype has a higher frequency in individuals of Asian descent, compared to those of European descent. The Jr(a-) phenotype is inherited as an autosomal recessive trait. Genetic variations in ABCG2 influence the variance in serum uric acid concentrations and define the serum uric acid concentration quantitative trait locus 1 (UAQTL1) [MIM:138900]. Excess serum accumulation of uric acid can lead to the development of gout, a common disorder characterized by tissue deposition of monosodium urate crystals as a consequence of hyperuricemia (PubMed:18834626, PubMed:19506252, PubMed:20368174). Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. Was originally proposed to function as a glutathione transporter (PubMed:20332504). However, some evidences suggest it is not the case (PubMed:24312054). Sequence=AF093771; Type=Frameshift; Evidence=; Sequence=AF093772; Type=Frameshift; Evidence=; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/abcg2/"; Name=ABCMdb; Note=Database for mutations in ABC proteins; URL="http://abcm2.hegelab.org/search"; Name=Protein Spotlight; Note=The unwalkable disease - Issue 222 of February 2020; URL="https://web.expasy.org/spotlight/back_issues/222/"; nucleotide binding protein binding ATP binding nucleus mitochondrion plasma membrane cellular iron ion homeostasis xenobiotic-transporting ATPase activity membrane integral component of membrane ATPase activity mitochondrial membrane ATPase activity, coupled to transmembrane movement of substances identical protein binding protein homodimerization activity urate metabolic process transmembrane transport cellular detoxification uc003hrg.1 uc003hrg.2 uc003hrg.3 uc003hrg.4 uc003hrg.5 
ENST00000237642.7 STBD1 ENST00000237642.7 starch binding domain 1 (from RefSeq NM_003943.5) B3KVZ9 ENST00000237642.1 ENST00000237642.2 ENST00000237642.3 ENST00000237642.4 ENST00000237642.5 ENST00000237642.6 GENX-3414 NM_003943 O95210 STBD1 STBD1_HUMAN uc003hka.1 uc003hka.2 uc003hka.3 uc003hka.4 uc003hka.5 Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes. Interacts with the ATG8 family proteins GABARAP and GABARAPL1 (PubMed:20810658, PubMed:21893048). Interacts with several glycogen- associated proteins, such as GYS2 (liver glycogen synthase), GDE (glycogen debranching enzyme), GBE1 (glycogen branching enzyme 1) and EPM2A (Laforin) (PubMed:24837458). O95210; O95166: GABARAP; NbExp=6; IntAct=EBI-2947137, EBI-712001; O95210; Q9H0R8: GABARAPL1; NbExp=8; IntAct=EBI-2947137, EBI-746969; O95210; P60520: GABARAPL2; NbExp=5; IntAct=EBI-2947137, EBI-720116; O95210; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2947137, EBI-749265; O95210; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-2947137, EBI-373144; Preautophagosomal structure membrane ; Single-pass type III membrane protein Endoplasmic reticulum membrane ; Single-pass type III membrane protein Cell membrane, sarcolemma, T-tubule Note=Also detected near the junctional sarcoplasmic reticulum (PubMed:9794794). Concentrates at perinuclear structures (PubMed:21893048). Expressed at high level in skeletal and cardiac muscles. Moderately expressed in liver and placenta. No expression is found in pancreas, kidney or lung. Present in skeletal muscle, heart and placenta (at protein level). The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family protein GABARAPL1. The C-terminal CBM20 domain is required for the interaction with glycogen and glycogen-associated proteins. Ubiquitinated, which leads to proteasomal degradation. protein binding endoplasmic reticulum endoplasmic reticulum membrane cytosol plasma membrane integral component of plasma membrane carbohydrate metabolic process glycogen metabolic process glycogen catabolic process autophagy membrane integral component of membrane enzyme binding carbohydrate binding polysaccharide binding T-tubule pre-autophagosomal structure membrane neutrophil degranulation intracellular transport perinuclear region of cytoplasm glycophagy tertiary granule membrane ficolin-1-rich granule membrane glycogen binding starch binding uc003hka.1 uc003hka.2 uc003hka.3 uc003hka.4 uc003hka.5 
ENST00000237654.9 CCNI ENST00000237654.9 cyclin I, transcript variant 1 (from RefSeq NM_006835.3) B2R6M0 B7Z6X4 CCNI CCNI_HUMAN ENST00000237654.1 ENST00000237654.2 ENST00000237654.3 ENST00000237654.4 ENST00000237654.5 ENST00000237654.6 ENST00000237654.7 ENST00000237654.8 NM_006835 Q14094 uc003hkm.1 uc003hkm.2 uc003hkm.3 uc003hkm.4 uc003hkm.5 uc003hkm.6 The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin shows the highest similarity with cyclin G. The transcript of this gene was found to be expressed constantly during cell cycle progression. [provided by RefSeq, Jan 2017]. Q14094; Q00526: CDK3; NbExp=3; IntAct=EBI-1104653, EBI-1245761; Q14094; Q00535: CDK5; NbExp=4; IntAct=EBI-1104653, EBI-1041567; Q14094; Q00534: CDK6; NbExp=3; IntAct=EBI-1104653, EBI-295663; Q14094; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1104653, EBI-746595; Nucleus membrane Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q14094-1; Sequence=Displayed; Name=2; IsoId=Q14094-2; Sequence=VSP_056682; Highest levels in adult heart, brain and skeletal muscle. Lower levels in adult placenta, lung, kidney and pancreas. Also high levels in fetal brain and lower levels in fetal lung, liver and kidney. Also abundant in testis and thyroid. Expression is independent of the cell cycle in lung fibroblasts. Belongs to the cyclin family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ccni/"; regulation of cyclin-dependent protein serine/threonine kinase activity cyclin-dependent protein kinase holoenzyme complex nucleus cytoplasm protein phosphorylation spermatogenesis cyclin-dependent protein serine/threonine kinase regulator activity protein kinase binding mitotic cell cycle phase transition regulation of cell cycle protein kinase activity uc003hkm.1 uc003hkm.2 uc003hkm.3 uc003hkm.4 uc003hkm.5 uc003hkm.6 
ENST00000237696.10 RARRES1 ENST00000237696.10 retinoic acid receptor responder 1, transcript variant 1 (from RefSeq NM_206963.2) ENST00000237696.1 ENST00000237696.2 ENST00000237696.3 ENST00000237696.4 ENST00000237696.5 ENST00000237696.6 ENST00000237696.7 ENST00000237696.8 ENST00000237696.9 NM_206963 P49788 PEIG1 Q8N1D7 TIG1 TIG1_HUMAN uc003fci.1 uc003fci.2 uc003fci.3 uc003fci.4 uc003fci.5 This gene was identified as a retinoid acid (RA) receptor-responsive gene. It encodes a type 1 membrane protein. The expression of this gene is upregulated by tazarotene as well as by retinoic acid receptors. The expression of this gene is found to be downregulated in prostate cancer, which is caused by the methylation of its promoter and CpG island. Alternatively spliced transcript variant encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]. Inhibitor of the cytoplasmic carboxypeptidase AGBL2, may regulate the alpha-tubulin tyrosination cycle. Interacts with AGBL2, KIF11 and MAPRE1. P49788; P20155: SPINK2; NbExp=5; IntAct=EBI-25504187, EBI-10200479; Membrane ; Single- pass type III membrane protein Secreted Event=Alternative splicing; Named isoforms=2; Name=2; IsoId=P49788-1; Sequence=Displayed; Name=1; IsoId=P49788-2; Sequence=VSP_010697, VSP_010698; Detected in urine (at protein level). By tazarotene and by all the retinoic acid receptors tested. Not N-glycosylated (PubMed:21303978). O-glycosylated; contains chondroitin sulfate (PubMed:27399812, PubMed:36213313). Belongs to the protease inhibitor I47 (latexin) family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42050/RARRES1"; extracellular space metalloendopeptidase inhibitor activity negative regulation of cell proliferation negative regulation of endopeptidase activity membrane integral component of membrane extracellular exosome uc003fci.1 uc003fci.2 uc003fci.3 uc003fci.4 uc003fci.5 
ENST00000237822.8 LDAH ENST00000237822.8 lipid droplet associated hydrolase, transcript variant 1 (from RefSeq NM_021925.4) B7ZA47 B7ZAJ5 C2orf43 D6W530 E7ESN0 ENST00000237822.1 ENST00000237822.2 ENST00000237822.3 ENST00000237822.4 ENST00000237822.5 ENST00000237822.6 ENST00000237822.7 LDAH LDAH_HUMAN NM_021925 Q53T37 Q53T58 Q9H6V9 uc002rec.1 uc002rec.2 uc002rec.3 uc002rec.4 uc002rec.5 uc002rec.6 Probable serine lipid hydrolase associated with lipid droplets. Appears to lack cholesterol esterase activity. Appears to lack triglyceride lipase activity. Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages. Lipid droplet Endoplasmic reticulum Note=Localizes to the endoplasmic reticulum in absence of lipid droplets and translocates to lipid droplets upon lipid storage induction. Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q9H6V9-1; Sequence=Displayed; Name=2; IsoId=Q9H6V9-2; Sequence=VSP_042202; Name=3; IsoId=Q9H6V9-3; Sequence=VSP_054624; Name=4; IsoId=Q9H6V9-4; Sequence=VSP_055283; Present in macrophage-rich areas in atherosclerotic lesionsv(at protein level). Belongs to the AB hydrolase superfamily. LDAH family. The catalytic activity is unsure despite catalytic sites being conserved. endoplasmic reticulum lipid particle lipid metabolic process lipid catabolic process lipase activity hydrolase activity uc002rec.1 uc002rec.2 uc002rec.3 uc002rec.4 uc002rec.5 uc002rec.6 
ENST00000237837.2 FGF23 ENST00000237837.2 fibroblast growth factor 23 (from RefSeq NM_020638.3) ENST00000237837.1 FGF23_HUMAN HYPF NM_020638 Q4V758 Q9GZV9 UNQ3027/PRO9828 uc001qmq.1 uc001qmq.2 This gene encodes a member of the fibroblast growth factor family of proteins, which possess broad mitogenic and cell survival activities and are involved in a variety of biological processes. The product of this gene regulates phosphate homeostasis and transport in the kidney. The full-length, functional protein may be deactivated via cleavage into N-terminal and C-terminal chains. Mutation of this cleavage site causes autosomal dominant hypophosphatemic rickets (ADHR). Mutations in this gene are also associated with hyperphosphatemic familial tumoral calcinosis (HFTC). [provided by RefSeq, Feb 2013]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB047858.1, AF263537.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2159607, SAMEA2162895 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000237837.2/ ENSP00000237837.1 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Regulator of phosphate homeostasis (PubMed:11062477). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (PubMed:11409890). Up-regulates EGR1 expression in the presence of KL (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism (PubMed:15040831). Negatively regulates osteoblast differentiation and matrix mineralization (PubMed:18282132). Interacts with FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:16597617). Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL and heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). Q9GZV9; P11362: FGFR1; NbExp=2; IntAct=EBI-6594125, EBI-1028277; Q9GZV9; O35082: Kl; Xeno; NbExp=5; IntAct=EBI-6594125, EBI-1570828; Secreted Note=Secretion is dependent on O-glycosylation. Expressed in osteogenic cells particularly during phases of active bone remodeling. In adult trabecular bone, expressed in osteocytes and flattened bone-lining cells (inactive osteoblasts). Following secretion this protein is inactivated by cleavage into a N-terminal fragment and a C-terminal fragment. The processing is effected by proprotein convertases. O-glycosylated at Thr-171 and Thr-178 by GALNT3 and glycosylation of Thr-178 requires previous glycosylation at Thr171. Glycosylation is necessary for secretion; it blocks processing by proprotein convertases when the O-glycan is alpha 2,6-sialylated. Competition between proprotein convertase cleavage and block of cleavage by O-glycosylation determines the level of secreted active FGF23. Phosphorylation at Ser-180 mediated by FAM20C slows down glycosylation at Thr-178 notably. Hypophosphatemic rickets, autosomal dominant (ADHR) [MIM:193100]: A disease characterized by isolated renal phosphate wasting, hypophosphatemia, and inappropriately normal 1,25- dihydroxyvitamin D3 (calcitriol) levels. Patients frequently present with bone pain, rickets, and tooth abscesses. te=The disease is caused by variants affecting the gene represented in this entry. Tumoral calcinosis, hyperphosphatemic, familial, 2 (HFTC2) [MIM:617993]: A form of hyperphosphatemic tumoral calcinosis, a rare autosomal recessive metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients have recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the heparin-binding growth factors family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fgf23/"; MAPK cascade fibroblast growth factor receptor binding type 1 fibroblast growth factor receptor binding protein binding extracellular region extracellular space endoplasmic reticulum lumen Golgi lumen phosphate-containing compound metabolic process growth factor activity fibroblast growth factor receptor signaling pathway regulation of phosphate transport positive regulation of vitamin D 24-hydroxylase activity cell differentiation regulation of bone mineralization negative regulation of bone mineralization cellular phosphate ion homeostasis response to magnesium ion vitamin D metabolic process vitamin D catabolic process post-translational protein modification cellular protein metabolic process cellular response to leptin stimulus negative regulation of osteoblast differentiation positive regulation of transcription, DNA-templated negative regulation of hormone secretion positive regulation of protein kinase B signaling phosphate ion homeostasis positive regulation of ERK1 and ERK2 cascade cellular response to vitamin D cellular response to interleukin-6 cellular response to parathyroid hormone stimulus positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway response to sodium phosphate uc001qmq.1 uc001qmq.2 
ENST00000237853.9 ELL2 ENST00000237853.9 elongation factor for RNA polymerase II 2 (from RefSeq NM_012081.6) B4DNK7 ELL2_HUMAN ENST00000237853.1 ENST00000237853.2 ENST00000237853.3 ENST00000237853.4 ENST00000237853.5 ENST00000237853.6 ENST00000237853.7 ENST00000237853.8 NM_012081 O00472 uc003klr.1 uc003klr.2 uc003klr.3 uc003klr.4 uc003klr.5 Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression. Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts with AFF4; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination. Interacts with EAF1 and EAF2. O00472; P07550: ADRB2; NbExp=3; IntAct=EBI-395274, EBI-491169; O00472; Q8TAX5: AFF4; NbExp=3; IntAct=EBI-395274, EBI-745478; O00472; Q92870-2: APBB2; NbExp=3; IntAct=EBI-395274, EBI-21535880; O00472; P54253: ATXN1; NbExp=6; IntAct=EBI-395274, EBI-930964; O00472; P55212: CASP6; NbExp=3; IntAct=EBI-395274, EBI-718729; O00472; P28329-3: CHAT; NbExp=3; IntAct=EBI-395274, EBI-25837549; O00472; Q96JC9: EAF1; NbExp=6; IntAct=EBI-395274, EBI-769261; O00472; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-395274, EBI-742102; O00472; P22607: FGFR3; NbExp=3; IntAct=EBI-395274, EBI-348399; O00472; P21333-2: FLNA; NbExp=3; IntAct=EBI-395274, EBI-9641086; O00472; Q14957: GRIN2C; NbExp=3; IntAct=EBI-395274, EBI-8285963; O00472; P06396: GSN; NbExp=3; IntAct=EBI-395274, EBI-351506; O00472; P30519: HMOX2; NbExp=3; IntAct=EBI-395274, EBI-712096; O00472; P13473-2: LAMP2; NbExp=3; IntAct=EBI-395274, EBI-21591415; O00472; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-395274, EBI-473160; O00472; O43741: PRKAB2; NbExp=3; IntAct=EBI-395274, EBI-1053424; O00472; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-395274, EBI-5280197; O00472; P49810: PSEN2; NbExp=3; IntAct=EBI-395274, EBI-2010251; O00472; P62826: RAN; NbExp=3; IntAct=EBI-395274, EBI-286642; O00472; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-395274, EBI-2623095; O00472; P37840: SNCA; NbExp=3; IntAct=EBI-395274, EBI-985879; O00472; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-395274, EBI-741480; Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O00472-1; Sequence=Displayed; Name=2; IsoId=O00472-2; Sequence=VSP_055476; Ubiquitinated by SIAH1, leading to its degradation by the proteasome. Interaction with AFF4 stabilizes ELL2 and prevents ELL2 ubiquitination. Belongs to the ELL/occludin family. protein binding nucleus nucleoplasm transcription elongation from RNA polymerase II promoter transcription elongation factor complex snRNA transcription from RNA polymerase II promoter uc003klr.1 uc003klr.2 uc003klr.3 uc003klr.4 uc003klr.5 
ENST00000237858.11 GLRX ENST00000237858.11 glutaredoxin, transcript variant 4 (from RefSeq NM_001243659.2) B2R4L2 ENST00000237858.1 ENST00000237858.10 ENST00000237858.2 ENST00000237858.3 ENST00000237858.4 ENST00000237858.5 ENST00000237858.6 ENST00000237858.7 ENST00000237858.8 ENST00000237858.9 GLRX1_HUMAN GRX NM_001243659 P35754 Q3KQS1 Q6ICT1 uc003klo.1 uc003klo.2 uc003klo.3 uc003klo.4 uc003klo.5 uc003klo.6 This gene encodes a member of the glutaredoxin family. The encoded protein is a cytoplasmic enzyme catalyzing the reversible reduction of glutathione-protein mixed disulfides. This enzyme highly contributes to the antioxidant defense system. It is crucial for several signalling pathways by controlling the S-glutathionylation status of signalling mediators. It is involved in beta-amyloid toxicity and Alzheimer's disease. Multiple alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Aug 2011]. Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. P35754; Q9BVG3: TRIM62; NbExp=5; IntAct=EBI-3905236, EBI-6929619; Cytoplasm. Belongs to the glutaredoxin family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/glrx/"; nucleus cytoplasm cytosol electron carrier activity protein disulfide oxidoreductase activity glutathione disulfide oxidoreductase activity nucleobase-containing small molecule interconversion electron transport chain cell redox homeostasis positive regulation of membrane potential protein N-terminus binding oxidation-reduction process extracellular exosome protein deglutathionylation glutathione oxidoreductase activity positive regulation of sodium ion transmembrane transporter activity uc003klo.1 uc003klo.2 uc003klo.3 uc003klo.4 uc003klo.5 uc003klo.6 
ENST00000237889.9 NDUFB3 ENST00000237889.9 NADH:ubiquinone oxidoreductase subunit B3, transcript variant 1 (from RefSeq NM_002491.3) ENST00000237889.1 ENST00000237889.2 ENST00000237889.3 ENST00000237889.4 ENST00000237889.5 ENST00000237889.6 ENST00000237889.7 ENST00000237889.8 NDUB3_HUMAN NM_002491 O43676 Q6IB80 uc002uwx.1 uc002uwx.2 uc002uwx.3 uc002uwx.4 uc002uwx.5 uc002uwx.6 uc002uwx.7 This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is the first enzyme in the electron transport chain of mitochondria. This protein localizes to the inner membrane of the mitochondrion as a single-pass membrane protein. Mutations in this gene contribute to mitochondrial complex 1 deficiency. Alternative splicing results in multiple transcript variants encoding the same protein. Humans have multiple pseudogenes of this gene. [provided by RefSeq, Mar 2012]. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Complex I is composed of 45 different subunits. Mitochondrion inner membrane ; Single-pass membrane protein ; Matrix side Methylation at His residues by METTL9 enhances complex I-mediated mitochondrial respiration. Mitochondrial complex I deficiency, nuclear type 25 (MC1DN25) [MIM:618246]: A form of mitochondrial complex I deficiency, the most common biochemical signature of mitochondrial disorders, a group of highly heterogeneous conditions characterized by defective oxidative phosphorylation, which collectively affects 1 in 5-10000 live births. Clinical disorders have variable severity, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. MC1DN25 transmission pattern is consistent with autosomal recessive inheritance. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the complex I NDUFB3 subunit family. mitochondrion mitochondrial inner membrane mitochondrial respiratory chain complex I mitochondrial electron transport, NADH to ubiquinone NADH dehydrogenase (ubiquinone) activity membrane integral component of membrane electron transport chain mitochondrial respiratory chain complex I assembly oxidation-reduction process respiratory chain uc002uwx.1 uc002uwx.2 uc002uwx.3 uc002uwx.4 uc002uwx.5 uc002uwx.6 uc002uwx.7 
ENST00000238044.8 ECRG4 ENST00000238044.8 ECRG4 augurin precursor (from RefSeq NM_032411.3) AUGN_HUMAN C2orf40 D3DVK2 ECRG4 ENST00000238044.1 ENST00000238044.2 ENST00000238044.3 ENST00000238044.4 ENST00000238044.5 ENST00000238044.6 ENST00000238044.7 NM_032411 Q9H1Z8 UNQ761/PRO1508 uc010fjf.1 uc010fjf.2 uc010fjf.3 uc010fjf.4 uc010fjf.5 Probable hormone that may attenuate cell proliferation and induce senescence of oligodendrocyte and neural precursor cells in the central nervous system (By similarity). ECRG4-induced senescence is characterized by G1 arrest, RB1 dephosphorylation and accelerated CCND1 and CCND3 proteasomal degradation (By similarity). Q9H1Z8; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12208839, EBI-947187; Q9H1Z8; O76024: WFS1; NbExp=3; IntAct=EBI-12208839, EBI-720609; Secreted Cytoplasm Apical cell membrane Expressed in the brain, with expression in the epithelial cell layer of the choroid plexus (at protein level). Belongs to the augurin family. neuropeptide hormone activity extracellular region extracellular space cytoplasm plasma membrane neuropeptide signaling pathway central nervous system development negative regulation of cell proliferation response to wounding membrane apical plasma membrane vasopressin secretion dense core granule anaphase-promoting complex-dependent catabolic process regulation of cell proliferation positive regulation of corticotropin secretion positive regulation of corticotropin-releasing hormone secretion G1 to G0 transition cellular senescence positive regulation of corticosterone secretion uc010fjf.1 uc010fjf.2 uc010fjf.3 uc010fjf.4 uc010fjf.5 
ENST00000238081.8 YWHAQ ENST00000238081.8 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta (from RefSeq NM_006826.4) 1433T_HUMAN D6W4Z5 ENST00000238081.1 ENST00000238081.2 ENST00000238081.3 ENST00000238081.4 ENST00000238081.5 ENST00000238081.6 ENST00000238081.7 NM_006826 P27348 Q567U5 Q5TZU8 Q9UP48 uc002qzx.1 uc002qzx.2 uc002qzx.3 uc002qzx.4 uc002qzx.5 uc002qzx.6 This gene product belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 99% identical to the mouse and rat orthologs. This gene is upregulated in patients with amyotrophic lateral sclerosis. It contains in its 5' UTR a 6 bp tandem repeat sequence which is polymorphic, however, there is no correlation between the repeat number and the disease. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.172956.1, SRR1803611.223311.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238081.8/ ENSP00000238081.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. Homodimer. Interacts with CDK16 (By similarity). Interacts with RGS7 (phosphorylated form) (PubMed:10862767). Interacts with SSH1. Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CDKN1B to the cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241' phosphorylated form of PDPK1. Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). Interacts with SLITRK1 (PubMed:19640509). Interacts with RIPOR2 isoform 2 (PubMed:25588844). Interacts with INAVA; the interaction increases upon PRR (pattern recognition receptor) stimulation and is required for cellular signaling pathway activation and cytokine secretion (PubMed:28436939). Interacts with MARK2, MARK3 and MARK4 (PubMed:16959763). Interacts with MEFV (PubMed:27030597). P27348; Q9P0K1-3: ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567267; P27348; P49407: ARRB1; NbExp=3; IntAct=EBI-359854, EBI-743313; P27348; P32121: ARRB2; NbExp=3; IntAct=EBI-359854, EBI-714559; P27348; P54253: ATXN1; NbExp=5; IntAct=EBI-359854, EBI-930964; P27348; Q92934: BAD; NbExp=6; IntAct=EBI-359854, EBI-700771; P27348; P22681: CBL; NbExp=7; IntAct=EBI-359854, EBI-518228; P27348; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-359854, EBI-11977221; P27348; P30304: CDC25A; NbExp=3; IntAct=EBI-359854, EBI-747671; P27348; O94921: CDK14; NbExp=4; IntAct=EBI-359854, EBI-1043945; P27348; P00533: EGFR; NbExp=7; IntAct=EBI-359854, EBI-297353; P27348; P23945: FSHR; NbExp=4; IntAct=EBI-359854, EBI-848239; P27348; P56524: HDAC4; NbExp=5; IntAct=EBI-359854, EBI-308629; P27348; P28290: ITPRID2; NbExp=4; IntAct=EBI-359854, EBI-722905; P27348; Q14678: KANK1; NbExp=2; IntAct=EBI-359854, EBI-2556221; P27348; Q14678-2: KANK1; NbExp=3; IntAct=EBI-359854, EBI-6173812; P27348; O43896: KIF1C; NbExp=4; IntAct=EBI-359854, EBI-1644048; P27348; Q5S007: LRRK2; NbExp=10; IntAct=EBI-359854, EBI-5323863; P27348; Q99759: MAP3K3; NbExp=4; IntAct=EBI-359854, EBI-307281; P27348; Q6WCQ1: MPRIP; NbExp=4; IntAct=EBI-359854, EBI-1022605; P27348; Q9UBF8: PI4KB; NbExp=3; IntAct=EBI-359854, EBI-1053214; P27348; P04049: RAF1; NbExp=21; IntAct=EBI-359854, EBI-365996; P27348; Q96JI7: SPG11; NbExp=2; IntAct=EBI-359854, EBI-2822128; P27348; Q8WYL5: SSH1; NbExp=2; IntAct=EBI-359854, EBI-1222387; P27348; Q8IWZ5: TRIM42; NbExp=4; IntAct=EBI-359854, EBI-5235829; P27348; P31946: YWHAB; NbExp=5; IntAct=EBI-359854, EBI-359815; P27348; P62258: YWHAE; NbExp=11; IntAct=EBI-359854, EBI-356498; P27348; P61981: YWHAG; NbExp=7; IntAct=EBI-359854, EBI-359832; P27348; P27348: YWHAQ; NbExp=2; IntAct=EBI-359854, EBI-359854; P27348; P67828: CSNK1A1; Xeno; NbExp=2; IntAct=EBI-359854, EBI-7540603; P27348; P61588: Rnd3; Xeno; NbExp=2; IntAct=EBI-359854, EBI-6930266; P27348; B7UM99: tir; Xeno; NbExp=6; IntAct=EBI-359854, EBI-2504426; Cytoplasm. Note=In neurons, axonally transported to the nerve terminals. Abundantly expressed in brain, heart and pancreas, and at lower levels in kidney and placenta. Up-regulated in the lumbar spinal cord from patients with sporadic amyotrophic lateral sclerosis (ALS) compared with controls, with highest levels of expression in individuals with predominant lower motor neuron involvement. Ser-232 is probably phosphorylated by CK1. Belongs to the 14-3-3 family. protein binding cytoplasm mitochondrion cytosol focal adhesion protein targeting small GTPase mediated signal transduction protein C-terminus binding membrane protein domain specific binding substantia nigra development macromolecular complex negative regulation of ion transmembrane transport identical protein binding ion channel binding synapse negative regulation of transcription, DNA-templated protein N-terminus binding membrane organization extracellular exosome 14-3-3 protein binding positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway uc002qzx.1 uc002qzx.2 uc002qzx.3 uc002qzx.4 uc002qzx.5 uc002qzx.6 
ENST00000238112.8 CPSF3 ENST00000238112.8 cleavage and polyadenylation specific factor 3, transcript variant 1 (from RefSeq NM_016207.4) CPSF3_HUMAN CPSF73 ENST00000238112.1 ENST00000238112.2 ENST00000238112.3 ENST00000238112.4 ENST00000238112.5 ENST00000238112.6 ENST00000238112.7 NM_016207 O14769 Q53RS2 Q96F36 Q9UKF6 uc002qzo.1 uc002qzo.2 uc002qzo.3 uc002qzo.4 This gene encodes a member of the metallo-beta-lactamase family. The encoded protein is a 73kDa subunit of the cleavage and polyadenylation specificity factor and functions as an endonuclease that recognizes the pre-mRNA 3'-cleavage site AAUAAA prior to polyadenylation. It also cleaves after the pre-mRNA sequence ACCCA during histone 3'-end pre-mRNA processing. [provided by RefSeq, Oct 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660803.92137.1, SRR1803615.243113.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238112.8/ ENSP00000238112.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as an mRNA 3'-end-processing endonuclease (PubMed:30507380). Also involved in the histone 3'-end pre-mRNA processing (PubMed:30507380). U7 snRNP- dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Required for entering/progressing through S-phase of the cell cycle (PubMed:30507380). Required for the selective processing of microRNAs (miRNAs) during embryonic stem cell differentiation via its interaction with ISY1 (By similarity). Required for the biogenesis of all miRNAs from the pri-miR-17-92 primary transcript except miR-92a (By similarity). Only required for the biogenesis of miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary transcripts, respectively (By similarity). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 2 Zn(2+) ions per subunit. ; Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with TUT1; the interaction is direct and mediates the recruitment of the CPSF complex on the 3'UTR of pre-mRNAs. Interacts with WDR33. Interacts with ZC3H3 (By similarity). Q9UKF6; P42858: HTT; NbExp=3; IntAct=EBI-1044699, EBI-466029; Nucleus Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3. Neurodevelopmental disorder with microcephaly, hypotonia, nystagmus, and seizures (NEDMHS) [MIM:619876]: An autosomal recessive disorder characterized by global developmental delay and impaired intellectual development apparent from infancy. Affected individuals have hypotonia, poor or absent motor skills, feeding difficulties with poor overall growth, microcephaly, mild dysmorphic features, and early- onset seizures. Additional variable features include nystagmus, cortical blindness, and spasticity. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. CPSF3 subfamily. mRNA splicing, via spliceosome RNA binding nuclease activity endonuclease activity endoribonuclease activity protein binding nucleus nucleoplasm mRNA cleavage and polyadenylation specificity factor complex termination of RNA polymerase II transcription mRNA polyadenylation mRNA cleavage mRNA processing mRNA 3'-end processing by stem-loop binding and cleavage mRNA export from nucleus 5'-3' exonuclease activity hydrolase activity mRNA 3'-end processing metal ion binding RNA phosphodiester bond hydrolysis, endonucleolytic uc002qzo.1 uc002qzo.2 uc002qzo.3 uc002qzo.4 
ENST00000238146.9 DDX55 ENST00000238146.9 DEAD-box helicase 55, transcript variant 3 (from RefSeq NR_135105.2) DDX55_HUMAN ENST00000238146.1 ENST00000238146.2 ENST00000238146.3 ENST00000238146.4 ENST00000238146.5 ENST00000238146.6 ENST00000238146.7 ENST00000238146.8 KIAA1595 NR_135105 Q658L6 Q8IYH0 Q8NHQ9 Q9HCH7 uc001ufi.1 uc001ufi.2 uc001ufi.3 uc001ufi.4 uc001ufi.5 This gene encodes a member of protein family containing a characteristic Asp-Glu-Ala-Asp (DEAD) motif. These proteins are putative RNA helicases, and may be involved in a range of nuclear processes including translational initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Multiple alternatively spliced transcript variants have been found for this gene. Pseudogenes have been identified on chromosomes 1 and 12. [provided by RefSeq, Feb 2016]. Probable ATP-binding RNA helicase. Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Q8NHQ9; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-5459844, EBI-741181; Q8NHQ9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-5459844, EBI-10171774; Q8NHQ9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5459844, EBI-79165; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8NHQ9-1; Sequence=Displayed; Name=2; IsoId=Q8NHQ9-2; Sequence=VSP_056155; The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. Belongs to the DEAD box helicase family. DDX55/SPB4 subfamily. nucleotide binding nucleic acid binding RNA binding RNA helicase activity helicase activity protein binding ATP binding nucleus nucleolus cytosol membrane hydrolase activity uc001ufi.1 uc001ufi.2 uc001ufi.3 uc001ufi.4 uc001ufi.5 
ENST00000238156.8 CCDC92 ENST00000238156.8 coiled-coil domain containing 92, transcript variant 1 (from RefSeq NM_025140.3) B3KNQ0 CCD92_HUMAN ENST00000238156.1 ENST00000238156.2 ENST00000238156.3 ENST00000238156.4 ENST00000238156.5 ENST00000238156.6 ENST00000238156.7 NM_025140 Q53HC0 Q9H697 uc001ufw.1 uc001ufw.2 uc001ufw.3 Interferon-stimulated protein that plays a role in innate immunity. Strongly inhibits ebolavirus transcription and replication. Forms a complex with viral RNA-bound nucleocapsid NP and thereby prevents the transport of NP to the cell surface. Interacts with CEP164. (Microbial infection) Interacts with ebolavirus protein NP; this interaction sequesters NP in the cytoplasm. Q53HC0; Q53HC0: CCDC92; NbExp=3; IntAct=EBI-719994, EBI-719994; Q53HC0; Q9UPV0: CEP164; NbExp=5; IntAct=EBI-719994, EBI-3937015; Q53HC0; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-719994, EBI-742887; Q53HC0; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-719994, EBI-11988027; Q53HC0; Q14192: FHL2; NbExp=10; IntAct=EBI-719994, EBI-701903; Q53HC0; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-719994, EBI-10175039; Q53HC0; P14373: TRIM27; NbExp=3; IntAct=EBI-719994, EBI-719493; Q53HC0; Q8N7C3: TRIML2; NbExp=6; IntAct=EBI-719994, EBI-11059915; Q53HC0; P14079: tax; Xeno; NbExp=3; IntAct=EBI-719994, EBI-9675698; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q53HC0-1; Sequence=Displayed; Name=2; IsoId=Q53HC0-2; Sequence=VSP_056906; Up to threefold after interferon treatment. Phosphorylated at Ser-209 by TTBK2. It is uncertain whether Met-1 or Met-18 is the initiator. Sequence=BAD96381.1; Type=Erroneous initiation; Evidence=; protein binding nucleoplasm cytoplasm centrosome centriole cytoskeleton intracellular membrane-bounded organelle uc001ufw.1 uc001ufw.2 uc001ufw.3 
ENST00000238256.8 FKBP15 ENST00000238256.8 FKBP prolyl isomerase family member 15 (from RefSeq NM_015258.2) ENST00000238256.1 ENST00000238256.2 ENST00000238256.3 ENST00000238256.4 ENST00000238256.5 ENST00000238256.6 ENST00000238256.7 FKB15_HUMAN KIAA0674 NM_015258 Q05DK8 Q5T1M2 Q5T1M5 Q6DD85 Q9Y4D0 uc004bgs.1 uc004bgs.2 uc004bgs.3 uc004bgs.4 May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. Interacts with WIP and actin (PubMed:19121306). Interacts with TBC1D23 (PubMed:29084197). Q5T1M5; Q9QZ88: Vps29; Xeno; NbExp=7; IntAct=EBI-5235934, EBI-8334188; Q5T1M5; Q9EQH3: Vps35; Xeno; NbExp=3; IntAct=EBI-5235934, EBI-775825; Cytoplasm Cell projection, axon Early endosome Note=Present in axons and neuronal growth cones. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q5T1M5-1; Sequence=Displayed; Name=2; IsoId=Q5T1M5-2; Sequence=VSP_027758; Name=3; IsoId=Q5T1M5-3; Sequence=VSP_027756, VSP_027757; The PPIase FKBP-type domain seems to be inactive both for FK506-binding and enzymatic activity. The central coiled-coil region is responsible for association with early endosomes. Belongs to the FKBP-type PPIase family. Sequence=AAH09609.1; Type=Erroneous initiation; Evidence=; Sequence=BAA31649.1; Type=Erroneous initiation; Evidence=; protein peptidyl-prolyl isomerization peptidyl-prolyl cis-trans isomerase activity actin binding protein binding cytoplasm endosome early endosome endocytosis negative regulation of phosphatase activity membrane axon growth cone cell projection actin filament uc004bgs.1 uc004bgs.2 uc004bgs.3 uc004bgs.4 
ENST00000238497.10 VPS4B ENST00000238497.10 vacuolar protein sorting 4 homolog B (from RefSeq NM_004869.4) ENST00000238497.1 ENST00000238497.2 ENST00000238497.3 ENST00000238497.4 ENST00000238497.5 ENST00000238497.6 ENST00000238497.7 ENST00000238497.8 ENST00000238497.9 MIG1 NM_004869 O75351 Q69HW4 Q9GZS7 SKD1 VPS42 VPS4B VPS4B_HUMAN uc002lix.1 uc002lix.2 uc002lix.3 uc002lix.4 uc002lix.5 The protein encoded by this gene is a member of the AAA protein family (ATPases associated with diverse cellular activities), and is the homolog of the yeast Vps4 protein. In humans, two paralogs of the yeast protein have been identified. The former share a high degree of aa sequence similarity with each other, and also with yeast Vps4 and mouse Skd1 proteins. Mouse Skd1 (suppressor of K+ transport defect 1) has been shown to be a yeast Vps4 ortholog. Functional studies indicate that both human paralogs associate with the endosomal compartments, and are involved in intracellular protein trafficking, similar to Vps4 protein in yeast. The gene encoding this paralog has been mapped to chromosome 18; the gene for the other resides on chromosome 16. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF195514.1, SRR1660803.10147.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238497.10/ ENSP00000238497.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their ATP-dependent disassembly, possibly in combination with membrane fission (PubMed:18687924). Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). (Microbial infection) In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence=; Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT- III substrates are translocated in an ATP-dependent manner. In vitro, associates on the inside of a helical tubular structure formed by a CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP4B and CHMP6. Interacts with VPS4A; the interaction suggests a heteromeric assembly with VPS4A. Interacts with VTA1. O75351; P54253: ATXN1; NbExp=3; IntAct=EBI-2514459, EBI-930964; O75351; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-2514459, EBI-1057156; O75351; Q9UQN3-1: CHMP2B; NbExp=2; IntAct=EBI-2514459, EBI-15663586; O75351; Q9NZZ3: CHMP5; NbExp=6; IntAct=EBI-2514459, EBI-751303; O75351; P42858: HTT; NbExp=3; IntAct=EBI-2514459, EBI-466029; O75351; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-2514459, EBI-743591; O75351; Q96K21: ZFYVE19; NbExp=7; IntAct=EBI-2514459, EBI-6448240; O75351; Q96K21-3: ZFYVE19; NbExp=3; IntAct=EBI-2514459, EBI-10187928; Late endosome membrane ; Peripheral membrane protein Note=Membrane-associated in the prevacuolar endosomal compartment. Localized in HIV-1 particles purified from acutely infected cells. Ubiquitously expressed. The MIT domain serves as an adapter for ESCRT-III proteins. It forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT interacting motif) helices along the groove between MIT helices 2 and 3 present in a subset of ESCRT-III proteins thus establishing the canonical MIM-MIT interaction. In an extended conformation along the groove between helices 1 and 3, also binds to a type-2 MIT interacting motif (MIM2). Belongs to the AAA ATPase family. nucleotide binding spindle pole protein binding ATP binding nucleus cytoplasm endosome centrosome cytosol potassium ion transport nucleus organization endosome organization vacuole organization cell cycle mitotic metaphase plate congression protein C-terminus binding endosome membrane regulation of centrosome duplication positive regulation of G2/M transition of mitotic cell cycle protein transport membrane endosomal transport macroautophagy hydrolase activity ATPase activity viral life cycle viral release from host cell cholesterol transport late endosome membrane endosome to lysosome transport via multivesicular body sorting pathway response to lipid multivesicular body assembly viral budding via host ESCRT complex ATPase activity, coupled identical protein binding protein homodimerization activity ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway positive regulation of viral process regulation of viral process protein depolymerization cell division negative regulation of cell death late endosomal microautophagy extracellular exosome Flemming body ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway regulation of mitotic spindle assembly positive regulation of viral release from host cell negative regulation of exosomal secretion positive regulation of exosomal secretion positive regulation of centriole elongation positive regulation of viral life cycle ESCRT III complex disassembly uc002lix.1 uc002lix.2 uc002lix.3 uc002lix.4 uc002lix.5 
ENST00000238508.8 SERPINB10 ENST00000238508.8 serpin family B member 10 (from RefSeq NM_005024.3) ENST00000238508.1 ENST00000238508.2 ENST00000238508.3 ENST00000238508.4 ENST00000238508.5 ENST00000238508.6 ENST00000238508.7 NM_005024 P48595 PI10 Q4VAX4 Q4VAX7 SPB10_HUMAN uc010xev.1 uc010xev.2 uc010xev.3 uc010xev.4 This gene is a member of the serpin peptidase inhibitor, clade B family and is found in a cluster of other similar genes on chromosome 18. The protein encoded by this gene appears to help control the regulation of protease functions during hematopoiesis. Variations in this gene may increase the risk of prostate cancer. [provided by RefSeq, Dec 2015]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163655.417906.1, SRR1163658.514721.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2149004, SAMEA2154529 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238508.8/ ENSP00000238508.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. May regulate protease activities in the cytoplasm and in the nucleus. Nucleus. Cytoplasm. Note=Mostly found in the nucleus. Expressed specifically in myeloid cells and the bone marrow. Belongs to the serpin family. Ov-serpin subfamily. serine-type endopeptidase inhibitor activity extracellular space nucleus cytoplasm plasma membrane negative regulation of peptidase activity negative regulation of endopeptidase activity peptidase inhibitor activity secretory granule membrane neutrophil degranulation ficolin-1-rich granule membrane uc010xev.1 uc010xev.2 uc010xev.3 uc010xev.4 
ENST00000238558.5 GSC ENST00000238558.5 goosecoid homeobox (from RefSeq NM_173849.3) ENST00000238558.1 ENST00000238558.2 ENST00000238558.3 ENST00000238558.4 GSC_HUMAN NM_173849 P56915 Q86YR1 uc001ydu.1 uc001ydu.2 uc001ydu.3 uc001ydu.4 uc001ydu.5 This gene encodes a member of the bicoid subfamily of the paired (PRD) homeobox family of proteins. The encoded protein acts as a transcription factor and may be autoregulatory. A similar protein in mice plays a role in craniofacial and rib cage development during embryogenesis. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AY177407.1, BC063580.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Regulates chordin (CHRD). May play a role in spatial programing within discrete embryonic fields or lineage compartments during organogenesis. In concert with NKX3-2, plays a role in defining the structural components of the middle ear; required for the development of the entire tympanic ring (By similarity). Probably involved in the regulatory networks that define neural crest cell fate specification and determine mesoderm cell lineages in mammals. Nucleus. Short stature, auditory canal atresia, mandibular hypoplasia, skeletal abnormalities (SAMS) [MIM:602471]: An autosomal recessive developmental disorder with features of a first and second branchial arch syndrome, and with unique rhizomelic skeletal anomalies. Craniofacial abnormalities can lead to conductive hearing loss, respiratory insufficiency, and feeding difficulties. Skeletal features include bilateral humeral hypoplasia, humeroscapular synostosis, pelvic abnormalities, and proximal defects of the femora. Affected individuals may also have some features of a neurocristopathy or abnormal mesoderm development, such as urogenital anomalies, that are distinct from other branchial arch syndromes. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the paired homeobox family. Bicoid subfamily. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding RNA polymerase II transcription factor binding RNA polymerase II repressing transcription factor binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding nucleus transcription factor complex regulation of transcription, DNA-templated multicellular organism development gastrulation anatomical structure morphogenesis neural crest cell fate specification nuclear body dorsal/ventral neural tube patterning signal transduction involved in regulation of gene expression negative regulation of Wnt signaling pathway forebrain development middle ear morphogenesis sequence-specific DNA binding ear development muscle organ morphogenesis embryonic skeletal system morphogenesis uc001ydu.1 uc001ydu.2 uc001ydu.3 uc001ydu.4 uc001ydu.5 
ENST00000238561.10 ADCK1 ENST00000238561.10 aarF domain containing kinase 1, transcript variant 8 (from RefSeq NR_158989.2) ADCK1 ADCK1_HUMAN B3KUD5 ENST00000238561.1 ENST00000238561.2 ENST00000238561.3 ENST00000238561.4 ENST00000238561.5 ENST00000238561.6 ENST00000238561.7 ENST00000238561.8 ENST00000238561.9 NR_158989 Q6PD65 Q86TW2 Q9UIE6 uc001xui.1 uc001xui.2 uc001xui.3 uc001xui.4 Appears to be essential for maintaining mitochondrial cristae formation and mitochondrial function by acting via YME1L1 in a kinase- independent manner to regulate essential mitochondrial structural proteins OPA1 and IMMT (PubMed:31125351). The action of this enzyme is not yet clear (Probable). It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr) (Probable). Mitochondrion Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q86TW2-1; Sequence=Displayed; Name=2; IsoId=Q86TW2-2; Sequence=VSP_020885; Name=3; IsoId=Q86TW2-3; Sequence=VSP_046794; Belongs to the protein kinase superfamily. ADCK protein kinase family. Sequence=CAD62620.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; Sequence=CAD62620.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence=; nucleotide binding protein serine/threonine kinase activity ATP binding extracellular region protein phosphorylation kinase activity phosphorylation transferase activity uc001xui.1 uc001xui.2 uc001xui.3 uc001xui.4 
ENST00000238609.4 IFI27L2 ENST00000238609.4 interferon alpha inducible protein 27 like 2 (from RefSeq NM_032036.3) ENST00000238609.1 ENST00000238609.2 ENST00000238609.3 FAM14A I27L2_HUMAN IFI27L2 NM_032036 Q8TBD7 Q9H2X8 Q9NYL0 TLH29 uc001ycq.1 uc001ycq.2 uc001ycq.3 uc001ycq.4 uc001ycq.5 Plays a role in the apoptotic process and has a pro-apoptotic activity. Mitochondrion membrane ; Multi-pass membrane protein Not up-regulated by type-I interferon. Belongs to the IFI6/IFI27 family. Sequence=AAF65760.1; Type=Frameshift; Evidence=; mitochondrion apoptotic process membrane integral component of membrane mitochondrial membrane uc001ycq.1 uc001ycq.2 uc001ycq.3 uc001ycq.4 uc001ycq.5 
ENST00000238616.10 NEK9 ENST00000238616.10 NIMA related kinase 9, transcript variant 2 (from RefSeq NM_033116.6) ENST00000238616.1 ENST00000238616.2 ENST00000238616.3 ENST00000238616.4 ENST00000238616.5 ENST00000238616.6 ENST00000238616.7 ENST00000238616.8 ENST00000238616.9 KIAA1995 NEK8 NEK9 NEK9_HUMAN NERCC NM_033116 Q52LK6 Q8NCN0 Q8TCY4 Q8TD19 Q9UPI4 Q9Y6S4 Q9Y6S5 Q9Y6S6 uc001xrl.1 uc001xrl.2 uc001xrl.3 uc001xrl.4 uc001xrl.5 This gene encodes a member of the NimA (never in mitosis A) family of serine/threonine protein kinases. The encoded protein is activated in mitosis and, in turn, activates other family members during mitosis. This protein also mediates cellular processes that are essential for interphase progression. [provided by RefSeq, Jul 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AB082526.1, SRR1803615.156200.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238616.10/ ENSP00000238616.5 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation (PubMed:12101123, PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2 (PubMed:11864968). Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues (PubMed:11864968). Important for G1/S transition and S phase progression (PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (PubMed:12840024, PubMed:14660563, PubMed:19941817, PubMed:26522158). Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence=; Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence= PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Activated during mitosis by intramolecular autophosphorylation (PubMed:11864968). Activity and autophosphorylation is activated by manganese >> magnesium ions (PubMed:11864968). Sensitive to increasing concentration of detergents (PubMed:11864968). It is not cell-cycle regulated but activity is higher in G0-arrested cells (PubMed:11864968). Homodimer; homodimerization is required to activate NEK7 (PubMed:26522158, PubMed:23482567). Binds to Ran GTPase (PubMed:12101123). Has a greater affinity for Ran-GDP over Ran-GTP (PubMed:12101123). Interacts with SSRP1 and SUPT16H, the 2 subunits of the FACT complex (PubMed:14660563). Interacts with DYNLL1; phosphorylation at Ser-944 strongly reduces DYNLL1 binding (PubMed:23482567). Q8TD19; P63167: DYNLL1; NbExp=4; IntAct=EBI-1044009, EBI-349105; Q8TD19; O95166: GABARAP; NbExp=5; IntAct=EBI-1044009, EBI-712001; Q8TD19; Q9H0R8: GABARAPL1; NbExp=6; IntAct=EBI-1044009, EBI-746969; Q8TD19; P60520: GABARAPL2; NbExp=7; IntAct=EBI-1044009, EBI-720116; Q8TD19; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1044009, EBI-352572; Q8TD19; Q9H492: MAP1LC3A; NbExp=2; IntAct=EBI-1044009, EBI-720768; Q8TD19; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-1044009, EBI-373144; Q8TD19; Q9BXW4: MAP1LC3C; NbExp=2; IntAct=EBI-1044009, EBI-2603996; Q8TD19; P53350: PLK1; NbExp=5; IntAct=EBI-1044009, EBI-476768; Q8TD19; P62258: YWHAE; NbExp=2; IntAct=EBI-1044009, EBI-356498; Cytoplasm Nucleus Most abundant in heart, liver, kidney and testis. Also expressed in smooth muscle cells and fibroblasts. Expression varied mildly across the cell cycle, with highest expression observed in G1 and stationary-phase cells. Dimerizes through its coiled-coil domain. Autophosphorylated on serine and threonine residues (PubMed:27153399). When complexed with FACT, exhibits markedly elevated phosphorylation on Thr-210. During mitosis, not phosphorylated on Thr- 210. Phosphorylated by CDK1 in vitro (PubMed:14660563). Lethal congenital contracture syndrome 10 (LCCS10) [MIM:617022]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non- progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. Note=The disease is caused by variants affecting the gene represented in this entry. Nevus comedonicus (NC) [MIM:617025]: A rare type of epidermal nevus characterized by closely arranged, dilated, plugged follicular ostia in a honeycomb pattern. The plugged ostia contain lamellated keratinaceous material, and their appearance resembles black dots. NC may be non-pyogenic with an acne-like appearance or associated with the formation of cysts, papules, pustules, and abscesses. Most commonly it affects the face and neck area and, by exception, other anatomical regions, including genital area, palms, and soles. NC lesions might present with various patterns of distribution: unilateral, bilateral, linear, interrupted, segmental, or blaschkoid. Note=The disease is caused by variants affecting the gene represented in this entry. Arthrogryposis, Perthes disease, and upward gaze palsy (APUG) [MIM:614262]: An autosomal recessive, syndromic form of arthrogryposis, a disease characterized by persistent joints flexure or contracture. APUG patients manifest an unusual combination of arthrogryposis, upward gaze palsy, and avascular necrosis of the hip (Perthes disease). Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily. Sequence=AAD31936.1; Type=Erroneous gene model prediction; Evidence=; Sequence=BAC02704.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding nucleus cytoplasm cytosol protein phosphorylation cell cycle mitotic nuclear envelope disassembly kinase activity phosphorylation transferase activity protein kinase binding metal ion binding cell division centrosome uc001xrl.1 uc001xrl.2 uc001xrl.3 uc001xrl.4 uc001xrl.5 
ENST00000238618.8 ACYP1 ENST00000238618.8 acylphosphatase 1, transcript variant 1 (from RefSeq NM_001107.5) A6NDV8 ACYP1_HUMAN ACYPE B2R590 ENST00000238618.1 ENST00000238618.2 ENST00000238618.3 ENST00000238618.4 ENST00000238618.5 ENST00000238618.6 ENST00000238618.7 NM_001107 P07311 uc001xrg.1 uc001xrg.2 uc001xrg.3 uc001xrg.4 uc001xrg.5 This gene is a member of the acylphosphatase family. The encoded protein is a small cytosolic enzyme that catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates. Two isoenzymes have been isolated and described based on their tissue localization: erythrocyte (common) type acylphosphatase encoded by this gene, and muscle type acylphosphatase. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2014]. Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate; Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7; Evidence=; Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P07311-1; Sequence=Displayed; Name=2; IsoId=P07311-2; Sequence=VSP_045688; Organ-common type isozyme is found in many different tissues. Belongs to the acylphosphatase family. acylphosphatase activity phosphate-containing compound metabolic process hydrolase activity uc001xrg.1 uc001xrg.2 uc001xrg.3 uc001xrg.4 uc001xrg.5 
ENST00000238647.5 IRF2BPL ENST00000238647.5 interferon regulatory factor 2 binding protein like (from RefSeq NM_024496.4) C14orf4 EAP1 ENST00000238647.1 ENST00000238647.2 ENST00000238647.3 ENST00000238647.4 I2BPL_HUMAN KIAA1865 My039 NM_024496 Q8NDQ2 Q96JG2 Q9H1B7 Q9H3I7 uc001xsy.1 uc001xsy.2 uc001xsy.3 uc001xsy.4 uc001xsy.5 This gene encodes a transcription factor that may play a role in regulating female reproductive function. [provided by RefSeq, Jun 2012]. ##Evidence-Data-START## Transcript is intronless :: BC108292.1, SRR7346977.1572721.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238647.5/ ENSP00000238647.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Probable E3 ubiquitin protein ligase involved in the proteasome-mediated ubiquitin-dependent degradation of target proteins (PubMed:29374064). Through the degradation of CTNNB1, functions downstream of FOXF2 to negatively regulate the Wnt signaling pathway (PubMed:29374064). Probably plays a role in the development of the central nervous system and in neuronal maintenance (Probable). Also acts as a transcriptional regulator of genes controlling female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity). Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence=; Protein modification; protein ubiquitination. Interacts with CTNNB1. Nucleus Highly expressed in the heart, moderately in skeletal muscle and pancreas, and weakly in brain, kidney, liver, testis, thyroid gland and lymphocytes. The poly-Gln region is polymorphic; the most frequent allele contained 24 Gln. Stretches of 20-31 Gln are observed in healthy individuals. Neurodevelopmental disorder with regression, abnormal movements, loss of speech, and seizures (NEDAMSS) [MIM:618088]: An autosomal dominant disorder characterized by global developmental delay or neurodevelopmental regression, hypotonia, progressive ataxia, intellectual disability, seizures, and abnormal movements. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the IRF2BP family. Sequence=BAB47494.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence=; negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding molecular_function protein binding extracellular space nucleus nucleoplasm nervous system development protein ubiquitination transferase activity positive regulation of transcription from RNA polymerase II promoter development of secondary female sexual characteristics metal ion binding ubiquitin protein ligase activity uc001xsy.1 uc001xsy.2 uc001xsy.3 uc001xsy.4 uc001xsy.5 
ENST00000238651.10 ACOT2 ENST00000238651.10 acyl-CoA thioesterase 2, transcript variant 1 (from RefSeq NM_006821.6) ACOT2_HUMAN ENST00000238651.1 ENST00000238651.2 ENST00000238651.3 ENST00000238651.4 ENST00000238651.5 ENST00000238651.6 ENST00000238651.7 ENST00000238651.8 ENST00000238651.9 NM_006821 P49753 PTE2 PTE2A Q3I5F8 Q53EK4 Q9NUX4 uc001xon.1 uc001xon.2 uc001xon.3 uc001xon.4 uc001xon.5 uc001xon.6 uc001xon.7 This gene encodes a member of the acyl-CoA thioesterase protein family, and is one of four acyl-CoA hydrolase genes located in a cluster on chromosome 14. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2012]. Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:16940157, PubMed:10944470). Displays higher activity toward long chain acyl CoAs (C14-C20) (PubMed:16940157, PubMed:10944470). The enzyme is involved in enhancing the hepatic fatty acid oxidation in mitochondria (By similarity). Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence=; Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence=; Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence=; Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence=; Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence=; Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence=; Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence=; Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence=; Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence=; Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence=; Kinetic parameters: KM=40.3 uM for C10-acyl-CoA ; KM=8.9 uM for C12-acyl-CoA ; KM=1.6 uM for C14-acyl-CoA ; KM=2.0 uM for C16-acyl-CoA ; KM=2.8 uM for C18-acyl-CoA ; KM=4.8 uM for C20-acyl-CoA ; KM=4.5 uM for C16:1-acyl-CoA ; KM=6.1 uM for C18:1-acyl-CoA ; KM=4.3 uM for C18:1-trans-acyl-CoA ; Vmax=212 nmol/min/mg enzyme with C10-acyl-CoA as substrate ; Vmax=681 nmol/min/mg enzyme with C12-acyl-CoA as substrate ; Vmax=766 nmol/min/mg enzyme with C14-acyl-CoA as substrate ; Vmax=656 nmol/min/mg enzyme with C16-acyl-CoA as substrate ; Vmax=488 nmol/min/mg enzyme with C18-acyl-CoA as substrate ; Vmax=408 nmol/min/mg enzyme with C20-acyl-CoA as substrate ; Vmax=661 nmol/min/mg enzyme with C16:1-acyl-CoA as substrate ; Vmax=304 nmol/min/mg enzyme with C18:1-acyl-CoA as substrate ; Vmax=418 nmol/min/mg enzyme with C18:1-trans-acyl-CoA as substrate ; Lipid metabolism; fatty acid metabolism. Monomer. P49753; Q9NZ94-2: NLGN3; NbExp=2; IntAct=EBI-1052865, EBI-16423037; Mitochondrion Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49753-1; Sequence=Displayed; Name=2; IsoId=P49753-2; Sequence=VSP_012225, VSP_012226; Strongest expression in heart, liver, muscle and kidney. Weak in placenta and pancreas. Belongs to the C/M/P thioester hydrolase family. Was originally (PubMed:10944470) thought to be peroxisomal but was later shown (PubMed:16940157) to be mitochondrial. Sequence=AAC42007.1; Type=Frameshift; Evidence=; very long-chain fatty acid metabolic process long-chain fatty acid metabolic process protein binding mitochondrion mitochondrial matrix peroxisomal matrix cytosol protein targeting to peroxisome lipid metabolic process fatty acid metabolic process acyl-CoA metabolic process palmitoyl-CoA hydrolase activity hydrolase activity thiolester hydrolase activity acyl-CoA hydrolase activity carboxylic ester hydrolase activity uc001xon.1 uc001xon.2 uc001xon.3 uc001xon.4 uc001xon.5 uc001xon.6 uc001xon.7 
ENST00000238667.9 FLVCR2 ENST00000238667.9 FLVCR choline and putative heme transporter 2, transcript variant 1 (from RefSeq NM_017791.3) B7Z485 C14orf58 ENST00000238667.1 ENST00000238667.2 ENST00000238667.3 ENST00000238667.4 ENST00000238667.5 ENST00000238667.6 ENST00000238667.7 ENST00000238667.8 FLVC2_HUMAN NM_017791 Q53ZT9 Q96JY3 Q9NX90 Q9UPI3 uc001xrs.1 uc001xrs.2 uc001xrs.3 uc001xrs.4 This gene encodes a member of the major facilitator superfamily. The encoded transmembrane protein is a calcium transporter. Unlike the related protein feline leukemia virus subgroup C receptor 1, the protein encoded by this locus does not bind to feline leukemia virus subgroup C envelope protein. The encoded protein may play a role in development of brain vascular endothelial cells, as mutations at this locus have been associated with proliferative vasculopathy and hydranencephaly-hydrocephaly syndrome. Alternatively spliced transcript variants have been described.[provided by RefSeq, Aug 2010]. Putative heme b importer/sensor involved in heme homeostasis in response to the metabolic state of the cell and to diet. May act as a sensor of cytosolic and/or mitochondrial heme levels to regulate mitochondrial respiration processes, ATP synthesis and thermogenesis. At low heme levels, interacts with components of electron transfer chain (ETC) complexes and ATP2A2, leading to ubiquitin-mediated degradation of ATP2A2 and inhibition of thermogenesis. Upon heme binding, dissociates from ETC complexes to allow switching from mitochondrial ATP synthesis to thermogenesis. Alternatively, in coordination with ATP2A2 may mediate calcium transport and signaling in response to heme. Reaction=heme b(in) = heme b(out); Xref=Rhea:RHEA:75443, ChEBI:CHEBI:60344; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75444; Evidence=; Interacts with components of electron transfer chain complexes III, IV and V including CYC1, NDUFA4, COX4I1, ATP5PD and ATP5F1C; these interactions occur in the absence of heme and are disrupted upon heme binding (By similarity). Interacts with ATP2A2; this interaction occurs in the absence of heme and promotes ATP2A2 proteasomal degradation; the complex is dissociated upon heme binding (By similarity). Interacts with HMOX1; this interaction is potentiated in the presence of heme (By similarity). Mitochondrion membrane ; Multi-pass membrane protein Endoplasmic reticulum membrane ; Multi-pass membrane protein Cell membrane ; Multi-pass membrane protein Note=Primarily resides in mitochondria where it interacts with components of the electron transfer chain complexes III, IV and V. Colocalizes with ATP2A2 at the mitochondrial- ER contact junction. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UPI3-1; Sequence=Displayed; Name=2; IsoId=Q9UPI3-2; Sequence=VSP_043048, VSP_043049; Expressed in non-hematopoietic tissues, with relative abundant expression in brain, placenta, lung, liver and kidney (PubMed:20823265). Also expressed in hematopoietic tissues (fetal liver, spleen, lymph node, thymus, leukocytes and bone marrow) (PubMed:20823265). Found in acidophil cells of the pituitary that secrete growth hormone and prolactin (at protein level) (PubMed:14729055). Expressed in follicular cells of the developing thyroid at 18 dpc (at protein level). The N-terminus contains histidine-proline motifs involved in heme binding. Can bind 2 to 3 heme molecules. Proliferative vasculopathy and hydranencephaly-hydrocephaly syndrome (PVHH) [MIM:225790]: A rare prenatally lethal disorder characterized by hydranencephaly, a distinctive glomerular vasculopathy in the central nervous system and retina, and diffuse ischemic lesions of the brain stem, basal ganglia, and spinal cord with calcifications. Hydranencephaly is a condition where the greater portions of the cerebral hemispheres and corpus striatum are replaced by cerebrospinal fluid and glial tissue. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the major facilitator superfamily. Feline leukemia virus subgroup C receptor (TC 2.A.1.28.1) family. Sequence=BAB55381.1; Type=Erroneous initiation; Evidence=; plasma membrane integral component of plasma membrane heme transporter activity membrane integral component of membrane heme binding transmembrane transport heme export uc001xrs.1 uc001xrs.2 uc001xrs.3 uc001xrs.4 
ENST00000238682.8 TGFB3 ENST00000238682.8 transforming growth factor beta 3, transcript variant 1 (from RefSeq NM_003239.5) ENST00000238682.1 ENST00000238682.2 ENST00000238682.3 ENST00000238682.4 ENST00000238682.5 ENST00000238682.6 ENST00000238682.7 NM_003239 P10600 Q8WV88 TGFB3_HUMAN uc001xsc.1 uc001xsc.2 uc001xsc.3 uc001xsc.4 This gene encodes a secreted ligand of the TGF-beta (transforming growth factor-beta) superfamily of proteins. Ligands of this family bind various TGF-beta receptors leading to recruitment and activation of SMAD family transcription factors that regulate gene expression. The encoded preproprotein is proteolytically processed to generate a latency-associated peptide (LAP) and a mature peptide, and is found in either a latent form composed of a mature peptide homodimer, a LAP homodimer, and a latent TGF-beta binding protein, or in an active form consisting solely of the mature peptide homodimer. The mature peptide may also form heterodimers with other TGF-beta family members. This protein is involved in embryogenesis and cell differentiation, and may play a role in wound healing. Mutations in this gene are a cause of aortic aneurysms and dissections, as well as familial arrhythmogenic right ventricular dysplasia 1. [provided by RefSeq, Aug 2016]. Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-3 (TGF-beta-3) chain in a latent state during storage in extracellular matrix (By similarity). Associates non- covalently with TGF-beta-3 and regulates its activation via interaction with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-3 (By similarity). Interaction with integrins results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-3 (By similarity). Transforming growth factor beta-3: Multifunctional protein that regulates embryogenesis and cell differentiation and is required in various processes such as secondary palate development (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency- associated peptide (LAP) and Transforming growth factor beta-3 (TGF- beta-3) chains remain non-covalently linked rendering TGF-beta-3 inactive during storage in extracellular matrix (By similarity). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1 and LRRC32/GARP that control activation of TGF-beta-3 and maintain it in a latent state during storage in extracellular milieus (By similarity). TGF-beta-3 is released from LAP by integrins: integrin- binding results in distortion of the LAP chain and subsequent release of the active TGF-beta-3 (By similarity). Once activated following release of LAP, TGF-beta-3 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). Interacts with ASPN (PubMed:8819159). Latency-associated peptide: Homodimer; disulfide-linked. Latency-associated peptide: Interacts with Transforming growth factor beta-3 (TGF-beta-3) chain; interaction is non-covalent and maintains (TGF-beta-3) in a latent state (By similarity). Latency-associated peptide: Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-3 and promote epithelial fusion during palate development (By similarity). Latency- associated peptide: Interacts (via cell attachment site) with integrins, leading to release of the active TGF-beta-3 (By similarity). Transforming growth factor beta-3: Homodimer; disulfide-linked (PubMed:8819159). Transforming growth factor beta-3: Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (By similarity). P10600; P10600: TGFB3; NbExp=2; IntAct=EBI-1033020, EBI-1033020; P10600; P37173: TGFBR2; NbExp=8; IntAct=EBI-1033020, EBI-296151; [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix [Transforming growth factor beta-3]: Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P10600-1; Sequence=Displayed; Name=2; IsoId=P10600-2; Sequence=VSP_056285; Transforming growth factor beta-3 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive. Methylated at Gln-293 by N6AMT1. Arrhythmogenic right ventricular dysplasia, familial, 1 (ARVD1) [MIM:107970]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. Note=The disease is caused by variants affecting the gene represented in this entry. Loeys-Dietz syndrome 5 (LDS5) [MIM:615582]: A form of Loeys- Dietz syndrome, a syndrome with widespread systemic involvement characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. LDS5 additional variable features include mitral valve disease, skeletal overgrowth, cervical spine instability, and clubfoot deformity. LDS5 patients do not manifest remarkable aortic or arterial tortuosity, and there is no strong evidence for early aortic dissection. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the TGF-beta family. Sequence=CAA33024.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tgfb3/"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/tgfb3/"; Name=Wikipedia; Note=TGF beta-3 entry; URL="https://en.wikipedia.org/wiki/TGF_beta_3"; activation of MAPK activity response to hypoxia in utero embryonic development platelet degranulation type II transforming growth factor beta receptor binding cytokine activity transforming growth factor beta receptor binding protein binding extracellular region extracellular space nucleus cytoplasm plasma membrane transforming growth factor beta receptor signaling pathway salivary gland morphogenesis female pregnancy aging growth factor activity positive regulation of cell proliferation negative regulation of cell proliferation cell surface positive regulation of epithelial to mesenchymal transition positive regulation of pathway-restricted SMAD protein phosphorylation negative regulation of macrophage cytokine production secretory granule T-tubule positive regulation of bone mineralization BMP signaling pathway negative regulation of transforming growth factor beta receptor signaling pathway mammary gland development platelet alpha granule lumen response to progesterone positive regulation of collagen biosynthetic process response to laminar fluid shear stress type I transforming growth factor beta receptor binding type III transforming growth factor beta receptor binding wound healing regulation of cell proliferation odontogenesis uterine wall breakdown identical protein binding regulation of apoptotic process neuronal cell body positive regulation of apoptotic process intracellular membrane-bounded organelle regulation of MAPK cascade negative regulation of neuron apoptotic process response to estrogen ossification involved in bone remodeling cell-cell junction organization positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity lung alveolus development cell development digestive tract development embryonic neurocranium morphogenesis inner ear development transforming growth factor beta binding positive regulation of protein secretion positive regulation of filopodium assembly positive regulation of stress fiber assembly positive regulation of cell division face morphogenesis frontal suture morphogenesis positive regulation of SMAD protein import into nucleus SMAD protein signal transduction detection of hypoxia negative regulation of vascular smooth muscle cell proliferation positive regulation of occluding junction disassembly regulation of epithelial to mesenchymal transition involved in endocardial cushion formation uc001xsc.1 uc001xsc.2 uc001xsc.3 uc001xsc.4 
ENST00000238714.8 PAPOLG ENST00000238714.8 poly(A) polymerase gamma (from RefSeq NM_022894.4) B2RBH4 ENST00000238714.1 ENST00000238714.2 ENST00000238714.3 ENST00000238714.4 ENST00000238714.5 ENST00000238714.6 ENST00000238714.7 NM_022894 PAP2 PAPG PAPOG_HUMAN PAPOLG Q59G05 Q969N1 Q9BWT3 Q9H8L2 Q9HAD0 uc002sai.1 uc002sai.2 uc002sai.3 uc002sai.4 uc002sai.5 This gene encodes a member of the poly(A) polymerase family which catalyzes template-independent extension of the 3' end of a DNA/RNA strand. This enzyme shares 60% identity to the well characterized poly(A) polymerase II (PAPII) at the amino acid level. These two enzymes have similar organization of structural and functional domains. This enzyme is exclusively localized in the nucleus and exhibits both nonspecific and CPSF (cleavage and polyadenylation specificity factor)/AAUAAA-dependent polyadenylation activity. This gene is located on chromosome 2 in contrast to the PAPII gene, which is located on chromosome 14. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: SRR1803615.233884.1, SRR1803612.281775.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238714.8/ ENSP00000238714.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA. Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence= Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Binds 2 magnesium ions. Also active with manganese. ; Kinetic parameters: KM=0.051 uM for poly(A)(15) ; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BWT3-1; Sequence=Displayed; Name=2; IsoId=Q9BWT3-2; Sequence=VSP_054379; Expressed predominantly in testis, and weakly in other tissues. Overexpressed in several tumors. Belongs to the poly(A) polymerase family. Sequence=BAB14604.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleotide binding RNA binding polynucleotide adenylyltransferase activity ATP binding nucleus nucleoplasm cytosol mRNA polyadenylation mRNA processing membrane nuclear body transferase activity nucleotidyltransferase activity RNA 3'-end processing RNA polyadenylation metal ion binding uc002sai.1 uc002sai.2 uc002sai.3 uc002sai.4 uc002sai.5 
ENST00000238721.9 TP53I3 ENST00000238721.9 tumor protein p53 inducible protein 3, transcript variant 2 (from RefSeq NM_147184.4) D6W533 ENST00000238721.1 ENST00000238721.2 ENST00000238721.3 ENST00000238721.4 ENST00000238721.5 ENST00000238721.6 ENST00000238721.7 ENST00000238721.8 NM_147184 O14679 O14685 PIG3 Q38G78 Q53FA7 Q6JLE7 Q9BWB8 QORX_HUMAN TP53I3 uc002rez.1 uc002rez.2 uc002rez.3 uc002rez.4 The protein encoded by this gene is similar to oxidoreductases, which are enzymes involved in cellular responses to oxidative stresses and irradiation. This gene is induced by the tumor suppressor p53 and is thought to be involved in p53-mediated cell death. It contains a p53 consensus binding site in its promoter region and a downstream pentanucleotide microsatellite sequence. P53 has been shown to transcriptionally activate this gene by interacting with the downstream pentanucleotide microsatellite sequence. The microsatellite is polymorphic, with a varying number of pentanucleotide repeats directly correlated with the extent of transcriptional activation by p53. It has been suggested that the microsatellite polymorphism may be associated with differential susceptibility to cancer. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2011]. Catalyzes the NADPH-dependent reduction of quinones (PubMed:19349281). Exhibits a low enzymatic activity with beta- naphthoquinones, with a strong preference for the ortho-quinone isomer (1,2-beta-naphthoquinone) over the para isomer (1,4-beta- naphthoquinone). Also displays a low reductase activity for non-quinone compounds such as diamine and 2,6-dichloroindophenol (in vitro) (PubMed:19349281). Involved in the generation of reactive oxygen species (ROS) (PubMed:19349281). Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone + NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225; EC=1.6.5.5; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14270; Evidence=; Kinetic parameters: KM=215 uM for 1,2-naphthoquinone ; Homodimer. Event=Alternative splicing; Named isoforms=2; Comment=UV radiation favors the production of isoform 2.; Name=1; IsoId=Q53FA7-1; Sequence=Displayed; Name=2; Synonyms=PIG3AS; IsoId=Q53FA7-2; Sequence=VSP_015783, VSP_015784; Isoform 1 and isoform 2 are both activated by p53/TP53, doxorubicin, etoposide and ionizing radiation. Isoform 2 is highly activated by UV radiation. [Isoform 1]: Major isoform under normal light conditions. [Isoform 2]: Major isoform under UV light exposure. Undergoes rapid proteolytic degradation by the proteasome. Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily. Sequence=AAC39535.1; Type=Erroneous gene model prediction; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tp53i3/"; NADPH:quinone reductase activity cytosol NADP metabolic process oxidoreductase activity protein homodimerization activity regulation of apoptotic process quinone binding oxidation-reduction process NADPH binding uc002rez.1 uc002rez.2 uc002rez.3 uc002rez.4 
ENST00000238738.9 RHOQ ENST00000238738.9 ras homolog family member Q (from RefSeq NM_012249.4) ENST00000238738.1 ENST00000238738.2 ENST00000238738.3 ENST00000238738.4 ENST00000238738.5 ENST00000238738.6 ENST00000238738.7 ENST00000238738.8 HEL-S-42 NM_012249 RHOQ V9HWD0 V9HWD0_HUMAN hCG_1995863 uc002rva.1 uc002rva.2 uc002rva.3 uc002rva.4 uc002rva.5 This gene encodes a member of the Rho family of small GTPases, which cycle between inactive GDP-bound and active GTP-bound states and function as molecular switches in signal transduction cascades. Rho proteins promote reorganization of the actin cytoskeleton and regulate cell shape, attachment, and motility. The encoded protein is an important signalling protein for sarcomere assembly and has been shown to play a significant role in the exocytosis of the solute carrier family 2, facilitated glucose transporter member 4 and other proteins, possibly acting as the signal that turns on the membrane fusion machinery. Three related pseudogene have been identified on chromosomes 2 and 14. [provided by RefSeq, Aug 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: EU794657.1, SRR1660807.165339.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238738.9/ ENSP00000238738.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## V9HWD0; Q9HD26: GOPC; NbExp=4; IntAct=EBI-10330219, EBI-349832; V9HWD0; Q15654: TRIP6; NbExp=3; IntAct=EBI-10330219, EBI-742327; nucleotide binding GTPase activity protein binding GTP binding plasma membrane small GTPase mediated signal transduction regulation of cell shape cortical actin cytoskeleton organization cellular response to insulin stimulus membrane raft negative regulation of protein localization to plasma membrane uc002rva.1 uc002rva.2 uc002rva.3 uc002rva.4 uc002rva.5 
ENST00000238788.14 TMEM214 ENST00000238788.14 transmembrane protein 214, transcript variant 1 (from RefSeq NM_017727.5) A6NNF2 B3KUI9 B5MCD8 D6W547 ENST00000238788.1 ENST00000238788.10 ENST00000238788.11 ENST00000238788.12 ENST00000238788.13 ENST00000238788.2 ENST00000238788.3 ENST00000238788.4 ENST00000238788.5 ENST00000238788.6 ENST00000238788.7 ENST00000238788.8 ENST00000238788.9 NM_017727 PP446 Q53SW1 Q69YH4 Q6NUQ4 Q8NC45 Q8WZ37 Q9NXH2 TM214_HUMAN uc002ria.1 uc002ria.2 uc002ria.3 uc002ria.4 uc002ria.5 uc002ria.6 Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress. Constitutively interacts with CASP4; required for the localization of procaspase 4 to the ER. Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6NUQ4-1; Sequence=Displayed; Name=2; IsoId=Q6NUQ4-2; Sequence=VSP_041155; Belongs to the TMEM214 family. Sequence=AAL55739.1; Type=Erroneous initiation; Evidence=; Sequence=BAA91038.1; Type=Erroneous initiation; Evidence=; Sequence=BAC11331.1; Type=Frameshift; Evidence=; Sequence=CAH10591.1; Type=Erroneous initiation; Evidence=; endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus cytosol cytoplasmic microtubule apoptotic process membrane integral component of membrane uc002ria.1 uc002ria.2 uc002ria.3 uc002ria.4 uc002ria.5 uc002ria.6 
ENST00000238789.10 ATAD2B ENST00000238789.10 ATPase family AAA domain containing 2B, transcript variant 3 (from RefSeq NR_125717.2) ATD2B_HUMAN B9ZVQ5 ENST00000238789.1 ENST00000238789.2 ENST00000238789.3 ENST00000238789.4 ENST00000238789.5 ENST00000238789.6 ENST00000238789.7 ENST00000238789.8 ENST00000238789.9 KIAA1240 NR_125717 Q6ZNA6 Q8N9E7 Q9ULI0 uc002rek.1 uc002rek.2 uc002rek.3 uc002rek.4 uc002rek.5 uc002rek.6 The protein encoded by this gene belongs to the AAA ATPase family. This family member includes an N-terminal bromodomain. It has been found to be localized to the nucleus, partly to replication sites, consistent with a chromatin-related function. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jul 2014]. ##Evidence-Data-START## Transcript exon combination :: BC171846.1 [ECO:0000332] ##Evidence-Data-END## Binds acetylated lysine residues in histone H1.4, H2A, H2B, H3 and H4 (in vitro). Nucleus te=Partially localizes to replication sites. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9ULI0-1; Sequence=Displayed; Name=2; IsoId=Q9ULI0-2; Sequence=VSP_023276; Belongs to the AAA ATPase family. Sequence=BAD18469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; nucleotide binding chromatin binding ATP binding nucleus nucleoplasm ATPase activity negative regulation of chromatin silencing histone binding positive regulation of transcription from RNA polymerase II promoter lysine-acetylated histone binding uc002rek.1 uc002rek.2 uc002rek.3 uc002rek.4 uc002rek.5 uc002rek.6 
ENST00000238823.13 FAM98A ENST00000238823.13 family with sequence similarity 98 member A, transcript variant 1 (from RefSeq NM_015475.5) B2RNA2 ENST00000238823.1 ENST00000238823.10 ENST00000238823.11 ENST00000238823.12 ENST00000238823.2 ENST00000238823.3 ENST00000238823.4 ENST00000238823.5 ENST00000238823.6 ENST00000238823.7 ENST00000238823.8 ENST00000238823.9 FA98A_HUMAN FAM98A NM_015475 Q8NCA5 Q9Y3Y6 uc002rpa.1 uc002rpa.2 uc002rpa.3 Positively stimulates PRMT1-induced protein arginine methylation (PubMed:28040436). Involved in skeletal homeostasis (By similarity). Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (By similarity). Interacts (via N- and C-terminus) with DDX1 (PubMed:28040436). Interacts (via N- and C-terminus) with C14orf166 (PubMed:28040436). Interacts with FAM98B (PubMed:28040436). Interacts with PLEKHM1 (via N- and C-terminus) (By similarity). Q8NCA5; Q92499: DDX1; NbExp=4; IntAct=EBI-1210765, EBI-358474; Q8NCA5; Q9Y224: RTRAF; NbExp=7; IntAct=EBI-1210765, EBI-1104547; Expressed strongly in colorectal cancer cells (PubMed:28040436). Expressed strongly in colorectal cancer tissues compared to wild-type colon samples (at protein level) (PubMed:28040436). Expressed strongly in colorectal cancer tissues compared to wild-type colon samples (PubMed:28040436). Belongs to the FAM98 family. RNA binding protein binding protein methylation protein methyltransferase activity positive regulation of cell proliferation positive regulation of gene expression lysosome localization tRNA-splicing ligase complex positive regulation of ruffle assembly uc002rpa.1 uc002rpa.2 uc002rpa.3 
ENST00000238831.9 YIPF4 ENST00000238831.9 Yip1 domain family member 4 (from RefSeq NM_032312.4) ENST00000238831.1 ENST00000238831.2 ENST00000238831.3 ENST00000238831.4 ENST00000238831.5 ENST00000238831.6 ENST00000238831.7 ENST00000238831.8 NM_032312 Nbla11189 Q9BSR8 YIPF4_HUMAN uc002rok.1 uc002rok.2 uc002rok.3 uc002rok.4 uc002rok.5 Involved in the maintenance of the Golgi structure. Interacts with YIPF3 and YIPF5. (Microbial infection) Interacts with human papillomavirus (HPV) E5 proteins. Q9BSR8; Q13520: AQP6; NbExp=3; IntAct=EBI-751253, EBI-13059134; Q9BSR8; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-751253, EBI-714543; Q9BSR8; P11912: CD79A; NbExp=3; IntAct=EBI-751253, EBI-7797864; Q9BSR8; P34972: CNR2; NbExp=3; IntAct=EBI-751253, EBI-2835940; Q9BSR8; Q15125: EBP; NbExp=3; IntAct=EBI-751253, EBI-3915253; Q9BSR8; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-751253, EBI-781551; Q9BSR8; Q969F0: FATE1; NbExp=6; IntAct=EBI-751253, EBI-743099; Q9BSR8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-751253, EBI-13345167; Q9BSR8; O15529: GPR42; NbExp=3; IntAct=EBI-751253, EBI-18076404; Q9BSR8; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-751253, EBI-18053395; Q9BSR8; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-751253, EBI-725665; Q9BSR8; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-751253, EBI-373355; Q9BSR8; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-751253, EBI-2863634; Q9BSR8; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-751253, EBI-7545592; Q9BSR8; Q96GF1: RNF185; NbExp=3; IntAct=EBI-751253, EBI-2340249; Q9BSR8; Q99942: RNF5; NbExp=3; IntAct=EBI-751253, EBI-348482; Q9BSR8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-751253, EBI-17247926; Q9BSR8; Q14973: SLC10A1; NbExp=3; IntAct=EBI-751253, EBI-3923031; Q9BSR8; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-751253, EBI-17595455; Q9BSR8; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-751253, EBI-10262251; Q9BSR8; Q96G79: SLC35A4; NbExp=3; IntAct=EBI-751253, EBI-12363689; Q9BSR8; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-751253, EBI-17295964; Q9BSR8; P30825: SLC7A1; NbExp=4; IntAct=EBI-751253, EBI-4289564; Q9BSR8; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-751253, EBI-5235586; Q9BSR8; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-751253, EBI-12947623; Q9BSR8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-751253, EBI-8638294; Q9BSR8; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-751253, EBI-12003468; Q9BSR8; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-751253, EBI-11343401; Q9BSR8; O95070: YIF1A; NbExp=3; IntAct=EBI-751253, EBI-2799703; Q9BSR8; Q9GZM5: YIPF3; NbExp=10; IntAct=EBI-751253, EBI-743787; Q9BSR8; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-751253, EBI-12837904; Golgi apparatus, cis-Golgi network membrane ulti-pass membrane protein Expressed in keratinocytes (at protein level). In primary foreskin keratinocytes, down-regulated during calcium-induced differentiation (at protein level). The physiological relevance of this observation is unclear as YIPF4 protein is expressed throughout the epithelial layers in organotypic raft cultures, a cell-culture model of stratified epithelium. (Microbial infection) Down-regulation upon calcium-induced keratinocyte differentiation is prevented in the presence of human papillomavirus (HPV), independently of HPV E5 protein (at protein level). The physiological relevance of this observation is unclear. Belongs to the YIP1 family. protein binding endoplasmic reticulum Golgi apparatus plasma membrane membrane integral component of membrane intracellular membrane-bounded organelle uc002rok.1 uc002rok.2 uc002rok.3 uc002rok.4 uc002rok.5 
ENST00000238875.10 LGALSL ENST00000238875.10 galectin like (from RefSeq NM_014181.3) B2RBG8 D6W5E8 ENST00000238875.1 ENST00000238875.2 ENST00000238875.3 ENST00000238875.4 ENST00000238875.5 ENST00000238875.6 ENST00000238875.7 ENST00000238875.8 ENST00000238875.9 GRP HSPC159 LEGL_HUMAN NM_014181 Q3ZCW2 Q6P5T6 Q9P005 uc002scy.1 uc002scy.2 uc002scy.3 uc002scy.4 uc002scy.5 uc002scy.6 Does not bind lactose, and may not bind carbohydrates. Monomer. Q3ZCW2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10241423, EBI-742054; Q3ZCW2; P50458: LHX2; NbExp=3; IntAct=EBI-10241423, EBI-12179869; Q3ZCW2; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-10241423, EBI-742610; Q3ZCW2; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-10241423, EBI-717399; Most of the residues in the galectin domain that have been shown to be critical for carbohydrate-binding in other galectins are not conserved. protein binding intracellular cytoplasm carbohydrate binding uc002scy.1 uc002scy.2 uc002scy.3 uc002scy.4 uc002scy.5 uc002scy.6 
ENST00000238892.4 CRIPT ENST00000238892.4 CXXC repeat containing interactor of PDZ3 domain (from RefSeq NM_014171.6) CRIPT_HUMAN ENST00000238892.1 ENST00000238892.2 ENST00000238892.3 HSPC139 NM_014171 Q9P021 uc002rve.1 uc002rve.2 uc002rve.3 uc002rve.4 uc002rve.5 uc002rve.6 This gene encodes a protein that binds to the PDZ3 peptide recognition domain. The encoded protein may modulates protein interactions with the cytoskeleton. A mutation in this gene resulted in short stature with microcephaly and distinctive facies. [provided by RefSeq, Jun 2014]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR7346977.2652604.1, SRR5189655.140977.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238892.4/ ENSP00000238892.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses (By similarity). Component of the minor spliceosome. Within this complex, interacts with RNF113A, as well as with SF3B1/SF3b155, SF3B2/SF3b145 and PHF5A/SF3b14b (PubMed:33509932). Interacts with TUBB1. Interacts strongly with the PDZ3 domain of members of the DLG4 family. Associates with microtubules (By similarity). Interacts with DLG4. Q9P021; P78352: DLG4; NbExp=5; IntAct=EBI-946968, EBI-80389; Q9P021; O76024: WFS1; NbExp=3; IntAct=EBI-946968, EBI-720609; Q9P021; Q62936: Dlg3; Xeno; NbExp=5; IntAct=EBI-946968, EBI-349596; Q9P021; P31016: Dlg4; Xeno; NbExp=2; IntAct=EBI-946968, EBI-375655; Cytoplasm Synapse Cell projection, dendritic spine Note=Colocalizes with DLG4 in asymmetric synapses. Short stature with microcephaly and distinctive facies (SSMCF) [MIM:615789]: An autosomal recessive disease characterized by dwarfism, microcephaly, and distinctive facial dysmorphism involving frontal bossing, high forehead, sparse hair and eyebrows, telecanthus, mild proptosis, anteverted nares, and flat nasal bridge. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the CRIPT family. fibrillar center protein binding nucleus nucleolus cytoplasm microtubule binding postsynaptic density cell junction PDZ domain binding dendrite cytoplasmic microtubule organization protein localization to microtubule cell projection neuronal cell body dendritic spine dendritic shaft macromolecular complex binding establishment of protein localization synapse scaffold protein binding regulation of postsynaptic density protein 95 clustering uc002rve.1 uc002rve.2 uc002rve.3 uc002rve.4 uc002rve.5 uc002rve.6 
ENST00000238936.8 MFSD13A ENST00000238936.8 major facilitator superfamily domain containing 13A (from RefSeq NM_024789.4) C10orf77 ENST00000238936.1 ENST00000238936.2 ENST00000238936.3 ENST00000238936.4 ENST00000238936.5 ENST00000238936.6 ENST00000238936.7 MF13A_HUMAN MFSD13A NM_024789 Q14CX5 Q6NWM8 Q6NWM9 Q6PEZ7 Q9H679 TMEM180 uc001kvt.1 uc001kvt.2 uc001kvt.3 uc001kvt.4 Q14CX5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12120958, EBI-3867333; Q14CX5; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12120958, EBI-10261141; Q14CX5; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12120958, EBI-22310682; Membrane ; Multi-pass membrane protein Sequence=AAH67530.2; Type=Erroneous initiation; Evidence=; Sequence=AAH67531.2; Type=Erroneous initiation; Evidence=; Sequence=BAB15385.1; Type=Erroneous initiation; Evidence=; membrane integral component of membrane uc001kvt.1 uc001kvt.2 uc001kvt.3 uc001kvt.4 
ENST00000238961.9 SLF2 ENST00000238961.9 SMC5-SMC6 complex localization factor 2, transcript variant 1 (from RefSeq NM_018121.4) A8K950 B1AL17 C10orf6 ENST00000238961.1 ENST00000238961.2 ENST00000238961.3 ENST00000238961.4 ENST00000238961.5 ENST00000238961.6 ENST00000238961.7 ENST00000238961.8 FAM178A NM_018121 Q5W0L8 Q6GMU6 Q8IX21 Q9NPE8 SLF2 SLF2_HUMAN uc001krt.1 uc001krt.2 uc001krt.3 uc001krt.4 uc001krt.5 uc001krt.6 Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance (PubMed:25931565). The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks (PubMed:25931565). Promotes the recruitment of the SMC5-SMC6 complex to DNA lesions (PubMed:25931565). Plays a role in SMC5-SMC6 complex recruitment for viral restriction. Forms a complex with SIMC1 and this complex is required to recruit SMC5-SMC6 complex to PML nuclear bodies and sites of viral replication (PubMed:36373674). Forms a heterodimer with SIMC1 (PubMed:36373674). Interacts with SLF1 (via N-terminus); this interaction links RAD18 to the SMC5- SMC6 complex (PubMed:25931565, PubMed:36333305, PubMed:36373674). Interacts with RAD18; this interaction is increased in a SLF1-dependent manner (PubMed:25931565, PubMed:36333305). Interacts with SMC5 and SMC6 (PubMed:25931565). Q8IX21; P25786: PSMA1; NbExp=3; IntAct=EBI-2682240, EBI-359352; Q8IX21; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-2682240, EBI-12025260; Q8IX21; Q8NDZ2: SIMC1; NbExp=7; IntAct=EBI-2682240, EBI-724973; Q8IX21; Q9BQI6: SLF1; NbExp=7; IntAct=EBI-2682240, EBI-10975834; Q8IX21; Q8IY18: SMC5; NbExp=3; IntAct=EBI-2682240, EBI-605405; Q8IX21; Q96SB8: SMC6; NbExp=5; IntAct=EBI-2682240, EBI-605415; Q8IX21; Q14142: TRIM14; NbExp=3; IntAct=EBI-2682240, EBI-2820256; Nucleus cleus, PML body Note=Mainly localizes in the nucleus (PubMed:24561620). Colocalizes with PCNA on replication sites (PubMed:24561620). Associates with chromatin (PubMed:25931565). Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner (PubMed:25931565). Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q8IX21-1; Sequence=Displayed; Name=2; IsoId=Q8IX21-2; Sequence=VSP_045621; Name=3; IsoId=Q8IX21-3; Sequence=VSP_054914, VSP_054915; Widely expressed (PubMed:12459258, PubMed:36333305). Expressed at higher level in skeletal muscle and at slightly lower level in brain, liver and heart, than in lung, kidney, spleen and thymus (PubMed:12459258). Atelis syndrome 1 (ATELS1) [MIM:620184]: A form of Atelis syndrome, an autosomal recessive neurodevelopmental disorder characterized by mild to severe developmental delay, learning difficulties, microcephaly, and growth restriction with short stature. Additional features include anemia, skin hyperpigmentation, ocular anomalies, congenital heart defects, and mild skeletal abnormalities. Death in childhood may occur. Patient cells show spontaneous chromosome breakage and chromosomal anomalies, hallmarked by segmented and dicentric chromosomes and mosaic variegated hyperploidy. Note=The disease is caused by variants affecting the gene represented in this entry. Localized in the locus associated with inherited infantile onset spinocerebellar ataxia (IOSCA). No mutation were found associated with IOSCA compared to control subjects. The expression level in the brain was not different between the 2 populations. Belongs to the FAM178 family. Sequence=BAA91657.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; chromatin protein binding nucleus DNA repair cellular response to DNA damage stimulus positive regulation of protein complex assembly ubiquitin protein ligase binding positive regulation of maintenance of mitotic sister chromatid cohesion site of double-strand break intracellular membrane-bounded organelle macromolecular complex binding protein localization to site of double-strand break positive regulation of double-strand break repair uc001krt.1 uc001krt.2 uc001krt.3 uc001krt.4 uc001krt.5 uc001krt.6 
ENST00000238983.9 LIPF ENST00000238983.9 lipase F, gastric type, transcript variant 2 (from RefSeq NM_004190.4) B7Z723 ENST00000238983.1 ENST00000238983.2 ENST00000238983.3 ENST00000238983.4 ENST00000238983.5 ENST00000238983.6 ENST00000238983.7 ENST00000238983.8 F5H1P4 LIPF_HUMAN NM_004190 P07098 Q2M1P6 Q5VXI7 Q5VXI8 Q658L8 uc001kfg.1 uc001kfg.2 uc001kfg.3 uc001kfg.4 This gene encodes gastric lipase, an enzyme involved in the digestion of dietary triglycerides in the gastrointestinal tract, and responsible for 30% of fat digestion processes occurring in human. It is secreted by gastric chief cells in the fundic mucosa of the stomach, and it hydrolyzes the ester bonds of triglycerides under acidic pH conditions. The gene is a member of a conserved gene family of lipases that play distinct roles in neutral lipid metabolism. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]. Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:2243091, PubMed:10358049). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (PubMed:2243091). Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence=; Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)- octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932; Evidence=; Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol + H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:76979; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048; Evidence=; P07098-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11979889, EBI-16439278; Secreted Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=P07098-1; Sequence=Displayed; Name=2; IsoId=P07098-2; Sequence=VSP_047296; Name=3; IsoId=P07098-3; Sequence=VSP_047295; Name=4; IsoId=P07098-4; Sequence=VSP_047295, VSP_047296; Belongs to the AB hydrolase superfamily. Lipase family. Sequence=CAA29414.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/lipf/"; triglyceride lipase activity cellular_component extracellular region mitochondrion malate metabolic process lipid metabolic process triglyceride metabolic process lipid binding lipid catabolic process malate dehydrogenase activity hydrolase activity hydrolase activity, acting on ester bonds intracellular membrane-bounded organelle oxidation-reduction process uc001kfg.1 uc001kfg.2 uc001kfg.3 uc001kfg.4 
ENST00000238994.6 PPP1R3C ENST00000238994.6 protein phosphatase 1 regulatory subunit 3C (from RefSeq NM_005398.7) B2R7X0 ENST00000238994.1 ENST00000238994.2 ENST00000238994.3 ENST00000238994.4 ENST00000238994.5 NM_005398 O95686 PPP1R3C PPP1R5 PPR3C_HUMAN Q9UQK1 uc001kho.1 uc001kho.2 uc001kho.3 uc001kho.4 uc001kho.5 This gene encodes a carbohydrate binding protein that is a subunit of the protein phosphatase 1 (PP1) complex. PP1 catalyzes reversible protein phosphorylation, which is important in a wide range of cellular activities. The encoded protein affects glycogen biosynthesis by activating glycogen synthase and limiting glycogen breakdown by reducing glycogen phosphorylase activity. DNA hypermethylation of this gene has been found in colorectal cancer patients. The encoded protein also interacts with the laforin protein, which is a protein tyrosine phosphatase implicated in Lafora disease. [provided by RefSeq, Sep 2016]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BX537399.1, SRR1660807.165536.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2145544, SAMEA2155770 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000238994.6/ ENSP00000238994.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. Interacts with PPP1CC catalytic subunit of PP1 and associates with glycogen. Forms complexes with glycogen phosphorylase, glycogen synthase and phosphorylase kinase which is necessary for its regulation of PP1 activity. Also interacts with EPM2A/laforin. Q9UQK1; O95278: EPM2A; NbExp=5; IntAct=EBI-2506727, EBI-2506661; Q9UQK1; P13807: GYS1; NbExp=2; IntAct=EBI-2506727, EBI-740553; Q9UQK1; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-2506727, EBI-2341787; Q9UQK1; Q9BS40: LXN; NbExp=3; IntAct=EBI-2506727, EBI-1044504; Q9UQK1; P62136: PPP1CA; NbExp=5; IntAct=EBI-2506727, EBI-357253; Q9UQK1; P62140: PPP1CB; NbExp=9; IntAct=EBI-2506727, EBI-352350; Q9UQK1; P36873: PPP1CC; NbExp=4; IntAct=EBI-2506727, EBI-356283; The N-terminal region is required for binding to PP1, the central region is required for binding to glycogen and the C-terminal region is required for binding to glycogen phosphorylase, glycogen synthase and phosphorylase kinase. Ubiquitinated by NHLRC1/malin in a EPM2A/laforin-dependent manner. Sequence=AAD33215.1; Type=Erroneous gene model prediction; Evidence=; protein serine/threonine phosphatase activity protein binding cytosol carbohydrate metabolic process glycogen metabolic process glycogen biosynthetic process protein dephosphorylation protein phosphatase binding glycogen binding uc001kho.1 uc001kho.2 uc001kho.3 uc001kho.4 uc001kho.5 
ENST00000239032.4 PRLHR ENST00000239032.4 prolactin releasing hormone receptor (from RefSeq NM_004248.3) ENST00000239032.1 ENST00000239032.2 ENST00000239032.3 GPR10 GR3 NM_004248 O75194 P49683 PRLHR_HUMAN Q502U8 Q5VXR9 uc001ldp.1 uc001ldp.2 uc001ldp.3 PRLHR is a 7-transmembrane domain receptor for prolactin-releasing hormone (PRLH; MIM 602663) that is highly expressed in anterior pituitary (Ozawa et al., 2002 [PubMed 11923475]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK290461.1, AK313269.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA2145544 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239032.4/ ENSP00000239032.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor for prolactin-releasing peptide (PrRP). Implicated in lactation, regulation of food intake and pain-signal processing. Interacts through its C-terminal region with the PDZ domain- containing proteins GRIP1, GRIP2 and PICK1. Interacts with PDZ domains 4 and 5 of GRIP1 and with the PDZ domain of PICK1. P49683; Q9Y3R0: GRIP1; NbExp=2; IntAct=EBI-8009236, EBI-5349621; Cell membrane; Multi-pass membrane protein. Only detected in the pituitary gland and in all cell types of pituitary adenomas. Repressed by bromocriptine, a dopamine agonist. Belongs to the G-protein coupled receptor 1 family. Sequence=AAC50504.1; Type=Frameshift; Evidence=; G-protein coupled receptor activity neuropeptide Y receptor activity protein binding plasma membrane integral component of plasma membrane cilium signal transduction G-protein coupled receptor signaling pathway neuropeptide signaling pathway female pregnancy feeding behavior neuropeptide receptor activity membrane integral component of membrane hormone metabolic process uc001ldp.1 uc001ldp.2 uc001ldp.3 
ENST00000239144.5 HOXB8 ENST00000239144.5 homeobox B8 (from RefSeq NM_024016.4) ENST00000239144.1 ENST00000239144.2 ENST00000239144.3 ENST00000239144.4 HOX2D HXB8_HUMAN NM_024016 P17481 Q9H1I2 uc002inw.1 uc002inw.2 uc002inw.3 uc002inw.4 This gene is a member of the Antp homeobox family and encodes a nuclear protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded protein functions as a sequence-specific transcription factor that is involved in development. Increased expression of this gene is associated with colorectal cancer. Mice that have had the murine ortholog of this gene knocked out exhibit an excessive pathologic grooming behavior. This behavior is similar to the behavior of humans suffering from the obsessive-compulsive spectrum disorder trichotillomania. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK096222.1, AW517327.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239144.5/ ENSP00000239144.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Forms a DNA-binding heterodimer with transcription factor PBX1. Nucleus. Expressed in whole embryos and fetuses at 5-9 weeks from conception. Belongs to the Antp homeobox family. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus nucleoplasm regulation of transcription, DNA-templated multicellular organism development grooming behavior adult locomotory behavior anterior/posterior pattern specification sensory perception of pain dorsal spinal cord development sequence-specific DNA binding negative regulation of myeloid cell differentiation embryonic skeletal system morphogenesis skeletal system morphogenesis uc002inw.1 uc002inw.2 uc002inw.3 uc002inw.4 
ENST00000239151.6 HOXB5 ENST00000239151.6 homeobox B5 (from RefSeq NM_002147.4) B2RC69 ENST00000239151.1 ENST00000239151.2 ENST00000239151.3 ENST00000239151.4 ENST00000239151.5 HOX2A HXB5_HUMAN NM_002147 P09067 P09069 Q17RP4 uc002inr.1 uc002inr.2 uc002inr.3 uc002inr.4 uc002inr.5 This gene is a member of the Antp homeobox family and encodes a nuclear protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded protein functions as a sequence-specific transcription factor that is involved in lung and gut development. Increased expression of this gene is associated with a distinct biologic subset of acute myeloid leukemia (AML) and the occurrence of bronchopulmonary sequestration (BPS) and congenital cystic adenomatoid malformation (CCAM) tissue. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BI766494.1, M92299.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. P09067; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-3893317, EBI-6425205; P09067; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-3893317, EBI-4400025; P09067; A2RRN7: CADPS; NbExp=3; IntAct=EBI-3893317, EBI-10179719; P09067; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-3893317, EBI-739580; P09067; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-3893317, EBI-11530605; P09067; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-3893317, EBI-347573; P09067; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-3893317, EBI-739624; P09067; Q9BYD5: CNFN; NbExp=3; IntAct=EBI-3893317, EBI-12819063; P09067; P67870: CSNK2B; NbExp=3; IntAct=EBI-3893317, EBI-348169; P09067; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-3893317, EBI-10171858; P09067; P56545-3: CTBP2; NbExp=8; IntAct=EBI-3893317, EBI-10171902; P09067; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-3893317, EBI-3867333; P09067; Q08379: GOLGA2; NbExp=3; IntAct=EBI-3893317, EBI-618309; P09067; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-3893317, EBI-11163335; P09067; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-3893317, EBI-5916454; P09067; P54257: HAP1; NbExp=3; IntAct=EBI-3893317, EBI-712814; P09067; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-3893317, EBI-748420; P09067; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-3893317, EBI-10961706; P09067; O75031: HSF2BP; NbExp=3; IntAct=EBI-3893317, EBI-7116203; P09067; Q92845: KIFAP3; NbExp=3; IntAct=EBI-3893317, EBI-954040; P09067; Q15323: KRT31; NbExp=3; IntAct=EBI-3893317, EBI-948001; P09067; O76011: KRT34; NbExp=3; IntAct=EBI-3893317, EBI-1047093; P09067; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-3893317, EBI-11959885; P09067; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-3893317, EBI-12012928; P09067; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-3893317, EBI-10171774; P09067; O95751: LDOC1; NbExp=3; IntAct=EBI-3893317, EBI-740738; P09067; P43364: MAGEA11; NbExp=3; IntAct=EBI-3893317, EBI-739552; P09067; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-3893317, EBI-10178634; P09067; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3893317, EBI-16439278; P09067; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-3893317, EBI-10172526; P09067; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-3893317, EBI-11522433; P09067; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-3893317, EBI-10271199; P09067; O43482: OIP5; NbExp=3; IntAct=EBI-3893317, EBI-536879; P09067; P40424: PBX1; NbExp=3; IntAct=EBI-3893317, EBI-301611; P09067; P40425: PBX2; NbExp=3; IntAct=EBI-3893317, EBI-348489; P09067; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-3893317, EBI-10302990; P09067; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-3893317, EBI-9640281; P09067; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-3893317, EBI-2339674; P09067; Q9Y4D7: PLXND1; NbExp=3; IntAct=EBI-3893317, EBI-310731; P09067; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-3893317, EBI-3957793; P09067; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-3893317, EBI-750487; P09067; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-3893317, EBI-11523345; P09067; Q08117-2: TLE5; NbExp=5; IntAct=EBI-3893317, EBI-11741437; P09067; Q13077: TRAF1; NbExp=3; IntAct=EBI-3893317, EBI-359224; P09067; Q12933: TRAF2; NbExp=3; IntAct=EBI-3893317, EBI-355744; P09067; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-3893317, EBI-3650647; P09067; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-3893317, EBI-492476; P09067; P36406: TRIM23; NbExp=6; IntAct=EBI-3893317, EBI-740098; P09067; P14373: TRIM27; NbExp=3; IntAct=EBI-3893317, EBI-719493; P09067; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-3893317, EBI-2130429; P09067; Q495M9: USH1G; NbExp=3; IntAct=EBI-3893317, EBI-8601749; P09067; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-3893317, EBI-2799833; P09067; Q9NQZ6: ZC4H2; NbExp=3; IntAct=EBI-3893317, EBI-747993; P09067; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-3893317, EBI-12030590; P09067; Q9HBT8: ZNF286A; NbExp=3; IntAct=EBI-3893317, EBI-10754950; P09067; Q9H707: ZNF552; NbExp=3; IntAct=EBI-3893317, EBI-2555731; P09067; Q8N720: ZNF655; NbExp=3; IntAct=EBI-3893317, EBI-625509; P09067; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-3893317, EBI-10251462; P09067; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-3893317, EBI-527853; Nucleus. Spinal cord. Embryo. Belongs to the Antp homeobox family. Sequence=AAA52681.1; Type=Erroneous initiation; Evidence=; nuclear chromatin RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding fibrillar center DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus cytosol regulation of transcription, DNA-templated multicellular organism development anatomical structure morphogenesis anterior/posterior pattern specification sequence-specific DNA binding endothelial cell differentiation positive regulation of transcription from RNA polymerase II promoter embryonic skeletal system morphogenesis embryonic skeletal system development uc002inr.1 uc002inr.2 uc002inr.3 uc002inr.4 uc002inr.5 
ENST00000239165.9 HOXB7 ENST00000239165.9 homeobox B7 (from RefSeq NM_004502.4) A8K3N8 ENST00000239165.1 ENST00000239165.2 ENST00000239165.3 ENST00000239165.4 ENST00000239165.5 ENST00000239165.6 ENST00000239165.7 ENST00000239165.8 HOX2C HXB7_HUMAN NM_004502 P09629 Q15957 Q53FN3 Q96BQ6 uc002inv.1 uc002inv.2 uc002inv.3 uc002inv.4 uc002inv.5 This gene is a member of the Antp homeobox family and encodes a protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded nuclear protein functions as a sequence-specific transcription factor that is involved in cell proliferation and differentiation. Increased expression of this gene is associated with some cases of melanoma and ovarian carcinoma. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M16937.1, SRR5189655.10159.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239165.9/ ENSP00000239165.7 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Forms a DNA-binding heterodimer with transcription factor PBX1. P09629; P49761: CLK3; NbExp=6; IntAct=EBI-1248457, EBI-745579; P09629; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1248457, EBI-10976677; P09629; P22607: FGFR3; NbExp=3; IntAct=EBI-1248457, EBI-348399; P09629; P78527: PRKDC; NbExp=2; IntAct=EBI-1248457, EBI-352053; P09629; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1248457, EBI-5235340; P09629; P13010: XRCC5; NbExp=9; IntAct=EBI-1248457, EBI-357997; Nucleus. Belongs to the Antp homeobox family. nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm cytosol regulation of transcription, DNA-templated multicellular organism development anterior/posterior pattern specification nuclear body myeloid cell differentiation sequence-specific DNA binding positive regulation of transcription from RNA polymerase II promoter embryonic skeletal system morphogenesis positive regulation of branching involved in ureteric bud morphogenesis uc002inv.1 uc002inv.2 uc002inv.3 uc002inv.4 uc002inv.5 
ENST00000239174.7 HOXB1 ENST00000239174.7 homeobox B1 (from RefSeq NM_002144.4) ENST00000239174.1 ENST00000239174.2 ENST00000239174.3 ENST00000239174.4 ENST00000239174.5 ENST00000239174.6 HOX2I HXB1_HUMAN NM_002144 P14653 Q4VB03 uc002ink.1 uc002ink.2 uc002ink.3 This gene belongs to the homeobox family of genes. The homeobox genes encode a highly conserved family of transcription factors that play an important role in morphogenesis in all multicellular organisms. Mammals possess four similar homeobox gene clusters, HOXA, HOXB, HOXC and HOXD, located on different chromosomes, consisting of 9 to 11 genes arranged in tandem. This gene is one of several homeobox HOXB genes located in a cluster on chromosome 17. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: X16666.1, CN264618.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158188 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239174.7/ ENSP00000355140.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P14653-1; Sequence=Displayed; Name=2; IsoId=P14653-2; Sequence=VSP_056813, VSP_056814; The two common alleles; HOX1B*A and HOX1B*B have a frequency of 78.8% and 21.2% respectively. Facial paresis, hereditary congenital, 3 (HCFP3) [MIM:614744]: A form of facial paresis, a disease characterized by isolated dysfunction of the facial nerve (CN VII). HCFP3 patients are affected by bilateral facial palsy, facial muscle weakness of muscles innervated by CN VII, hearing loss, and strabismus. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the Antp homeobox family. Labial subfamily. nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding nucleus regulation of transcription, DNA-templated multicellular organism development pattern specification process anatomical structure morphogenesis anterior/posterior pattern specification protein domain specific binding rhombomere development rhombomere 4 development rhombomere 5 development facial nerve structural organization facial nucleus development sequence-specific DNA binding positive regulation of transcription from RNA polymerase II promoter anatomical structure formation involved in morphogenesis embryonic skeletal system morphogenesis uc002ink.1 uc002ink.2 uc002ink.3 
ENST00000239223.4 DUSP1 ENST00000239223.4 dual specificity phosphatase 1 (from RefSeq NM_004417.4) CL100 D3DQL9 DUS1_HUMAN DUSP1 ENST00000239223.1 ENST00000239223.2 ENST00000239223.3 MKP1 NM_004417 P28562 PTPN10 Q2V508 VH1 uc003mbv.1 uc003mbv.2 uc003mbv.3 uc003mbv.4 The protein encoded by this gene is a phosphatase with dual specificity for tyrosine and threonine. The encoded protein can dephosphorylate MAP kinase MAPK1/ERK2, which results in its involvement in several cellular processes. This protein appears to play an important role in the human cellular response to environmental stress as well as in the negative regulation of cellular proliferation. Finally, the encoded protein can make some solid tumors resistant to both chemotherapy and radiotherapy, making it a target for cancer therapy. [provided by RefSeq, Aug 2017]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC022463.1, X68277.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA2142670 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239223.4/ ENSP00000239223.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle. Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence= Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence=; Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence=; P28562; P28482: MAPK1; NbExp=3; IntAct=EBI-975493, EBI-959949; P28562; Q16539: MAPK14; NbExp=4; IntAct=EBI-975493, EBI-73946; P28562; P27361: MAPK3; NbExp=3; IntAct=EBI-975493, EBI-73995; P28562; Q13309: SKP2; NbExp=3; IntAct=EBI-975493, EBI-456291; P28562; P0CG47: UBB; NbExp=2; IntAct=EBI-975493, EBI-413034; Nucleus Expressed at high levels in the lung, liver placenta and pancreas. Moderate levels seen in the heart and skeletal muscle. Lower levels found in the brain and kidney. By oxidative stress and heat shock. Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation. Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/dusp1/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/40371/DUSP1"; inactivation of MAPK activity phosphoprotein phosphatase activity protein serine/threonine phosphatase activity protein tyrosine phosphatase activity protein binding nucleus cytoplasm protein dephosphorylation cell cycle negative regulation of cell adhesion protein tyrosine/serine/threonine phosphatase activity negative regulation of cell proliferation protein tyrosine/threonine phosphatase activity response to light stimulus response to organic substance dephosphorylation hydrolase activity phosphatase activity MAP kinase tyrosine/serine/threonine phosphatase activity growth factor binding response to estradiol response to retinoic acid cellular response to hormone stimulus response to testosterone peptidyl-tyrosine dephosphorylation intracellular signal transduction peptidyl-threonine dephosphorylation response to hydrogen peroxide positive regulation of apoptotic process negative regulation of apoptotic process negative regulation of MAP kinase activity negative regulation of MAPK cascade mitogen-activated protein kinase binding response to glucocorticoid negative regulation of meiotic cell cycle response to cAMP response to calcium ion peptidyl-serine dephosphorylation negative regulation of ERK1 and ERK2 cascade mitotic cell cycle arrest negative regulation of monocyte chemotaxis regulation of mitotic cell cycle spindle assembly checkpoint negative regulation of p38MAPK cascade cellular response to chemokine negative regulation of DNA biosynthetic process uc003mbv.1 uc003mbv.2 uc003mbv.3 uc003mbv.4 
ENST00000239231.7 PANK3 ENST00000239231.7 pantothenate kinase 3 (from RefSeq NM_024594.4) D3DQL1 ENST00000239231.1 ENST00000239231.2 ENST00000239231.3 ENST00000239231.4 ENST00000239231.5 ENST00000239231.6 NM_024594 PANK3_HUMAN Q53FJ9 Q7RTX4 Q9H999 uc003lzy.1 uc003lzy.2 uc003lzy.3 uc003lzy.4 uc003lzy.5 This gene encodes a protein belonging to the pantothenate kinase family. Pantothenate kinase is a key regulatory enzyme in the biosynthesis of coenzyme A (CoA) in bacteria and mammalian cells. It catalyzes the first committed step in the universal biosynthetic pathway leading to CoA and is itself subject to regulation through feedback inhibition by CoA. This family member is expressed most abundantly in the liver. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.11331.1, SRR3476690.841492.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239231.7/ ENSP00000239231.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the phosphorylation of pantothenate to generate 4'- phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis. Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33; Evidence= Subject to allosteric regulation, exists in two distinct conformational states, a catalytically incompetent (or open) conformation stabilized by the binding of acetyl(acyl)-CoA, and a catalytically competent (or closed) conformation stabilized by ATP- binding (PubMed:27555321). Inhibited by acetyl-CoA and its thioesters which act as allosteric inhibitors and compete with the ATP-binding site (PubMed:30927326, PubMed:17631502, PubMed:20797618, PubMed:27555321). Inhibited by sulfonylureas and thiazolidinediones (PubMed:20797618). Activated by oleoylethanolamide, palmitoyl-carnitine and oleoyl-carnitine (PubMed:20797618). Kinetic parameters: KM=175 uM for ATP ; KM=311 uM for ATP ; KM=17 uM for pantothenate ; KM=14 uM for pantothenate ; Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- pantothenate: step 1/5. Homodimer. Cytoplasm Highly expressed in the liver. Belongs to the type II pantothenate kinase family. nucleotide binding pantothenate kinase activity ATP binding nucleus cytoplasm cytosol coenzyme A biosynthetic process kinase activity phosphorylation transferase activity vitamin binding protein homodimerization activity acetyl-CoA binding uc003lzy.1 uc003lzy.2 uc003lzy.3 uc003lzy.4 uc003lzy.5 
ENST00000239243.7 MSX2 ENST00000239243.7 msh homeobox 2, transcript variant 1 (from RefSeq NM_002449.5) D3DQN1 ENST00000239243.1 ENST00000239243.2 ENST00000239243.3 ENST00000239243.4 ENST00000239243.5 ENST00000239243.6 HOX8 MSX2_HUMAN NM_002449 P35548 Q53XM4 Q9UD60 uc003mcy.1 uc003mcy.2 uc003mcy.3 uc003mcy.4 uc003mcy.5 This gene encodes a member of the muscle segment homeobox gene family. The encoded protein is a transcriptional repressor whose normal activity may establish a balance between survival and apoptosis of neural crest-derived cells required for proper craniofacial morphogenesis. The encoded protein may also have a role in promoting cell growth under certain conditions and may be an important target for the RAS signaling pathways. Mutations in this gene are associated with parietal foramina 1 and craniosynostosis type 2. [provided by RefSeq, Jul 2008]. Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antagonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter. Interacts with MINT (By similarity). Interacts with XRCC6 (Ku70) and XRCC5 (Ku80). P35548; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-6447480, EBI-10171570; P35548; O95833: CLIC3; NbExp=3; IntAct=EBI-6447480, EBI-10192241; P35548; G5E9A7: DMWD; NbExp=3; IntAct=EBI-6447480, EBI-10976677; P35548; O15197-2: EPHB6; NbExp=3; IntAct=EBI-6447480, EBI-10182490; P35548; O75593: FOXH1; NbExp=3; IntAct=EBI-6447480, EBI-1759806; P35548; P23769: GATA2; NbExp=3; IntAct=EBI-6447480, EBI-2806671; P35548; P31274: HOXC9; NbExp=3; IntAct=EBI-6447480, EBI-1779423; P35548; P42858: HTT; NbExp=12; IntAct=EBI-6447480, EBI-466029; P35548; Q96PV6: LENG8; NbExp=3; IntAct=EBI-6447480, EBI-739546; P35548; P28482: MAPK1; NbExp=3; IntAct=EBI-6447480, EBI-959949; P35548; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-6447480, EBI-741424; P35548; Q96HR8: NAF1; NbExp=3; IntAct=EBI-6447480, EBI-2515597; P35548; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-6447480, EBI-11022007; P35548; P78337: PITX1; NbExp=3; IntAct=EBI-6447480, EBI-748265; P35548; P28069: POU1F1; NbExp=3; IntAct=EBI-6447480, EBI-8673859; P35548; P09086-4: POU2F2; NbExp=3; IntAct=EBI-6447480, EBI-12918396; P35548; P78424: POU6F2; NbExp=3; IntAct=EBI-6447480, EBI-12029004; P35548; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-6447480, EBI-740924; P35548; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-6447480, EBI-11987469; P35548; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-6447480, EBI-372094; P35548; Q01974: ROR2; NbExp=3; IntAct=EBI-6447480, EBI-6422642; P35548; Q8WU79: SMAP2; NbExp=3; IntAct=EBI-6447480, EBI-2822515; P35548; P35711-4: SOX5; NbExp=3; IntAct=EBI-6447480, EBI-11954419; P35548; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-6447480, EBI-5235340; P35548; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-6447480, EBI-11746252; P35548; Q8NEK8: TENT5D; NbExp=3; IntAct=EBI-6447480, EBI-744726; P35548; Q08117-2: TLE5; NbExp=3; IntAct=EBI-6447480, EBI-11741437; P35548; O43711: TLX3; NbExp=3; IntAct=EBI-6447480, EBI-3939165; P35548; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-6447480, EBI-74615; P35548; Q86WV8: TSC1; NbExp=3; IntAct=EBI-6447480, EBI-12806590; P35548; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-6447480, EBI-3918381; P35548; Q14119: VEZF1; NbExp=3; IntAct=EBI-6447480, EBI-11980193; P35548; Q9BYJ9: YTHDF1; NbExp=3; IntAct=EBI-6447480, EBI-1051237; P35548; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-6447480, EBI-742550; P35548; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-6447480, EBI-10237226; Nucleus. Parietal foramina 1 (PFM1) [MIM:168500]: Autosomal dominant disease characterized by oval defects of the parietal bones caused by deficient ossification around the parietal notch, which is normally obliterated during the fifth fetal month. te=The disease is caused by variants affecting the gene represented in this entry. Parietal foramina with cleidocranial dysplasia (PFMCCD) [MIM:168550]: Combines skull defects in the form of enlarged parietal foramina and deficient ossification of the clavicles. Note=The disease is caused by variants affecting the gene represented in this entry. Craniosynostosis 2 (CRS2) [MIM:604757]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability. CRS2 is characterized by either fronto-orbital recession, or frontal bossing, or turribrachycephaly, or cloverleaf skull. Associated features include severe headache, high incidence of visual problems (myopia or hyperopia), and short first metatarsals. Intelligence is normal. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the Msh homeobox family. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding ossification osteoblast differentiation chondrocyte development osteoblast development outflow tract septum morphogenesis outflow tract morphogenesis epithelial to mesenchymal transition involved in endocardial cushion formation endochondral bone growth DNA binding transcription cofactor activity protein binding nucleus cytosol regulation of transcription, DNA-templated multicellular organism development transcription factor binding negative regulation of cell proliferation anterior/posterior pattern specification nuclear speck signal transduction involved in regulation of gene expression embryonic limb morphogenesis BMP signaling pathway positive regulation of BMP signaling pathway negative regulation of CREB transcription factor activity embryonic forelimb morphogenesis embryonic hindlimb morphogenesis wound healing, spreading of epidermal cells embryonic nail plate morphogenesis wound healing odontogenesis embryonic digit morphogenesis regulation of apoptotic process negative regulation of apoptotic process sequence-specific DNA binding transcription regulatory region DNA binding negative regulation of fat cell differentiation negative regulation of keratinocyte differentiation positive regulation of osteoblast differentiation negative regulation of transcription, DNA-templated embryonic morphogenesis stem cell differentiation cartilage development positive regulation of catagen bone trabecula formation bone morphogenesis cranial suture morphogenesis frontal suture morphogenesis branching involved in mammary gland duct morphogenesis mammary gland epithelium development BMP signaling pathway involved in heart development enamel mineralization cellular response to growth factor stimulus cellular response to estradiol stimulus activation of meiosis negative regulation of transcription regulatory region DNA binding positive regulation of mesenchymal cell apoptotic process uc003mcy.1 uc003mcy.2 uc003mcy.3 uc003mcy.4 uc003mcy.5 
ENST00000239316.4 INSL4 ENST00000239316.4 insulin like 4 (from RefSeq NM_002195.2) A8K678 ENST00000239316.1 ENST00000239316.2 ENST00000239316.3 INSL4_HUMAN NM_002195 Q14641 Q5W127 uc003ziy.1 uc003ziy.2 uc003ziy.3 uc003ziy.4 INSL4 encodes the insulin-like 4 protein, a member of the insulin superfamily. INSL4 encodes a precursor that undergoes post-translational cleavage to produce 3 polypeptide chains, A-C, that form tertiary structures composed of either all three chains, or just the A and B chains. Expression of INSL4 products occurs within the early placental cytotrophoblast and syncytiotrophoblast. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AU136752.2, AK291543.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142853, SAMEA2146236 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239316.4/ ENSP00000239316.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## May play an important role in trophoblast development and in the regulation of bone formation. Secreted Expressed in placenta, uterus and in fetal perichondrium. Expression levels were increased in both early placentas and molar pregnancies and were reduced in choriocarcinoma cells. Highly expressed in the early placenta. Expression of epil peptides in the villous cytotrophoblast is different from that displayed by the syncytiotrophoblast. In fetal tissues it was identified in the perichondrium of all four limbs, vertebrae, and ribs. It was abundant in interbone ligaments. Belongs to the insulin family. receptor binding insulin-like growth factor receptor binding hormone activity extracellular region extracellular space signal transduction cell-cell signaling positive regulation of chorionic trophoblast cell proliferation uc003ziy.1 uc003ziy.2 uc003ziy.3 uc003ziy.4 
ENST00000239347.3 IFNA7 ENST00000239347.3 interferon alpha 7 (from RefSeq NM_021057.2) ENST00000239347.1 ENST00000239347.2 IFNA7_HUMAN NM_021057 P01567 Q14607 Q5VV14 uc003zop.1 Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. Secreted. Belongs to the alpha/beta interferon family. adaptive immune response T cell activation involved in immune response natural killer cell activation involved in immune response cytokine activity cytokine receptor binding type I interferon receptor binding extracellular region extracellular space defense response humoral immune response cell-cell signaling blood coagulation response to virus cytokine-mediated signaling pathway B cell differentiation positive regulation of peptidyl-serine phosphorylation of STAT protein B cell proliferation response to exogenous dsRNA defense response to virus type I interferon signaling pathway uc003zop.1 
ENST00000239367.7 LRP11 ENST00000239367.7 LDL receptor related protein 11, transcript variant 1 (from RefSeq NM_032832.6) ENST00000239367.1 ENST00000239367.2 ENST00000239367.3 ENST00000239367.4 ENST00000239367.5 ENST00000239367.6 LRP11_HUMAN NM_032832 Q5VYC0 Q86VZ4 Q96SN6 uc003qng.1 uc003qng.2 uc003qng.3 uc003qng.4 Membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q86VZ4-1; Sequence=Displayed; Name=2; IsoId=Q86VZ4-2; Sequence=VSP_017535, VSP_017536; Belongs to the LDLR family. plasma membrane response to heat response to cold response to water deprivation response to mechanical stimulus membrane integral component of membrane multicellular organismal response to stress response to immobilization stress response to starvation phosphoprotein binding uc003qng.1 uc003qng.2 uc003qng.3 uc003qng.4 
ENST00000239374.8 CCDC170 ENST00000239374.8 coiled-coil domain containing 170 (from RefSeq NM_025059.4) C6orf97 CC170_HUMAN CCDC170 ENST00000239374.1 ENST00000239374.2 ENST00000239374.3 ENST00000239374.4 ENST00000239374.5 ENST00000239374.6 ENST00000239374.7 NM_025059 Q5VXB7 Q6P9E4 Q8IYT3 Q96KA9 Q9H5M3 uc003qol.1 uc003qol.2 uc003qol.3 uc003qol.4 uc003qol.5 The function of this gene and its encoded protein is not known. Several genome-wide association studies have implicated the region around this gene to be involved in breast cancer and bone mineral density, but no link to this specific gene has been found. [provided by RefSeq, May 2010]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC035003.2, SRR1803616.68769.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239374.8/ ENSP00000239374.6 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Plays a role in Golgi-associated microtubules organization and stabilization. Binds Golgi-associated microtubules. Q8IYT3; P51946: CCNH; NbExp=3; IntAct=EBI-2808089, EBI-741406; Q8IYT3; Q96I25: RBM17; NbExp=3; IntAct=EBI-2808089, EBI-740272; Golgi apparatus Sequence=BAB55025.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; protein binding uc003qol.1 uc003qol.2 uc003qol.3 uc003qol.4 uc003qol.5 
ENST00000239440.9 ARAP3 ENST00000239440.9 ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 3 (from RefSeq NM_022481.6) ARAP3_HUMAN B4DIT1 CENTD3 D3DQE3 ENST00000239440.1 ENST00000239440.2 ENST00000239440.3 ENST00000239440.4 ENST00000239440.5 ENST00000239440.6 ENST00000239440.7 ENST00000239440.8 NM_022481 Q8WWN8 uc003llm.1 uc003llm.2 uc003llm.3 uc003llm.4 uc003llm.5 This gene encodes a phosphoinositide binding protein containing ARF-GAP, RHO-GAP, RAS-associating, and pleckstrin homology domains. The ARF-GAP and RHO-GAP domains cooperate in mediating rearrangements in the cell cytoskeleton and cell shape. It is a specific PtdIns(3,4,5)P3/PtdIns(3,4)P2-stimulated Arf6-GAP protein. An alternatively spliced transcript has been found for this gene, but its biological validity has not been determined. [provided by RefSeq, Sep 2015]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AJ310567.1, AK290052.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239440.9/ ENSP00000239440.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase- activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts on ARF6, RAC1, RHOA and CDC42. Plays a role in the internalization of anthrax toxin. Interacts (via SAM domain) with INPPL1/SHIP2. Q8WWN8; Q96B97: SH3KBP1; NbExp=4; IntAct=EBI-4402732, EBI-346595; Cytoplasm Cytoplasm, cytoskeleton Cell membrane ; Peripheral membrane protein Cell projection, lamellipodium Cell projection, ruffle Note=Cytoplasmic, and associated with F-actin-rich membrane ruffles and lamellipodia. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8WWN8-1; Sequence=Displayed; Name=2; IsoId=Q8WWN8-2; Sequence=VSP_056214, VSP_056215; Tyrosine phosphorylated at a low basal level. PDGF treatment stimulates phosphorylation. Tyrosine phosphorylation is increased in cells that are in the process of becoming attached to a substrate and that start spreading and flattening (By similarity). ruffle GTPase activator activity protein binding phosphatidylinositol-3,4,5-trisphosphate binding cytoplasm cytosol cytoskeleton plasma membrane cytoskeleton organization signal transduction membrane vesicle-mediated transport lamellipodium cell projection phosphatidylinositol-3,4-bisphosphate binding positive regulation of GTPase activity metal ion binding regulation of small GTPase mediated signal transduction uc003llm.1 uc003llm.2 uc003llm.3 uc003llm.4 uc003llm.5 
ENST00000239444.4 PCDHB8 ENST00000239444.4 protocadherin beta 8 (from RefSeq NM_019120.5) B9EGV1 ENST00000239444.1 ENST00000239444.2 ENST00000239444.3 NM_019120 PCDB8_HUMAN PCDH3I PCDHB8 Q9UN66 uc011dai.1 uc011dai.2 uc011dai.3 uc011dai.4 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: BC136801.1, SRR1803614.254952.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239444.4/ ENSP00000239444.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain. Forms homodimers in trans (molecules expressed by two different cells). Forms promiscuous heterodimers in cis (at the plasma membrane of the same cell) with other protocadherins. Cell membrane ; Single-pass type I membrane protein Cadherin 1 to cadherin 4 domains mediate homophilic trans- interaction, the interaction with an identical protocadherin expressed by a neighboring cell. This is a head-to-tail interaction, the cadherin 1 domain interacting with the cadherin 4 domain and the cadherin 2 domain interacting the cadherin 3 domain of the other protocadherin. The cadherin 6 domain mediates promiscuous interactions with protocadherins on the same cell membrane. Each cadherin domain binds three calcium ions. calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules membrane integral component of membrane identical protein binding metal ion binding uc011dai.1 uc011dai.2 uc011dai.3 uc011dai.4 
ENST00000239446.6 PCDHB10 ENST00000239446.6 protocadherin beta 10 (from RefSeq NM_018930.4) ENST00000239446.1 ENST00000239446.2 ENST00000239446.3 ENST00000239446.4 ENST00000239446.5 NM_018930 PCDBA_HUMAN Q96T99 Q9UN67 UNQ1906/PRO4352 uc003lix.1 uc003lix.2 uc003lix.3 uc003lix.4 uc003lix.5 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: SRR1660805.27693.1, AK315583.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239446.6/ ENSP00000239446.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Cell membrane ; Single-pass type I membrane protein calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules chemical synaptic transmission synapse assembly membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules uc003lix.1 uc003lix.2 uc003lix.3 uc003lix.4 uc003lix.5 
ENST00000239449.7 PCDHB14 ENST00000239449.7 protocadherin beta 14 (from RefSeq NM_018934.4) B4DPE2 ENST00000239449.1 ENST00000239449.2 ENST00000239449.3 ENST00000239449.4 ENST00000239449.5 ENST00000239449.6 NM_018934 PCDBE_HUMAN Q4FZA4 Q4KN11 Q9Y5E9 uc003ljb.1 uc003ljb.2 uc003ljb.3 uc003ljb.4 uc003ljb.5 uc003ljb.6 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Q9Y5E9; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-10329013, EBI-357530; Q9Y5E9; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10329013, EBI-5916454; Q9Y5E9; P61978: HNRNPK; NbExp=6; IntAct=EBI-10329013, EBI-304185; Q9Y5E9; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-10329013, EBI-7060731; Q9Y5E9; O43390-2: HNRNPR; NbExp=3; IntAct=EBI-10329013, EBI-12236340; Q9Y5E9; O75525: KHDRBS3; NbExp=3; IntAct=EBI-10329013, EBI-722504; Q9Y5E9; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-10329013, EBI-3044087; Q9Y5E9; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-10329013, EBI-11522433; Q9Y5E9; O43586: PSTPIP1; NbExp=6; IntAct=EBI-10329013, EBI-1050964; Q9Y5E9; Q96QR8: PURB; NbExp=3; IntAct=EBI-10329013, EBI-2880222; Q9Y5E9; P38159: RBMX; NbExp=3; IntAct=EBI-10329013, EBI-743526; Q9Y5E9; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-10329013, EBI-8638511; Q9Y5E9; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-10329013, EBI-11994018; Q9Y5E9; Q15415: RBMY1J; NbExp=6; IntAct=EBI-10329013, EBI-8642021; Q9Y5E9; P84103: SRSF3; NbExp=3; IntAct=EBI-10329013, EBI-372557; Q9Y5E9; P62995: TRA2B; NbExp=3; IntAct=EBI-10329013, EBI-725485; Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y5E9-1; Sequence=Displayed; Name=2; IsoId=Q9Y5E9-2; Sequence=VSP_055932; calcium ion binding protein binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules chemical synaptic transmission synapse assembly membrane integral component of membrane calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules uc003ljb.1 uc003ljb.2 uc003ljb.3 uc003ljb.4 uc003ljb.5 uc003ljb.6 
ENST00000239450.4 PCDHB12 ENST00000239450.4 protocadherin beta 12 (from RefSeq NM_018932.4) B4DDU1 ENST00000239450.1 ENST00000239450.2 ENST00000239450.3 NM_018932 PCDBC_HUMAN Q9Y5F1 uc003liz.1 uc003liz.2 uc003liz.3 uc003liz.4 This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript is intronless :: BC045637.1, SRR1660807.225080.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239450.4/ ENSP00000239450.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. Q9Y5F1; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-12012016, EBI-2548012; Q9Y5F1; P0C7W6: CCDC172; NbExp=3; IntAct=EBI-12012016, EBI-2548868; Q9Y5F1; Q9BT78: COPS4; NbExp=3; IntAct=EBI-12012016, EBI-742413; Q9Y5F1; Q15006: EMC2; NbExp=3; IntAct=EBI-12012016, EBI-359031; Q9Y5F1; P23527: H2BC17; NbExp=3; IntAct=EBI-12012016, EBI-1642161; Q9Y5F1; P08727: KRT19; NbExp=3; IntAct=EBI-12012016, EBI-742756; Q9Y5F1; Q9Y6N9-4: USH1C; NbExp=3; IntAct=EBI-12012016, EBI-11523636; Q9Y5F1; Q3MJ62: ZSCAN23; NbExp=3; IntAct=EBI-12012016, EBI-5667532; Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y5F1-1; Sequence=Displayed; Name=2; IsoId=Q9Y5F1-2; Sequence=VSP_053862; calcium ion binding plasma membrane integral component of plasma membrane cell adhesion homophilic cell adhesion via plasma membrane adhesion molecules nervous system development membrane integral component of membrane uc003liz.1 uc003liz.2 uc003liz.3 uc003liz.4 
ENST00000239451.7 SLC25A2 ENST00000239451.7 solute carrier family 25 member 2 (from RefSeq NM_031947.4) ENST00000239451.1 ENST00000239451.2 ENST00000239451.3 ENST00000239451.4 ENST00000239451.5 ENST00000239451.6 NM_031947 ORC2 ORNT2 ORNT2_HUMAN Q496C1 Q6XUI0 Q8NFZ2 Q9BXI2 SLC25A2 uc003ljf.1 uc003ljf.2 uc003ljf.3 uc003ljf.4 This intronless gene encodes a protein that localizes to the mitochondrial inner membrane and likely functions as a transporter of small molecules such as ornithine. This gene is located between the protocadherin beta and gamma gene clusters on chromosome 5. [provided by RefSeq, Dec 2014]. ##Evidence-Data-START## Transcript is intronless :: SRR5189667.155397.1, AF378119.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000239451.7/ ENSP00000239451.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Mitochondrial transporter of the positively charged amino acids ornithine, lysine and arginine, and the neutral amino acid citrulline (PubMed:12807890). In addition, transports the basic amino acids histidine, homoarginine, and asymmetric dimethylarginine (aDMA), but not symmetric DMA, and the D-forms of lysine, arginine, ornithine and histidine (PubMed:26403849, PubMed:12807890). Functions by both counter-exchange and uniport mechanisms (PubMed:26403849). Reaction=L-lysine(in) + L-ornithine(out) = L-lysine(out) + L- ornithine(in); Xref=Rhea:RHEA:70799, ChEBI:CHEBI:32551, ChEBI:CHEBI:46911; Evidence=; Reaction=H(+)(in) + L-histidine(in) + L-ornithine(out) = H(+)(out) + L- histidine(out) + L-ornithine(in); Xref=Rhea:RHEA:70815, ChEBI:CHEBI:15378, ChEBI:CHEBI:46911, ChEBI:CHEBI:57595; Evidence=; Reaction=L-homoarginine(in) + L-ornithine(out) = L-homoarginine(out) + L-ornithine(in); Xref=Rhea:RHEA:70819, ChEBI:CHEBI:46911, ChEBI:CHEBI:143006; Evidence=; Reaction=H(+)(in) + L-citrulline(in) + L-ornithine(out) = H(+)(out) + L-citrulline(out) + L-ornithine(in); Xref=Rhea:RHEA:70787, ChEBI:CHEBI:15378, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743; Evidence=; Reaction=L-arginine(out) + N(omega),N(omega)-dimethyl-L-arginine(in) = L-arginine(in) + N(omega),N(omega)-dimethyl-L-arginine(out); Xref=Rhea:RHEA:72811, ChEBI:CHEBI:32682, ChEBI:CHEBI:58326; Evidence=; Reaction=L-lysine(out) + N(omega),N(omega)-dimethyl-L-arginine(in) = L- lysine(in) + N(omega),N(omega)-dimethyl-L-arginine(out); Xref=Rhea:RHEA:72815, ChEBI:CHEBI:32551, ChEBI:CHEBI:58326; Evidence=; Reaction=L-ornithine(out) + N(omega),N(omega)-dimethyl-L-arginine(in) = L-ornithine(in) + N(omega),N(omega)-dimethyl-L-arginine(out); Xref=Rhea:RHEA:72819, ChEBI:CHEBI:46911, ChEBI:CHEBI:58326; Evidence=; Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence= Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935, ChEBI:CHEBI:32551; Evidence= Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199, ChEBI:CHEBI:46911; Evidence= Reaction=D-lysine(in) + L-ornithine(out) = D-lysine(out) + L- ornithine(in); Xref=Rhea:RHEA:73483, ChEBI:CHEBI:32557, ChEBI:CHEBI:46911; Evidence=; Reaction=D-histidine(in) + H(+)(in) + L-ornithine(out) = D- histidine(out) + H(+)(out) + L-ornithine(in); Xref=Rhea:RHEA:73479, ChEBI:CHEBI:15378, ChEBI:CHEBI:46911, ChEBI:CHEBI:142967; Evidence=; Reaction=D-arginine(in) + L-ornithine(out) = D-arginine(out) + L- ornithine(in); Xref=Rhea:RHEA:73475, ChEBI:CHEBI:32689, ChEBI:CHEBI:46911; Evidence=; Reaction=D-ornithine(in) + L-ornithine(out) = D-ornithine(out) + L- ornithine(in); Xref=Rhea:RHEA:73471, ChEBI:CHEBI:46911, ChEBI:CHEBI:57668; Evidence=; Inhibited by pyridoxal 5'-phosphate, N- ethylmaleimide, spermine and spermidine. Kinetic parameters: KM=0.4 mM for L-ornithine ; KM=0.71 mM for L-arginine ; KM=1.28 mM for L-histidine ; KM=0.32 mM for L-lysine ; Vmax=1200 umol/min/g enzyme with L-ornithine as substrate ; Vmax=1200 umol/min/g enzyme with L-arginine as substrate ; Vmax=1200 umol/min/g enzyme with L-histidine as substrate ; Vmax=1200 umol/min/g enzyme with L-lysine as substrate ; Q9BXI2; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-17590310, EBI-17589229; Mitochondrion membrane ; Multi-pass membrane protein Mitochondrion inner membrane ; Multi-pass membrane protein Expressed in liver, testis, spleen, lung, pancreas, and small intestine and expressed poorly in other tissues. In mice, SLC25A2/ORNT2 is a pseudogene. Belongs to the mitochondrial carrier (TC 2.A.29) family. urea cycle L-ornithine transmembrane transporter activity mitochondrion mitochondrial inner membrane membrane integral component of membrane mitochondrial L-ornithine transmembrane transport uc003ljf.1 uc003ljf.2 uc003ljf.3 uc003ljf.4 
ENST00000239461.11 PRRX1 ENST00000239461.11 paired related homeobox 1, transcript variant pmx-1b (from RefSeq NM_022716.4) B5BUM7 ENST00000239461.1 ENST00000239461.10 ENST00000239461.2 ENST00000239461.3 ENST00000239461.4 ENST00000239461.5 ENST00000239461.6 ENST00000239461.7 ENST00000239461.8 ENST00000239461.9 NM_022716 O60807 P54821 PMX1 PRRX1_HUMAN uc001ghf.1 uc001ghf.2 uc001ghf.3 uc001ghf.4 uc001ghf.5 The DNA-associated protein encoded by this gene is a member of the paired family of homeobox proteins localized to the nucleus. The protein functions as a transcription co-activator, enhancing the DNA-binding activity of serum response factor, a protein required for the induction of genes by growth and differentiation factors. The protein regulates muscle creatine kinase, indicating a role in the establishment of diverse mesodermal muscle types. Alternative splicing yields two isoforms that differ in abundance and expression patterns. [provided by RefSeq, Jul 2008]. Master transcription factor of stromal fibroblasts for myofibroblastic lineage progression. Orchestrates the functional drift of fibroblasts into myofibroblastic phenotype via TGF-beta signaling by remodeling a super-enhancer landscape. Through this function, plays an essential role in wound healing process (PubMed:35589735). Acts as a transcriptional regulator of muscle creatine kinase (MCK) and so has a role in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer (By similarity). May play a role in homeostasis and regeneration of bone, white adipose tissue and derm (By similarity). [Isoform 1]: Transcriptional activator, when transfected in fibroblastic or myoblastic cell lines. This activity may be masked by the C-terminal OAR domain. [Isoform 2]: Transcriptional repressor, when transfected in fibroblastic or myoblastic cell lines. Interacts with SMAD3. P54821; Q9BW66: CINP; NbExp=3; IntAct=EBI-12828023, EBI-739784; P54821; P51687: SUOX; NbExp=3; IntAct=EBI-12828023, EBI-3921347; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=PRRX1a , PMX1-B ; IsoId=P54821-1; Sequence=Displayed; Name=2; Synonyms=PRRX1b ; IsoId=P54821-2; Sequence=VSP_002278; [Isoform 1]: Widely expressed in embryonic and adult tissues, with highest levels in skeletal muscle. Isoform 1 is either expressed at similar or higher levels compared to isoform 2 in all embryonic tissues but skeletal muscle and heart. In adult tissues, expressed at lower levels compared to isoform 2. [Isoform 2]: Widely expressed in embryonic and adult tissues, with highest levels in skeletal muscle. Isoform 2 is either expressed at similar or lower levels compared to isoform 1 in all embryonic tissues but skeletal muscle and heart, where it is expressed at higher levels. In adult tissues, expressed at higher levels compared to isoform 1. Agnathia-otocephaly complex (AGOTC) [MIM:202650]: A rare condition characterized by mandibular hypoplasia or agnathia, ventromedial auricular malposition (melotia) and/or auricular fusion (synotia), and microstomia with oroglossal hypoplasia or aglossia. Holoprosencephaly is the most commonly identified association, but skeletal, genitourinary, and cardiovascular anomalies, and situs inversus have been reported. The disorder is almost always lethal. Note=The disease is caused by variants affecting the gene represented in this entry. Note=Strongly expressed in cancer-associated fibroblasts (CAFs) in various cancer types. Its expression correlates with unfavorable clinical outcome. May be essential for the tumorigenicity and metastasis-inducing capacity of CAFs. Can reprogram tumor- suppressive normal fibroblasts into CAFs. Belongs to the paired homeobox family. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding positive regulation of mesenchymal cell proliferation DNA binding transcription coactivator activity nucleus nucleoplasm cytosol regulation of transcription, DNA-templated multicellular organism development embryonic limb morphogenesis inner ear morphogenesis middle ear morphogenesis sequence-specific DNA binding positive regulation of smoothened signaling pathway positive regulation of transcription from RNA polymerase II promoter neuron fate determination embryonic cranial skeleton morphogenesis embryonic skeletal system morphogenesis artery morphogenesis cartilage development palate development regulation of neuron projection regeneration HMG box domain binding neuronal stem cell population maintenance uc001ghf.1 uc001ghf.2 uc001ghf.3 uc001ghf.4 uc001ghf.5 
ENST00000239462.9 TNN ENST00000239462.9 tenascin N (from RefSeq NM_022093.2) A0A0A6YY94 B9EGP3 ENST00000239462.1 ENST00000239462.2 ENST00000239462.3 ENST00000239462.4 ENST00000239462.5 ENST00000239462.6 ENST00000239462.7 ENST00000239462.8 NM_022093 Q5R360 Q9UQP3 TENN_HUMAN TNN TNW uc001gkl.1 uc001gkl.2 Extracellular matrix protein that seems to be a ligand for ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1 (By similarity) (PubMed:17909022). Involved in neurite outgrowth and cell migration in hippocampal explants (By similarity). During endochondral bone formation, inhibits proliferation and differentiation of proteoblasts mediated by canonical WNT signaling (By similarity). In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells (PubMed:19884327). Expressed in most mammary tumors, may facilitate tumorigenesis by supporting the migratory behavior of breast cancer cells (PubMed:17909022). Homohexamer. Secreted, extracellular space, extracellular matrix Not detected in normal adult mammary tissues or brain but expressed in most breast tumors and brain tumors, such as glioblastomas, astrocytomas and oligodendrogliomas, tested (PubMed:17909022, PubMed:19884327). In brain tumors, detected around the endothelial cell layer of the clood vessels (PubMed:19884327). Belongs to the tenascin family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44209/TNN"; osteoblast development molecular_function integrin binding cellular_component extracellular region cell-matrix adhesion axonogenesis cell surface extracellular matrix negative regulation of osteoblast proliferation identical protein binding neuron projection neuronal cell body negative regulation of osteoblast differentiation dendrite self-avoidance CA3 pyramidal cell dendrite negative regulation of canonical Wnt signaling pathway involved in osteoblast differentiation hippocampal mossy fiber expansion negative regulation of neuron migration uc001gkl.1 uc001gkl.2 
ENST00000239587.10 TTLL2 ENST00000239587.10 tubulin tyrosine ligase like 2, transcript variant 1 (from RefSeq NM_031949.5) B2RB11 B3KS77 C6orf104 ENST00000239587.1 ENST00000239587.2 ENST00000239587.3 ENST00000239587.4 ENST00000239587.5 ENST00000239587.6 ENST00000239587.7 ENST00000239587.8 ENST00000239587.9 NM_031949 Q7Z6R8 Q86X22 Q9BWV7 TTLL2 TTLL2_HUMAN uc003qvs.1 uc003qvs.2 uc003qvs.3 Probable tubulin polyglutamylase that generates side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of target proteins (By similarity). Similar to TTLL1, may acquire enzymatic activity only in complex with other proteins as it is most likely lacking domains important for autonomous activity (By similarity). Probably involved in the side-chain initiation step of the polyglutamylation reaction rather than the elongation step (By similarity). Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Testis. Arg-218 is the main determinant for regioselectivity, which segregates between initiases and elongases in all tubulin--tyrosine ligase family. A glutamine residue at this position is found in elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate- chain elongation, whereas an arginine residue is found in initiases TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation. Belongs to the tubulin--tyrosine ligase family. nucleotide binding ATP binding cellular protein modification process ligase activity uc003qvs.1 uc003qvs.2 uc003qvs.3 
ENST00000239666.9 PDZD11 ENST00000239666.9 PDZ domain containing 11, transcript variant 1 (from RefSeq NM_016484.5) AIPP1 D3DVU3 ENST00000239666.1 ENST00000239666.2 ENST00000239666.3 ENST00000239666.4 ENST00000239666.5 ENST00000239666.6 ENST00000239666.7 ENST00000239666.8 HSPC227 NM_016484 PDZ11_HUMAN PDZK11 PISP Q5EBL8 Q6UWE1 Q9P0Q1 UNQ6486/PRO21335 uc004dyd.1 uc004dyd.2 uc004dyd.3 Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10- binding protein TSPAN33. Interacts with ATP2B1, ATP2B2, ATP2B3, ATP2B4 and ATP7A (PubMed:12763866, PubMed:16051599). Interacts with PLEKHA7 (via WW domains) at zonula adherens; this interaction is essential for the interaction between PLEKHA7 and the ADAM10-binding protein TSPAN33 (PubMed:30463011). Interacts with SLC5A6 (PubMed:21183659). Q5EBL8; Q04656: ATP7A; NbExp=4; IntAct=EBI-1644207, EBI-7706409; Q5EBL8; Q86UL8-2: MAGI2; NbExp=3; IntAct=EBI-1644207, EBI-12081182; Q5EBL8; Q9HAU0: PLEKHA5; NbExp=11; IntAct=EBI-1644207, EBI-945934; Q5EBL8; Q9Y289: SLC5A6; NbExp=6; IntAct=EBI-1644207, EBI-3915941; [Isoform 2]: Secreted [Isoform 1]: Cytoplasm Cell junction, adherens junction Cell membrane Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=AIPP1a; IsoId=Q5EBL8-1; Sequence=Displayed; Name=2; Synonyms=AIPP1b; IsoId=Q5EBL8-2; Sequence=VSP_015077; Widely expressed (at protein level). protein binding extracellular region cytoplasm cytosol plasma membrane cell-cell junction adherens junction biotin metabolic process neurotransmitter secretion protein C-terminus binding pantothenate metabolic process membrane basolateral plasma membrane antimicrobial humoral response cell junction ion transmembrane transport maintenance of epithelial cell apical/basal polarity synapse pore complex pore complex assembly transmembrane transport presynapse protein localization to basolateral plasma membrane uc004dyd.1 uc004dyd.2 uc004dyd.3 
ENST00000239690.9 NUDCD1 ENST00000239690.9 NudC domain containing 1, transcript variant 1 (from RefSeq NM_032869.4) B4DVX6 CML66 ENST00000239690.1 ENST00000239690.2 ENST00000239690.3 ENST00000239690.4 ENST00000239690.5 ENST00000239690.6 ENST00000239690.7 ENST00000239690.8 NM_032869 NUDC1_HUMAN NUDCD1 Q4G130 Q8NDQ5 Q8NG18 Q96RS6 Q96SI4 Q9BVR5 uc003ynb.1 uc003ynb.2 uc003ynb.3 uc003ynb.4 uc003ynb.5 uc003ynb.6 Q96RS6; P53618: COPB1; NbExp=3; IntAct=EBI-2512429, EBI-359063; Q96RS6; Q9Y678: COPG1; NbExp=2; IntAct=EBI-2512429, EBI-1049127; Q96RS6; Q92620: DHX38; NbExp=2; IntAct=EBI-2512429, EBI-1043041; Q96RS6-1; O43143: DHX15; NbExp=2; IntAct=EBI-20724008, EBI-1237044; [Isoform 1]: Cytoplasm. Nucleus. [Isoform 2]: Cytoplasm. [Isoform 3]: Cytoplasm. Nucleus. Event=Alternative splicing; Named isoforms=3; Name=1 ; Synonyms=CML66-L ; IsoId=Q96RS6-1; Sequence=Displayed; Name=2 ; Synonyms=CML66-S ; IsoId=Q96RS6-2; Sequence=VSP_052558, VSP_052559; Name=3 ; IsoId=Q96RS6-3; Sequence=VSP_052557, VSP_052560; Isoform 1 is specifically expressed in leukemias and a variety of solid tumor cell lines and is also detected in testis and heart. Isoform 2 is predominantly expressed in testis and weakly expressed in tumor cells. Isoform 1 is the dominant immunogenic isoform and is capable of eliciting a humoral response in individuals with a variety of solid tumors. Expression of isoform 1 in a wide variety of malignancies as well as the presence of an immunogenic epitope suggest that it may be a suitable target for antigen-specific immunotherapy. [Isoform 3]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. immune system process protein binding nucleus nucleoplasm cytoplasm cytosol uc003ynb.1 uc003ynb.2 uc003ynb.3 uc003ynb.4 uc003ynb.5 uc003ynb.6 
ENST00000239830.9 CCDC77 ENST00000239830.9 coiled-coil domain containing 77, transcript variant 1 (from RefSeq NM_032358.4) B4DDE8 CCD77_HUMAN ENST00000239830.1 ENST00000239830.2 ENST00000239830.3 ENST00000239830.4 ENST00000239830.5 ENST00000239830.6 ENST00000239830.7 ENST00000239830.8 NM_032358 Q9BR77 uc001qig.1 uc001qig.2 uc001qig.3 uc001qig.4 uc001qig.5 Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BR77-1; Sequence=Displayed; Name=2; IsoId=Q9BR77-2; Sequence=VSP_043135; centrosome membrane uc001qig.1 uc001qig.2 uc001qig.3 uc001qig.4 uc001qig.5 
ENST00000239859.8 CCDC169 ENST00000239859.8 coiled-coil domain containing 169, transcript variant 1 (from RefSeq NM_001144981.3) A6NC13 A6NCT2 A6NNP5 B7ZW45 B7ZW49 B9EJF2 C13orf38 CC169_HUMAN ENST00000239859.1 ENST00000239859.2 ENST00000239859.3 ENST00000239859.4 ENST00000239859.5 ENST00000239859.6 ENST00000239859.7 NM_001144981 Q9H1T4 Q9H1T5 uc010abm.1 uc010abm.2 uc010abm.3 uc010abm.4 uc010abm.5 Event=Alternative splicing; Named isoforms=6; Name=1; IsoId=A6NNP5-1; Sequence=Displayed; Name=2; IsoId=A6NNP5-2; Sequence=VSP_035636, VSP_035637; Name=3; IsoId=A6NNP5-3; Sequence=VSP_040479, VSP_040480; Name=4; IsoId=A6NNP5-4; Sequence=VSP_040480; Name=5; IsoId=A6NNP5-5; Sequence=VSP_040479; Name=6; IsoId=A6NNP5-6; Sequence=VSP_043810, VSP_043811, VSP_040480; Belongs to the CCDC169 family. uc010abm.1 uc010abm.2 uc010abm.3 uc010abm.4 uc010abm.5 
ENST00000239878.9 UFM1 ENST00000239878.9 ubiquitin fold modifier 1, transcript variant 7 (from RefSeq NR_104585.2) BM-002 C13orf20 ENST00000239878.1 ENST00000239878.2 ENST00000239878.3 ENST00000239878.4 ENST00000239878.5 ENST00000239878.6 ENST00000239878.7 ENST00000239878.8 NR_104585 P61960 Q14346 Q5VXS0 Q6IAG6 Q9CPX2 Q9NZF2 UFM1 UFM1_HUMAN uc001uwu.1 uc001uwu.2 uc001uwu.3 uc001uwu.4 uc001uwu.5 uc001uwu.6 UFM1 is a ubiquitin-like protein that is conjugated to target proteins by E1-like activating enzyme UBA5 (UBE1DC1; MIM 610552) and E2-like conjugating enzyme UFC1 (MIM 610554) in a manner analogous to ubiquitylation (see UBE2M; MIM 603173) (Komatsu et al., 2004 [PubMed 15071506]).[supplied by OMIM, Dec 2008]. Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer (PubMed:15071506, PubMed:20018847, PubMed:29868776, PubMed:27653677). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847, PubMed:29868776, PubMed:27653677). Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:32160526). Ufmylation of TRIP4 regulates nuclear receptors-mediated transcription (PubMed:25219498). Interacts with UBA5 (PubMed:26872069, PubMed:29295865, PubMed:27653677, PubMed:26929408, PubMed:28360427, PubMed:30412706). Interacts with UFC1 (PubMed:29868776). P61960; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1045061, EBI-6509505; P61960; Q4G0X4: KCTD21; NbExp=3; IntAct=EBI-1045061, EBI-11976683; P61960; Q9GZZ9: UBA5; NbExp=4; IntAct=EBI-1045061, EBI-747805; Nucleus Cytoplasm Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P61960-1; Sequence=Displayed; Name=2; IsoId=P61960-2; Sequence=VSP_041186; Up-regulated by thapsigargin. Leukodystrophy, hypomyelinating, 14 (HLD14) [MIM:617899]: An autosomal recessive, severe disorder characterized by atrophy of the basal ganglia and cerebellum, hypomyelination, severe developmental delay, typically without intentional movements and language development, and microcephaly. Almost all patients exhibit spasticity, extrapyramidal movement abnormalities, and severe drug-resistant epilepsy. Disease onset is early in infancy, and most patients die in the first years of life. te=The disease is caused by variants affecting the gene represented in this entry. The disease-causing variant may be a homozygous 3-bp deletion in the promoter region of the UFM1 gene, which segregates with the disorder in affected families. In vitro expression studies in different cell lines showed that the mutation significantly reduces transcriptional activity in certain neuronal cell lines (SY5Y and U373), but not in other cell lines, including HeLa and HOF-F2. Belongs to the UFM1 family. protein binding nucleus cytoplasm endoplasmic reticulum brain development regulation of intracellular estrogen receptor signaling pathway response to endoplasmic reticulum stress negative regulation of apoptotic process protein ufmylation protein K69-linked ufmylation uc001uwu.1 uc001uwu.2 uc001uwu.3 uc001uwu.4 uc001uwu.5 uc001uwu.6 
ENST00000239882.7 ELF1 ENST00000239882.7 E74 like ETS transcription factor 1, transcript variant 1 (from RefSeq NM_172373.4) B4E2I5 E9PDQ9 ELF1_HUMAN ENST00000239882.1 ENST00000239882.2 ENST00000239882.3 ENST00000239882.4 ENST00000239882.5 ENST00000239882.6 NM_172373 P32519 Q8N6F6 Q9UDE1 uc001uxs.1 uc001uxs.2 uc001uxs.3 uc001uxs.4 uc001uxs.5 This gene encodes an E26 transformation-specific related transcription factor. The encoded protein is primarily expressed in lymphoid cells and acts as both an enhancer and a repressor to regulate transcription of various genes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2009]. Transcription factor that activates the LYN and BLK promoters. Appears to be required for the T-cell-receptor-mediated trans activation of HIV-2 gene expression. Binds specifically to two purine-rich motifs in the HIV-2 enhancer. Binds to the underphosphorylated form of RB. May interact with other transcription factors in order to regulate specific genes. Interacts with RUNX1. P32519; P31276: HOXC13; NbExp=3; IntAct=EBI-765526, EBI-2293590; P32519; Q13952-2: NFYC; NbExp=3; IntAct=EBI-765526, EBI-11956831; P32519; P08047: SP1; NbExp=2; IntAct=EBI-765526, EBI-298336; Nucleus. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P32519-1; Sequence=Displayed; Name=2; IsoId=P32519-2; Sequence=VSP_045682; In fetal tissues, it is highly expressed in heart, lung liver and kidney, and weakly expressed in brain. In adult, it is highly expressed in pancreas, spleen, thymus and peripheral blood leukocytes, expressed at moderate levels in heart, placenta, lung, liver, skeletal muscle, kidney, prostate, ovary, small intestine and colon, and weakly expressed in brain and testis. Belongs to the ETS family. nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding regulation of cytokine production regulation of cytokine-mediated signaling pathway DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter cell differentiation sequence-specific DNA binding positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter regulation of B cell receptor signaling pathway negative regulation of T cell receptor signaling pathway uc001uxs.1 uc001uxs.2 uc001uxs.3 uc001uxs.4 uc001uxs.5 
ENST00000239891.4 ALG5 ENST00000239891.4 ALG5 dolichyl-phosphate beta-glucosyltransferase, transcript variant 1 (from RefSeq NM_013338.5) ALG5_HUMAN B4DR37 ENST00000239891.1 ENST00000239891.2 ENST00000239891.3 HSPC149 NM_013338 Q5TBA6 Q9Y673 uc001uvy.1 uc001uvy.2 uc001uvy.3 uc001uvy.4 uc001uvy.5 This gene encodes a member of the glycosyltransferase 2 family. The encoded protein participates in glucosylation of the oligomannose core in N-linked glycosylation of proteins. The addition of glucose residues to the oligomannose core is necessary to ensure substrate recognition, and therefore, effectual transfer of the oligomannose core to the nascent glycoproteins. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2008]. Required for the assembly of lipid-linked oligosaccharides in kidney epithelial cells, and protein N-glycosylation. Required for polycystin-1 (PKD1) glycosylation and maturation. Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta- D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA- COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117; Protein modification; protein glycosylation. Q9Y673; P0DTC3: 3a; Xeno; NbExp=4; IntAct=EBI-11725055, EBI-25475894; Endoplasmic reticulum membrane ; Single-pass type II membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y673-1; Sequence=Displayed; Name=2; IsoId=Q9Y673-2; Sequence=VSP_041019; Expressed in pancreas, placenta, liver, heart, brain, kidney, skeletal muscle, and lung. Polycystic kidney disease 7 (PKD7) [MIM:620056]: A form of polycystic kidney disease, a disorder characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occur in other organs, particularly the liver. PKD7 inheritance is autosomal dominant. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyltransferase 2 family. oligosaccharyl transferase activity dolichyl-phosphate beta-glucosyltransferase activity endoplasmic reticulum endoplasmic reticulum membrane protein glycosylation protein N-linked glycosylation determination of left/right symmetry membrane integral component of membrane transferase activity transferase activity, transferring glycosyl groups protein N-linked glycosylation via asparagine uc001uvy.1 uc001uvy.2 uc001uvy.3 uc001uvy.4 uc001uvy.5 
ENST00000239906.10 FAM53C ENST00000239906.10 family with sequence similarity 53 member C, transcript variant 2 (from RefSeq NM_016605.3) B2RDJ5 C5orf6 D3DQB9 ENST00000239906.1 ENST00000239906.2 ENST00000239906.3 ENST00000239906.4 ENST00000239906.5 ENST00000239906.6 ENST00000239906.7 ENST00000239906.8 ENST00000239906.9 FA53C_HUMAN FAM53C NM_016605 Q9NYF3 uc003lcw.1 uc003lcw.2 uc003lcw.3 uc003lcw.4 uc003lcw.5 The protein encoded by this gene belongs to the FAM53 protein family. FAM53 protein family members bind to a transcriptional regulator that modulates cell proliferation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2017]. Q9NYF3; V9HW98: HEL2; NbExp=3; IntAct=EBI-1644252, EBI-10190883; Q9NYF3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1644252, EBI-16439278; Q9NYF3; O43639: NCK2; NbExp=8; IntAct=EBI-1644252, EBI-713635; Q9NYF3; P31947: SFN; NbExp=3; IntAct=EBI-1644252, EBI-476295; Q9NYF3; O60504: SORBS3; NbExp=3; IntAct=EBI-1644252, EBI-741237; Q9NYF3; P61981: YWHAG; NbExp=7; IntAct=EBI-1644252, EBI-359832; Belongs to the FAM53 family. protein binding nucleus protein import into nucleus uc003lcw.1 uc003lcw.2 uc003lcw.3 uc003lcw.4 uc003lcw.5 
ENST00000239926.9 MYOT ENST00000239926.9 myotilin, transcript variant 1 (from RefSeq NM_006790.3) A0A0C4DFM5 A0A0C4DFM5_HUMAN ENST00000239926.1 ENST00000239926.2 ENST00000239926.3 ENST00000239926.4 ENST00000239926.5 ENST00000239926.6 ENST00000239926.7 ENST00000239926.8 MYOT NM_006790 hCG_39937 uc003lbv.1 uc003lbv.2 uc003lbv.3 uc003lbv.4 uc003lbv.5 This gene encodes a cystoskeletal protein which plays a significant role in the stability of thin filaments during muscle contraction. This protein binds F-actin, crosslinks actin filaments, and prevents latrunculin A-induced filament disassembly. Mutations in this gene have been associated with limb-girdle muscular dystrophy and myofibrillar myopathies. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.[provided by RefSeq, Oct 2008]. Z disc uc003lbv.1 uc003lbv.2 uc003lbv.3 uc003lbv.4 uc003lbv.5 
ENST00000239938.5 EGR1 ENST00000239938.5 early growth response 1 (from RefSeq NM_001964.3) EGR1 ENST00000239938.1 ENST00000239938.2 ENST00000239938.3 ENST00000239938.4 NM_001964 Q546S1 Q546S1_HUMAN hCG_18777 uc003ldb.1 uc003ldb.2 uc003ldb.3 The protein encoded by this gene belongs to the EGR family of C2H2-type zinc-finger proteins. It is a nuclear protein and functions as a transcriptional regulator. The products of target genes it activates are required for differentitation and mitogenesis. Studies suggest this is a cancer suppressor gene. [provided by RefSeq, Dec 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M62829.1, X52541.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000239938.5/ ENSP00000239938.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Cytoplasm Nucleus Belongs to the EGR C2H2-type zinc-finger protein family. negative regulation of transcription from RNA polymerase II promoter RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding response to hypoxia response to ischemia nucleic acid binding DNA binding transcription factor activity, sequence-specific DNA binding nucleus nucleoplasm regulation of transcription, DNA-templated response to glucose T cell differentiation BMP signaling pathway response to insulin circadian regulation of gene expression skeletal muscle cell differentiation regulation of apoptotic process transcription regulatory region DNA binding estrous cycle positive regulation of chemokine biosynthetic process locomotor rhythm positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter metal ion binding positive regulation of hormone biosynthetic process positive regulation of interleukin-1 beta biosynthetic process circadian temperature homeostasis regulation of transcription from RNA polymerase II promoter in response to hypoxia cellular response to organic substance cellular response to gamma radiation negative regulation of canonical Wnt signaling pathway positive regulation of neuron death positive regulation of tau-protein kinase activity regulation of progesterone biosynthetic process uc003ldb.1 uc003ldb.2 uc003ldb.3 
ENST00000239940.12 PFN2 ENST00000239940.12 profilin 2, transcript variant 1 (from RefSeq NM_053024.4) B2R4C8 D3DNI4 ENST00000239940.1 ENST00000239940.10 ENST00000239940.11 ENST00000239940.2 ENST00000239940.3 ENST00000239940.4 ENST00000239940.5 ENST00000239940.6 ENST00000239940.7 ENST00000239940.8 ENST00000239940.9 NM_053024 P35080 PROF2_HUMAN Q4VBQ4 Q8WVF9 Q9HBK2 uc003ext.1 uc003ext.2 uc003ext.3 uc003ext.4 The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. There are two alternatively spliced transcript variants encoding different isoforms described for this gene. [provided by RefSeq, Jul 2008]. Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio (PubMed:7758455). Interacts with PFN2 (By similarity). [Isoform IIa]: Interacts with ACTMAP (via N-terminus); the interaction may facilitate efficient cleavage of the acetylated N- terminus of immature actin by ACTMAP. [Isoform IIb]: Interacts with ACTMAP (via N-terminus); the interaction may facilitate efficient cleavage of the acetylated N- terminus of immature actin by ACTMAP. P35080; Q14789: GOLGB1; NbExp=2; IntAct=EBI-473138, EBI-709973; P35080; P42858: HTT; NbExp=7; IntAct=EBI-473138, EBI-466029; P35080; O08816: Wasl; Xeno; NbExp=3; IntAct=EBI-473138, EBI-6142604; Cytoplasm, cytoskeleton. Event=Alternative splicing; Named isoforms=2; Name=IIa; IsoId=P35080-1; Sequence=Displayed; Name=IIb; IsoId=P35080-2; Sequence=VSP_005217; Highly expressed in brain, skeletal muscle and kidney and less strongly in heart, placenta, lung and liver. Belongs to the profilin family. actin binding actin monomer binding protein binding phosphatidylinositol-4,5-bisphosphate binding cytoplasm cytoskeleton negative regulation of epithelial cell migration ATPase activity actin cytoskeleton organization regulation of actin filament polymerization negative regulation of actin filament polymerization positive regulation of actin filament polymerization positive regulation of actin filament bundle assembly positive regulation of ATPase activity positive regulation of peptidyl-serine phosphorylation protein stabilization positive regulation of stress fiber assembly extracellular exosome presynapse postsynapse modification of postsynaptic actin cytoskeleton glutamatergic synapse negative regulation of ruffle assembly regulation of synaptic vesicle exocytosis uc003ext.1 uc003ext.2 uc003ext.3 uc003ext.4 
ENST00000239944.7 SERP1 ENST00000239944.7 stress associated endoplasmic reticulum protein 1 (from RefSeq NM_014445.4) D3DNI6 ENST00000239944.1 ENST00000239944.2 ENST00000239944.3 ENST00000239944.4 ENST00000239944.5 ENST00000239944.6 NM_014445 Q9Y6X1 RAMP4 SERP1_HUMAN uc003exy.1 uc003exy.2 uc003exy.3 uc003exy.4 uc003exy.5 Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins. Interacts with SEC61B, SEC61A1 and the SEC61 complex. Interacts with CANX. Q9Y6X1; Q92685: ALG3; NbExp=3; IntAct=EBI-10329948, EBI-2848814; Q9Y6X1; Q96BI3: APH1A; NbExp=3; IntAct=EBI-10329948, EBI-2606935; Q9Y6X1; Q13520: AQP6; NbExp=3; IntAct=EBI-10329948, EBI-13059134; Q9Y6X1; O94778: AQP8; NbExp=3; IntAct=EBI-10329948, EBI-19124986; Q9Y6X1; Q13323: BIK; NbExp=3; IntAct=EBI-10329948, EBI-700794; Q9Y6X1; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-10329948, EBI-11532900; Q9Y6X1; P04233-2: CD74; NbExp=3; IntAct=EBI-10329948, EBI-12222807; Q9Y6X1; P11912: CD79A; NbExp=3; IntAct=EBI-10329948, EBI-7797864; Q9Y6X1; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-10329948, EBI-17233035; Q9Y6X1; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-10329948, EBI-8637742; Q9Y6X1; Q15125: EBP; NbExp=3; IntAct=EBI-10329948, EBI-3915253; Q9Y6X1; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-10329948, EBI-18636064; Q9Y6X1; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10329948, EBI-18304435; Q9Y6X1; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-10329948, EBI-18938272; Q9Y6X1; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-10329948, EBI-6911547; Q9Y6X1; O75712: GJB3; NbExp=3; IntAct=EBI-10329948, EBI-3908586; Q9Y6X1; O95377: GJB5; NbExp=3; IntAct=EBI-10329948, EBI-3909454; Q9Y6X1; Q9NS71: GKN1; NbExp=3; IntAct=EBI-10329948, EBI-3933251; Q9Y6X1; O60883: GPR37L1; NbExp=3; IntAct=EBI-10329948, EBI-2927498; Q9Y6X1; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10329948, EBI-11721746; Q9Y6X1; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-10329948, EBI-18053395; Q9Y6X1; P26951: IL3RA; NbExp=3; IntAct=EBI-10329948, EBI-1757512; Q9Y6X1; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-10329948, EBI-10266796; Q9Y6X1; Q9H3M0: KCNF1; NbExp=4; IntAct=EBI-10329948, EBI-6918743; Q9Y6X1; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-10329948, EBI-17272405; Q9Y6X1; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-10329948, EBI-2820517; Q9Y6X1; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-10329948, EBI-373355; Q9Y6X1; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-10329948, EBI-3923617; Q9Y6X1; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-10329948, EBI-18063495; Q9Y6X1; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-10329948, EBI-7545592; Q9Y6X1; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10329948, EBI-3920694; Q9Y6X1; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-10329948, EBI-2855401; Q9Y6X1; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-10329948, EBI-18159983; Q9Y6X1; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-10329948, EBI-17295964; Q9Y6X1; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10329948, EBI-17280858; Q9Y6X1; Q16623: STX1A; NbExp=3; IntAct=EBI-10329948, EBI-712466; Q9Y6X1; P32856-2: STX2; NbExp=3; IntAct=EBI-10329948, EBI-11956649; Q9Y6X1; Q12846: STX4; NbExp=3; IntAct=EBI-10329948, EBI-744942; Q9Y6X1; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-10329948, EBI-12947623; Q9Y6X1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10329948, EBI-8638294; Q9Y6X1; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10329948, EBI-18178701; Q9Y6X1; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-10329948, EBI-8649725; Q9Y6X1; Q07011: TNFRSF9; NbExp=3; IntAct=EBI-10329948, EBI-12945620; Membrane ; Single- pass membrane protein Endoplasmic reticulum membrane ; Single-pass membrane protein Belongs to the RAMP4 family. skeletal system development protein binding endoplasmic reticulum endoplasmic reticulum membrane cytosol ribosome cytoplasmic microtubule glucose metabolic process cellular protein modification process protein glycosylation plasma membrane organization post-embryonic development multicellular organism aging protein transport membrane integral component of membrane endoplasmic reticulum unfolded protein response positive regulation of insulin secretion IRE1-mediated unfolded protein response positive regulation of translation positive regulation of organ growth muscle organ morphogenesis positive regulation of growth hormone secretion uc003exy.1 uc003exy.2 uc003exy.3 uc003exy.4 uc003exy.5 
ENST00000240050.9 MTERF2 ENST00000240050.9 mitochondrial transcription termination factor 2, transcript variant 1 (from RefSeq NM_001033050.3) ENST00000240050.1 ENST00000240050.2 ENST00000240050.3 ENST00000240050.4 ENST00000240050.5 ENST00000240050.6 ENST00000240050.7 ENST00000240050.8 MTEF2_HUMAN MTERFD3 NM_001033050 Q49AM1 Q53HM2 Q9H4L6 Q9H7Y9 uc001tmf.1 uc001tmf.2 uc001tmf.3 Binds mitochondrial DNA and plays a role in the regulation of transcription of mitochondrial mRNA and rRNA species. Monomer. Q49AM1; P05090: APOD; NbExp=3; IntAct=EBI-17857560, EBI-715495; Q49AM1; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-17857560, EBI-3917235; Q49AM1; O43752: STX6; NbExp=3; IntAct=EBI-17857560, EBI-2695795; Mitochondrion Mitochondrion matrix, mitochondrion nucleoid Expressed in skeletal muscle, heart, liver and pancreas. Belongs to the mTERF family. DNA binding double-stranded DNA binding mitochondrion regulation of transcription, DNA-templated termination of mitochondrial transcription mitochondrial nucleoid uc001tmf.1 uc001tmf.2 uc001tmf.3 
ENST00000240055.8 NFYB ENST00000240055.8 nuclear transcription factor Y subunit beta, transcript variant 3 (from RefSeq NM_006166.4) A8K7B9 ENST00000240055.1 ENST00000240055.2 ENST00000240055.3 ENST00000240055.4 ENST00000240055.5 ENST00000240055.6 ENST00000240055.7 HAP3 NFYB_HUMAN NM_006166 P25208 Q96IY8 uc001tkl.1 uc001tkl.2 uc001tkl.3 The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a variety of genes. This gene product, subunit B, forms a tight dimer with the C subunit, a prerequisite for subunit A association. The resulting trimer binds to DNA with high specificity and affinity. Subunits B and C each contain a histone-like motif. Observation of the histone nature of these subunits is supported by two types of evidence; protein sequence alignments and experiments with mutants. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1660809.247352.1, SRR1803615.55114.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240055.8/ ENSP00000240055.3 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. Heterotrimeric transcription factor composed of three components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and dimerize for NF-YA association and DNA binding. Interacts with C1QBP. P25208; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-389728, EBI-741181; P25208; P06307: CCK; NbExp=3; IntAct=EBI-389728, EBI-6624398; P25208; Q14919: DRAP1; NbExp=4; IntAct=EBI-389728, EBI-712941; P25208; P13473-2: LAMP2; NbExp=3; IntAct=EBI-389728, EBI-21591415; P25208; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-389728, EBI-16439278; P25208; P23511: NFYA; NbExp=8; IntAct=EBI-389728, EBI-389739; P25208; P23511-2: NFYA; NbExp=6; IntAct=EBI-389728, EBI-11061759; P25208; Q13952: NFYC; NbExp=6; IntAct=EBI-389728, EBI-389755; P25208; Q13952-2: NFYC; NbExp=6; IntAct=EBI-389728, EBI-11956831; P25208; Q9NR33: POLE4; NbExp=12; IntAct=EBI-389728, EBI-867034; P25208; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-389728, EBI-2623095; P25208; P04637: TP53; NbExp=6; IntAct=EBI-389728, EBI-366083; Nucleus. Can be divided into 3 domains: the weakly conserved A domain, the highly conserved B domain thought to be involved in subunit interaction and DNA binding, and the Glu-rich C domain. Monoubiquitination at Lys-140 plays an important role in transcriptional activation by allowing the deposition of histone H3 methylations as well as histone H2B monoubiquitination at 'Lys-121'. Belongs to the NFYB/HAP3 subunit family. Sequence=CAA42230.1; Type=Erroneous initiation; Evidence=; nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter CCAAT-binding factor complex protein-DNA complex sequence-specific DNA binding transcription regulatory region DNA binding macromolecular complex binding regulation of cholesterol biosynthetic process positive regulation of transcription, DNA-templated protein heterodimerization activity repressing transcription factor binding RNA polymerase II transcription factor complex cellular response to leukemia inhibitory factor RNA polymerase II distal enhancer sequence-specific DNA binding uc001tkl.1 uc001tkl.2 uc001tkl.3 
ENST00000240079.11 WASHC3 ENST00000240079.11 WASH complex subunit 3, transcript variant 1 (from RefSeq NM_016053.4) AD-016 B2RC74 CCDC53 CGI-116 ENST00000240079.1 ENST00000240079.10 ENST00000240079.2 ENST00000240079.3 ENST00000240079.4 ENST00000240079.5 ENST00000240079.6 ENST00000240079.7 ENST00000240079.8 ENST00000240079.9 NM_016053 Q53FF0 Q6IAI4 Q96QK0 Q9Y3C0 WASC3_HUMAN WASHC3 uc010svw.1 uc010svw.2 uc010svw.3 uc010svw.4 x0009 Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Component of the WASH core complex also described as WASH regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or WASH3P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5. The WASH core complex associates via WASHC2 with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex. Q9Y3C0; Q9NYB9: ABI2; NbExp=4; IntAct=EBI-712969, EBI-743598; Q9Y3C0; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-712969, EBI-11096309; Q9Y3C0; Q13515: BFSP2; NbExp=3; IntAct=EBI-712969, EBI-10229433; Q9Y3C0; Q6QNY1: BLOC1S2; NbExp=4; IntAct=EBI-712969, EBI-465872; Q9Y3C0; Q9UL45: BLOC1S6; NbExp=8; IntAct=EBI-712969, EBI-465781; Q9Y3C0; A1L168: C20orf202; NbExp=3; IntAct=EBI-712969, EBI-18396958; Q9Y3C0; Q8NCU1: CCDC197; NbExp=7; IntAct=EBI-712969, EBI-750686; Q9Y3C0; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-712969, EBI-10175300; Q9Y3C0; Q9BS16: CENPK; NbExp=3; IntAct=EBI-712969, EBI-6871750; Q9Y3C0; Q53EZ4: CEP55; NbExp=7; IntAct=EBI-712969, EBI-747776; Q9Y3C0; Q9Y2V7: COG6; NbExp=4; IntAct=EBI-712969, EBI-3866319; Q9Y3C0; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-712969, EBI-465804; Q9Y3C0; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-712969, EBI-11427343; Q9Y3C0; Q08379: GOLGA2; NbExp=6; IntAct=EBI-712969, EBI-618309; Q9Y3C0; Q96CS2: HAUS1; NbExp=10; IntAct=EBI-712969, EBI-2514791; Q9Y3C0; O75506: HSBP1; NbExp=13; IntAct=EBI-712969, EBI-748664; Q9Y3C0; Q8IY31: IFT20; NbExp=4; IntAct=EBI-712969, EBI-744203; Q9Y3C0; Q70UQ0-4: IKBIP; NbExp=4; IntAct=EBI-712969, EBI-12190633; Q9Y3C0; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-712969, EBI-4311436; Q9Y3C0; O60341: KDM1A; NbExp=3; IntAct=EBI-712969, EBI-710124; Q9Y3C0; Q9Y448: KNSTRN; NbExp=6; IntAct=EBI-712969, EBI-373334; Q9Y3C0; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-712969, EBI-3044087; Q9Y3C0; Q3SY84: KRT71; NbExp=3; IntAct=EBI-712969, EBI-2952676; Q9Y3C0; O95678: KRT75; NbExp=3; IntAct=EBI-712969, EBI-2949715; Q9Y3C0; Q969G2: LHX4; NbExp=3; IntAct=EBI-712969, EBI-2865388; Q9Y3C0; Q03252: LMNB2; NbExp=3; IntAct=EBI-712969, EBI-2830427; Q9Y3C0; Q96EZ8: MCRS1; NbExp=13; IntAct=EBI-712969, EBI-348259; Q9Y3C0; Q9H8S9: MOB1A; NbExp=3; IntAct=EBI-712969, EBI-748229; Q9Y3C0; Q7L9L4: MOB1B; NbExp=3; IntAct=EBI-712969, EBI-2558745; Q9Y3C0; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-712969, EBI-744402; Q9Y3C0; O14777: NDC80; NbExp=10; IntAct=EBI-712969, EBI-715849; Q9Y3C0; P37198: NUP62; NbExp=8; IntAct=EBI-712969, EBI-347978; Q9Y3C0; Q96CV9: OPTN; NbExp=17; IntAct=EBI-712969, EBI-748974; Q9Y3C0; P26367: PAX6; NbExp=3; IntAct=EBI-712969, EBI-747278; Q9Y3C0; Q96AQ6: PBXIP1; NbExp=4; IntAct=EBI-712969, EBI-740845; Q9Y3C0; Q15154: PCM1; NbExp=5; IntAct=EBI-712969, EBI-741421; Q9Y3C0; Q15154-3: PCM1; NbExp=3; IntAct=EBI-712969, EBI-11742977; Q9Y3C0; Q96FA3: PELI1; NbExp=3; IntAct=EBI-712969, EBI-448369; Q9Y3C0; Q8TCD6: PHOSPHO2; NbExp=5; IntAct=EBI-712969, EBI-2861380; Q9Y3C0; Q15276: RABEP1; NbExp=3; IntAct=EBI-712969, EBI-447043; Q9Y3C0; O76064: RNF8; NbExp=3; IntAct=EBI-712969, EBI-373337; Q9Y3C0; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-712969, EBI-12823227; Q9Y3C0; O00560: SDCBP; NbExp=6; IntAct=EBI-712969, EBI-727004; Q9Y3C0; O95295: SNAPIN; NbExp=3; IntAct=EBI-712969, EBI-296723; Q9Y3C0; A0A286YEY3: SRGAP2B; NbExp=3; IntAct=EBI-712969, EBI-17766455; Q9Y3C0; Q8N0S2: SYCE1; NbExp=4; IntAct=EBI-712969, EBI-6872807; Q9Y3C0; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-712969, EBI-12833746; Q9Y3C0; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-712969, EBI-1105213; Q9Y3C0; P40222: TXLNA; NbExp=8; IntAct=EBI-712969, EBI-359793; Q9Y3C0; Q8N3L3: TXLNB; NbExp=4; IntAct=EBI-712969, EBI-6116822; Q9Y3C0; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-712969, EBI-2799833; Q9Y3C0; A8K2R3; NbExp=3; IntAct=EBI-712969, EBI-9977437; Early endosome Belongs to the CCDC53 family. One study reported a nucleation-promoting factor (NPF) activity towards the Arp2/3 complex using partially purified samples of the WASH complex (PubMed:19922875). In another study, the in vitro reconstituted and purified recombinant WASH core complex, consisting of WASHC3, WASHC4, WASHC5, WASHC1 and the N-terminal residues 1-356 of WASHC2, did not show activity toward Arp2/3 complex (PubMed:20498093). protein binding endosome early endosome exocytosis biological_process protein transport actin filament polymerization WASH complex uc010svw.1 uc010svw.2 uc010svw.3 uc010svw.4 
ENST00000240093.8 FZD3 ENST00000240093.8 frizzled class receptor 3, transcript variant 18 (from RefSeq NR_182070.1) A8K615 ENST00000240093.1 ENST00000240093.2 ENST00000240093.3 ENST00000240093.4 ENST00000240093.5 ENST00000240093.6 ENST00000240093.7 FZD3_HUMAN NR_182070 Q9NPG1 uc003xgx.1 uc003xgx.2 uc003xgx.3 uc003xgx.4 uc003xgx.5 Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Required for the development of major fiber tracts in the central nervous system, including: the anterior commissure, the corpus callosum, the thalamocortical, corticothalamic and nigrostriatal tracts, the corticospinal tract, the fasciculus retroflexus, the mammillothalamic tract, the medial lemniscus, and ascending fiber tracts from the spinal cord to the brain. In the peripheral nervous system, controls axon growth in distinct populations of cranial and spinal motor neurons, including the facial branchimotor nerve, the hypoglossal nerve, the phrenic nerve, and motor nerves innervating dorsal limbs. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta- catenin-dependent manner (By similarity). Interacts with VANGL2. Membrane; Multi-pass membrane protein. Cell membrane ; Multi-pass membrane protein Cell surface Apical cell membrane ; Multi-pass membrane protein. Note=Colocalizes with FZD6 at the apical face of the cell (By similarity). Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=Q9NPG1-1; Sequence=Displayed; Name=Short; Synonyms=FZD3deltaC; IsoId=Q9NPG1-2; Sequence=Not described; Widely expressed. Relatively high expression in the CNS, including regions of the limbic system, in kidney, pancreas, skeletal muscle, uterus and testis. Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. The FZ domain is involved in binding with Wnt ligands. Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. Belongs to the G-protein coupled receptor Fz/Smo family. establishment of planar polarity neuron migration neural tube closure hair follicle development positive regulation of neuroblast proliferation transmembrane signaling receptor activity G-protein coupled receptor activity protein binding cytoplasm plasma membrane signal transduction cell surface receptor signaling pathway G-protein coupled receptor signaling pathway Wnt signaling pathway, calcium modulating pathway multicellular organism development nervous system development brain development cell surface membrane integral component of membrane Wnt signaling pathway apical plasma membrane lateral plasma membrane Wnt-protein binding PDZ domain binding neuron differentiation axon dendrite midbrain development filopodium tip cell proliferation in midbrain non-canonical Wnt signaling pathway post-anal tail morphogenesis dopaminergic neuron axon guidance serotonergic neuron axon guidance inner ear morphogenesis response to drug Wnt-activated receptor activity neuronal cell body apical part of cell negative regulation of mitotic cell cycle, embryonic presynaptic active zone response to electrical stimulus canonical Wnt signaling pathway Wnt signaling pathway, planar cell polarity pathway sympathetic ganglion development commissural neuron axon guidance negative regulation of execution phase of apoptosis midbrain morphogenesis planar cell polarity pathway involved in axon guidance uc003xgx.1 uc003xgx.2 uc003xgx.3 uc003xgx.4 uc003xgx.5 
ENST00000240100.7 DUSP4 ENST00000240100.7 dual specificity phosphatase 4, transcript variant 1 (from RefSeq NM_001394.7) B2RBU5 D3DSU4 DUS4_HUMAN ENST00000240100.1 ENST00000240100.2 ENST00000240100.3 ENST00000240100.4 ENST00000240100.5 ENST00000240100.6 G5E930 MKP2 NM_001394 Q13115 Q13524 VH2 uc003xhm.1 uc003xhm.2 uc003xhm.3 uc003xhm.4 uc003xhm.5 The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus. Two alternatively spliced transcript variants, encoding distinct isoforms, have been observed for this gene. In addition, multiple polyadenylation sites have been reported. [provided by RefSeq, Jul 2008]. Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2. Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence= Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence=; Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence=; Hollow spherical complex composed of 24 subunits with pseudooctahedral symmetry, has a tetramer as the basic unit. Q13115; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-6591081, EBI-739467; Q13115; Q96S90: LYSMD1; NbExp=3; IntAct=EBI-6591081, EBI-10293291; Q13115; Q8IV50-2: LYSMD2; NbExp=3; IntAct=EBI-6591081, EBI-19761491; Q13115; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-6591081, EBI-741037; Q13115; P28482: MAPK1; NbExp=6; IntAct=EBI-6591081, EBI-959949; Q13115; P45984: MAPK9; NbExp=4; IntAct=EBI-6591081, EBI-713568; Q13115; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-6591081, EBI-12025760; Q13115; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-6591081, EBI-742388; Q13115; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-6591081, EBI-11139477; Q13115; Q13077: TRAF1; NbExp=3; IntAct=EBI-6591081, EBI-359224; Q13115; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-6591081, EBI-743265; Q13115; Q8N720: ZNF655; NbExp=3; IntAct=EBI-6591081, EBI-625509; Nucleus Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=MKP-2-L; IsoId=Q13115-1; Sequence=Displayed; Name=2; Synonyms=MKP-2-S; IsoId=Q13115-2; Sequence=VSP_044667, VSP_044668; Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal degradation and stabilizes the protein. [Isoform 2]: Does not bind to JNK or ERK, and is more susceptible to proteasomal degradation. Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily. inactivation of MAPK activity phosphoprotein phosphatase activity protein tyrosine phosphatase activity protein binding nucleus nucleoplasm cytoplasm protein dephosphorylation protein tyrosine/serine/threonine phosphatase activity protein tyrosine/threonine phosphatase activity dephosphorylation hydrolase activity phosphatase activity MAP kinase tyrosine/serine/threonine phosphatase activity peptidyl-tyrosine dephosphorylation peptidyl-threonine dephosphorylation negative regulation of ERK1 and ERK2 cascade MAP kinase threonine phosphatase activity uc003xhm.1 uc003xhm.2 uc003xhm.3 uc003xhm.4 uc003xhm.5 
ENST00000240123.12 SORBS3 ENST00000240123.12 sorbin and SH3 domain containing 3, transcript variant 1 (from RefSeq NM_005775.5) ENST00000240123.1 ENST00000240123.10 ENST00000240123.11 ENST00000240123.2 ENST00000240123.3 ENST00000240123.4 ENST00000240123.5 ENST00000240123.6 ENST00000240123.7 ENST00000240123.8 ENST00000240123.9 NM_005775 O60504 Q5BJE4 Q6NX54 Q96FY4 Q9UQE4 SCAM1 VINEX_HUMAN uc003xbv.1 uc003xbv.2 uc003xbv.3 uc003xbv.4 uc003xbv.5 This gene encodes an SH3 domain-containing adaptor protein. The presence of SH3 domains play a role in this protein's ability to bind other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2011]. Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain. Interacts with DLG5 through its third SH3 domain (By similarity). Interacts with vinculin by the first two SH3 domains and the proline rich region of vinculin. Binds to SOS (guanine nucleotide exchange factor of RAS and RAC), through its third SH3 domain. The formation of this complex is down-regulated by phosphorylation of SOS. Interacts with INPPL1/SHIP2, SAFB2, SOCS7 and SRCIN1. Interacts with FASLG. Interacts with MAPK1/ERK2 (By similarity). O60504; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-741237, EBI-11096309; O60504; Q96EY9: ADAT3; NbExp=3; IntAct=EBI-741237, EBI-3922811; O60504; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-741237, EBI-8643161; O60504; Q53H80: AKIRIN2; NbExp=3; IntAct=EBI-741237, EBI-742928; O60504; P31751: AKT2; NbExp=3; IntAct=EBI-741237, EBI-296058; O60504; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-741237, EBI-11954519; O60504; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-741237, EBI-745689; O60504; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-741237, EBI-744545; O60504; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-741237, EBI-11954144; O60504; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-741237, EBI-10171570; O60504; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-741237, EBI-744556; O60504; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-741237, EBI-10961624; O60504; Q16204: CCDC6; NbExp=3; IntAct=EBI-741237, EBI-1045350; O60504; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-741237, EBI-10175300; O60504; P51946: CCNH; NbExp=3; IntAct=EBI-741237, EBI-741406; O60504; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-741237, EBI-2836773; O60504; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-741237, EBI-396137; O60504; P42773: CDKN2C; NbExp=3; IntAct=EBI-741237, EBI-711290; O60504; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-741237, EBI-749051; O60504; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-741237, EBI-2555370; O60504; Q9H9E3: COG4; NbExp=3; IntAct=EBI-741237, EBI-368382; O60504; Q99829: CPNE1; NbExp=3; IntAct=EBI-741237, EBI-1642542; O60504; Q96FN4: CPNE2; NbExp=6; IntAct=EBI-741237, EBI-7097057; O60504; Q86YQ8: CPNE8; NbExp=3; IntAct=EBI-741237, EBI-1642325; O60504; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-741237, EBI-739773; O60504; P26196: DDX6; NbExp=3; IntAct=EBI-741237, EBI-351257; O60504; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-741237, EBI-10233719; O60504; Q92997: DVL3; NbExp=3; IntAct=EBI-741237, EBI-739789; O60504; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-741237, EBI-743105; O60504; O15372: EIF3H; NbExp=3; IntAct=EBI-741237, EBI-709735; O60504; Q6IB98: EIF3S3; NbExp=3; IntAct=EBI-741237, EBI-10184995; O60504; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-741237, EBI-744099; O60504; Q9NYF3: FAM53C; NbExp=3; IntAct=EBI-741237, EBI-1644252; O60504; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-741237, EBI-11959077; O60504; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-741237, EBI-744935; O60504; O95995: GAS8; NbExp=3; IntAct=EBI-741237, EBI-1052570; O60504; P55040: GEM; NbExp=3; IntAct=EBI-741237, EBI-744104; O60504; P23415: GLRA1; NbExp=3; IntAct=EBI-741237, EBI-12020340; O60504; O95872: GPANK1; NbExp=3; IntAct=EBI-741237, EBI-751540; O60504; Q92917: GPKOW; NbExp=3; IntAct=EBI-741237, EBI-746309; O60504; P13807: GYS1; NbExp=3; IntAct=EBI-741237, EBI-740553; O60504; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-741237, EBI-14103818; O60504; O14964: HGS; NbExp=3; IntAct=EBI-741237, EBI-740220; O60504; P52597: HNRNPF; NbExp=3; IntAct=EBI-741237, EBI-352986; O60504; P61978: HNRNPK; NbExp=4; IntAct=EBI-741237, EBI-304185; O60504; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-741237, EBI-7060731; O60504; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-741237, EBI-1018153; O60504; Q9NV31: IMP3; NbExp=3; IntAct=EBI-741237, EBI-747481; O60504; Q1MX18: INSC; NbExp=3; IntAct=EBI-741237, EBI-12081118; O60504; Q8NA54: IQUB; NbExp=3; IntAct=EBI-741237, EBI-10220600; O60504; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-741237, EBI-2556193; O60504; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-741237, EBI-739493; O60504; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-741237, EBI-14069005; O60504; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-741237, EBI-14086479; O60504; Q13064: MKRN3; NbExp=3; IntAct=EBI-741237, EBI-2340269; O60504; Q15742: NAB2; NbExp=3; IntAct=EBI-741237, EBI-8641936; O60504; Q96HR8: NAF1; NbExp=3; IntAct=EBI-741237, EBI-2515597; O60504; A0A0S2Z4D7: NCK1; NbExp=3; IntAct=EBI-741237, EBI-16429340; O60504; Q9NZQ3: NCKIPSD; NbExp=3; IntAct=EBI-741237, EBI-745080; O60504; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-741237, EBI-11750983; O60504; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-741237, EBI-10271199; O60504; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-741237, EBI-2859639; O60504; Q9UHY1: NRBP1; NbExp=3; IntAct=EBI-741237, EBI-749731; O60504; O43482: OIP5; NbExp=3; IntAct=EBI-741237, EBI-536879; O60504; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-741237, EBI-9057006; O60504; Q13177: PAK2; NbExp=6; IntAct=EBI-741237, EBI-1045887; O60504; Q9P286: PAK5; NbExp=3; IntAct=EBI-741237, EBI-741896; O60504; Q8N4B1-4: PHETA1; NbExp=3; IntAct=EBI-741237, EBI-14131832; O60504; O43189: PHF1; NbExp=3; IntAct=EBI-741237, EBI-530034; O60504; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-741237, EBI-14066006; O60504; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-741237, EBI-12014286; O60504; O60568: PLOD3; NbExp=3; IntAct=EBI-741237, EBI-741582; O60504; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-741237, EBI-10171633; O60504; P56282: POLE2; NbExp=3; IntAct=EBI-741237, EBI-713847; O60504; O15160: POLR1C; NbExp=3; IntAct=EBI-741237, EBI-1055079; O60504; O75145: PPFIA3; NbExp=3; IntAct=EBI-741237, EBI-1763225; O60504; Q8IXY8: PPIL6; NbExp=3; IntAct=EBI-741237, EBI-12226639; O60504; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-741237, EBI-2557469; O60504; P47897: QARS1; NbExp=3; IntAct=EBI-741237, EBI-347462; O60504; O75771: RAD51D; NbExp=3; IntAct=EBI-741237, EBI-1055693; O60504; Q13671: RIN1; NbExp=3; IntAct=EBI-741237, EBI-366017; O60504; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-741237, EBI-1378139; O60504; Q9BST9: RTKN; NbExp=3; IntAct=EBI-741237, EBI-446694; O60504; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-741237, EBI-11984663; O60504; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-741237, EBI-3957636; O60504; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-741237, EBI-748391; O60504; Q9C0A6-3: SETD5; NbExp=3; IntAct=EBI-741237, EBI-12233047; O60504; Q9H788: SH2D4A; NbExp=6; IntAct=EBI-741237, EBI-747035; O60504; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-741237, EBI-10308083; O60504; O14512: SOCS7; NbExp=3; IntAct=EBI-741237, EBI-1539606; O60504; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-741237, EBI-742688; O60504; Q9H987-2: SYNPO2L; NbExp=3; IntAct=EBI-741237, EBI-12082116; O60504; Q9NU19: TBC1D22B; NbExp=4; IntAct=EBI-741237, EBI-8787464; O60504; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-741237, EBI-11955057; O60504; Q15561: TEAD4; NbExp=3; IntAct=EBI-741237, EBI-747736; O60504; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-741237, EBI-11139477; O60504; Q63HR2: TNS2; NbExp=3; IntAct=EBI-741237, EBI-949753; O60504; P36406: TRIM23; NbExp=6; IntAct=EBI-741237, EBI-740098; O60504; P14373: TRIM27; NbExp=3; IntAct=EBI-741237, EBI-719493; O60504; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-741237, EBI-725997; O60504; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-741237, EBI-744794; O60504; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-741237, EBI-10241197; O60504; P40222: TXLNA; NbExp=3; IntAct=EBI-741237, EBI-359793; O60504; O75604: USP2; NbExp=3; IntAct=EBI-741237, EBI-743272; O60504; Q5ST30: VARS2; NbExp=3; IntAct=EBI-741237, EBI-2116622; O60504; Q5ST30-4: VARS2; NbExp=3; IntAct=EBI-741237, EBI-10244997; O60504; P18206-2: VCL; NbExp=3; IntAct=EBI-741237, EBI-11027067; O60504; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-741237, EBI-4400866; O60504; A5D8V6: VPS37C; NbExp=6; IntAct=EBI-741237, EBI-2559305; O60504; Q8TF74: WIPF2; NbExp=3; IntAct=EBI-741237, EBI-2850112; O60504; O15156: ZBTB7B; NbExp=3; IntAct=EBI-741237, EBI-740434; O60504; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-741237, EBI-14104088; O60504; Q9NQZ6: ZC4H2; NbExp=3; IntAct=EBI-741237, EBI-747993; O60504; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-741237, EBI-744257; O60504-1; O15357: INPPL1; NbExp=2; IntAct=EBI-1222953, EBI-1384248; O60504-2; P00519: ABL1; NbExp=5; IntAct=EBI-1222956, EBI-375543; O60504-2; P13631: RARG; NbExp=2; IntAct=EBI-1222956, EBI-2568901; O60504-2; Q9BST9: RTKN; NbExp=3; IntAct=EBI-1222956, EBI-446694; O60504-2; Q14151: SAFB2; NbExp=3; IntAct=EBI-1222956, EBI-352869; O60504-2; Q9Y6W5: WASF2; NbExp=3; IntAct=EBI-1222956, EBI-4290615; O60504-2; O00401: WASL; NbExp=3; IntAct=EBI-1222956, EBI-957615; O60504-2; Q9QWI6-2: Srcin1; Xeno; NbExp=4; IntAct=EBI-1222956, EBI-775607; [Isoform Alpha]: Cell junction Cytoplasm, cytoskeleton Note=Localized at cell- extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites. [Isoform Beta]: Cell junction Nucleus. Cytoplasm, cytoskeleton Note=Localized at cell- extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites, vinexin beta was also found in the nucleus. Event=Alternative splicing; Named isoforms=2; Name=Alpha; IsoId=O60504-1; Sequence=Displayed; Name=Beta; IsoId=O60504-2; Sequence=VSP_004489; Both isoforms are expressed in different tissues like heart, placenta, brain, skeletal muscle and pancreas. Isoform beta is especially found in liver. Phosphorylated at Ser-530 by MAPK1/ERK2 during cell spreading. negative regulation of transcription from RNA polymerase II promoter structural constituent of cytoskeleton protein binding nucleus cytoplasm cytosol cytoskeleton focal adhesion muscle contraction actin filament organization cell adhesion transcription factor binding vinculin binding cell junction cell-substrate adhesion positive regulation of MAPK cascade positive regulation of cytoskeleton organization positive regulation of stress fiber assembly uc003xbv.1 uc003xbv.2 uc003xbv.3 uc003xbv.4 uc003xbv.5 
ENST00000240139.10 PPP3CC ENST00000240139.10 protein phosphatase 3 catalytic subunit gamma, transcript variant 2 (from RefSeq NM_005605.5) B4DRT5 CALNA3 CNA3 ENST00000240139.1 ENST00000240139.2 ENST00000240139.3 ENST00000240139.4 ENST00000240139.5 ENST00000240139.6 ENST00000240139.7 ENST00000240139.8 ENST00000240139.9 NM_005605 P48454 PP2BC_HUMAN Q9BSS6 Q9H4M5 uc003xbs.1 uc003xbs.2 uc003xbs.3 uc003xbs.4 uc003xbs.5 Calcineurin is a calcium-dependent, calmodulin-stimulated protein phosphatase involved in the downstream regulation of dopaminergic signal transduction. Calcineurin is composed of a regulatory subunit and a catalytic subunit. The protein encoded by this gene represents one of the regulatory subunits that has been found for calcineurin. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2011]. Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence=; Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence=; Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. ; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit. ; Activated by Ca(2+)-bound calmodulin following an increase in intracellular Ca(2+). At low Ca(2+) concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca(2+). In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca(2+) causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A. The subsequent binding of Ca(2+)-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A. Kinetic parameters: KM=1.27 uM for NFATC1 ; KM=0.94 uM for DARPP32 ; Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B) (PubMed:19154138). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). In response to an increase in Ca(2+) intracellular levels, forms a complex composed of PPP3CC/calcineurin A, calcineurin B and calmodulin (By similarity). Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca(2+) (By similarity). Interacts with UNC119 (By similarity). Interacts with SPATA33 (via PQIIIT motif) (PubMed:34446558). Interacts with VDAC2 in a SPATA33- dependent manner (By similarity). P48454; P49418: AMPH; NbExp=3; IntAct=EBI-2827192, EBI-7121510; P48454; P05067: APP; NbExp=3; IntAct=EBI-2827192, EBI-77613; P48454; P63098: PPP3R1; NbExp=4; IntAct=EBI-2827192, EBI-915984; P48454; Q96N06: SPATA33; NbExp=3; IntAct=EBI-2827192, EBI-17572815; P48454; Q13432: UNC119; NbExp=3; IntAct=EBI-2827192, EBI-711260; Mitochondrion Note=Localizes in the mitochondria in a SPATA33-dependent manner. Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P48454-1; Sequence=Displayed; Name=2; IsoId=P48454-2; Sequence=VSP_037946; Name=3; IsoId=P48454-3; Sequence=VSP_045211; Testis. The autoinhibitory domain prevents access to the catalytic site. The autoinhibitory segment prevents access to the substrate binding site. Possible isomerization of Pro-305 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA. Belongs to the PPP phosphatase family. PP-2B subfamily. phosphoprotein phosphatase activity protein binding calmodulin binding cytoplasm mitochondrion cytosol calcineurin complex protein dephosphorylation brain development hydrolase activity calcineurin-NFAT signaling cascade calmodulin-dependent protein phosphatase activity metal ion binding calcineurin-mediated signaling presynapse glutamatergic synapse presynaptic cytosol regulation of synaptic vesicle endocytosis positive regulation of synaptic vesicle endocytosis positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway uc003xbs.1 uc003xbs.2 uc003xbs.3 uc003xbs.4 uc003xbs.5 
ENST00000240185.8 TARDBP ENST00000240185.8 TAR DNA binding protein (from RefSeq NM_007375.4) A4GUK4 A4GUK5 A4GUK6 B2R629 B4DJ45 E2PU12 ENST00000240185.1 ENST00000240185.2 ENST00000240185.3 ENST00000240185.4 ENST00000240185.5 ENST00000240185.6 ENST00000240185.7 NM_007375 Q13148 Q53H27 Q6FI92 Q96DJ0 TADBP_HUMAN TARDBP TDP43 uc001art.1 uc001art.2 uc001art.3 uc001art.4 uc001art.5 HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, this protein regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC095435.1, AL050265.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240185.8/ ENSP00000240185.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## RNA-binding protein that is involved in various steps of RNA biogenesis and processing (PubMed:23519609). Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases (PubMed:21358640, PubMed:29438978). Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts (PubMed:28794432). Regulates also mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening (PubMed:30520513). In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival (PubMed:23398327, PubMed:19765185). Participates also in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively regulates the expression of CDK6 (PubMed:19760257). Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner (PubMed:25678563). Homodimer (PubMed:20043239, PubMed:24464995). Homooligomer (via its N-terminal domain) (PubMed:28663553, PubMed:29438978). Interacts with BRDT (By similarity). Binds specifically to pyrimidine- rich motifs of TAR DNA and to single stranded TG repeated sequences. Binds to RNA, specifically to UG repeated sequences with a minimum of six contiguous repeats. Interacts with ATXN2; the interaction is RNA- dependent (PubMed:20740007). Interacts with MATR3 (PubMed:24686783). Interacts with UBQLN2 (PubMed:23541532). Interacts with HNRNPA2B1 (PubMed:19429692). Interacts with ZNF106 (By similarity). Interacts with CNOT7/CAF1 (PubMed:30520513). Interacts with CRY2 (PubMed:27123980). Interacts with PPIA/CYPA; the interaction is dependent on RNA-binding activity of TARDBP and PPIase activity of PPIA/CYPA and acetylation of PPIA/CYPA at 'Lys-125' favors the interaction (PubMed:25678563). Q13148; Q969K4: ABTB1; NbExp=3; IntAct=EBI-372899, EBI-7223971; Q13148; P55265: ADAR; NbExp=3; IntAct=EBI-372899, EBI-2462104; Q13148; Q6ZTN6-2: ANKRD13D; NbExp=3; IntAct=EBI-372899, EBI-25840993; Q13148; P13928: ANXA8; NbExp=6; IntAct=EBI-372899, EBI-2556915; Q13148; P63010-2: AP2B1; NbExp=6; IntAct=EBI-372899, EBI-11529439; Q13148; P05067: APP; NbExp=6; IntAct=EBI-372899, EBI-77613; Q13148; P05067-2: APP; NbExp=3; IntAct=EBI-372899, EBI-17264467; Q13148; Q0P5N6: ARL16; NbExp=6; IntAct=EBI-372899, EBI-10186132; Q13148; Q8WXK3: ASB13; NbExp=3; IntAct=EBI-372899, EBI-707573; Q13148; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-372899, EBI-14199987; Q13148; Q96DX5: ASB9; NbExp=3; IntAct=EBI-372899, EBI-745641; Q13148; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-372899, EBI-25843552; Q13148; Q96FT7-4: ASIC4; NbExp=6; IntAct=EBI-372899, EBI-9089489; Q13148; P18847: ATF3; NbExp=6; IntAct=EBI-372899, EBI-712767; Q13148; O95352-2: ATG7; NbExp=3; IntAct=EBI-372899, EBI-15980880; Q13148; P15313: ATP6V1B1; NbExp=6; IntAct=EBI-372899, EBI-2891281; Q13148; Q99700: ATXN2; NbExp=3; IntAct=EBI-372899, EBI-697691; Q13148; P46379-2: BAG6; NbExp=6; IntAct=EBI-372899, EBI-10988864; Q13148; Q8TBE0: BAHD1; NbExp=6; IntAct=EBI-372899, EBI-742750; Q13148; Q5H9J7: BEX5; NbExp=6; IntAct=EBI-372899, EBI-10243741; Q13148; O15392: BIRC5; NbExp=6; IntAct=EBI-372899, EBI-518823; Q13148; Q9H0C5: BTBD1; NbExp=3; IntAct=EBI-372899, EBI-935503; Q13148; Q5SZD1: C6orf141; NbExp=6; IntAct=EBI-372899, EBI-10697767; Q13148; Q96LL4: C8orf48; NbExp=6; IntAct=EBI-372899, EBI-751596; Q13148; Q13191: CBLB; NbExp=6; IntAct=EBI-372899, EBI-744027; Q13148; Q9ULV8: CBLC; NbExp=3; IntAct=EBI-372899, EBI-2341018; Q13148; Q14781-2: CBX2; NbExp=6; IntAct=EBI-372899, EBI-11974585; Q13148; Q13939: CCIN; NbExp=3; IntAct=EBI-372899, EBI-25879469; Q13148; Q13042: CDC16; NbExp=3; IntAct=EBI-372899, EBI-994830; Q13148; Q13042-2: CDC16; NbExp=3; IntAct=EBI-372899, EBI-10974085; Q13148; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-372899, EBI-396137; Q13148; Q92879-3: CELF1; NbExp=3; IntAct=EBI-372899, EBI-21370617; Q13148; Q8NHQ1-3: CEP70; NbExp=6; IntAct=EBI-372899, EBI-11526150; Q13148; Q494V2-2: CFAP100; NbExp=6; IntAct=EBI-372899, EBI-11953200; Q13148; O14647: CHD2; NbExp=2; IntAct=EBI-372899, EBI-1210503; Q13148; Q16740: CLPP; NbExp=3; IntAct=EBI-372899, EBI-1056029; Q13148; Q8IUI8: CRLF3; NbExp=6; IntAct=EBI-372899, EBI-2872414; Q13148; P48730-2: CSNK1D; NbExp=6; IntAct=EBI-372899, EBI-9087876; Q13148; P61962: DCAF7; NbExp=3; IntAct=EBI-372899, EBI-359808; Q13148; Q5TAQ9-2: DCAF8; NbExp=6; IntAct=EBI-372899, EBI-25842815; Q13148; Q5TDH0-2: DDI2; NbExp=3; IntAct=EBI-372899, EBI-25858598; Q13148; Q92841: DDX17; NbExp=6; IntAct=EBI-372899, EBI-746012; Q13148; O00571: DDX3X; NbExp=6; IntAct=EBI-372899, EBI-353779; Q13148; P17844: DDX5; NbExp=3; IntAct=EBI-372899, EBI-351962; Q13148; O75398: DEAF1; NbExp=3; IntAct=EBI-372899, EBI-718185; Q13148; Q96EY1-3: DNAJA3; NbExp=6; IntAct=EBI-372899, EBI-11526226; Q13148; Q92782-2: DPF1; NbExp=6; IntAct=EBI-372899, EBI-23669343; Q13148; Q86TI2-2: DPP9; NbExp=6; IntAct=EBI-372899, EBI-21529239; Q13148; O75530-2: EED; NbExp=3; IntAct=EBI-372899, EBI-11132357; Q13148; O00303: EIF3F; NbExp=6; IntAct=EBI-372899, EBI-711990; Q13148; Q15717: ELAVL1; NbExp=7; IntAct=EBI-372899, EBI-374260; Q13148; Q8TC29: ENKUR; NbExp=6; IntAct=EBI-372899, EBI-9246952; Q13148; P29323-3: EPHB2; NbExp=6; IntAct=EBI-372899, EBI-25838727; Q13148; Q6NXG1: ESRP1; NbExp=6; IntAct=EBI-372899, EBI-10213520; Q13148; O00471: EXOC5; NbExp=6; IntAct=EBI-372899, EBI-949824; Q13148; Q6P1L5: FAM117B; NbExp=6; IntAct=EBI-372899, EBI-3893327; Q13148; Q17RN3: FAM98C; NbExp=6; IntAct=EBI-372899, EBI-5461838; Q13148; Q8IZU1: FAM9A; NbExp=6; IntAct=EBI-372899, EBI-8468186; Q13148; Q9UKA1: FBXL5; NbExp=3; IntAct=EBI-372899, EBI-2692340; Q13148; Q9UKT5: FBXO4; NbExp=3; IntAct=EBI-372899, EBI-960409; Q13148; P35637: FUS; NbExp=8; IntAct=EBI-372899, EBI-400434; Q13148; Q06547-2: GABPB1; NbExp=6; IntAct=EBI-372899, EBI-618189; Q13148; Q96IJ6: GMPPA; NbExp=6; IntAct=EBI-372899, EBI-750953; Q13148; P62879: GNB2; NbExp=7; IntAct=EBI-372899, EBI-356942; Q13148; Q9Y4H4: GPSM3; NbExp=6; IntAct=EBI-372899, EBI-347538; Q13148; Q969Y2: GTPBP3; NbExp=6; IntAct=EBI-372899, EBI-740290; Q13148; Q9UBN7: HDAC6; NbExp=3; IntAct=EBI-372899, EBI-301697; Q13148; Q9HCC6: HES4; NbExp=6; IntAct=EBI-372899, EBI-2680288; Q13148; P07910: HNRNPC; NbExp=3; IntAct=EBI-372899, EBI-357966; Q13148; P07910-2: HNRNPC; NbExp=6; IntAct=EBI-372899, EBI-5280084; Q13148; O14979: HNRNPDL; NbExp=3; IntAct=EBI-372899, EBI-299727; Q13148; P31943: HNRNPH1; NbExp=7; IntAct=EBI-372899, EBI-351590; Q13148; P61978: HNRNPK; NbExp=3; IntAct=EBI-372899, EBI-304185; Q13148; P61978-2: HNRNPK; NbExp=6; IntAct=EBI-372899, EBI-7060731; Q13148; O43390-2: HNRNPR; NbExp=3; IntAct=EBI-372899, EBI-12236340; Q13148; Q00839-2: HNRNPU; NbExp=6; IntAct=EBI-372899, EBI-351143; Q13148; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-372899, EBI-1018153; Q13148; Q9BUJ2-2: HNRNPUL1; NbExp=3; IntAct=EBI-372899, EBI-11018029; Q13148; Q9BTB7: HNRPUL1; NbExp=3; IntAct=EBI-372899, EBI-10298318; Q13148; Q02363: ID2; NbExp=6; IntAct=EBI-372899, EBI-713450; Q13148; P80217-2: IFI35; NbExp=6; IntAct=EBI-372899, EBI-12823003; Q13148; Q9Y6M1: IGF2BP2; NbExp=3; IntAct=EBI-372899, EBI-1024419; Q13148; O00425: IGF2BP3; NbExp=6; IntAct=EBI-372899, EBI-1058566; Q13148; Q12906-6: ILF3; NbExp=6; IntAct=EBI-372899, EBI-12904528; Q13148; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-372899, EBI-743980; Q13148; Q6DN90-2: IQSEC1; NbExp=6; IntAct=EBI-372899, EBI-21911304; Q13148; O43187: IRAK2; NbExp=2; IntAct=EBI-372899, EBI-447733; Q13148; Q92613: JADE3; NbExp=6; IntAct=EBI-372899, EBI-10278909; Q13148; Q9NVX7-2: KBTBD4; NbExp=6; IntAct=EBI-372899, EBI-25871195; Q13148; Q96SI1-2: KCTD15; NbExp=6; IntAct=EBI-372899, EBI-12382297; Q13148; Q8N5Z5: KCTD17; NbExp=6; IntAct=EBI-372899, EBI-743960; Q13148; Q9UIH9: KLF15; NbExp=6; IntAct=EBI-372899, EBI-2796400; Q13148; Q6TDP4: KLHL17; NbExp=3; IntAct=EBI-372899, EBI-21328926; Q13148; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-372899, EBI-714379; Q13148; Q53GT1: KLHL22; NbExp=3; IntAct=EBI-372899, EBI-1996072; Q13148; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-372899, EBI-724915; Q13148; Q96NJ5: KLHL32; NbExp=3; IntAct=EBI-372899, EBI-6426390; Q13148; Q8N4N3-2: KLHL36; NbExp=6; IntAct=EBI-372899, EBI-10973851; Q13148; O00629: KPNA4; NbExp=3; IntAct=EBI-372899, EBI-396343; Q13148; Q9BYQ4: KRTAP9-2; NbExp=6; IntAct=EBI-372899, EBI-1044640; Q13148; Q96JM7-2: L3MBTL3; NbExp=6; IntAct=EBI-372899, EBI-11985629; Q13148; Q9BYZ2: LDHAL6B; NbExp=6; IntAct=EBI-372899, EBI-1108377; Q13148; Q6DKI2: LGALS9C; NbExp=6; IntAct=EBI-372899, EBI-9088829; Q13148; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-372899, EBI-739832; Q13148; Q8N448: LNX2; NbExp=6; IntAct=EBI-372899, EBI-2340947; Q13148; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-372899, EBI-2510853; Q13148; O95777: LSM8; NbExp=6; IntAct=EBI-372899, EBI-347779; Q13148; Q8TD91-2: MAGEC3; NbExp=6; IntAct=EBI-372899, EBI-10694180; Q13148; Q15759: MAPK11; NbExp=6; IntAct=EBI-372899, EBI-298304; Q13148; P43243: MATR3; NbExp=6; IntAct=EBI-372899, EBI-352602; Q13148; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-372899, EBI-13288755; Q13148; Q8N6F8: METTL27; NbExp=6; IntAct=EBI-372899, EBI-8487781; Q13148; Q8TDB4: MGARP; NbExp=6; IntAct=EBI-372899, EBI-4397720; Q13148; Q8N108-16: MIER1; NbExp=6; IntAct=EBI-372899, EBI-25830642; Q13148; A4FUJ8: MKL1; NbExp=6; IntAct=EBI-372899, EBI-21250407; Q13148; Q9H000: MKRN2; NbExp=6; IntAct=EBI-372899, EBI-2341005; Q13148; Q13064: MKRN3; NbExp=3; IntAct=EBI-372899, EBI-2340269; Q13148; Q15049: MLC1; NbExp=6; IntAct=EBI-372899, EBI-8475277; Q13148; P51948: MNAT1; NbExp=3; IntAct=EBI-372899, EBI-716139; Q13148; O95396: MOCS3; NbExp=3; IntAct=EBI-372899, EBI-373206; Q13148; Q8N594: MPND; NbExp=6; IntAct=EBI-372899, EBI-2512452; Q13148; Q9Y483-4: MTF2; NbExp=3; IntAct=EBI-372899, EBI-10698053; Q13148; P01106: MYC; NbExp=6; IntAct=EBI-372899, EBI-447544; Q13148; O00746: NME4; NbExp=6; IntAct=EBI-372899, EBI-744871; Q13148; Q9UNZ2: NSFL1C; NbExp=4; IntAct=EBI-372899, EBI-721577; Q13148; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-372899, EBI-1059321; Q13148; O15381-5: NVL; NbExp=6; IntAct=EBI-372899, EBI-18577082; Q13148; Q96FW1: OTUB1; NbExp=8; IntAct=EBI-372899, EBI-1058491; Q13148; Q6GQQ9-2: OTUD7B; NbExp=6; IntAct=EBI-372899, EBI-25830200; Q13148; P32242: OTX1; NbExp=6; IntAct=EBI-372899, EBI-740446; Q13148; Q6VY07: PACS1; NbExp=6; IntAct=EBI-372899, EBI-2555014; Q13148; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-372899, EBI-17159452; Q13148; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-372899, EBI-11022007; Q13148; Q9BYU1: PBX4; NbExp=6; IntAct=EBI-372899, EBI-10302990; Q13148; Q9NV79: PCMTD2; NbExp=3; IntAct=EBI-372899, EBI-6309018; Q13148; Q6ZMN7-2: PDZRN4; NbExp=3; IntAct=EBI-372899, EBI-25984441; Q13148; P09565: PP9974; NbExp=6; IntAct=EBI-372899, EBI-10196507; Q13148; O75807: PPP1R15A; NbExp=10; IntAct=EBI-372899, EBI-714746; Q13148; Q6ZMI0-5: PPP1R21; NbExp=6; IntAct=EBI-372899, EBI-25835994; Q13148; O60260-5: PRKN; NbExp=3; IntAct=EBI-372899, EBI-21251460; Q13148; Q6P2Q9: PRPF8; NbExp=3; IntAct=EBI-372899, EBI-538479; Q13148; P60891: PRPS1; NbExp=6; IntAct=EBI-372899, EBI-749195; Q13148; P28070: PSMB4; NbExp=3; IntAct=EBI-372899, EBI-603350; Q13148; P28062-2: PSMB8; NbExp=6; IntAct=EBI-372899, EBI-372312; Q13148; Q13200: PSMD2; NbExp=3; IntAct=EBI-372899, EBI-357648; Q13148; P26599-3: PTBP1; NbExp=3; IntAct=EBI-372899, EBI-16437588; Q13148; Q9NS91: RAD18; NbExp=3; IntAct=EBI-372899, EBI-2339393; Q13148; Q09028: RBBP4; NbExp=6; IntAct=EBI-372899, EBI-620823; Q13148; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-372899, EBI-2340624; Q13148; P98175: RBM10; NbExp=3; IntAct=EBI-372899, EBI-721525; Q13148; Q8TBY0: RBM46; NbExp=3; IntAct=EBI-372899, EBI-12068216; Q13148; P38159: RBMX; NbExp=3; IntAct=EBI-372899, EBI-743526; Q13148; Q04206: RELA; NbExp=3; IntAct=EBI-372899, EBI-73886; Q13148; Q9H871: RMND5A; NbExp=3; IntAct=EBI-372899, EBI-2797992; Q13148; Q96G75: RMND5B; NbExp=3; IntAct=EBI-372899, EBI-745055; Q13148; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-372899, EBI-714023; Q13148; Q9ULX5: RNF112; NbExp=6; IntAct=EBI-372899, EBI-25829984; Q13148; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-372899, EBI-749039; Q13148; Q9UBS8: RNF14; NbExp=3; IntAct=EBI-372899, EBI-2130308; Q13148; Q96A37: RNF166; NbExp=3; IntAct=EBI-372899, EBI-2130320; Q13148; Q96D59: RNF183; NbExp=3; IntAct=EBI-372899, EBI-743938; Q13148; Q8N488: RYBP; NbExp=6; IntAct=EBI-372899, EBI-752324; Q13148; Q15393: SF3B3; NbExp=6; IntAct=EBI-372899, EBI-346977; Q13148; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-372899, EBI-11522811; Q13148; Q9GZS3: SKIC8; NbExp=6; IntAct=EBI-372899, EBI-358545; Q13148; Q8NCS7: SLC44A5; NbExp=6; IntAct=EBI-372899, EBI-21504521; Q13148; Q96GM5: SMARCD1; NbExp=6; IntAct=EBI-372899, EBI-358489; Q13148; Q9HCE7-2: SMURF1; NbExp=3; IntAct=EBI-372899, EBI-9845742; Q13148; O14544: SOCS6; NbExp=3; IntAct=EBI-372899, EBI-3929549; Q13148; Q99932-2: SPAG8; NbExp=6; IntAct=EBI-372899, EBI-11959123; Q13148; Q8NHS9: SPATA22; NbExp=6; IntAct=EBI-372899, EBI-7067260; Q13148; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-372899, EBI-2659201; Q13148; O95630: STAMBP; NbExp=3; IntAct=EBI-372899, EBI-396676; Q13148; Q92797-2: SYMPK; NbExp=6; IntAct=EBI-372899, EBI-21560407; Q13148; O60506-4: SYNCRIP; NbExp=6; IntAct=EBI-372899, EBI-11123832; Q13148; Q13148: TARDBP; NbExp=31; IntAct=EBI-372899, EBI-372899; Q13148; Q5VWN6: TASOR2; NbExp=6; IntAct=EBI-372899, EBI-745958; Q13148; Q9Y458: TBX22; NbExp=6; IntAct=EBI-372899, EBI-6427217; Q13148; Q15554-4: TERF2; NbExp=6; IntAct=EBI-372899, EBI-25840535; Q13148; Q8WTV1: THAP3; NbExp=6; IntAct=EBI-372899, EBI-17438286; Q13148; Q92956-2: TNFRSF14; NbExp=6; IntAct=EBI-372899, EBI-25985089; Q13148; P50616: TOB1; NbExp=4; IntAct=EBI-372899, EBI-723281; Q13148; P36406: TRIM23; NbExp=3; IntAct=EBI-372899, EBI-740098; Q13148; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-372899, EBI-11993364; Q13148; L8E9Q5: TRIM65; NbExp=3; IntAct=EBI-372899, EBI-25843781; Q13148; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-372899, EBI-11525489; Q13148; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-372899, EBI-10259086; Q13148; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-372899, EBI-2340370; Q13148; Q9C026: TRIM9; NbExp=6; IntAct=EBI-372899, EBI-720828; Q13148; P41226: UBA7; NbExp=3; IntAct=EBI-372899, EBI-751921; Q13148; Q13404: UBE2V1; NbExp=3; IntAct=EBI-372899, EBI-1050671; Q13148; O94941: UBOX5; NbExp=3; IntAct=EBI-372899, EBI-751901; Q13148; Q8IYU4: UBQLNL; NbExp=3; IntAct=EBI-372899, EBI-12295223; Q13148; Q92995: USP13; NbExp=3; IntAct=EBI-372899, EBI-714351; Q13148; O75604-3: USP2; NbExp=6; IntAct=EBI-372899, EBI-10696113; Q13148; Q86UV5: USP48; NbExp=3; IntAct=EBI-372899, EBI-2512161; Q13148; P40337-2: VHL; NbExp=3; IntAct=EBI-372899, EBI-12157263; Q13148; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-372899, EBI-2850578; Q13148; Q8NEZ2-2: VPS37A; NbExp=3; IntAct=EBI-372899, EBI-10270911; Q13148; P58304: VSX2; NbExp=6; IntAct=EBI-372899, EBI-6427899; Q13148; Q9GZL7: WDR12; NbExp=3; IntAct=EBI-372899, EBI-2490660; Q13148; Q9BRX9: WDR83; NbExp=6; IntAct=EBI-372899, EBI-7705033; Q13148; O00308: WWP2; NbExp=3; IntAct=EBI-372899, EBI-743923; Q13148; Q9H0D6: XRN2; NbExp=7; IntAct=EBI-372899, EBI-372110; Q13148; P67809: YBX1; NbExp=6; IntAct=EBI-372899, EBI-354065; Q13148; O43167-2: ZBTB24; NbExp=3; IntAct=EBI-372899, EBI-25842419; Q13148; P24278: ZBTB25; NbExp=3; IntAct=EBI-372899, EBI-739899; Q13148; Q8N895: ZNF366; NbExp=4; IntAct=EBI-372899, EBI-2813661; Q13148; Q9P0T4: ZNF581; NbExp=6; IntAct=EBI-372899, EBI-745520; Q13148; Q8NBB4-2: ZSCAN1; NbExp=6; IntAct=EBI-372899, EBI-12021938; Q13148; A0A384ME25; NbExp=6; IntAct=EBI-372899, EBI-10211777; Q13148; Q9H669; NbExp=6; IntAct=EBI-372899, EBI-10307430; Q13148; Q9WMX2; Xeno; NbExp=2; IntAct=EBI-372899, EBI-710918; Nucleus toplasm toplasm, Stress granule Mitochondrion te=Continuously travels in and out of the nucleus (PubMed:18957508). Localizes to stress granules in response to oxidative stress (PubMed:19765185). A small subset localizes in mitochondria (PubMed:28794432). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13148-1; Sequence=Displayed; Name=2; IsoId=Q13148-4; Sequence=VSP_056406, VSP_056407; Ubiquitously expressed. In particular, expression is high in pancreas, placenta, lung, genital tract and spleen. Consists of an N-terminal domain (NTD) and two tandem RNA recognition motifs, RRM1 and RRM2, followed by a C-terminal glycine- rich region. Contains a nuclear localization sequence and is mostly nuclear; however, its nuclear export sequence permits it to transport mRNAs to the cytoplasm and even to synapses as part of neuronal granules. Hyperphosphorylated in hippocampus, neocortex, and spinal cord from individuals affected with ALS and FTLDU. Phosphorylated upon cellular stress. Ubiquitinated in hippocampus, neocortex, and spinal cord from individuals affected with ALS and FTLDU. Cleaved to generate C-terminal fragments in hippocampus, neocortex, and spinal cord from individuals affected with ALS and FTLDU. Amyotrophic lateral sclerosis 10 (ALS10) [MIM:612069]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. te=The disease is caused by variants affecting the gene represented in this entry. Neurodegeneration is caused by activation of the cGAS-STING pathway: defects in TARDBP trigger mitochondrial DNA release into the cytosol via the permeability transition pore (PubMed:33031745). Released mitochondrial DNA is then detected by CGAS, leading to activation of the cGAS-STING pathway, triggering type-I interferon production and autoinflammation (PubMed:33031745). Sequence=ABO32290.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence=; Sequence=ABO32292.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence=; RNA polymerase II distal enhancer sequence-specific DNA binding negative regulation of protein phosphorylation nucleic acid binding DNA binding double-stranded DNA binding transcription factor activity, sequence-specific DNA binding RNA binding mRNA 3'-UTR binding protein binding nucleus nucleoplasm perichromatin fibrils cytoplasm regulation of transcription, DNA-templated transcription from RNA polymerase II promoter mRNA processing RNA splicing gene expression cytoplasmic stress granule negative regulation of gene expression nuclear speck regulation of protein stability positive regulation of insulin secretion response to endoplasmic reticulum stress interchromatin granule positive regulation of protein import into nucleus regulation of circadian rhythm identical protein binding regulation of apoptotic process sequence-specific DNA binding negative regulation by host of viral transcription rhythmic process regulation of cell cycle 3'-UTR-mediated mRNA stabilization nuclear inner membrane organization pre-mRNA intronic binding sequence-specific double-stranded DNA binding ribonucleoprotein complex uc001art.1 uc001art.2 uc001art.3 uc001art.4 uc001art.5 
ENST00000240189.2 PRAMEF2 ENST00000240189.2 PRAME family member 2 (from RefSeq NM_023014.1) ENST00000240189.1 NM_023014 O60811 PRAM2_HUMAN PRAMEF2 uc001aum.1 Belongs to the PRAME family. cytoplasm positive regulation of cell proliferation negative regulation of apoptotic process negative regulation of cell differentiation negative regulation of transcription, DNA-templated uc001aum.1 
ENST00000240285.10 RDH10 ENST00000240285.10 retinol dehydrogenase 10 (from RefSeq NM_172037.5) ENST00000240285.1 ENST00000240285.2 ENST00000240285.3 ENST00000240285.4 ENST00000240285.5 ENST00000240285.6 ENST00000240285.7 ENST00000240285.8 ENST00000240285.9 NM_172037 Q8IZV5 RDH10_HUMAN SDR16C4 UNQ9375/PRO34191 uc003xzi.1 uc003xzi.2 uc003xzi.3 uc003xzi.4 uc003xzi.5 This gene encodes a retinol dehydrogenase, which converts all-trans-retinol to all-trans-retinal, with preference for NADP as a cofactor. Studies in mice suggest that this protein is essential for synthesis of embryonic retinoic acid and is required for limb, craniofacial, and organ development. [provided by RefSeq, Dec 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC067131.1, SRR1660805.173060.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240285.10/ ENSP00000240285.5 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol. Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.300; Evidence=; Cofactor metabolism; retinol metabolism. Q8IZV5; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-11913715, EBI-2876502; Q8IZV5; Q9BW61: DDA1; NbExp=3; IntAct=EBI-11913715, EBI-2510241; Q8IZV5; Q05329: GAD2; NbExp=3; IntAct=EBI-11913715, EBI-9304251; Q8IZV5; Q96LZ7: RMDN2; NbExp=3; IntAct=EBI-11913715, EBI-2806908; Microsome membrane ; Single-pass membrane protein Endoplasmic reticulum membrane ; Single-pass membrane protein Detected in retina, kidney, liver, small intestine, placenta, lung, heart and skeletal muscle. Belongs to the short-chain dehydrogenases/reductases (SDR) family. retinoid metabolic process metanephros development in utero embryonic development retinoic acid biosynthetic process retinol dehydrogenase activity cytoplasm endoplasmic reticulum endoplasmic reticulum membrane lipid particle visual perception gonad development animal organ morphogenesis neural crest cell development membrane integral component of membrane oxidoreductase activity embryonic camera-type eye development organelle membrane embryonic forelimb morphogenesis retinol metabolic process retinal metabolic process intracellular membrane-bounded organelle ear development nose development embryonic organ development embryonic viscerocranium morphogenesis NADP-retinol dehydrogenase activity oxidation-reduction process primary lung bud formation bud elongation involved in lung branching positive regulation of retinoic acid biosynthetic process nucleus uc003xzi.1 uc003xzi.2 uc003xzi.3 uc003xzi.4 uc003xzi.5 
ENST00000240306.5 DLX4 ENST00000240306.5 distal-less homeobox 4, transcript variant 1 (from RefSeq NM_138281.3) BP1 D3DTX2 D3DTX3 DLX4_HUMAN DLX7 DLX8 DLX9 ENST00000240306.1 ENST00000240306.2 ENST00000240306.3 ENST00000240306.4 NM_138281 O60480 Q13265 Q6PJK0 Q92988 Q9HBE0 uc002ipv.1 uc002ipv.2 uc002ipv.3 uc002ipv.4 uc002ipv.5 Many vertebrate homeo box-containing genes have been identified on the basis of their sequence similarity with Drosophila developmental genes. Members of the Dlx gene family contain a homeobox that is related to that of Distal-less (Dll), a gene expressed in the head and limbs of the developing fruit fly. The Distal-less (Dlx) family of genes comprises at least 6 different members, DLX1-DLX6. The DLX proteins are postulated to play a role in forebrain and craniofacial development. Three transcript variants have been described for this gene, however, the full length nature of one variant has not been described. Studies of the two splice variants revealed that one encoded isoform functions as a repressor of the beta-globin gene while the other isoform lacks that function. [provided by RefSeq, Jul 2008]. May play a role in determining the production of hemoglobin S. May act as a repressor. During embryonic development, plays a role in palatogenesis. Q92988; P16333: NCK1; NbExp=3; IntAct=EBI-1752755, EBI-389883; Q92988; Q13485: SMAD4; NbExp=5; IntAct=EBI-1752755, EBI-347263; Q92988; P08047: SP1; NbExp=4; IntAct=EBI-1752755, EBI-298336; Nucleus Event=Alternative splicing; Named isoforms=3; Comment=Additional isoforms seem to exist. PubMed:9073066 (AAC51171) sequence may be an additional isoform.; Name=1; IsoId=Q92988-1; Sequence=Displayed; Name=2; IsoId=Q92988-2; Sequence=VSP_002236; Name=3; IsoId=Q92988-3; Sequence=VSP_002236, VSP_017043; Expressed in leukemia cells and placenta. Also expressed in kidney and fetal liver. Non-syndromic orofacial cleft 15 (OFC15) [MIM:616788]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. OFC15 inheritance is autosomal dominant. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the distal-less homeobox family. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/49827/DLX4"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter multicellular organism development cell differentiation sequence-specific DNA binding positive regulation of transcription from RNA polymerase II promoter uc002ipv.1 uc002ipv.2 uc002ipv.3 uc002ipv.4 uc002ipv.5 
ENST00000240316.5 COIL ENST00000240316.5 coilin (from RefSeq NM_004645.3) B2R931 CLN80 COIL_HUMAN ENST00000240316.1 ENST00000240316.2 ENST00000240316.3 ENST00000240316.4 NM_004645 P38432 uc002iuu.1 uc002iuu.2 uc002iuu.3 uc002iuu.4 uc002iuu.5 The protein encoded by this gene is an integral component of Cajal bodies (also called coiled bodies). Cajal bodies are nuclear suborganelles of varying number and composition that are involved in the post-transcriptional modification of small nuclear and small nucleolar RNAs. The N-terminus of the coilin protein directs its self-oligomerization while the C-terminus influences the number of nuclear bodies assembled per cell. Differential methylation and phosphorylation of coilin likely influences its localization among nuclear bodies and the composition and assembly of Cajal bodies. This gene has pseudogenes on chromosome 4 and chromosome 14. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.621235.1, BC010385.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240316.5/ ENSP00000240316.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. Interacts with ANKS1B (PubMed:15862129). Interacts with SMN1 (via Tudor domain) (PubMed:11641277). Interacts (via C-terminus) with AK6 (PubMed:16079131). Interacts with WRAP53/TCAB1 (PubMed:21072240). Interacts with HMBOX1 (PubMed:23685356). Interacts with PSME3; the interaction is inhibited by PSME3IP1 (PubMed:29934401). Interacts wit UBL5 (PubMed:23726919). P38432; P58397-3: ADAMTS12; NbExp=3; IntAct=EBI-945751, EBI-12048761; P38432; Q9Y3D8: AK6; NbExp=5; IntAct=EBI-945751, EBI-2896123; P38432; Q7Z6G8-1: ANKS1B; NbExp=3; IntAct=EBI-945751, EBI-20771343; P38432; Q7Z6G8-2: ANKS1B; NbExp=3; IntAct=EBI-945751, EBI-20771303; P38432; Q9P291: ARMCX1; NbExp=3; IntAct=EBI-945751, EBI-2843626; P38432; P54253: ATXN1; NbExp=9; IntAct=EBI-945751, EBI-930964; P38432; P54253-1: ATXN1; NbExp=6; IntAct=EBI-945751, EBI-930975; P38432; Q13895: BYSL; NbExp=11; IntAct=EBI-945751, EBI-358049; P38432; Q96LT7: C9orf72; NbExp=3; IntAct=EBI-945751, EBI-2961725; P38432; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-945751, EBI-10961624; P38432; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-945751, EBI-396137; P38432; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-945751, EBI-739624; P38432; P38432: COIL; NbExp=3; IntAct=EBI-945751, EBI-945751; P38432; Q9Y295: DRG1; NbExp=3; IntAct=EBI-945751, EBI-719554; P38432; Q96EX3: DYNC2I2; NbExp=3; IntAct=EBI-945751, EBI-2556091; P38432; P61328: FGF12; NbExp=3; IntAct=EBI-945751, EBI-6657662; P38432; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-945751, EBI-14103818; P38432; O75031: HSF2BP; NbExp=3; IntAct=EBI-945751, EBI-7116203; P38432; O60341: KDM1A; NbExp=3; IntAct=EBI-945751, EBI-710124; P38432; Q8TBB1: LNX1; NbExp=2; IntAct=EBI-945751, EBI-739832; P38432; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-945751, EBI-348259; P38432; P55081: MFAP1; NbExp=3; IntAct=EBI-945751, EBI-1048159; P38432; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-945751, EBI-725252; P38432; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-945751, EBI-3920396; P38432; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-945751, EBI-741158; P38432; Q08499: PDE4D; NbExp=3; IntAct=EBI-945751, EBI-1642831; P38432; Q08499-8: PDE4D; NbExp=3; IntAct=EBI-945751, EBI-9090666; P38432; Q96HC4: PDLIM5; NbExp=4; IntAct=EBI-945751, EBI-751267; P38432; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-945751, EBI-79165; P38432; O60568: PLOD3; NbExp=3; IntAct=EBI-945751, EBI-741582; P38432; P62875: POLR2L; NbExp=3; IntAct=EBI-945751, EBI-359527; P38432; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-945751, EBI-5452779; P38432; P61289: PSME3; NbExp=6; IntAct=EBI-945751, EBI-355546; P38432; Q03393: PTS; NbExp=3; IntAct=EBI-945751, EBI-712344; P38432; Q16637: SMN2; NbExp=4; IntAct=EBI-945751, EBI-395421; P38432; P62306: SNRPF; NbExp=6; IntAct=EBI-945751, EBI-356900; P38432; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-945751, EBI-12023934; P38432; P78362: SRPK2; NbExp=3; IntAct=EBI-945751, EBI-593303; P38432; Q99986: VRK1; NbExp=9; IntAct=EBI-945751, EBI-1769146; P38432; Q9BUR4: WRAP53; NbExp=4; IntAct=EBI-945751, EBI-2563542; P38432; P13010: XRCC5; NbExp=6; IntAct=EBI-945751, EBI-357997; P38432; P12956: XRCC6; NbExp=3; IntAct=EBI-945751, EBI-353208; P38432; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-945751, EBI-597063; P38432; G5E9M4: ZNF277; NbExp=3; IntAct=EBI-945751, EBI-11995620; P38432; Q8WWA6: ZNF277; NbExp=3; IntAct=EBI-945751, EBI-10192794; Nucleus Nucleus, Cajal body Found in all the cell types examined. The atypical Tudor domain at the C-terminus contains two large unstructured loops, and does not bind methylated residues. Symmetrical dimethylation of arginine residues within the RG repeat region enhances affinity for SMN, and thus localization of SMN complexes to CBs. Phosphorylation during mitosis is associated with disassembly of CBs. Belongs to the coilin family. spliceosomal snRNP assembly fibrillar center protein binding nucleus nucleoplasm nucleolus protein C-terminus binding Cajal body membrane nuclear body U1 snRNA binding U2 snRNA binding identical protein binding uc002iuu.1 uc002iuu.2 uc002iuu.3 uc002iuu.4 uc002iuu.5 
ENST00000240328.4 TBX2 ENST00000240328.4 T-box transcription factor 2 (from RefSeq NM_005994.4) ENST00000240328.1 ENST00000240328.2 ENST00000240328.3 NM_005994 Q13207 Q16424 Q7Z647 TBX2_HUMAN uc010wox.1 uc010wox.2 uc010wox.3 uc010wox.4 This gene is a member of a phylogenetically conserved family of genes that share a common DNA-binding domain, the T-box. T-box genes encode transcription factors involved in the regulation of developmental processes. This gene product is the human homolog of mouse Tbx2, and shares strong sequence similarity with Drosophila omb protein. Expression studies indicate that this gene may have a potential role in tumorigenesis as an immortalizing agent. Transcript heterogeneity due to alternative polyadenylation has been noted for this gene. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC052566.1, AL832900.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240328.4/ ENSP00000240328.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcription factor which acts as a transcriptional repressor (PubMed:11111039, PubMed:11062467, PubMed:12000749, PubMed:22844464, PubMed:30599067). May also function as a transcriptional activator (By similarity). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (PubMed:11111039, PubMed:12000749, PubMed:22844464, PubMed:30599067). Required for cardiac atrioventricular canal formation (PubMed:29726930). May cooperate with NKX2.5 to negatively modulate expression of NPPA/ANF in the atrioventricular canal (By similarity). May play a role as a positive regulator of TGFB2 expression, perhaps acting in concert with GATA4 in the developing outflow tract myocardium (By similarity). Plays a role in limb pattern formation (PubMed:29726930). Acts as a transcriptional repressor of ADAM10 gene expression, perhaps in concert with histone deacetylase HDAC1 as cofactor (PubMed:30599067). Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX3 (By similarity). Required, together with TBX3, to maintain cell proliferation in the embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and TGFbeta signaling (By similarity). Involved in modulating early inner ear development, acting independently of, and also redundantly with TBX3, in different subregions of the developing ear (By similarity). Acts as a negative regulator of PML function in cellular senescence (PubMed:22002537). Acts as a negative regulator of expression of CDKN1A/p21, IL33 and CCN4; repression of CDKN1A is enhanced in response to UV-induced stress, perhaps as a result of phosphorylation by p38 MAPK (By similarity). Negatively modulates expression of CDKN2A/p14ARF and CDH1/E-cadherin (PubMed:11062467, PubMed:12000749, PubMed:22844464). Plays a role in induction of the epithelial-mesenchymal transition (EMT) (PubMed:22844464). Plays a role in melanocyte proliferation, perhaps via regulation of cyclin CCND1 (By similarity). Involved in melanogenesis, acting via negative modulation of expression of DHICA oxidase/TYRP1 and P protein/OCA2 (By similarity). Involved in regulating retinal pigment epithelium (RPE) cell proliferation, perhaps via negatively modulating transcription of the transcription factor CEBPD (PubMed:28910203). Binds DNA as a monomer (PubMed:11111039). Interacts with PML (isoform PML-2, isoform PML-3 and isoform PML-4) (PubMed:22002537). Q13207; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-2853051, EBI-8624731; Q13207; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-2853051, EBI-7062247; Q13207; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-2853051, EBI-743033; Q13207; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2853051, EBI-3867333; Q13207; P25791-3: LMO2; NbExp=3; IntAct=EBI-2853051, EBI-11959475; Q13207; O14770-4: MEIS2; NbExp=3; IntAct=EBI-2853051, EBI-8025850; Q13207; P29590: PML; NbExp=2; IntAct=EBI-2853051, EBI-295890; Q13207; O14787-2: TNPO2; NbExp=3; IntAct=EBI-2853051, EBI-12076664; Q13207; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-2853051, EBI-948354; Nucleus Expressed primarily in adult in kidney, lung, and placenta. Weak expression in heart and ovary. Expressed in the outflow tract and the atrioventricular canal at embryonic stage 12 and gradually reduced by stage 16 (at protein level). Repression domain 1 (RD1) is involved in transcriptional repression (PubMed:11062467, PubMed:30599067). RD1 is necessary for its interaction with PML (PubMed:22002537). Vertebral anomalies and variable endocrine and T-cell dysfunction (VETD) [MIM:618223]: An autosomal dominant syndrome characterized by skeletal malformations primarily involving the vertebrae, immunodeficiency, endocrine abnormalities such as hypoparathyroidism and growth hormone deficiency, craniofacial dysmorphism, congenital cardiac anomalies consisting of double-outlet right ventricle, pulmonary valve stenosis and atrial septal defect, and developmental impairments. Note=The disease is caused by variants affecting the gene represented in this entry. Sequence=AAA73861.1; Type=Frameshift; Evidence=; Sequence=AAH52566.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/42485/TBX2"; Name=Undiagnosed Disease Network; Note=TBX2; URL="https://undiagnosed.hms.harvard.edu/updates/genes-of-interest/tbx2-gene/"; negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding RNA polymerase II activating transcription factor binding transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding cell fate specification heart looping heart morphogenesis outflow tract septum morphogenesis outflow tract morphogenesis endocardial cushion morphogenesis cardiac chamber development regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus transcription factor complex regulation of transcription, DNA-templated Notch signaling pathway multicellular organism development central nervous system development muscle cell fate determination cell aging regulation of heart contraction positive regulation of cell proliferation embryonic heart tube development aorta morphogenesis atrioventricular canal development embryonic digit morphogenesis sequence-specific DNA binding negative regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter embryonic camera-type eye morphogenesis cardiac muscle tissue development palate development positive regulation of cardiac muscle cell proliferation pharynx development developmental growth involved in morphogenesis mammary placode formation cellular senescence negative regulation of heart looping negative regulation of cardiac chamber formation uc010wox.1 uc010wox.2 uc010wox.3 uc010wox.4 
ENST00000240333.12 SLC35B1 ENST00000240333.12 solute carrier family 35 member B1, transcript variant 1 (from RefSeq NM_005827.4) B4DEC4 ENST00000240333.1 ENST00000240333.10 ENST00000240333.11 ENST00000240333.2 ENST00000240333.3 ENST00000240333.4 ENST00000240333.5 ENST00000240333.6 ENST00000240333.7 ENST00000240333.8 ENST00000240333.9 J3KQV4 NM_005827 P78383 Q96EW7 S35B1_HUMAN SLC35B1 UGTREL1 uc285oet.1 uc285oet.2 This gene encodes a nucleotide sugar transporter which is a member of solute carrier family 35. The transporters in this family are highly conserved hydrophobic proteins with multiple transmembrane domains. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2013]. ATP:ADP antiporter that catalyzes the exchange of ATP and ADP across the endoplasmic reticulum (ER) membrane. Imports ATP from the cytosol to the ER lumen and exports ADP in the opposite direction (PubMed:30154480, PubMed:35041824). Regulates ER energy metabolism and protein biogenesis. Appears to be part of a calcium-dependent ER to cytosol low energy response axis, where calcium efflux from ER to the cytosol triggers ATP import into the ER lumen to maintain sufficient ATP supply. Provides ATP to ER chaperone HSPA5 that drives protein folding and trafficking in the ER (PubMed:30154480, PubMed:35041824). Can transport dATP, UTP or UDP in exchange for ATP, but the physiological relevance of this process remains to be established (PubMed:30154480, PubMed:35041824). [Isoform 1]: ATP:ADP antiporter. [Isoform 2]: ATP:ADP antiporter. [Isoform 1]: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35001; Evidence=; [Isoform 1]: Reaction=ATP(in) + UDP(out) = ATP(out) + UDP(in); Xref=Rhea:RHEA:73707, ChEBI:CHEBI:30616, ChEBI:CHEBI:58223; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73708; Evidence=; [Isoform 1]: Reaction=ATP(in) + UTP(out) = ATP(out) + UTP(in); Xref=Rhea:RHEA:73711, ChEBI:CHEBI:30616, ChEBI:CHEBI:46398; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73712; Evidence=; [Isoform 1]: Reaction=ATP(in) + dATP(out) = ATP(out) + dATP(in); Xref=Rhea:RHEA:73715, ChEBI:CHEBI:30616, ChEBI:CHEBI:61404; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73716; Evidence=; [Isoform 2]: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence=; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35001; Evidence=; [Isoform 1]: Kinetic parameters: KM=34.7 uM for ATP ; KM=37.3 uM for ADP ; Vmax=871 pmol/h/mg enzyme toward ATP ; Vmax=962.3 pmol/h/mg enzyme toward ADP ; Temperature dependence: Optimum temperature is 37 degrees Celsius. ; [Isoform 2]: Kinetic parameters: KM=28.7 uM for ATP ; KM=22.5 uM for ADP ; Vmax=676.8 pmol/h/mg enzyme toward ATP ; Vmax=710.5 pmol/h/mg enzyme toward ADP ; P78383; Q13520: AQP6; NbExp=3; IntAct=EBI-12147661, EBI-13059134; P78383; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12147661, EBI-11343438; P78383; Q12983: BNIP3; NbExp=3; IntAct=EBI-12147661, EBI-749464; P78383; Q8WV48: CCDC107; NbExp=3; IntAct=EBI-12147661, EBI-947033; P78383; P04233-2: CD74; NbExp=3; IntAct=EBI-12147661, EBI-12222807; P78383; P11912: CD79A; NbExp=3; IntAct=EBI-12147661, EBI-7797864; P78383; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12147661, EBI-6942903; P78383; Q14318: FKBP8; NbExp=3; IntAct=EBI-12147661, EBI-724839; P78383; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-12147661, EBI-12175685; P78383; Q13467: FZD5; NbExp=3; IntAct=EBI-12147661, EBI-3913027; P78383; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12147661, EBI-13345167; P78383; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12147661, EBI-11956541; P78383; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12147661, EBI-716063; P78383; P54829: PTPN5; NbExp=3; IntAct=EBI-12147661, EBI-1220572; P78383; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-12147661, EBI-1059156; P78383; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-12147661, EBI-744988; Endoplasmic reticulum membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P78383-1; Sequence=Displayed; Name=2; IsoId=P78383-2; Sequence=VSP_054234; The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. Belongs to the nucleotide-sugar transporter family. SLC35B subfamily. UDP-galactose transmembrane transporter activity UDP-glucose transmembrane transporter activity endoplasmic reticulum endoplasmic reticulum membrane carbohydrate transport UDP-glucose transport membrane integral component of membrane transmembrane transporter activity integral component of Golgi membrane integral component of endoplasmic reticulum membrane intracellular membrane-bounded organelle transmembrane transport UDP-galactose transmembrane transport uc285oet.1 uc285oet.2 
ENST00000240364.7 FAM117A ENST00000240364.7 family with sequence similarity 117 member A, transcript variant 1 (from RefSeq NM_030802.4) B7Z7Q3 ENST00000240364.1 ENST00000240364.2 ENST00000240364.3 ENST00000240364.4 ENST00000240364.5 ENST00000240364.6 F117A_HUMAN NM_030802 Q9C073 uc002ipk.1 uc002ipk.2 uc002ipk.3 uc002ipk.4 uc002ipk.5 Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9C073-1; Sequence=Displayed; Name=2; IsoId=Q9C073-2; Sequence=VSP_056129; Belongs to the FAM117 family. uc002ipk.1 uc002ipk.2 uc002ipk.3 uc002ipk.4 uc002ipk.5 
ENST00000240423.9 NCAPH ENST00000240423.9 non-SMC condensin I complex subunit H, transcript variant 1 (from RefSeq NM_015341.5) B4E189 BRRN BRRN1 CAPH CND2_HUMAN ENST00000240423.1 ENST00000240423.2 ENST00000240423.3 ENST00000240423.4 ENST00000240423.5 ENST00000240423.6 ENST00000240423.7 ENST00000240423.8 KIAA0074 NCAPH NM_015341 Q15003 Q8TB87 uc002svz.1 uc002svz.2 uc002svz.3 uc002svz.4 This gene encodes a member of the barr gene family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein encoded by this gene is associated with mitotic chromosomes, except during the early phase of chromosome condensation. During interphase, the protein has a distinct punctate nucleolar localization. Alternatively spliced transcript variants encoding different proteins have been described. [provided by RefSeq, Jul 2013]. Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (PubMed:11136719). Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. Q15003; O00571: DDX3X; NbExp=2; IntAct=EBI-1046410, EBI-353779; Q15003; Q15021: NCAPD2; NbExp=7; IntAct=EBI-1046410, EBI-1044041; Q15003; Q9BPX3: NCAPG; NbExp=8; IntAct=EBI-1046410, EBI-970214; Q15003; O95347: SMC2; NbExp=5; IntAct=EBI-1046410, EBI-355822; Q15003; Q9NTJ3: SMC4; NbExp=3; IntAct=EBI-1046410, EBI-356173; Q15003; P04910: hta2; Xeno; NbExp=2; IntAct=EBI-1046410, EBI-15929287; Nucleus Cytoplasm Chromosome Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q15003-1; Sequence=Displayed; Name=2; IsoId=Q15003-2; Sequence=VSP_055179; Widely expressed at low level. Expressed in proliferating cells. Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPG subunits, activates the condensin complex and is required for chromosome condensation (By similarity). Microcephaly 23, primary, autosomal recessive (MCPH23) [MIM:617985]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the CND2 (condensin subunit 2) family. Sequence=BAA07556.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; condensin complex nuclear condensin complex chromatin binding protein binding nucleus chromosome cytoplasm cytosol cell cycle mitotic chromosome condensation female meiotic division meiotic chromosome condensation membrane chromosome condensation DNA topoisomerase binding meiotic chromosome segregation cell division female meiosis chromosome separation DNA topoisomerase (ATP-hydrolyzing) activator activity positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity uc002svz.1 uc002svz.2 uc002svz.3 uc002svz.4 
ENST00000240488.8 MND1 ENST00000240488.8 meiotic nuclear divisions 1, transcript variant 1 (from RefSeq NM_032117.4) B2R5F9 ENST00000240488.1 ENST00000240488.2 ENST00000240488.3 ENST00000240488.4 ENST00000240488.5 ENST00000240488.6 ENST00000240488.7 GAJ MND1 MND1_HUMAN NM_032117 Q9BWT6 uc003ink.1 uc003ink.2 uc003ink.3 uc003ink.4 The product of the MND1 gene associates with HOP2 (MIM 608665) to form a stable heterodimeric complex that binds DNA and stimulates the recombinase activity of RAD51 (MIM 179617) and DMC1 (MIM 602721) (Chi et al., 2007 [PubMed 17639080]). Both the MND1 and HOP2 genes are indispensable for meiotic recombination.[supplied by OMIM, Mar 2008]. Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis (By similarity). Stimulates both DMC1- and RAD51-mediated homologous strand assimilation, which is required for the resolution of meiotic double- strand breaks. Heterodimer with PSMC3IP/HOP2. MND1-PSMC3IP interacts with DMC1 and RAD51 and binds preferentially to dsDNA. Q9BWT6; Q9P2W1: PSMC3IP; NbExp=5; IntAct=EBI-11137441, EBI-9057595; Nucleus Belongs to the MND1 family. DNA binding double-stranded DNA binding nucleus DNA recombination reciprocal meiotic recombination meiotic cell cycle uc003ink.1 uc003ink.2 uc003ink.3 uc003ink.4 
ENST00000240499.8 ZNF141 ENST00000240499.8 zinc finger protein 141, transcript variant 1 (from RefSeq NM_003441.4) D4S90 ENST00000240499.1 ENST00000240499.2 ENST00000240499.3 ENST00000240499.4 ENST00000240499.5 ENST00000240499.6 ENST00000240499.7 NM_003441 Q15928 Q6DK07 ZN141_HUMAN uc003gaa.1 uc003gaa.2 uc003gaa.3 uc003gaa.4 The protein encoded by this gene is a zinc finger protein that may be a tumor suppressor. Defects in this gene have been associated with autosomal recessive postaxial polydactyly type A. [provided by RefSeq, Jan 2017]. May be involved in transcriptional regulation as a repressor. Plays a role in limb development. Nucleus Ubiquitously low expression. Polydactyly, postaxial A6 (PAPA6) [MIM:615226]: A condition characterized by the occurrence of supernumerary digits in the upper and/or lower extremities. In postaxial polydactyly type A, the extra digit is well-formed and articulates with the fifth or a sixth metacarpal/metatarsal. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the krueppel C2H2-type zinc-finger protein family. nucleic acid binding DNA binding nucleus regulation of transcription, DNA-templated transcription from RNA polymerase II promoter multicellular organism development anatomical structure morphogenesis limb morphogenesis metal ion binding uc003gaa.1 uc003gaa.2 uc003gaa.3 uc003gaa.4 
ENST00000240587.5 TSHZ3 ENST00000240587.5 teashirt zinc finger homeobox 3, transcript variant 1 (from RefSeq NM_020856.4) A1L0U7 ENST00000240587.1 ENST00000240587.2 ENST00000240587.3 ENST00000240587.4 KIAA1474 NM_020856 Q63HK5 Q9H0G6 Q9P254 TSH3 TSH3_HUMAN ZNF537 uc002nsy.1 uc002nsy.2 uc002nsy.3 uc002nsy.4 uc002nsy.5 uc002nsy.6 This gene encodes a zinc-finger transcription factor that regulates smooth muscle cell differentiation in the developing urinary tract. Consistent with this role, mice in which this gene has been inactivated exhibit abnormal gene expression in urinary tract smooth muscle cell precursors and kidney defects including hydronephrosis. The encoded transcription factor comprises a gene silencing complex that inhibits caspase expression. Reduced expression of this gene and consequent caspase upregulation may be correlated with progression of Alzheimer's disease in human patients. [provided by RefSeq, Jul 2016]. Transcriptional regulator involved in developmental processes. Functions in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s) (PubMed:19343227). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up-regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter (By similarity). Involved in the modulation of glutamatergic synaptic transmission and long-term synaptic potentiation (By similarity). Interacts (via homeobox domain) with APBB1 (via PID domain 1). Interacts (via N-terminus) with HDAC1 and HDAC2; the interaction is direct. Found in a trimeric complex with APBB1 and HDAC1; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Q63HK5; Q9H9E1: ANKRA2; NbExp=3; IntAct=EBI-9053916, EBI-10215533; Q63HK5; Q9UBZ4: APEX2; NbExp=3; IntAct=EBI-9053916, EBI-742588; Q63HK5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-9053916, EBI-10175300; Q63HK5; Q96MT8: CEP63; NbExp=3; IntAct=EBI-9053916, EBI-741977; Q63HK5; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-9053916, EBI-739624; Q63HK5; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-9053916, EBI-3866319; Q63HK5; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-9053916, EBI-10171858; Q63HK5; P56545-3: CTBP2; NbExp=6; IntAct=EBI-9053916, EBI-10171902; Q63HK5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-9053916, EBI-618309; Q63HK5; O75031: HSF2BP; NbExp=3; IntAct=EBI-9053916, EBI-7116203; Q63HK5; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-9053916, EBI-749265; Q63HK5; Q15323: KRT31; NbExp=3; IntAct=EBI-9053916, EBI-948001; Q63HK5; Q6A162: KRT40; NbExp=3; IntAct=EBI-9053916, EBI-10171697; Q63HK5; Q5JTD7: LRRC73; NbExp=3; IntAct=EBI-9053916, EBI-12003882; Q63HK5; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-9053916, EBI-742610; Q63HK5; Q13084: MRPL28; NbExp=3; IntAct=EBI-9053916, EBI-723426; Q63HK5; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-9053916, EBI-742948; Q63HK5; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-9053916, EBI-11522433; Q63HK5; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-9053916, EBI-14066006; Q63HK5; Q6NUQ1: RINT1; NbExp=5; IntAct=EBI-9053916, EBI-726876; Q63HK5; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-9053916, EBI-1378139; Q63HK5; Q96R06: SPAG5; NbExp=3; IntAct=EBI-9053916, EBI-413317; Q63HK5; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-9053916, EBI-529518; Q63HK5; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-9053916, EBI-11139477; Q63HK5; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-9053916, EBI-1105213; Q63HK5; Q12933: TRAF2; NbExp=3; IntAct=EBI-9053916, EBI-355744; Q63HK5; P36406: TRIM23; NbExp=3; IntAct=EBI-9053916, EBI-740098; Q63HK5; P14373: TRIM27; NbExp=3; IntAct=EBI-9053916, EBI-719493; Q63HK5; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-9053916, EBI-2130429; Q63HK5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-9053916, EBI-12806590; Nucleus ll projection, growth cone Note=Colocalizes with APBB1 in axonal growth cone (By similarity). Colocalizes with APBB1 in the nucleus. Expressed in brain; strongly reduced in post-mortem elderly subjects with Alzheimer disease (PubMed:18776146, PubMed:19343227). Expressed in the fetal neocortex (PubMed:27668656). Expressed in peri-urothelial cells of the proximal ureter and renal pelvis at 9 weeks of gestation. Note=TSHZ3 haploinsufficiency due to proximal chromosome 19q13.11 deletions causes a neurodevelopmental disorder characterized by developmental delay, absent or delayed speech, intellectual disability, and autistic features. Some patients may have reanal tract abnormalities. Belongs to the teashirt C2H2-type zinc-finger protein family. Sequence=AAI27096.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=AAI27097.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Sequence=CAB66739.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; Name=Protein Spotlight; Note=Life's first breath - Issue 122 of October 2010; URL="https://web.expasy.org/spotlight/back_issues/122"; nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding regulation of respiratory gaseous exchange by neurological system process nucleic acid binding DNA binding chromatin binding protein binding nucleus nucleoplasm regulation of transcription from RNA polymerase II promoter multicellular organism development regulation of gene expression growth cone cell projection negative regulation of transcription, DNA-templated metal ion binding positive regulation of synaptic transmission, glutamatergic long-term synaptic potentiation uc002nsy.1 uc002nsy.2 uc002nsy.3 uc002nsy.4 uc002nsy.5 uc002nsy.6 
ENST00000240615.3 TAS2R8 ENST00000240615.3 taste 2 receptor member 8 (from RefSeq NM_023918.3) ENST00000240615.1 ENST00000240615.2 NM_023918 Q4KN29 Q645Y2 Q9NYW2 TA2R8_HUMAN uc010shh.1 uc010shh.2 uc010shh.3 uc010shh.4 This gene product belongs to the family of candidate taste receptors that are members of the G-protein-coupled receptor superfamily. These proteins are specifically expressed in the taste receptor cells of the tongue and palate epithelia. They are organized in the genome in clusters and are genetically linked to loci that influence bitter perception in mice and humans. In functional expression studies, they respond to bitter tastants. This gene maps to the taste receptor gene cluster on chromosome 12p13. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript is intronless :: BC096735.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5. Q9NYW2; Q86UT5-3: NHERF4; NbExp=3; IntAct=EBI-12092809, EBI-12092811; Membrane; Multi-pass membrane protein. Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Most taste cells may be activated by a limited number of bitter compounds; individual taste cells can discriminate among bitter stimuli. Belongs to the G-protein coupled receptor T2R family. detection of chemical stimulus involved in sensory perception of bitter taste G-protein coupled receptor activity plasma membrane signal transduction G-protein coupled receptor signaling pathway taste receptor activity membrane integral component of membrane bitter taste receptor activity response to stimulus sensory perception of taste uc010shh.1 uc010shh.2 uc010shh.3 uc010shh.4 
ENST00000240617.10 PLBD1 ENST00000240617.10 phospholipase B domain containing 1 (from RefSeq NM_024829.6) A8K4E9 ENST00000240617.1 ENST00000240617.2 ENST00000240617.3 ENST00000240617.4 ENST00000240617.5 ENST00000240617.6 ENST00000240617.7 ENST00000240617.8 ENST00000240617.9 NM_024829 PLBL1_HUMAN Q6P4A8 Q9BVV3 Q9H625 uc001rcc.1 uc001rcc.2 uc001rcc.3 In view of the small size of the putative binding pocket, it has been proposed that it may act as an amidase or a peptidase (By similarity). Exhibits a weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids. pH dependence: Optimum pH is 7.4. ; May form a homodimer, each monomer is composed of a chain A and a chain B. Lysosome Expressed in neutrophils and monocytes. The maturation cleavages that produces chains A and B are required to open the putative substrate binding pocket. Both chains A and B remain associated in the mature protein. Belongs to the phospholipase B-like family. Sequence=AAH00909.2; Type=Erroneous initiation; Evidence=; Sequence=BAB15442.1; Type=Erroneous initiation; Evidence=; phospholipase activity extracellular space lysosome cytosol lipid metabolic process phospholipid metabolic process lipid catabolic process hydrolase activity phosphatidylinositol acyl-chain remodeling phosphatidylcholine acyl-chain remodeling phosphatidylethanolamine acyl-chain remodeling uc001rcc.1 uc001rcc.2 uc001rcc.3 
ENST00000240618.11 KLRK1 ENST00000240618.11 killer cell lectin like receptor K1 (from RefSeq NM_007360.4) A8K7K5 A8K7P4 D12S2489E ENST00000240618.1 ENST00000240618.10 ENST00000240618.2 ENST00000240618.3 ENST00000240618.4 ENST00000240618.5 ENST00000240618.6 ENST00000240618.7 ENST00000240618.8 ENST00000240618.9 NKG2D NKG2D_HUMAN NM_007360 P26718 Q9NR41 uc009zhj.1 uc009zhj.2 uc009zhj.3 uc009zhj.4 uc009zhj.5 Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. NK cells preferentially express several calcium-dependent (C-type) lectins, which have been implicated in the regulation of NK cell function. The NKG2 gene family is located within the NK complex, a region that contains several C-type lectin genes preferentially expressed in NK cells. This gene encodes a member of the NKG2 family. The encoded transmembrane protein is characterized by a type II membrane orientation (has an extracellular C terminus) and the presence of a C-type lectin domain. It binds to a diverse family of ligands that include MHC class I chain-related A and B proteins and UL-16 binding proteins, where ligand-receptor interactions can result in the activation of NK and T cells. The surface expression of these ligands is important for the recognition of stressed cells by the immune system, and thus this protein and its ligands are therapeutic targets for the treatment of immune diseases and cancers. Read-through transcription exists between this gene and the upstream KLRC4 (killer cell lectin-like receptor subfamily C, member 4) family member in the same cluster. [provided by RefSeq, Dec 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC039836.1, AK292059.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240618.11/ ENSP00000240618.6 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress- inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell- mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including MICA, MICB, RAET1E, RAET1G, RAET1L/ULBP6, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4. Homodimer; disulfide-linked. Heterohexamer composed of two subunits of KLRK1 and four subunits of HCST/DAP10. Interacts (via transmembrane domain) with HCST/DAP10 (via transmembrane domain); the interaction is required for KLRK1 NK cell surface and induces NK cell- mediated cytotoxicity. Does not interact with TYROBP. Interacts with CEACAM1; recruits PTPN6 that dephosphorylates VAV1 (PubMed:23696226). P26718; Q29983: MICA; NbExp=2; IntAct=EBI-458344, EBI-1031130; P26718; Q08493-2: PDE4C; NbExp=3; IntAct=EBI-458344, EBI-12169289; P26718; Q8TD07: RAET1E; NbExp=4; IntAct=EBI-458344, EBI-16365677; P26718; Q8TD07-1: RAET1E; NbExp=2; IntAct=EBI-458344, EBI-16747021; P26718; Q8TD07-2: RAET1E; NbExp=2; IntAct=EBI-458344, EBI-16417277; P26718; Q8TD07-5: RAET1E; NbExp=2; IntAct=EBI-458344, EBI-16747044; P26718; Q8TD07-6: RAET1E; NbExp=2; IntAct=EBI-458344, EBI-16747033; P26718; Q6H3X3: RAET1G; NbExp=6; IntAct=EBI-458344, EBI-458334; P26718; Q5VY80: RAET1L; NbExp=4; IntAct=EBI-458344, EBI-16364752; P26718; Q9BZM6: ULBP1; NbExp=2; IntAct=EBI-458344, EBI-16365037; P26718; Q9BZM5: ULBP2; NbExp=6; IntAct=EBI-458344, EBI-3919993; P26718; Q9BZM4: ULBP3; NbExp=4; IntAct=EBI-458344, EBI-1032551; Cell membrane ingle-pass type II membrane protein Note=Colocalized with HCST on the cell surface. Event=Alternative splicing; Named isoforms=1; Comment=A number of isoforms are produced.; Name=1; IsoId=P26718-1; Sequence=Displayed; Expressed in natural killer (NK) cells, CD8(+) alpha-beta and gamma-delta T-cells. Expressed on essentially all CD56+CD3- NK cells from freshly isolated PBMC. Expressed in interferon- producing killer dendritic cells (IKDCs). Up-regulated by interleukin IL15 in primary NK cells. Is not capable of signal transduction by itself, but operates through the adapter protein HCST (PubMed:10426994, PubMed:15894612). Some families of ligands for human and mouse KLRK1 receptors have been characterized being very similar in structure and highly likely to be orthologs. In humans, an additional distinct subfamily of ligands (MICA and MICB) differs structurally, having an extra MHC alpha 3-like domain (PubMed:23298206). Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/41094/KLRK1"; Name=Functional Glycomics Gateway - Glycan Binding; Note=NKG-2D; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_246"; stimulatory C-type lectin receptor signaling pathway adaptive immune response immune system process protein binding plasma membrane integral component of plasma membrane signal transduction external side of plasma membrane cell surface membrane integral component of membrane natural killer cell activation cell differentiation carbohydrate binding T cell costimulation MHC class Ib receptor activity positive regulation of interferon-gamma production negative regulation of GTPase activity signaling receptor activity natural killer cell mediated cytotoxicity MHC class I protein binding protein homodimerization activity innate immune response positive regulation of nitric oxide biosynthetic process positive regulation of natural killer cell mediated cytotoxicity regulation of immune response defense response to Gram-positive bacterium cellular response to lipopolysaccharide negative regulation of natural killer cell chemotaxis uc009zhj.1 uc009zhj.2 uc009zhj.3 uc009zhj.4 uc009zhj.5 
ENST00000240619.3 TAS2R10 ENST00000240619.3 taste 2 receptor member 10 (from RefSeq NM_023921.2) ENST00000240619.1 ENST00000240619.2 NM_023921 Q3MIM9 Q6NTD9 Q9NYW0 T2R10_HUMAN uc001qyy.1 uc001qyy.2 uc001qyy.3 This gene product belongs to the family of candidate taste receptors that are members of the G-protein-coupled receptor superfamily. These proteins are specifically expressed in the taste receptor cells of the tongue and palate epithelia. They are organized in the genome in clusters and are genetically linked to loci that influence bitter perception in mice and humans. In functional expression studies, they respond to bitter tastants. This gene maps to the taste receptor gene cluster on chromosome 12p13. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript is intronless :: BC069089.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Gustducin-coupled strychnine receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. Q9NYW0; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-12963900, EBI-2868124; Q9NYW0; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-12963900, EBI-16427978; Q9NYW0; Q96DX8: RTP4; NbExp=3; IntAct=EBI-12963900, EBI-12275482; Q9NYW0; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12963900, EBI-17280858; Membrane; Multi-pass membrane protein. Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Several bitter taste receptors are expressed in a single taste receptor cell. Belongs to the G-protein coupled receptor T2R family. detection of chemical stimulus involved in sensory perception of bitter taste G-protein coupled receptor activity plasma membrane signal transduction G-protein coupled receptor signaling pathway taste receptor activity membrane integral component of membrane bitter taste receptor activity response to stimulus sensory perception of taste uc001qyy.1 uc001qyy.2 uc001qyy.3 
ENST00000240651.14 PYROXD1 ENST00000240651.14 pyridine nucleotide-disulphide oxidoreductase domain 1, transcript variant 1 (from RefSeq NM_024854.5) A6NKI6 B3KWN8 ENST00000240651.1 ENST00000240651.10 ENST00000240651.11 ENST00000240651.12 ENST00000240651.13 ENST00000240651.2 ENST00000240651.3 ENST00000240651.4 ENST00000240651.5 ENST00000240651.6 ENST00000240651.7 ENST00000240651.8 ENST00000240651.9 NM_024854 PYRD1_HUMAN Q8WU10 Q9H6P1 uc001rew.1 uc001rew.2 uc001rew.3 uc001rew.4 uc001rew.5 This gene encodes a nuclear-cytoplasmic pyridine nucleotide-disulphide reductase (PNDR). PNDRs are flavoproteins that catalyze the pyridine nucleotide-dependent reduction of thiol residues in other proteins. The encoded protein belongs to the class I pyridine nucleotide-disulphide oxidoreductase family but lacks the C-terminal dimerization domain found in other family members and instead has a C-terminal nitrile reductase domain. It localizes to the nucleus and to striated sarcomeric compartments. Naturally occurring mutations in this gene cause early-onset myopathy with internalized nuclei and myofibrillar disorganization. A pseudogene of this gene has been defined on chromosome 11. [provided by RefSeq, Apr 2017]. Probable FAD-dependent oxidoreductase; involved in the cellular oxidative stress response (PubMed:27745833). Required for normal sarcomere structure and muscle fiber integrity (By similarity). Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence=; Note=Binds 1 FAD per subunit. ; Q8WU10; Q96BW1: UPRT; NbExp=10; IntAct=EBI-742933, EBI-742943; Nucleus Cytoplasm Cytoplasm, myofibril, sarcomere Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8WU10-1; Sequence=Displayed; Name=2; IsoId=Q8WU10-2; Sequence=VSP_055828; Myopathy, myofibrillar, 8 (MFM8) [MIM:617258]: A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM8 is an autosomal recessive form, clinically characterized by slowly progressive symmetrical weakness affecting both proximal and distal muscles, with normal to moderately elevated creatine kinase. Mild facial weakness, a high palate, nasal speech, and swallowing difficulties are typical features, mild restrictive lung disease is common, and late-onset cardiac involvement may be present. Note=The disease is caused by variants affecting the gene represented in this entry. Note=A mutation in PYROXD1 is the cause of autosomal recessive limb-girdle muscular dystrophy. The affected individual with a homozygous recessive PYROXD1 mutation showed progressive muscle weakness with an onset at the age of 9 years. Initial symptoms included excessive falling while running, with slowly progressive weakness. Difficulty navigating stairs by the age if 18, and loss of ambulation at the age of 37 years. Neurological examination showed proximal symmetrical muscle weakness and wasting, along with calf muscle pseudohypertrophy. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. PYROXD1 subfamily. Sequence=BAB15214.1; Type=Frameshift; Evidence=; protein binding nucleus cytoplasm oxidoreductase activity sarcomere cellular response to oxidative stress oxidation-reduction process uc001rew.1 uc001rew.2 uc001rew.3 uc001rew.4 uc001rew.5 
ENST00000240652.8 IAPP ENST00000240652.8 islet amyloid polypeptide, transcript variant 1 (from RefSeq NM_000415.3) ENST00000240652.1 ENST00000240652.2 ENST00000240652.3 ENST00000240652.4 ENST00000240652.5 ENST00000240652.6 ENST00000240652.7 IAPP_HUMAN NM_000415 P10997 Q0ZD87 Q14598 uc001rev.1 uc001rev.2 uc001rev.3 uc001rev.4 uc001rev.5 This gene encodes a member of the calcitonin family of peptide hormones. This hormone is released from pancreatic beta cells following food intake to regulate blood glucose levels and act as a satiation signal. Human patients with type 1 and advanced type 2 diabetes exhibit reduced levels of the encoded hormone in blood and pancreas. This protein also exhibits a bactericidal, antimicrobial activity. [provided by RefSeq, Jul 2016]. Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. Interacts with IDE and INS. Can form homodimers. Interaction with INS inhibits homodimerization and fibril formation. P10997; P56817: BACE1; NbExp=2; IntAct=EBI-8526679, EBI-2433139; P10997; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-8526679, EBI-11282723; P10997; P10997: IAPP; NbExp=14; IntAct=EBI-8526679, EBI-8526679; P10997; P14735-1: IDE; NbExp=3; IntAct=EBI-8526679, EBI-15607031; Secreted The mature protein is largely unstructured in the absence of a cognate ligand, and has a strong tendency to form fibrillar aggregates. Homodimerization may be the first step of amyloid formation. Amyloid fibrils are degraded by IDE. Mass=3936; Method=MALDI; Evidence=; IAPP is the peptide subunit of amyloid found in pancreatic islets of type 2 diabetic patients and in insulinomas. Belongs to the calcitonin family. Name=Wikipedia; Note=Amylin entry; URL="https://en.wikipedia.org/wiki/Amylin"; beta-amyloid binding receptor binding hormone activity protein binding extracellular region extracellular space apoptotic process signal transduction G-protein coupled receptor signaling pathway adenylate cyclase-activating G-protein coupled receptor signaling pathway positive regulation of cytosolic calcium ion concentration cell-cell signaling negative regulation of cell proliferation positive regulation of gene expression positive regulation of protein kinase A signaling negative regulation of mitochondrion organization positive regulation of cell death inclusion body sensory perception of pain negative regulation of protein complex assembly protein destabilization positive regulation of peptidyl-serine phosphorylation eating behavior identical protein binding neuronal cell body positive regulation of apoptotic process positive regulation of MAPK cascade cellular protein metabolic process negative regulation of cell differentiation negative regulation of bone resorption protein homooligomerization positive regulation of protein kinase B signaling positive regulation of ERK1 and ERK2 cascade amylin receptor signaling pathway positive regulation of calcium ion import across plasma membrane amyloid fibril formation regulation of protein kinase C activity uc001rev.1 uc001rev.2 uc001rev.3 uc001rev.4 uc001rev.5 
ENST00000240662.3 KCNJ8 ENST00000240662.3 potassium inwardly rectifying channel subfamily J member 8 (from RefSeq NM_004982.4) ENST00000240662.1 ENST00000240662.2 KCNJ8_HUMAN NM_004982 O00657 Q15842 uc001rff.1 uc001rff.2 uc001rff.3 uc001rff.4 uc001rff.5 Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins. Defects in this gene may be a cause of J-wave syndromes and sudden infant death syndrome (SIDS). [provided by RefSeq, May 2012]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803611.245201.1, SRR1803611.65273.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240662.3/ ENSP00000240662.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium (By similarity). Q15842; P50402: EMD; NbExp=3; IntAct=EBI-17440235, EBI-489887; Q15842; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-17440235, EBI-2844246; Q15842; Q969K7: TMEM54; NbExp=3; IntAct=EBI-17440235, EBI-3922833; Membrane; Multi-pass membrane protein Predominantly detected in fetal and adult heart. Note=Defects in KCNJ8 may be associated with susceptibility to J-wave syndromes, a group of heart disorders characterized by early repolarization events as indicated by abnormal J-wave manifestation on electrocardiogram (ECG). The J point denotes the junction of the QRS complex and the ST segment on the ECG, marking the end of depolarization and the beginning of repolarization. An abnormal J wave is a deflection with a dome or hump morphology immediately following the QRS complex of the surface ECG. Examples of J-wave disorders are arrhythmias associated with an early repolarization pattern in the inferior or mid to lateral precordial leads, Brugada syndrome, some cases of idiopathic ventricular fibrillation (VF) with an early repolarization pattern in the inferior, inferolateral or global leads, as well as arrhythmias associated with hypothermia. Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Hypertrichotic osteochondrodysplasia (HTOCD) [MIM:239850]: A rare disorder characterized by congenital hypertrichosis, neonatal macrosomia, a distinct osteochondrodysplasia, and cardiomegaly. The hypertrichosis leads to thick scalp hair, which extends onto the forehead, and a general increase in body hair. In addition, macrocephaly and coarse facial features, including a broad nasal bridge, epicanthal folds, a wide mouth, and full lips, can be suggestive of a storage disorder. About half of affected individuals are macrosomic and edematous at birth, whereas in childhood they usually have a muscular appearance with little subcutaneous fat. Thickened calvarium, narrow thorax, wide ribs, flattened or ovoid vertebral bodies, coxa valga, osteopenia, enlarged medullary canals, and metaphyseal widening of long bones have been reported. Cardiac manifestations such as patent ductus arteriosus, ventricular hypertrophy, pulmonary hypertension, and pericardial effusions are present in approximately 80% of cases. Motor development is usually delayed due to hypotonia. Most patients have a mild speech delay, and a small percentage have learning difficulties or intellectual disability. te=The disease may be caused by variants affecting distinct genetic loci, including the gene represented in this entry. Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ8 subfamily. inward rectifier potassium channel activity voltage-gated ion channel activity plasma membrane ion transport potassium ion transport voltage-gated potassium channel complex ATP-activated inward rectifier potassium channel activity membrane integral component of membrane regulation of ion transmembrane transport membrane repolarization during ventricular cardiac muscle cell action potential voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization potassium ion import across plasma membrane uc001rff.1 uc001rff.2 uc001rff.3 uc001rff.4 uc001rff.5 
ENST00000240687.2 TAS2R7 ENST00000240687.2 taste 2 receptor member 7 (from RefSeq NM_023919.2) ENST00000240687.1 NM_023919 Q645Y1 Q9NYW3 TA2R7_HUMAN uc001qyv.1 uc001qyv.2 uc001qyv.3 This gene product belongs to the family of candidate taste receptors that are members of the G-protein-coupled receptor superfamily. These proteins are specifically expressed in the taste receptor cells of the tongue and palate epithelia. They are organized in the genome in clusters and are genetically linked to loci that influence bitter perception in mice and humans. In functional expression studies, they respond to bitter tastants. This gene maps to the taste receptor gene cluster on chromosome 12p13. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript is intronless :: BC093992.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240687.2/ ENSP00000240687.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. Membrane; Multi-pass membrane protein. Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Several bitter taste receptors are expressed in a single taste receptor cell. Belongs to the G-protein coupled receptor T2R family. detection of chemical stimulus involved in sensory perception of bitter taste G-protein coupled receptor activity plasma membrane signal transduction G-protein coupled receptor signaling pathway taste receptor activity membrane integral component of membrane bitter taste receptor activity response to stimulus sensory perception of taste uc001qyv.1 uc001qyv.2 uc001qyv.3 
ENST00000240691.4 TAS2R9 ENST00000240691.4 taste 2 receptor member 9 (from RefSeq NM_023917.2) ENST00000240691.1 ENST00000240691.2 ENST00000240691.3 NM_023917 Q502V7 Q50KT0 Q50KT1 Q645W9 Q9NYW1 TA2R9_HUMAN uc001qyx.1 uc001qyx.2 uc001qyx.3 uc001qyx.4 uc001qyx.5 This gene product belongs to the family of candidate taste receptors that are members of the G-protein-coupled receptor superfamily. These proteins are specifically expressed in the taste receptor cells of the tongue and palate epithelia. They are organized in the genome in clusters and are genetically linked to loci that influence bitter perception in mice and humans. In functional expression studies, they respond to bitter tastants. This gene maps to the taste receptor gene cluster on chromosome 12p13. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript is intronless :: BC095519.1 [ECO:0000345] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000240691.4/ ENSP00000240691.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). Membrane; Multi-pass membrane protein. Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Several bitter taste receptors are expressed in a single taste receptor cell. Belongs to the G-protein coupled receptor T2R family. detection of chemical stimulus involved in sensory perception of bitter taste G-protein coupled receptor activity plasma membrane signal transduction G-protein coupled receptor signaling pathway biological_process taste receptor activity membrane integral component of membrane bitter taste receptor activity response to stimulus sensory perception of taste uc001qyx.1 uc001qyx.2 uc001qyx.3 uc001qyx.4 uc001qyx.5 
ENST00000240731.5 ZNF211 ENST00000240731.5 zinc finger protein 211, transcript variant 1 (from RefSeq NM_006385.5) B4DH10 B4DLC9 B4E3C9 B9ZVS7 B9ZVW1 ENST00000240731.1 ENST00000240731.2 ENST00000240731.3 ENST00000240731.4 F8WDV2 NM_006385 Q05BQ7 Q13398 Q2TAL7 Q59EG4 Q59G36 Q5EBL6 ZN211_HUMAN uc002qpp.1 uc002qpp.2 uc002qpp.3 uc002qpp.4 This gene encodes a protein containing a Kruppel-associated box domain and multiple zinc finger domains. This protein may play a role in developmental processes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2014]. May be involved in transcriptional regulation. Nucleus Event=Alternative splicing; Named isoforms=8; Name=1; IsoId=Q13398-1; Sequence=Displayed; Name=2; IsoId=Q13398-2; Sequence=VSP_035702; Name=3; IsoId=Q13398-3; Sequence=VSP_035704; Name=4; IsoId=Q13398-4; Sequence=VSP_035705; Name=5; IsoId=Q13398-5; Sequence=VSP_035703; Name=6; IsoId=Q13398-6; Sequence=VSP_035706; Name=7; IsoId=Q13398-7; Sequence=VSP_045643; Name=8; IsoId=Q13398-8; Sequence=VSP_045643, VSP_046769; Belongs to the krueppel C2H2-type zinc-finger protein family. Sequence=AAA93261.1; Type=Erroneous initiation; Evidence=; Sequence=AAH34351.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence=; Sequence=BAD93084.1; Type=Erroneous initiation; Evidence=; nucleic acid binding DNA binding nucleus regulation of transcription, DNA-templated metal ion binding uc002qpp.1 uc002qpp.2 uc002qpp.3 uc002qpp.4 
ENST00000240851.9 TFG ENST00000240851.9 trafficking from ER to golgi regulator, transcript variant 1 (from RefSeq NM_006070.6) D3DN49 ENST00000240851.1 ENST00000240851.2 ENST00000240851.3 ENST00000240851.4 ENST00000240851.5 ENST00000240851.6 ENST00000240851.7 ENST00000240851.8 G5E9V1 K0J5S8 K0J6K2 NM_006070 Q15656 Q92734 Q969I2 TFG_HUMAN uc003due.1 uc003due.2 uc003due.3 uc003due.4 uc003due.5 There are several documented fusion oncoproteins encoded partially by this gene. This gene also participates in several oncogenic rearrangements resulting in anaplastic lymphoma and mixoid chondrosarcoma, and may play a role in the NF-kappaB pathway. Multiple transcript variants have been found for this gene. [provided by RefSeq, Sep 2010]. Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858). Self-associates to form an oligomeric complex (PubMed:23479643). Interacts with PDCD6; promoting localization and polymerization of TFG at endoplasmic reticulum exit site (PubMed:27813252). Interacts with SEC16B (PubMed:21478858). Q92734; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-357061, EBI-11976299; Q92734; P50995: ANXA11; NbExp=4; IntAct=EBI-357061, EBI-715243; Q92734; Q5T0G8: ANXA11; NbExp=3; IntAct=EBI-357061, EBI-10245225; Q92734; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-357061, EBI-1057448; Q92734; Q8N9W6: BOLL; NbExp=4; IntAct=EBI-357061, EBI-998198; Q92734; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-357061, EBI-11983447; Q92734; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-357061, EBI-953896; Q92734; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-357061, EBI-747776; Q92734; P13569: CFTR; NbExp=7; IntAct=EBI-357061, EBI-349854; Q92734; O43186: CRX; NbExp=3; IntAct=EBI-357061, EBI-748171; Q92734; P33240: CSTF2; NbExp=6; IntAct=EBI-357061, EBI-711360; Q92734; Q15038: DAZAP2; NbExp=5; IntAct=EBI-357061, EBI-724310; Q92734; Q92997: DVL3; NbExp=3; IntAct=EBI-357061, EBI-739789; Q92734; Q01844: EWSR1; NbExp=3; IntAct=EBI-357061, EBI-739737; Q92734; O00167-2: EYA2; NbExp=3; IntAct=EBI-357061, EBI-12807776; Q92734; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-357061, EBI-11978259; Q92734; O75593: FOXH1; NbExp=3; IntAct=EBI-357061, EBI-1759806; Q92734; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-357061, EBI-16429135; Q92734; O14964: HGS; NbExp=3; IntAct=EBI-357061, EBI-740220; Q92734; P52597: HNRNPF; NbExp=3; IntAct=EBI-357061, EBI-352986; Q92734; P42858: HTT; NbExp=3; IntAct=EBI-357061, EBI-466029; Q92734; Q0VD86: INCA1; NbExp=3; IntAct=EBI-357061, EBI-6509505; Q92734; Q5TA45: INTS11; NbExp=3; IntAct=EBI-357061, EBI-748258; Q92734; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-357061, EBI-3957672; Q92734; Q14847-2: LASP1; NbExp=3; IntAct=EBI-357061, EBI-9088686; Q92734; Q96PV6: LENG8; NbExp=3; IntAct=EBI-357061, EBI-739546; Q92734; Q9Y5V3: MAGED1; NbExp=8; IntAct=EBI-357061, EBI-716006; Q92734; Q8NDC0: MAPK1IP1L; NbExp=6; IntAct=EBI-357061, EBI-741424; Q92734; Q71SY5: MED25; NbExp=3; IntAct=EBI-357061, EBI-394558; Q92734; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-357061, EBI-8487781; Q92734; Q4VC12: MSS51; NbExp=3; IntAct=EBI-357061, EBI-11599933; Q92734; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-357061, EBI-748610; Q92734; Q8IV28: NID2; NbExp=3; IntAct=EBI-357061, EBI-10261509; Q92734; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-357061, EBI-12813389; Q92734; Q9UBV8: PEF1; NbExp=6; IntAct=EBI-357061, EBI-724639; Q92734; Q99471: PFDN5; NbExp=3; IntAct=EBI-357061, EBI-357275; Q92734; O15496: PLA2G10; NbExp=3; IntAct=EBI-357061, EBI-726466; Q92734; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-357061, EBI-949255; Q92734; O15162: PLSCR1; NbExp=2; IntAct=EBI-357061, EBI-740019; Q92734; Q16633: POU2AF1; NbExp=3; IntAct=EBI-357061, EBI-943588; Q92734; P86480: PRR20D; NbExp=3; IntAct=EBI-357061, EBI-12754095; Q92734; Q93062: RBPMS; NbExp=3; IntAct=EBI-357061, EBI-740322; Q92734; P78317: RNF4; NbExp=5; IntAct=EBI-357061, EBI-2340927; Q92734; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-357061, EBI-12000762; Q92734; O95486: SEC24A; NbExp=3; IntAct=EBI-357061, EBI-749911; Q92734; Q15428: SF3A2; NbExp=3; IntAct=EBI-357061, EBI-2462271; Q92734; Q15427: SF3B4; NbExp=3; IntAct=EBI-357061, EBI-348469; Q92734; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-357061, EBI-12275818; Q92734; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-357061, EBI-742688; Q92734; Q96LM6: SPMIP9; NbExp=3; IntAct=EBI-357061, EBI-743976; Q92734; Q8IWL8: STH; NbExp=3; IntAct=EBI-357061, EBI-12843506; Q92734; O60806: TBX19; NbExp=3; IntAct=EBI-357061, EBI-12096770; Q92734; Q92734: TFG; NbExp=7; IntAct=EBI-357061, EBI-357061; Q92734; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-357061, EBI-2514383; Q92734; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-357061, EBI-10180829; Q92734; A5D8V6: VPS37C; NbExp=6; IntAct=EBI-357061, EBI-2559305; Q92734; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-357061, EBI-12040603; Q92734; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-357061, EBI-17634549; Endoplasmic reticulum Note=Localizes to endoplasmic reticulum exit site (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:27813252, PubMed:21478858). Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q92734-1; Sequence=Displayed; Name=2; IsoId=Q92734-2; Sequence=VSP_047131; Name=3; IsoId=Q92734-3; Sequence=VSP_057414, VSP_057415; Name=4; IsoId=Q92734-4; Sequence=VSP_047131, VSP_057414, VSP_057415; Ubiquitous. Note=A chromosomal aberration involving TFG is found in papillary thyroid carcinomas (PTCs). Translocation t(1;3)(q21;q11) with NTRK1. The TFG sequence is fused to the 3'-end of NTRK1 generating the TRKT3 (TRK-T3) fusion transcript. Neuropathy, hereditary motor and sensory, Okinawa type (HMSNO) [MIM:604484]: A neurodegenerative disorder characterized by young adult onset of proximal muscle weakness and atrophy, muscle cramps, and fasciculations, with later onset of distal sensory impairment. The disorder is slowly progressive and clinically resembles amyotrophic lateral sclerosis. te=The disease is caused by variants affecting the gene represented in this entry. Spastic paraplegia 57, autosomal recessive (SPG57) [MIM:615658]: A complicated form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. Complicated forms are recognized by additional variable features including spastic quadriparesis, seizures, dementia, amyotrophy, extrapyramidal disturbance, cerebral or cerebellar atrophy, optic atrophy, and peripheral neuropathy, as well as by extra neurological manifestations. te=The disease is caused by variants affecting the gene represented in this entry. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/281/TFG"; Golgi membrane protein binding cytoplasm endoplasmic reticulum cytosol ER to Golgi vesicle-mediated transport vesicle-mediated transport identical protein binding positive regulation of I-kappaB kinase/NF-kappaB signaling COPII vesicle coating endoplasmic reticulum exit site uc003due.1 uc003due.2 uc003due.3 uc003due.4 uc003due.5 
ENST00000240922.8 NAA50 ENST00000240922.8 N-alpha-acetyltransferase 50, NatE catalytic subunit, transcript variant 1 (from RefSeq NM_025146.4) D3DN74 ENST00000240922.1 ENST00000240922.2 ENST00000240922.3 ENST00000240922.4 ENST00000240922.5 ENST00000240922.6 ENST00000240922.7 MAK3 NAA50 NAA50_HUMAN NAT13 NAT5 NM_025146 Q68DQ1 Q9GZZ1 uc003ean.1 uc003ean.2 uc003ean.3 uc003ean.4 N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:22311970, PubMed:21900231, PubMed:27484799). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929). Autoacetylates in vivo (PubMed:19744929). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929). Component of N-alpha- acetyltransferase complexes containing NAA10 and NAA15, which has N- alpha-acetyltransferase activity (PubMed:16507339, PubMed:29754825, PubMed:27484799, PubMed:32042062). Does not influence the acetyltransferase activity of NAA10 (PubMed:16507339, PubMed:27484799). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (PubMed:32042062). The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821). Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258; Evidence= Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein]; Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258; Evidence= Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein]; Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258; Evidence= Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258; Evidence= Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein]; Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258; Evidence= Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]; Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258; Evidence= Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl- [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA- COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258; Evidence= Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein]; Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258; Evidence= Kinetic parameters: KM=132.6 uM for M-A-A-A peptide ; KM=126.1 uM for L-A-A-A peptide ; KM=5 uM for Acetyl-CoA ; KM=79 uM for M-L-G-P-E peptide ; KM=91 uM for M-L-D-P-E peptide ; KM=185 uM for M-I-G-P-E peptide ; KM=190 uM for M-L-A-L-I peptide ; KM=320 uM for M-L-G-T-G peptide ; KM=416 uM for M-L-G-T-E peptide ; KM=460 uM for M-L-R-P-E peptide ; KM=478 uM for M-L-L-P-E peptide ; KM=3734 uM for M-F-G-P-E peptide ; Note=kcat is 7.2 min(-1) with M-L-G-P-E peptide. kcat is 7.2 min(-1) with M-L-D-P-E peptide. kcat is 10.9 min(-1) with M-I-G-P-E peptide. kcat is 6.8 min(-1) with M-L-A-L-I peptide. kcat is 2.3 min(-1) with M-L-G-T-G peptide. kcat is 5.6 min(-1) with M-L-G-T-E peptide. ; pH dependence: Optimum pH is 7.5-8.0. ; Component of the N-terminal acetyltransferase E (NatE) complex at least composed of NAA10, NAA15 and NAA50 (PubMed:16507339, PubMed:29754825, PubMed:32042062). Interacts with NAA10 (PubMed:16507339, PubMed:32042062). Interacts with NAA15 (PubMed:16507339, PubMed:29754825, PubMed:32042062). Predominantly interacts with NAA15 in the N-terminal acetyltransferase A complex (NatA complex); the interactions reduce the acetylation activity of the NatA complex (PubMed:16507339, PubMed:32042062). Component of the N- terminal acetyltransferase E (NatE)/HYPK complex at least composed of NAA10, NAA15, NAA50 and HYPK (PubMed:32042062). Within the complex interacts with NAA15 (PubMed:32042062). Its capacity to interact with the NatA complex is reduced by HYPK (PubMed:32042062). Interacts with NAA35 (By similarity). Q9GZZ1; O14503: BHLHE40; NbExp=6; IntAct=EBI-1052523, EBI-711810; Q9GZZ1; Q6NYC1: JMJD6; NbExp=6; IntAct=EBI-1052523, EBI-8464037; Q9GZZ1; P41227: NAA10; NbExp=3; IntAct=EBI-1052523, EBI-747693; Q9GZZ1; Q9BXJ9: NAA15; NbExp=3; IntAct=EBI-1052523, EBI-1042540; Q9GZZ1; P32243-2: OTX2; NbExp=3; IntAct=EBI-1052523, EBI-9087860; Cytoplasm cleus Note=Localizes to the cytoplasm in interphase cells (PubMed:17502424). Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9GZZ1-1; Sequence=Displayed; Name=2; IsoId=Q9GZZ1-2; Sequence=VSP_024747; Belongs to the acetyltransferase family. GNAT subfamily. peptide alpha-N-acetyltransferase activity protein binding nucleus cytoplasm cytosol N-terminal protein amino acid acetylation mitotic sister chromatid cohesion N-acetyltransferase activity H4 histone acetyltransferase activity histone acetylation transferase activity transferase activity, transferring acyl groups NatA complex establishment of mitotic sister chromatid cohesion histone H4 acetylation peptidyl-lysine acetyltransferase activity extracellular exosome mitotic sister chromatid cohesion, centromeric uc003ean.1 uc003ean.2 uc003ean.3 uc003ean.4 
ENST00000241014.6 MAPK8IP1 ENST00000241014.6 mitogen-activated protein kinase 8 interacting protein 1 (from RefSeq NM_005456.4) D3DQP4 ENST00000241014.1 ENST00000241014.2 ENST00000241014.3 ENST00000241014.4 ENST00000241014.5 IB1 JIP1 JIP1_HUMAN NM_005456 O43407 PRKM8IP Q9UQF2 uc001nbr.1 uc001nbr.2 uc001nbr.3 uc001nbr.4 This gene encodes a regulator of the pancreatic beta-cell function. It is highly similar to JIP-1, a mouse protein known to be a regulator of c-Jun amino-terminal kinase (Mapk8). This protein has been shown to prevent MAPK8 mediated activation of transcription factors, and to decrease IL-1 beta and MAP kinase kinase 1 (MEKK1) induced apoptosis in pancreatic beta cells. This protein also functions as a DNA-binding transactivator of the glucose transporter GLUT2. RE1-silencing transcription factor (REST) is reported to repress the expression of this gene in insulin-secreting beta cells. This gene is found to be mutated in a type 2 diabetes family, and thus is thought to be a susceptibility gene for type 2 diabetes. [provided by RefSeq, May 2011]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC068470.1, AF074091.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000241014.6/ ENSP00000241014.2 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells. Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely, MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAP2K7/MKK7, MAP3K11/MLK3 and DLK1. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Interacts, via the PID domain, with ARHGEF28. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of KNS2, then the pre-assembled MAPK8IP1 scaffolding complexes are transported as a cargo of kinesin, to the required subcellular location. Interacts with the cytoplasmic domain of APP. Interacts with DCLK2 (By similarity). Interacts with MAP3K7/TAK1. Interacts with isoform 1 and isoform 2 of VRK2. Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1. Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and MAPK9/JNK2. Interacts with SH3RF2 (By similarity). Q9UQF2; P05067: APP; NbExp=3; IntAct=EBI-78404, EBI-77613; Q9UQF2; P00533: EGFR; NbExp=3; IntAct=EBI-78404, EBI-297353; Q9UQF2; P04626: ERBB2; NbExp=4; IntAct=EBI-78404, EBI-641062; Q9UQF2; O14733: MAP2K7; NbExp=5; IntAct=EBI-78404, EBI-492605; Q9UQF2; O43318: MAP3K7; NbExp=11; IntAct=EBI-78404, EBI-358684; Q9UQF2; P45983: MAPK8; NbExp=7; IntAct=EBI-78404, EBI-286483; Q9UQF2; P12023: App; Xeno; NbExp=2; IntAct=EBI-78404, EBI-78814; Cytoplasm Cytoplasm, perinuclear region Nucleus Endoplasmic reticulum membrane. Mitochondrion membrane. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity). Highly expressed in brain. Expressed in neurons, localizing to neurite tips in differentiating cells. Also expressed in the pancreas, testis and prostate. Low levels in heart, ovary and small intestine. Decreased levels in pancreatic beta cells sensitize cells to IL-1-beta-induced apoptosis. The destruction boxes (D-box) may act as recognition signals for degradation via the ubiquitin-proteasome pathway. A minimal inhibitory domain prevents pancreatic beta cell apoptosis in vitro, and prevents activation of c-jun by MAPK8, MAPK9 and MAPK10. The SH3 domain mediates homodimerization. Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr- 103 is also necessary for the dissociation and activation of MAP3K12. Phosphorylated by isoform 1 and isoform 2 of VRK2. Hyperphosphorylated during mitosis following activation of stress-activated and MAP kinases. Ubiquitinated. Two preliminary events are required to prime for ubiquitination; phosphorylation and an increased in intracellular calcium concentration. Then, the calcium influx initiates ubiquitination and degradation by the ubiquitin-proteasome pathway. Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry. A chemically synthesized cell-permeable peptide of the minimal inhibitory domain decreases brain lesions in both transient and permanent ischemia. The level of protection is still high when administered 6 or 12 hours after ischemia. Belongs to the JIP scaffold family. protein kinase inhibitor activity MAP-kinase scaffold activity protein binding nucleus cytoplasm mitochondrion endoplasmic reticulum endoplasmic reticulum membrane cytosol plasma membrane regulation of transcription, DNA-templated receptor-mediated endocytosis signal transduction JUN phosphorylation JUN kinase binding membrane vesicle-mediated transport kinesin binding protein kinase binding axon dendrite mitogen-activated protein kinase kinase binding mitogen-activated protein kinase kinase kinase binding mitochondrial membrane neuron projection negative regulation of apoptotic process negative regulation of JUN kinase activity dendritic growth cone axonal growth cone cell body dentate gyrus mossy fiber synapse positive regulation of endocytosis regulation of JNK cascade negative regulation of JNK cascade positive regulation of JNK cascade perinuclear region of cytoplasm negative regulation of canonical Wnt signaling pathway regulation of CD8-positive, alpha-beta T cell proliferation negative regulation of intrinsic apoptotic signaling pathway uc001nbr.1 uc001nbr.2 uc001nbr.3 uc001nbr.4 
ENST00000241051.8 DEPDC7 ENST00000241051.8 DEP domain containing 7, transcript variant 1 (from RefSeq NM_001077242.2) DEPD7_HUMAN ENST00000241051.1 ENST00000241051.2 ENST00000241051.3 ENST00000241051.4 ENST00000241051.5 ENST00000241051.6 ENST00000241051.7 G5E941 NM_001077242 Q8N602 Q8NCU9 Q96QD5 Q9UGK5 uc001mub.1 uc001mub.2 uc001mub.3 uc001mub.4 Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96QD5-1; Sequence=Displayed; Name=2; IsoId=Q96QD5-2; Sequence=VSP_047180; Expressed in liver. Belongs to the DEPDC7 family. Sequence=AAM22871.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; molecular_function cellular_component cytosol biological_process intracellular signal transduction regulation of small GTPase mediated signal transduction uc001mub.1 uc001mub.2 uc001mub.3 uc001mub.4 
ENST00000241052.5 CAT ENST00000241052.5 catalase (from RefSeq NM_001752.4) A8K6C0 B2RCZ9 CATA_HUMAN D3DR07 ENST00000241052.1 ENST00000241052.2 ENST00000241052.3 ENST00000241052.4 NM_001752 P04040 Q2M1U4 Q4VXX5 Q9BWT9 Q9UC85 uc001mvm.1 uc001mvm.2 uc001mvm.3 uc001mvm.4 uc001mvm.5 This gene encodes catalase, a key antioxidant enzyme in the bodies defense against oxidative stress. Catalase is a heme enzyme that is present in the peroxisome of nearly all aerobic cells. Catalase converts the reactive oxygen species hydrogen peroxide to water and oxygen and thereby mitigates the toxic effects of hydrogen peroxide. Oxidative stress is hypothesized to play a role in the development of many chronic or late-onset diseases such as diabetes, asthma, Alzheimer's disease, systemic lupus erythematosus, rheumatoid arthritis, and cancers. Polymorphisms in this gene have been associated with decreases in catalase activity but, to date, acatalasemia is the only disease known to be caused by this gene. [provided by RefSeq, Oct 2009]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1080032.1, SRR3476690.186343.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000241052.5/ ENSP00000241052.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:7882369). Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:7882369). Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence= Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence=; Homotetramer (PubMed:21976670, PubMed:10666617, PubMed:10656833). Interacts (via microbody targeting signal) with PEX5, monomeric form interacts with PEX5, leading to its translocation into peroxisomes (PubMed:21976670). P04040; P04040: CAT; NbExp=5; IntAct=EBI-2432181, EBI-2432181; Peroxisome Acatalasemia (ACATLAS) [MIM:614097]: A metabolic disorder characterized by a total or near total loss of catalase activity in red cells. It is often associated with ulcerating oral lesions. Acatalasemia is inherited as an autosomal recessive trait. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the catalase family. Name=Wikipedia; Note=Catalase entry; URL="https://en.wikipedia.org/wiki/Catalase"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cat/"; response to reactive oxygen species osteoblast differentiation ureteric bud development response to hypoxia kidney development aminoacylase activity catalase activity peroxidase activity receptor binding extracellular region extracellular space mitochondrial intermembrane space lysosome peroxisome peroxisomal membrane peroxisomal matrix endoplasmic reticulum Golgi apparatus cytosol plasma membrane focal adhesion protein targeting to peroxisome triglyceride metabolic process response to oxidative stress aging cholesterol metabolic process aerobic respiration response to radiation response to UV response to toxic substance response to light intensity UV protection response to ozone response to lead ion positive regulation of phosphatidylinositol 3-kinase signaling response to activity response to inactivity membrane antioxidant activity oxidoreductase activity oxidoreductase activity, acting on peroxide as acceptor enzyme binding hemoglobin metabolic process heme binding negative regulation of NF-kappaB transcription factor activity response to estradiol response to insulin response to vitamin A response to vitamin E response to L-ascorbic acid cellular response to oxidative stress secretory granule lumen response to drug response to hydrogen peroxide hydrogen peroxide catabolic process identical protein binding protein homodimerization activity negative regulation of apoptotic process intracellular membrane-bounded organelle neutrophil degranulation response to ethanol response to cadmium ion metal ion binding NADP binding positive regulation of NF-kappaB transcription factor activity protein tetramerization protein homotetramerization positive regulation of cell division response to hyperoxia oxidation-reduction process extracellular exosome response to fatty acid cellular response to growth factor stimulus response to phenylpropanoid cellular oxidant detoxification ficolin-1-rich granule lumen uc001mvm.1 uc001mvm.2 uc001mvm.3 uc001mvm.4 uc001mvm.5 
ENST00000241069.11 ACHE ENST00000241069.11 acetylcholinesterase (Cartwright blood group), transcript variant 11 (from RefSeq NR_160408.2) A4D2E2 ACES_HUMAN ACHE B7ZKZ0 D6W5X7 ENST00000241069.1 ENST00000241069.10 ENST00000241069.2 ENST00000241069.3 ENST00000241069.4 ENST00000241069.5 ENST00000241069.6 ENST00000241069.7 ENST00000241069.8 ENST00000241069.9 NR_160408 P22303 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 uc003uxf.1 uc003uxf.2 uc003uxf.3 uc003uxf.4 uc003uxf.5 uc003uxf.6 uc003uxf.7 Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally. AChE activity may constitute a sensitive biomarker of RBC ageing in vivo, and thus, may be of aid in understanding the effects of transfusion[provided by RefSeq, Sep 2019]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.17025.1 [ECO:0000332] ##Evidence-Data-END## Hydrolyzes rapidly the acetylcholine neurotransmitter released into the synaptic cleft allowing to terminate the signal transduction at the neuromuscular junction. Role in neuronal apoptosis. Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17562; Evidence=; Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers (By similarity). Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers. Isoform R may be monomeric. P22303; Q9Y215: COLQ; NbExp=2; IntAct=EBI-1637793, EBI-1637847; P22303; P06733: ENO1; NbExp=2; IntAct=EBI-1637793, EBI-353877; P22303; P63244: RACK1; NbExp=2; IntAct=EBI-1637793, EBI-296739; Synapse creted Cell membrane ; Peripheral membrane protein [Isoform T]: Nucleus. Note=Only observed in apoptotic nuclei. [Isoform H]: Cell membrane ; Lipid- anchor, GPI-anchor ; Extracellular side Event=Alternative splicing; Named isoforms=4; Name=T; Synonyms=ACHE-S, synaptic; IsoId=P22303-1; Sequence=Displayed; Name=H; Synonyms=ACHE-E, erythrocytic, E4-E5; IsoId=P22303-2; Sequence=VSP_001457; Name=R; Synonyms=ACHE-R, readthrough; IsoId=P22303-4; Sequence=VSP_035569, VSP_035570; Name=4; IsoId=P22303-3; Sequence=VSP_035568; Isoform H is highly expressed in erythrocytes. ACHE is responsible for the Yt blood group system [MIM:112100]. The molecular basis of the Yt(a)=Yt1/Yt(b)=Yt2 blood group antigens is a single variation in position 353; His-353 corresponds to Yt(a) and the rare variant with Asn-353 to Yt(b). Belongs to the type-B carboxylesterase/lipase family. Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation database; URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=yt"; Name=Wikipedia; Note=Acetylcholinesterase entry; URL="https://en.wikipedia.org/wiki/Acetylcholinesterase"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ache/"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44317/ACHE"; acetylcholine catabolic process in synaptic cleft beta-amyloid binding regulation of receptor recycling osteoblast development acetylcholinesterase activity cholinesterase activity protein binding collagen binding extracellular region basement membrane extracellular space nucleus Golgi apparatus plasma membrane acetylcholine catabolic process phosphatidylcholine biosynthetic process cell adhesion nervous system development synapse assembly muscle organ development cell proliferation response to wounding cell surface membrane hydrolase activity serine hydrolase activity cell junction anchored component of membrane neuromuscular junction receptor internalization negative regulation of synaptic transmission, cholinergic neurotransmitter catabolic process neurotransmitter biosynthetic process acetylcholine binding identical protein binding protein homodimerization activity amyloid precursor protein metabolic process synaptic cleft laminin binding protein self-association synapse neurotransmitter receptor biosynthetic process perinuclear region of cytoplasm positive regulation of protein secretion carboxylic ester hydrolase activity retina development in camera-type eye uc003uxf.1 uc003uxf.2 uc003uxf.3 uc003uxf.4 uc003uxf.5 uc003uxf.6 uc003uxf.7 
ENST00000241071.11 FBXO24 ENST00000241071.11 F-box protein 24, transcript variant 1 (from RefSeq NM_033506.3) A4D2D4 B4DX91 B4DY42 ENST00000241071.1 ENST00000241071.10 ENST00000241071.2 ENST00000241071.3 ENST00000241071.4 ENST00000241071.5 ENST00000241071.6 ENST00000241071.7 ENST00000241071.8 ENST00000241071.9 FBX24 FBX24_HUMAN NM_033506 O75426 Q9H0G1 uc003uvm.1 uc003uvm.2 uc003uvm.3 This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2009]. Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Directly interacts with SKP1 and CUL1. O75426; P08238: HSP90AB1; NbExp=2; IntAct=EBI-6425658, EBI-352572; O75426; Q8WVJ2: NUDCD2; NbExp=2; IntAct=EBI-6425658, EBI-1052153; O75426; Q96LA8: PRMT6; NbExp=3; IntAct=EBI-6425658, EBI-912440; Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=O75426-1; Sequence=Displayed; Name=2; IsoId=O75426-2; Sequence=VSP_011351, VSP_011352, VSP_011353; Name=3; IsoId=O75426-3; Sequence=VSP_043459; Name=4; IsoId=O75426-4; Sequence=VSP_043458; ubiquitin ligase complex ubiquitin-protein transferase activity protein binding protein ubiquitination uc003uvm.1 uc003uvm.2 uc003uvm.3 
ENST00000241125.4 GJA3 ENST00000241125.4 gap junction protein alpha 3 (from RefSeq NM_021954.4) CXA3_HUMAN ENST00000241125.1 ENST00000241125.2 ENST00000241125.3 NM_021954 Q0VAB7 Q9H537 Q9Y6H8 uc001umx.1 uc001umx.2 uc001umx.3 The protein encoded by this gene is a connexin and is a component of lens fiber gap junctions. Defects in this gene are a cause of zonular pulverulent cataract type 3 (CZP3). [provided by RefSeq, Jan 2010]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DR003755.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2142348, SAMEA2142853 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000241125.4/ ENSP00000241125.3 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Structural component of lens fiber gap junctions (PubMed:30044662). Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells (By similarity). They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore (PubMed:30044662). A hemichannel or connexon is composed of a hexamer of connexins. A functional gap junction is formed by the apposition of two hemichannels. Forms heteromeric channels with GJA8. Cell membrane ; Multi-pass membrane protein Cell junction, gap junction Cataract 14, multiple types (CTRCT14) [MIM:601885]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT14 includes zonular pulverulent cataract, among others. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the connexin family. Alpha-type (group II) subfamily. gap junction channel activity plasma membrane integral component of plasma membrane gap junction connexin complex cell communication visual perception membrane integral component of membrane cell junction gap junction hemi-channel activity transmembrane transport gap junction-mediated intercellular transport uc001umx.1 uc001umx.2 uc001umx.3 
ENST00000241256.3 GHSR ENST00000241256.3 growth hormone secretagogue receptor, transcript variant 1a (from RefSeq NM_198407.2) ENST00000241256.1 ENST00000241256.2 GHSR_HUMAN NM_198407 Q14D12 Q6ISR8 Q92847 Q92848 Q96RJ7 uc003fib.1 uc003fib.2 uc003fib.3 uc003fib.4 This gene encodes a member of the G-protein coupled receptor family. The encoded protein may play a role in energy homeostasis and regulation of body weight. Two identified transcript variants are expressed in several tissues and are evolutionary conserved in fish and swine. One transcript, 1a, excises an intron and encodes the functional protein; this protein is the receptor for the Ghrelin ligand and defines a neuroendocrine pathway for growth hormone release. The second transcript (1b) retains the intron and does not function as a receptor for Ghrelin; however, it may function to attenuate activity of isoform 1a. Mutations in this gene are associated with autosomal idiopathic short stature.[provided by RefSeq, Apr 2010]. Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK- 0677, adenosine). Q92847-1; Q92847-1: GHSR; NbExp=12; IntAct=EBI-21459171, EBI-21459171; Q92847-1; Q92847-2: GHSR; NbExp=10; IntAct=EBI-21459171, EBI-21459245; Q92847-1; Q99720: SIGMAR1; NbExp=8; IntAct=EBI-21459171, EBI-3248663; Cell membrane; Multi-pass membrane protein. Event=Alternative splicing; Named isoforms=2; Name=1A; IsoId=Q92847-1; Sequence=Displayed; Name=1B; IsoId=Q92847-2; Sequence=VSP_001916, VSP_001917; Pituitary and hypothalamus. Growth hormone deficiency, isolated partial (GHDP) [MIM:615925]: A disorder characterized by partial growth hormone deficiency resulting in growth delay and short stature, sometimes associated with recurrent episodes of abdominal pain, vomiting, ketosis and hypoglycemia. te=The disease is caused by variants affecting the gene represented in this entry. Belongs to the G-protein coupled receptor 1 family. growth hormone secretagogue receptor activity G-protein coupled receptor activity plasma membrane signal transduction G-protein coupled receptor signaling pathway spermatogenesis female pregnancy learning or memory actin polymerization or depolymerization adult feeding behavior response to hormone hormone-mediated signaling pathway cell surface negative regulation of norepinephrine secretion membrane integral component of membrane growth hormone-releasing hormone receptor activity peptide hormone binding growth hormone secretion response to food negative regulation of appetite positive regulation of appetite response to follicle-stimulating hormone response to estradiol negative regulation of interleukin-1 beta production cellular response to insulin stimulus ghrelin secretion positive regulation of multicellular organism growth negative regulation of tumor necrosis factor biosynthetic process hormone binding neuron projection regulation of hindgut contraction positive regulation of insulin-like growth factor receptor signaling pathway membrane raft negative regulation of interleukin-6 biosynthetic process positive regulation of fatty acid metabolic process positive regulation of growth negative regulation of insulin secretion decidualization negative regulation of inflammatory response regulation of synapse assembly regulation of transmission of nerve impulse regulation of growth hormone secretion regulation of feeding behavior response to growth hormone cellular response to lipopolysaccharide response to dexamethasone negative regulation of locomotion involved in locomotory behavior cellular response to thyroid hormone stimulus postsynapse glutamatergic synapse positive regulation of sprouting angiogenesis positive regulation of eating behavior response to monosodium glutamate positive regulation of small intestine smooth muscle contraction negative regulation of tumor necrosis factor secretion regulation of gastric motility positive regulation of vascular endothelial cell proliferation cellular response to insulin-like growth factor stimulus negative regulation of macrophage apoptotic process uc003fib.1 uc003fib.2 uc003fib.3 uc003fib.4 
ENST00000241261.7 TNFSF10 ENST00000241261.7 TNF superfamily member 10, transcript variant 4 (from RefSeq NR_033994.2) ENST00000241261.1 ENST00000241261.2 ENST00000241261.3 ENST00000241261.4 ENST00000241261.5 ENST00000241261.6 NR_033994 Q6IBA9 Q6IBA9_HUMAN TNFSF10 hCG_20249 uc003fid.1 uc003fid.2 uc003fid.3 uc003fid.4 The protein encoded by this gene is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. This protein binds to several members of TNF receptor superfamily including TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4, and possibly also to TNFRSF11B/OPG. The activity of this protein may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4, and TNFRSF11B/OPG that cannot induce apoptosis. The binding of this protein to its receptors has been shown to trigger the activation of MAPK8/JNK, caspase 8, and caspase 3. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2010]. Homotrimer. Membrane ; Single- pass type II membrane protein Belongs to the tumor necrosis factor family. cytokine activity tumor necrosis factor receptor binding extracellular space immune response signal transduction male gonad development membrane integral component of membrane tumor necrosis factor receptor superfamily binding response to insulin positive regulation of apoptotic process TRAIL binding metal ion binding positive regulation of extrinsic apoptotic signaling pathway uc003fid.1 uc003fid.2 uc003fid.3 uc003fid.4 
ENST00000241305.4 CPXM2 ENST00000241305.4 carboxypeptidase X, M14 family member 2 (from RefSeq NM_198148.3) B4E3Q2 CPX2 CPXM2_HUMAN ENST00000241305.1 ENST00000241305.2 ENST00000241305.3 NM_198148 Q8N436 UNQ676/PRO1310 uc001lhk.1 uc001lhk.2 uc001lhk.3 May be involved in cell-cell interactions. Secreted Belongs to the peptidase M14 family. Although related to peptidase M14 family, lacks the active site residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity. metallocarboxypeptidase activity extracellular region extracellular space proteolysis peptide metabolic process zinc ion binding protein processing uc001lhk.1 uc001lhk.2 uc001lhk.3 
ENST00000241337.9 GSTM2 ENST00000241337.9 glutathione S-transferase mu 2, transcript variant 1 (from RefSeq NM_000848.4) B4DRY4 E9PEM9 ENST00000241337.1 ENST00000241337.2 ENST00000241337.3 ENST00000241337.4 ENST00000241337.5 ENST00000241337.6 ENST00000241337.7 ENST00000241337.8 GST4 GSTM2 GSTM2_HUMAN NM_000848 P28161 Q2M318 Q5TZY5 Q8WWE1 uc001dyj.1 uc001dyj.2 uc001dyj.3 uc001dyj.4 uc001dyj.5 Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. [provided by RefSeq, Jul 2008]. Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence=; Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)- eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925, ChEBI:CHEBI:132200, ChEBI:CHEBI:132201; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence=; Homodimer. P28161; P46439: GSTM5; NbExp=6; IntAct=EBI-9023362, EBI-4312072; Cytoplasm. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P28161-1; Sequence=Displayed; Name=2; IsoId=P28161-2; Sequence=VSP_045614; Muscle. Belongs to the GST superfamily. Mu family. glutathione transferase activity glutathione peroxidase activity receptor binding protein binding cytoplasm cytosol glutathione metabolic process regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion sarcoplasmic reticulum transferase activity nitrobenzene metabolic process enzyme binding xenobiotic catabolic process protein homodimerization activity glutathione binding linoleic acid metabolic process intercellular bridge relaxation of cardiac muscle negative regulation of ryanodine-sensitive calcium-release channel activity positive regulation of ryanodine-sensitive calcium-release channel activity extracellular exosome cellular detoxification of nitrogen compound cellular response to caffeine cellular oxidant detoxification glutathione derivative biosynthetic process uc001dyj.1 uc001dyj.2 uc001dyj.3 uc001dyj.4 uc001dyj.5 
ENST00000241356.5 ADORA3 ENST00000241356.5 adenosine A3 receptor, transcript variant C (from RefSeq NM_001302679.2) A2A3P4 AA3R_HUMAN ADORA3 ENST00000241356.1 ENST00000241356.2 ENST00000241356.3 ENST00000241356.4 NM_001302679 P0DMS8 P33765 Q6UWU0 Q9BYZ1 uc001ebh.1 uc001ebh.2 uc001ebh.3 uc001ebh.4 uc001ebh.5 uc001ebh.6 This gene encodes a protein that belongs to the family of adenosine receptors, which are G-protein-coupled receptors that are involved in a variety of intracellular signaling pathways and physiological functions. The receptor encoded by this gene mediates a sustained cardioprotective function during cardiac ischemia, it is involved in the inhibition of neutrophil degranulation in neutrophil-mediated tissue injury, it has been implicated in both neuroprotective and neurodegenerative effects, and it may also mediate both cell proliferation and cell death. Alternative splicing results in multiple transcript variants. This gene shares its 5' terminal exon with some transcripts from overlapping GeneID:57413, which encodes an immunoglobulin domain-containing protein. [provided by RefSeq, Nov 2014]. [Isoform 2]: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase (PubMed:8234299). Cell membrane ; Multi-pass membrane protein Event=Alternative splicing; Named isoforms=3; Name=2; Synonyms=A3AR i2 , A3AR ; IsoId=P0DMS8-1; Sequence=Displayed; Name=1; Synonyms=TMIGD3 i1 , A3AR i1 ; IsoId=P0DMS9-2; Sequence=External; Name=3; Synonyms=TMIGD3 i3, A3AR i3; IsoId=P0DMS9-1; Sequence=External; Expressed in the lung and bone. Expressed at lower levels in osteosarcoma tissues (at protein level). Belongs to the G-protein coupled receptor 1 family. G-protein coupled adenosine receptor activity adenosine receptor signaling pathway G-protein coupled receptor activity plasma membrane integral component of plasma membrane inflammatory response signal transduction G-protein coupled receptor signaling pathway activation of adenylate cyclase activity regulation of heart contraction negative regulation of cell proliferation response to wounding membrane integral component of membrane negative regulation of cell migration negative regulation of NF-kappaB transcription factor activity uc001ebh.1 uc001ebh.2 uc001ebh.3 uc001ebh.4 uc001ebh.5 uc001ebh.6 
ENST00000241393.4 CXCR4 ENST00000241393.4 C-X-C motif chemokine receptor 4, transcript variant 2 (from RefSeq NM_003467.3) B2R5N0 CXCR4_HUMAN ENST00000241393.1 ENST00000241393.2 ENST00000241393.3 NM_003467 O60835 P30991 P56438 P61073 Q53S69 Q9BXA0 Q9UKN2 uc002tuz.1 uc002tuz.2 uc002tuz.3 uc002tuz.4 uc002tuz.5 This gene encodes a CXC chemokine receptor specific for stromal cell-derived factor-1. The protein has 7 transmembrane regions and is located on the cell surface. It acts with the CD4 protein to support HIV entry into cells and is also highly expressed in breast cancer cells. Mutations in this gene have been associated with WHIM (warts, hypogammaglobulinemia, infections, and myelokathexis) syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008]. Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10452968, PubMed:28978524, PubMed:18799424, PubMed:24912431). Involved in the AKT signaling cascade (PubMed:24912431). Plays a role in regulation of cell migration, e.g. during wound healing (PubMed:28978524). Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (PubMed:20228059). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity). (Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) for human immunodeficiency virus-1/HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env- mediated fusion of the virus (PubMed:8849450, PubMed:8929542, PubMed:9427609, PubMed:10074122, PubMed:10756055). Monomer. Can form homodimers (PubMed:20929726). Interacts with CD164 (PubMed:17077324). Interacts with ARRB2; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3. Interacts with ARR3; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates calcium mobilization (PubMed:20048153). Interacts with RNF113A; the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and subsequent degradation (PubMed:28978524). Interacts (via the cytoplasmic C-terminal) with ITCH (via the WW domains I and II); the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and leads to its degradation. Interacts with extracellular ubiquitin. Interacts with DBN1; this interaction is enhanced by antigenic stimulation. Following LPS binding, may form a complex with GDF5, HSP90AA1 and HSPA8. (Microbial infection) Interacts with HIV-1 surface protein gp120 and Tat. (Microbial infection) Interacts with HHV-8 protein ORF K4 (PubMed:25612609). (Microbial infection) May interact with human cytomegalovirus/HHV-5 protein UL78. (Microbial infection) Interacts with Staphylococcus aureus protein SSL10. P61073; P25106: ACKR3; NbExp=18; IntAct=EBI-489411, EBI-1965291; P61073; P51681: CCR5; NbExp=4; IntAct=EBI-489411, EBI-489374; P61073; Q04900: CD164; NbExp=2; IntAct=EBI-489411, EBI-2115896; P61073; P04233: CD74; NbExp=4; IntAct=EBI-489411, EBI-2622890; P61073; P49682: CXCR3; NbExp=5; IntAct=EBI-489411, EBI-12836456; P61073; P32302: CXCR5; NbExp=3; IntAct=EBI-489411, EBI-2835269; P61073; Q16643: DBN1; NbExp=5; IntAct=EBI-489411, EBI-351394; P61073; Q96J02-2: ITCH; NbExp=3; IntAct=EBI-489411, EBI-6672198; P61073; P35579: MYH9; NbExp=5; IntAct=EBI-489411, EBI-350338; P61073; O60603: TLR2; NbExp=3; IntAct=EBI-489411, EBI-973722; P61073; Q07266-1: Dbn1; Xeno; NbExp=3; IntAct=EBI-489411, EBI-8786792; Cell membrane ulti-pass membrane protein Cell junction. Early endosome. Late endosome. Lysosome. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated. In the presence of antigen, distributes to the immunological synapse forming at the T- cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC). Event=Alternative splicing; Named isoforms=2; Comment=Additional isoforms seem to exist.; Name=1; IsoId=P61073-1, P30991-1; Sequence=Displayed; Name=2; Synonyms=CXCR4-LO; IsoId=P61073-2, P30991-2; Sequence=VSP_001890; Expressed in numerous tissues, such as peripheral blood leukocytes, spleen, thymus, spinal cord, heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, cerebellum, cerebral cortex and medulla (in microglia as well as in astrocytes), brain microvascular, coronary artery and umbilical cord endothelial cells. Isoform 1 is predominant in all tissues tested. (Microbial infection) May be down-regulated by Human cytomegalovirus/HHV-5. (Microbial infection) May be down-regulated by HIV-1 tat. The amino-terminus is critical for ligand binding. Residues in all four extracellular regions contribute to HIV-1 coreceptor activity. Phosphorylated on agonist stimulation. Rapidly phosphorylated on serine and threonine residues in the C-terminal. Phosphorylation at Ser-324 and Ser-325 leads to recruitment of ITCH, ubiquitination and protein degradation. Ubiquitinated after ligand binding, leading to its degradation (PubMed:28978524). Ubiquitinated by ITCH at the cell membrane on agonist stimulation (PubMed:14602072, PubMed:34927784). The ubiquitin- dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S. Sulfation on Tyr-21 is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. Tyr-7 and Tyr-12 are sulfated in a sequential manner after Tyr-21 is almost fully sulfated, with the binding affinity for CXCL12/SDF-1alpha increasing with the number of sulfotyrosines present. Sulfotyrosines Tyr-7 and Tyr-12 occupy clefts on opposing CXCL12 subunits, thus bridging the CXCL12 dimer interface and promoting CXCL12 dimerization. O- and N-glycosylated. Asn-11 is the principal site of N- glycosylation. There appears to be very little or no glycosylation on Asn-176. N-glycosylation masks coreceptor function in both X4 and R5 laboratory-adapted and primary HIV-1 strains through inhibiting interaction with their Env glycoproteins. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity. WHIM syndrome 1 (WHIMS1) [MIM:193670]: An autosomal dominant immunologic disease characterized by neutropenia, hypogammaglobulinemia and extensive human papillomavirus (HPV) infection. Despite the peripheral neutropenia, bone marrow aspirates from affected individuals contain abundant mature myeloid cells, a condition termed myelokathexis. te=The disease is caused by variants affecting the gene represented in this entry. Note=CXCR4 mutations play a role in the pathogenesis of Waldenstroem macroglobulinemia (WM) and influence disease presentation and outcome, as well as response to therapy. WM is a B-cell lymphoma characterized by accumulation of malignant lymphoplasmacytic cells in the bone marrow, lymph nodes and spleen, and hypersecretion of monoclonal immunoglobulin M (IgM). Excess IgM production results in serum hyperviscosity, tissue infiltration, and autoimmune-related pathology. Plerixafor (AMD3100), an antagonist of CXCR4 activity, blocks HIV-1 entry, interaction with CXCL12 and subsequent CXCR4 signaling. Belongs to the G-protein coupled receptor 1 family. Was originally thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R) (PubMed:8329116, PubMed:8234909). Later reports showed that it acts as a receptor for the C-X-C chemokine CXCL12/SDF-1 (PubMed:9427609, PubMed:10825158, PubMed:12034737). Sequence=CAA12166.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence=; Name=CXCR4base; Note=CXCR4 mutation db; URL="http://structure.bmc.lu.se/idbase/CXCR4base/"; Name=Wikipedia; Note=CXC chemokine receptors entry; URL="https://en.wikipedia.org/wiki/CXC_chemokine_receptors"; Name=Wikipedia; Note=CXCR4 entry; URL="https://en.wikipedia.org/wiki/CXCR4"; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cxcr4/"; activation of MAPK activity virus receptor activity response to hypoxia neuron migration epithelial cell development dendritic cell chemotaxis actin binding G-protein coupled receptor activity chemokine receptor activity protein binding nucleus cytoplasm lysosome endosome early endosome late endosome plasma membrane apoptotic process chemotaxis inflammatory response immune response signal transduction G-protein coupled receptor signaling pathway positive regulation of cytosolic calcium ion concentration axon guidance brain development neuron recognition drug binding response to virus external side of plasma membrane cell surface response to activity coreceptor activity membrane integral component of membrane viral process cell migration C-C chemokine receptor activity C-X-C chemokine receptor activity fusion of virus membrane with host plasma membrane calcium-mediated signaling cytokine binding chemokine binding C-C chemokine binding neurogenesis telencephalon cell migration cell junction regulation of cell adhesion entry into host cell positive regulation of cell migration cell leading edge cytoplasmic vesicle ubiquitin protein ligase binding myosin light chain binding macromolecular complex positive regulation of vascular wound healing cellular response to drug C-X-C motif chemokine 12 receptor activity CXCL12-activated CXCR4 signaling pathway identical protein binding regulation of programmed cell death ubiquitin binding myelin maintenance response to morphine endothelial cell differentiation positive regulation of oligodendrocyte differentiation positive regulation of neurogenesis regulation of viral process regulation of chemotaxis positive regulation of chemotaxis detection of temperature stimulus involved in sensory perception of pain detection of mechanical stimulus involved in sensory perception of pain regulation of calcium ion transport cardiac muscle contraction cell chemotaxis endothelial tube morphogenesis extracellular exosome cellular response to cytokine stimulus positive regulation of dendrite extension positive regulation of mesenchymal stem cell migration response to ultrasound positive regulation of macrophage migration inhibitory factor signaling pathway uc002tuz.1 uc002tuz.2 uc002tuz.3 uc002tuz.4 uc002tuz.5 
ENST00000241416.12 ACVR2A ENST00000241416.12 activin A receptor type 2A, transcript variant 2 (from RefSeq NM_001616.5) ACVR2 ACVR2A AVR2A_HUMAN B2RAB8 B4DWQ2 D3DP85 ENST00000241416.1 ENST00000241416.10 ENST00000241416.11 ENST00000241416.2 ENST00000241416.3 ENST00000241416.4 ENST00000241416.5 ENST00000241416.6 ENST00000241416.7 ENST00000241416.8 ENST00000241416.9 NM_001616 P27037 Q53TH4 Q6NWV2 Q92474 uc002twh.1 uc002twh.2 uc002twh.3 uc002twh.4 uc002twh.5 uc002twh.6 This gene encodes a receptor that mediates the functions of activins, which are members of the transforming growth factor-beta (TGF-beta) superfamily involved in diverse biological processes. The encoded protein is a transmembrane serine-threonine kinase receptor which mediates signaling by forming heterodimeric complexes with various combinations of type I and type II receptors and ligands in a cell-specific manner. The encoded type II receptor is primarily involved in ligand-binding and includes an extracellular ligand-binding domain, a transmembrane domain and a cytoplasmic serine-threonine kinase domain. This gene may be associated with susceptibility to preeclampsia, a pregnancy-related disease which can result in maternal and fetal morbidity and mortality. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jun 2013]. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A (PubMed:17911401). Mediates induction of adipogenesis by GDF6 (By similarity). Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho- L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA- COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881; Evidence=; Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L- seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Part of a complex consisting of MAGI2/ARIP1, ACVR2A, ACVR1B and SMAD3 (By similarity). Interacts with MAGI2/ARIP1 (By similarity). Interacts with type I receptor ACVR1 (PubMed:17911401). Interacts with BMP7 (PubMed:12667445). Interacts with TSC22D1/TSC-22 (PubMed:21791611). Cell membrane ; Single-pass type I membrane protein Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P27037-1; Sequence=Displayed; Name=2; IsoId=P27037-2; Sequence=VSP_054689; Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/567/ACVR2"; nucleotide binding gastrulation with mouth forming second positive regulation of protein phosphorylation protein kinase activity protein serine/threonine kinase activity transmembrane receptor protein serine/threonine kinase activity transforming growth factor beta-activated receptor activity transforming growth factor beta receptor activity, type II protein binding ATP binding cytoplasm plasma membrane integral component of plasma membrane protein phosphorylation transmembrane receptor protein serine/threonine kinase signaling pathway transforming growth factor beta receptor signaling pathway spermatogenesis determination of left/right symmetry pattern specification process mesoderm development male gonad development anterior/posterior pattern specification regulation of signal transduction cell surface positive regulation of pathway-restricted SMAD protein phosphorylation coreceptor activity membrane integral component of membrane kinase activity phosphorylation transferase activity growth factor binding PDZ domain binding positive regulation of bone mineralization BMP signaling pathway activin receptor signaling pathway positive regulation of activin receptor signaling pathway inhibin-betaglycan-ActRII complex inhibin binding type I transforming growth factor beta receptor binding sperm ejaculation penile erection receptor complex protein self-association positive regulation of erythrocyte differentiation positive regulation of osteoblast differentiation positive regulation of transcription from RNA polymerase II promoter SMAD binding metal ion binding activin receptor complex activin binding embryonic skeletal system development regulation of nitric-oxide synthase activity Sertoli cell proliferation cellular response to BMP stimulus BMP receptor activity activin-activated receptor activity uc002twh.1 uc002twh.2 uc002twh.3 uc002twh.4 uc002twh.5 uc002twh.6 
ENST00000241436.9 POLK ENST00000241436.9 DNA polymerase kappa, transcript variant 10 (from RefSeq NR_170560.3) B2RBD2 DINB1 ENST00000241436.1 ENST00000241436.2 ENST00000241436.3 ENST00000241436.4 ENST00000241436.5 ENST00000241436.6 ENST00000241436.7 ENST00000241436.8 NR_170560 POLK_HUMAN Q5Q9G5 Q5Q9G6 Q5Q9G7 Q5Q9G8 Q86VJ8 Q8IZY0 Q8IZY1 Q8NB30 Q96L01 Q96Q86 Q96Q87 Q9UBT6 Q9UHC5 uc003kdw.1 uc003kdw.2 uc003kdw.3 uc003kdw.4 uc003kdw.5 DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence=; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence=; Note=Divalent metal cations. Prefers Mg(2+), but can also use Mn(2+). ; pH dependence: Optimum pH is 6.5-7.5. ; Temperature dependence: Optimum temperature is 37 degrees Celsius. ; Interacts with REV1 (By similarity). Interacts with PCNA (PubMed:11784855). Nucleus te=Detected throughout the nucleus and at replication foci (PubMed:12414988). Recruited to DNA damage sites in response to ultraviolet irradiation: N6-methyladenosine (m6A)- containing mRNAs accumulate in the vicinity of DNA damage sites and their presence is required to recruit POLK (PubMed:28297716). Event=Alternative splicing; Named isoforms=8; Name=1; IsoId=Q9UBT6-1; Sequence=Displayed; Name=2; IsoId=Q9UBT6-2; Sequence=VSP_012801, VSP_012802; Name=3; IsoId=Q9UBT6-3; Sequence=VSP_012803; Name=4; IsoId=Q9UBT6-4; Sequence=VSP_012804, VSP_012805, VSP_012806; Name=5; IsoId=Q9UBT6-5; Sequence=VSP_053406, VSP_053409; Name=6; IsoId=Q9UBT6-6; Sequence=VSP_053407, VSP_053408; Name=7; IsoId=Q9UBT6-7; Sequence=VSP_012804, VSP_053407, VSP_053408; Name=8; IsoId=Q9UBT6-8; Sequence=VSP_012804; Detected at low levels in testis, spleen, prostate and ovary. Detected at very low levels in kidney, colon, brain, heart, liver, lung, placenta, pancreas and peripheral blood leukocytes. The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. [Isoform 4]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the DNA polymerase type-Y family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/polk/"; DNA binding damaged DNA binding DNA-directed DNA polymerase activity nucleus nucleoplasm DNA replication DNA repair transcription-coupled nucleotide-excision repair nucleotide-excision repair, DNA incision, 5'-to lesion nucleotide-excision repair, DNA gap filling cellular response to DNA damage stimulus nuclear body transferase activity nucleotidyltransferase activity translesion synthesis nucleotide-excision repair, DNA incision cellular response to UV error-prone translesion synthesis metal ion binding DNA biosynthetic process uc003kdw.1 uc003kdw.2 uc003kdw.3 uc003kdw.4 uc003kdw.5 
ENST00000241453.12 FLT3 ENST00000241453.12 fms related receptor tyrosine kinase 3, transcript variant 1 (from RefSeq NM_004119.3) A0AVG9 B7ZLT7 B7ZLT8 CD135 ENST00000241453.1 ENST00000241453.10 ENST00000241453.11 ENST00000241453.2 ENST00000241453.3 ENST00000241453.4 ENST00000241453.5 ENST00000241453.6 ENST00000241453.7 ENST00000241453.8 ENST00000241453.9 F5H0A0 FLK2 FLT3_HUMAN NM_004119 P36888 Q13414 STK1 uc001urw.1 uc001urw.2 uc001urw.3 uc001urw.4 This gene encodes a class III receptor tyrosine kinase that regulates hematopoiesis. This receptor is activated by binding of the fms-related tyrosine kinase 3 ligand to the extracellular domain, which induces homodimer formation in the plasma membrane leading to autophosphorylation of the receptor. The activated receptor kinase subsequently phosphorylates and activates multiple cytoplasmic effector molecules in pathways involved in apoptosis, proliferation, and differentiation of hematopoietic cells in bone marrow. Mutations that result in the constitutive activation of this receptor result in acute myeloid leukemia and acute lymphoblastic leukemia. [provided by RefSeq, Jan 2015]. Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways. Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence= Present in an inactive conformation in the absence of bound ligand. FLT3LG binding leads to dimerization and activation by autophosphorylation. Monomer in the absence of bound FLT3LG. Homodimer in the presence of bound FLT3LG. Interacts with FIZ1 following ligand activation (By similarity). Interacts with FES, FER, LYN, FGR, HCK, SRC and GRB2. Interacts with PTPRJ/DEP-1 and PTPN11/SHP2. Interacts with RNF115 and RNF126 (By similarity). (Microbial infection) Interacts with human cytomegalovirus protein UL7. P36888; P00519: ABL1; NbExp=2; IntAct=EBI-3946257, EBI-375543; P36888; P42684: ABL2; NbExp=3; IntAct=EBI-3946257, EBI-1102694; P36888; P46108: CRK; NbExp=2; IntAct=EBI-3946257, EBI-886; P36888; P46109: CRKL; NbExp=2; IntAct=EBI-3946257, EBI-910; P36888; P06241: FYN; NbExp=2; IntAct=EBI-3946257, EBI-515315; P36888; Q13322: GRB10; NbExp=6; IntAct=EBI-3946257, EBI-80275; P36888; Q9Y6K9: IKBKG; NbExp=2; IntAct=EBI-3946257, EBI-81279; P36888; P06239: LCK; NbExp=2; IntAct=EBI-3946257, EBI-1348; P36888; P27986: PIK3R1; NbExp=2; IntAct=EBI-3946257, EBI-79464; P36888; P20936: RASA1; NbExp=2; IntAct=EBI-3946257, EBI-1026476; P36888; P43405: SYK; NbExp=22; IntAct=EBI-3946257, EBI-78302; P36888; Q8R4L0: Sla2; Xeno; NbExp=14; IntAct=EBI-3946257, EBI-20766300; Membrane; Single-pass type I membrane protein. Endoplasmic reticulum lumen. Note=Constitutively activated mutant forms with internal tandem duplications are less efficiently transported to the cell surface and a significant proportion is retained in an immature form in the endoplasmic reticulum lumen. The activated kinase is rapidly targeted for degradation. Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P36888-1; Sequence=Displayed; Name=2; IsoId=P36888-2; Sequence=VSP_041796; Detected in bone marrow, in hematopoietic stem cells, in myeloid progenitor cells and in granulocyte/macrophage progenitor cells (at protein level). Detected in bone marrow, liver, thymus, spleen and lymph node, and at low levels in kidney and pancreas. Highly expressed in T-cell leukemia. The juxtamembrane autoregulatory region is important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand. Upon tyrosine phosphorylation, it mediates interaction with the SH2 domains of numerous signaling partners. In-frame internal tandem duplications (ITDs) result in constitutive activation of the kinase. The activity of the mutant kinase can be stimulated further by FLT3LG binding. N-glycosylated, contains complex N-glycans with sialic acid. Autophosphorylated on several tyrosine residues in response to FLT3LG binding. FLT3LG binding also increases phosphorylation of mutant kinases that are constitutively activated. Dephosphorylated by PTPRJ/DEP-1, PTPN1, PTPN6/SHP-1, and to a lesser degree by PTPN12. Dephosphorylation is important for export from the endoplasmic reticulum and location at the cell membrane. Rapidly ubiquitinated by UBE2L6 and the E3 ubiquitin-protein ligase SIAH1 after autophosphorylation, leading to its proteasomal degradation. Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. te=The gene represented in this entry may be involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of FLT3 are frequent in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the activation loop of the kinase domain can result in a constitutively activated kinase. Can be used as diagnostic tool to establish the exact cause of acute myeloid leukemia, and to determine the optimal therapy. Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/144/FLT3"; MAPK cascade nucleotide binding leukocyte homeostasis hematopoietic progenitor cell differentiation myeloid progenitor cell differentiation pro-B cell differentiation leukocyte differentiation protein kinase activity protein tyrosine kinase activity transmembrane receptor protein tyrosine kinase activity cytokine receptor activity vascular endothelial growth factor-activated receptor activity protein binding ATP binding nucleus cytoplasm endoplasmic reticulum endoplasmic reticulum lumen cytosol plasma membrane integral component of plasma membrane protein phosphorylation transmembrane receptor protein tyrosine kinase signaling pathway positive regulation of cell proliferation response to organonitrogen compound positive regulation of phosphatidylinositol 3-kinase signaling membrane integral component of membrane viral process kinase activity phosphorylation transferase activity peptidyl-tyrosine phosphorylation cytokine-mediated signaling pathway hemopoiesis lymphocyte differentiation cell differentiation B cell differentiation animal organ regeneration macromolecular complex glucocorticoid receptor binding common myeloid progenitor cell proliferation vascular endothelial growth factor signaling pathway positive regulation of tyrosine phosphorylation of STAT protein protein homodimerization activity regulation of apoptotic process receptor complex positive regulation of MAP kinase activity positive regulation of MAPK cascade positive regulation of phosphatidylinositol 3-kinase activity protein self-association macromolecular complex binding lymphocyte proliferation protein autophosphorylation cellular response to cytokine stimulus cellular response to glucocorticoid stimulus dendritic cell differentiation uc001urw.1 uc001urw.2 uc001urw.3 uc001urw.4 
ENST00000241463.5 RASL11A ENST00000241463.5 RAS like family 11 member A, transcript variant 1 (from RefSeq NM_206827.2) B2RN97 ENST00000241463.1 ENST00000241463.2 ENST00000241463.3 ENST00000241463.4 NM_206827 Q6T310 RASL11A RSLBA_HUMAN uc001urd.1 uc001urd.2 RASL11A is a member of the small GTPase protein family with a high degree of similarity to RAS (see HRAS, MIM 190020) proteins.[supplied by OMIM, Nov 2008]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. ##Evidence-Data-START## Transcript exon combination :: DRR138515.829203.1, AY439004.1 [ECO:0000332] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000241463.5/ ENSP00000241463.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Regulator of rDNA transcription. Acts in cooperation UBF/UBTF and positively regulates RNA polymerase I transcription (By similarity). Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence=; Interacts with UBF/UBTF. Q6T310; P42858: HTT; NbExp=3; IntAct=EBI-4401868, EBI-466029; Nucleus, nucleolus Note=Associates with rDNA transcription unit throughout the cell cycle. Widely expressed. Down-regulated in prostate tumors compared to normal prostate tissue. High levels found in colon tumor and normal colon tissue followed by small intestine, liver, jejunum, ileum, bladder and aorta. Lowest levels observed in endothelial cells. Down-regulated during development of THP-1 monocytes into macrophages. Down-regulated by TGFB1. Belongs to the small GTPase superfamily. Ras family. Although highly related to the Ras family, lacks the conserved prenylation motif at the C-terminus, which serves to target Ras proteins to membrane compartments. nucleotide binding GTPase activity GTP binding nucleus nucleolus signal transduction membrane positive regulation of transcription from RNA polymerase I promoter uc001urd.1 uc001urd.2 
ENST00000241502.9 FYTTD1 ENST00000241502.9 forty-two-three domain containing 1, transcript variant 1 (from RefSeq NM_032288.7) A8MY74 B2RCB2 B7Z3R4 B7Z7V1 B7Z8I0 B7ZAJ3 C9J7P6 C9JNG6 C9JTH3 C9JY50 ENST00000241502.1 ENST00000241502.2 ENST00000241502.3 ENST00000241502.4 ENST00000241502.5 ENST00000241502.6 ENST00000241502.7 ENST00000241502.8 NM_032288 Q96QD9 Q96SL9 Q9BQI8 UIF UIF_HUMAN uc003fyi.1 uc003fyi.2 uc003fyi.3 uc003fyi.4 Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4. Interacts with CHTOP (By similarity). Interacts with DDX39B/UAP56 and NXF1; interaction with DDX39B/UAP56 and NXF1 are mutually exclusive. Interacts with SSRP1; required for its recruitment to mRNAs. Q96QD9; Q13838: DDX39B; NbExp=3; IntAct=EBI-724553, EBI-348622; Q96QD9; Q2HR75: ORF57; Xeno; NbExp=9; IntAct=EBI-724553, EBI-6884751; Nucleus, nucleoplasm Nucleus speckle Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q96QD9-1; Sequence=Displayed; Name=2; IsoId=Q96QD9-2; Sequence=VSP_038659; Name=3; IsoId=Q96QD9-3; Sequence=VSP_038658; Name=4; IsoId=Q96QD9-4; Sequence=VSP_038660, VSP_038661; Expressed in a wide variety of cancer types. Belongs to the UIF family. RNA binding mRNA binding protein binding nucleus nucleoplasm mRNA export from nucleus nuclear speck mRNA transport uc003fyi.1 uc003fyi.2 uc003fyi.3 uc003fyi.4 
ENST00000241600.10 MRPS2 ENST00000241600.10 mitochondrial ribosomal protein S2, transcript variant 1 (from RefSeq NM_016034.5) CGI-91 ENST00000241600.1 ENST00000241600.2 ENST00000241600.3 ENST00000241600.4 ENST00000241600.5 ENST00000241600.6 ENST00000241600.7 ENST00000241600.8 ENST00000241600.9 NM_016034 Q5T899 Q9BSQ4 Q9Y399 RT02_HUMAN uc064wyt.1 uc064wyt.2 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S2 family. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, May 2012]. Sequence Note: A downstream translational start codon is selected for this RefSeq based on its better conservation in mammalian species, a strong Kozak signal and on the presence of a predicted mitochondrial targeting sequence in the protein N-terminus. An upstream in-frame start codon is also present but has a weaker Kozak signal and is poorly conserved, and use of the upstream start codon would result in a protein that is 23 aa longer at the N-terminus and lacks a predicted mitochondrial targeting sequence. Leaky scanning by ribosomes may allow translation initiation at the downstream start codon. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.317210.1, SRR3476690.962129.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968832 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta MANE Ensembl match :: ENST00000241600.10/ ENSP00000241600.5 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Required for mitoribosome formation and stability, and mitochondrial translation. Component of the mitochondrial small ribosomal subunit (mt- SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins. Mitochondrion Combined oxidative phosphorylation deficiency 36 (COXPD36) [MIM:617950]: An autosomal recessive, multisystem disease resulting from deficiencies of mitochondrial respiratory enzyme complexes and mitochondrial dysfunction. Clinical manifestations include sensorineural hearing impairment, mild developmental delay, hypoglycemia, and intellectual disability. Note=The disease is caused by variants affecting the gene represented in this entry. Belongs to the universal ribosomal protein uS2 family. Sequence=AAH04905.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence=; structural constituent of ribosome mitochondrion mitochondrial inner membrane mitochondrial small ribosomal subunit ribosome translation small ribosomal subunit mitochondrial translation mitochondrial ribosome assembly mitochondrial translational elongation mitochondrial translational termination uc064wyt.1 uc064wyt.2 
ENST00000241651.5 MYOG ENST00000241651.5 myogenin (from RefSeq NM_002479.6) BHLHC3 ENST00000241651.1 ENST00000241651.2 ENST00000241651.3 ENST00000241651.4 MYF4 MYOG_HUMAN NM_002479 P15173 Q53XW6 uc001gzd.1 uc001gzd.2 uc001gzd.3 uc001gzd.4 uc001gzd.5 uc001gzd.6 Myogenin is a muscle-specific transcription factor that can induce myogenesis in a variety of cell types in tissue culture. It is a member of a large family of proteins related by sequence homology, the helix-loop-helix (HLH) proteins. It is essential for the development of functional skeletal muscle. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC053899.1, ERR279849.7471.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2158800, SAMEA2162946 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000241651.5/ ENSP00000241651.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin- remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts (By similarity). Homodimer and heterodimer with E12; heterodimerization enhances MYOG DNA-binding and transcriptional activities. Interacts with SMARCA4/BRG1/BAF190A. Interacts (via C-terminal region) with SSRP1 and SUPT16H; the interaction is indicative of an interaction with the FACT complex (By similarity). Interacts with CSRP3. P15173; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-3906629, EBI-11096309; P15173; Q96RK4: BBS4; NbExp=3; IntAct=EBI-3906629, EBI-1805814; P15173; Q13515: BFSP2; NbExp=3; IntAct=EBI-3906629, EBI-10229433; P15173; Q7RTS1: BHLHA15; NbExp=3; IntAct=EBI-3906629, EBI-8844218; P15173; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-3906629, EBI-744556; P15173; Q7Z6N9: CCDC28A; NbExp=6; IntAct=EBI-3906629, EBI-10258115; P15173; Q8IWP9: CCDC28A; NbExp=4; IntAct=EBI-3906629, EBI-355471; P15173; Q96M91: CFAP53; NbExp=3; IntAct=EBI-3906629, EBI-742422; P15173; Q96AJ1: CLUAP1; NbExp=7; IntAct=EBI-3906629, EBI-739780; P15173; O95639-2: CPSF4; NbExp=3; IntAct=EBI-3906629, EBI-13063650; P15173; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-3906629, EBI-11962928; P15173; O60573: EIF4E2; NbExp=4; IntAct=EBI-3906629, EBI-398610; P15173; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-3906629, EBI-1752811; P15173; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-3906629, EBI-6658203; P15173; Q6QHK4: FIGLA; NbExp=5; IntAct=EBI-3906629, EBI-11976617; P15173; P02792: FTL; NbExp=4; IntAct=EBI-3906629, EBI-713279; P15173; P55040: GEM; NbExp=3; IntAct=EBI-3906629, EBI-744104; P15173; O75409: H2AP; NbExp=6; IntAct=EBI-3906629, EBI-6447217; P15173; P41134: ID1; NbExp=4; IntAct=EBI-3906629, EBI-1215527; P15173; Q70UQ0: IKBIP; NbExp=4; IntAct=EBI-3906629, EBI-2557212; P15173; Q70UQ0-4: IKBIP; NbExp=4; IntAct=EBI-3906629, EBI-12190633; P15173; Q14005-2: IL16; NbExp=3; IntAct=EBI-3906629, EBI-17178971; P15173; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-3906629, EBI-739890; P15173; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-3906629, EBI-11742507; P15173; O60336: MAPKBP1; NbExp=3; IntAct=EBI-3906629, EBI-947402; P15173; O95983-2: MBD3; NbExp=3; IntAct=EBI-3906629, EBI-11978579; P15173; P40692: MLH1; NbExp=12; IntAct=EBI-3906629, EBI-744248; P15173; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-3906629, EBI-11750983; P15173; Q96NG3: ODAD4; NbExp=3; IntAct=EBI-3906629, EBI-1046387; P15173; Q8N7B6: PACRGL; NbExp=3; IntAct=EBI-3906629, EBI-3925298; P15173; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-3906629, EBI-10694433; P15173; P52435: POLR2J; NbExp=3; IntAct=EBI-3906629, EBI-394753; P15173; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-3906629, EBI-742688; P15173; Q08117-2: TLE5; NbExp=3; IntAct=EBI-3906629, EBI-11741437; P15173; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-3906629, EBI-3918381; P15173; O14530: TXNDC9; NbExp=4; IntAct=EBI-3906629, EBI-707554; P15173; Q8N6Y0: USHBP1; NbExp=5; IntAct=EBI-3906629, EBI-739895; P15173; Q8WYQ9: ZCCHC14; NbExp=3; IntAct=EBI-3906629, EBI-3937908; Nucleus. Note=Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos. Phosphorylated by CAMK2G on threonine and serine amino acids in a muscle activity-dependent manner. Phosphorylation of Thr-87 impairs both DNA-binding and trans-activation functions in contracting muscles (By similarity). nuclear chromatin RNA polymerase II regulatory region sequence-specific DNA binding RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding core promoter proximal region sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding ossification DNA binding transcription factor activity, sequence-specific DNA binding protein binding nucleus nucleoplasm transcription factor complex regulation of transcription, DNA-templated cell cycle multicellular organism development muscle organ development skeletal muscle tissue development negative regulation of cell proliferation response to gravity positive regulation of myotube differentiation skeletal muscle atrophy positive regulation of muscle atrophy regulation of skeletal muscle satellite cell proliferation response to muscle activity response to muscle activity involved in regulation of muscle adaptation response to electrical stimulus involved in regulation of muscle adaptation striated muscle atrophy response to denervation involved in regulation of muscle adaptation myotube differentiation cell differentiation chromatin DNA binding protein-DNA complex skeletal muscle cell differentiation muscle cell fate commitment mRNA transcription from RNA polymerase II promoter skeletal muscle tissue regeneration sequence-specific DNA binding myoblast differentiation positive regulation of myoblast differentiation negative regulation of glycolytic process positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity protein dimerization activity skeletal muscle fiber development positive regulation of skeletal muscle fiber development positive regulation of muscle cell differentiation E-box binding positive regulation of cell cycle arrest cellular response to magnetism cellular response to lithium ion cellular response to retinoic acid cellular response to tumor necrosis factor cellular response to growth factor stimulus cellular response to estradiol stimulus regulation of myoblast fusion positive regulation of myoblast fusion positive regulation of oxidative phosphorylation uc001gzd.1 uc001gzd.2 uc001gzd.3 uc001gzd.4 uc001gzd.5 uc001gzd.6 
ENST00000241704.8 COPA ENST00000241704.8 COPI coat complex subunit alpha, transcript variant 2 (from RefSeq NM_004371.4) COPA_HUMAN ENST00000241704.1 ENST00000241704.2 ENST00000241704.3 ENST00000241704.4 ENST00000241704.5 ENST00000241704.6 ENST00000241704.7 NM_004371 P53621 Q5T201 Q8IXZ9 uc009wti.1 uc009wti.2 uc009wti.3 uc009wti.4 uc009wti.5 In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). Seven coat proteins have been identified, and they represent subunits of a complex known as coatomer. The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP. The alpha-COP, encoded by COPA, shares high sequence similarity with RET1P, the alpha subunit of the coatomer complex in yeast. Also, the N-terminal 25 amino acids of alpha-COP encode the bioactive peptide, xenin, which stimulates exocrine pancreatic secretion and may act as a gastrointestinal hormone. Alternative splicing results in multiple splice forms encoding distinct isoforms. [provided by RefSeq, Jul 2008]. The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor. Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits (By similarity). Interacts with SCYL1 (By similarity). Interacts with JAGN1 (PubMed:25129144). Interacts with TMEM41B (PubMed:30352685). Interacts with SVEP1 (By similarity). Probably interacts with PEX11A. Cytoplasm Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side Cytoplasmic vesicle, COPI-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. [Xenin]: Secreted Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P53621-1; Sequence=Displayed; Name=2; IsoId=P53621-2; Sequence=VSP_035043; Uniformly expressed in a wide range of adult and fetal tissues. Xenin is found in gastric, duodenal and jejunal mucosa. Circulates in the blood. Seems to be confined to specific endocrine cells. Xenin is released into the circulation after a meal. Modified_positions=164 ; Note=Edited at about 31%.; Autoimmune interstitial lung, joint, and kidney disease (AILJK) [MIM:616414]: An autoimmune disease characterized by inflammatory arthritis, interstitial lung disease, and immune complex- mediated renal disease. Note=The disease is caused by variants affecting the gene represented in this entry. Name=Wikipedia; Note=Xenin entry; URL="https://en.wikipedia.org/wiki/Xenin"; Golgi membrane hormone activity structural molecule activity extracellular region extracellular space cytoplasm endoplasmic reticulum membrane Golgi apparatus cytosol intracellular protein transport ER to Golgi vesicle-mediated transport retrograde vesicle-mediated transport, Golgi to ER intra-Golgi vesicle-mediated transport signal transduction protein transport membrane vesicle-mediated transport membrane coat COPI vesicle coat transport vesicle pancreatic juice secretion COPI-coated vesicle membrane cytoplasmic vesicle extracellular exosome uc009wti.1 uc009wti.2 uc009wti.3 uc009wti.4 uc009wti.5 
ENST00000241802.9 HLA-DQA2 ENST00000241802.9 major histocompatibility complex, class II, DQ alpha 2 (from RefSeq NM_020056.5) A2BF37 B0V0E7 DQA2_HUMAN ENST00000241802.1 ENST00000241802.2 ENST00000241802.3 ENST00000241802.4 ENST00000241802.5 ENST00000241802.6 ENST00000241802.7 ENST00000241802.8 HLA-DXA NM_020056 O19789 P01906 Q5SQ94 Q5SR04 uc302who.1 This gene belongs to the HLA class II alpha chain family. The encoded protein forms a heterodimer with a class II beta chain. It is located in intracellular vesicles and plays a central role in the peptide loading of MHC class II molecules by helping to release the CLIP molecule from the peptide binding site. Class II molecules are expressed in antigen presenting cells (B lymphocytes, dendritic cells, macrophages) and are used to present antigenic peptides on the cell surface to be recognized by CD4 T-cells. [provided by RefSeq, Jun 2010]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## RNAseq introns :: single sample supports all introns SAMEA2144335, SAMEA2145893 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000374940.4/ ENSP00000364076.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. Heterodimer of an alpha and a beta subunit; also referred as MHC class II molecule. Dimer formation with HLA-DQB2, but not with HLA- DQB1, is required for efficient exit from the endoplasmic reticulum (ER). In the ER, forms a heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also known as invariant chain or HLA class II histocompatibility antigen gamma chain). In the endosomal/lysosomal system; CD74 undergoes sequential degradation by various proteases; leaving a small fragment termed CLIP on each MHC class II molecule. MHC class II molecule interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP and facilitate the binding of antigenic peptides. Association with HLA-DMA also occurs in skin Langerhans cells, in post- Golgi compartments. P01906; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-19949550, EBI-2820517; Cell membrane ; Single-pass type I membrane protein Endoplasmic reticulum membrane ; Single- pass type I membrane protein Golgi apparatus, trans-Golgi network membrane ; Single-pass type I membrane protein Endosome membrane ; Single-pass type I membrane protein Lysosome membrane ; Single-pass type I membrane protein Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation. Restricted to skin Langerhans cells, although some expression at low levels may occur at the surface of B lymphoblastoid cells. Belongs to the MHC class II family. Golgi membrane adaptive immune response immune system process antigen processing and presentation of peptide or polysaccharide antigen via MHC class II lysosome lysosomal membrane endosome endoplasmic reticulum endoplasmic reticulum membrane Golgi apparatus plasma membrane integral component of plasma membrane immune response endosome membrane ER to Golgi transport vesicle membrane membrane integral component of membrane antigen processing and presentation antigen processing and presentation of exogenous peptide antigen via MHC class II transport vesicle membrane endocytic vesicle membrane clathrin-coated endocytic vesicle membrane MHC class II receptor activity trans-Golgi network membrane MHC class II protein complex T cell receptor signaling pathway interferon-gamma-mediated signaling pathway integral component of lumenal side of endoplasmic reticulum membrane uc302who.1 
ENST00000241808.9 PRM2 ENST00000241808.9 protamine 2, transcript variant 6 (from RefSeq NR_104428.2) ENST00000241808.1 ENST00000241808.2 ENST00000241808.3 ENST00000241808.4 ENST00000241808.5 ENST00000241808.6 ENST00000241808.7 ENST00000241808.8 NR_104428 PRM2 Q1LZN1 Q1LZN1_HUMAN hCG_15066 uc002dau.1 uc002dau.2 uc002dau.3 Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis, and are the major DNA-binding proteins in the nucleus of sperm in many vertebrates. They package the sperm DNA into a highly condensed complex in a volume less than 5% of a somatic cell nucleus. Many mammalian species have only one protamine (protamine 1); however, a few species, including human and mouse, have two. This gene encodes protamine 2, which is cleaved to give rise to a family of protamine 2 peptides. Alternatively spliced transcript variants have also been found for this gene. [provided by RefSeq, Sep 2015]. Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. Interacts with TDRP. Belongs to the protamine P2 family. DNA binding protein binding DNA packaging spermatid development uc002dau.1 uc002dau.2 uc002dau.3 
ENST00000241891.10 OPN4 ENST00000241891.10 opsin 4, transcript variant 1 (from RefSeq NM_033282.4) B7ZLB3 ENST00000241891.1 ENST00000241891.2 ENST00000241891.3 ENST00000241891.4 ENST00000241891.5 ENST00000241891.6 ENST00000241891.7 ENST00000241891.8 ENST00000241891.9 MOP NM_033282 OPN4_HUMAN Q14D01 Q2PP22 Q8NGQ9 Q9UHM6 uc001kdq.1 uc001kdq.2 uc001kdq.3 uc001kdq.4 uc001kdq.5 Opsins are members of the guanine nucleotide-binding protein (G protein)-coupled receptor superfamily. This gene encodes a photoreceptive opsin protein that is expressed within the ganglion and amacrine cell layers of the retina. In mouse, retinal ganglion cell axons expressing this gene projected to the suprachiasmatic nucleus and other brain nuclei involved in circadian photoentrainment. In mouse, this protein is coupled to a transient receptor potential (TRP) ion channel through a G protein signaling pathway and produces a physiologic light response via membrane depolarization and increased intracellular calcium. The protein functions as a sensory photopigment and may also have photoisomerase activity. Experiments with knockout mice indicate that this gene attenuates, but does not abolish, photoentrainment. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]. Photoreceptor that binds cis-retinaldehydes (PubMed:15674244). Contributes to pupillar reflex, photoentrainment and other non-image forming responses to light (By similarity). May be involved in the optokinetic visual tracking response (By similarity). May be involved in the regulation of retinal hyaloid vessel growth and regression (By similarity). Q9UHM6; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-18058356, EBI-947187; Cell membrane ; Multi-pass membrane protein Cell projection, axon Cell projection, dendrite Perikaryon Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UHM6-1; Sequence=Displayed; Name=2; IsoId=Q9UHM6-2; Sequence=VSP_041123; Expressed in the retina. Belongs to the G-protein coupled receptor 1 family. Opsin subfamily. Sequence=BAC05951.1; Type=Erroneous gene model prediction; Evidence=; Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/opn4/"; G-protein coupled receptor activity 11-cis retinal binding plasma membrane integral component of plasma membrane signal transduction G-protein coupled receptor signaling pathway visual perception phototransduction G-protein coupled photoreceptor activity detection of visible light photoreceptor activity membrane integral component of membrane protein-chromophore linkage regulation of circadian rhythm rhythmic process response to stimulus cellular response to light stimulus photoreceptor disc membrane uc001kdq.1 uc001kdq.2 uc001kdq.3 uc001kdq.4 uc001kdq.5 
ENST00000242057.9 AHR ENST00000242057.9 aryl hydrocarbon receptor (from RefSeq NM_001621.5) A4D130 AHR AHR_HUMAN BHLHE76 ENST00000242057.1 ENST00000242057.2 ENST00000242057.3 ENST00000242057.4 ENST00000242057.5 ENST00000242057.6 ENST00000242057.7 ENST00000242057.8 NM_001621 P35869 Q13728 Q13803 Q13804 uc011jxz.1 uc011jxz.2 uc011jxz.3 The protein encoded by this gene is a ligand-activated helix-loop-helix transcription factor involved in the regulation of biological responses to planar aromatic hydrocarbons. This receptor has been shown to regulate xenobiotic-metabolizing enzymes such as cytochrome P450. Before ligand binding, the encoded protein is sequestered in the cytoplasm; upon ligand binding, this protein moves to the nucleus and stimulates transcription of target genes. [provided by RefSeq, Sep 2015]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1803617.231889.1, SRR1660809.233497.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000242057.9/ ENSP00000242057.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:30373764, PubMed:23275542, PubMed:7961644, PubMed:32818467). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (PubMed:30373764, PubMed:23275542, PubMed:7961644). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (PubMed:12213388). Xenobiotics can act as ligands: upon xenobiotic- binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) (PubMed:7961644). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons (PubMed:7961644, PubMed:34521881). Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists (PubMed:18076143). Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands (PubMed:32866000, PubMed:32818467). Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity (PubMed:32818467). Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 (PubMed:28602820). Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 (PubMed:28602820). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820). Homodimer (By similarity). Heterodimer; efficient DNA binding requires dimerization with another bHLH protein (PubMed:10395741, PubMed:28602820). Interacts with ARNT; the heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820, PubMed:34521881). Binds MYBBP1A (By similarity). Interacts with coactivators including SRC-1, RIP140 and NOCA7, and with the corepressor SMRT (PubMed:10395741). Interacts with NEDD8 and IVNS1ABP (PubMed:12215427, PubMed:16582008). Interacts with BMAL1 (By similarity). Interacts with HSP90AB1 (By similarity). Interacts with TIPARP; leading to mono-ADP-ribosylation of AHR and subsequent inhibition of AHR (PubMed:23275542, PubMed:30373764). P35869; P27540: ARNT; NbExp=6; IntAct=EBI-80780, EBI-80809; P35869; Q8NI08: NCOA7; NbExp=2; IntAct=EBI-80780, EBI-80799; P35869; Q9Y618: NCOR2; NbExp=2; IntAct=EBI-80780, EBI-80830; P35869; P12977: EBNA3; Xeno; NbExp=5; IntAct=EBI-80780, EBI-993115; Cytoplasm Nucleus Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus. Expressed in all tissues tested including blood, brain, heart, kidney, liver, lung, pancreas and skeletal muscle. Expressed in retinal photoreceptors (PubMed:29726989). Induced or repressed by TGFB1 and dioxin in a cell-type specific fashion. Repressed by cAMP, retinoic acid, and 12-O- tetradecanoyl phorbol-13 acetate (TPA). The PAS 1 domain is essential for dimerization and also required for AHR:ARNT heterodimerization. Mono-ADP-ribosylated, leading to inhibit transcription activator activity of AHR. Retinitis pigmentosa 85 (RP85) [MIM:618345]: A form of retinitis pigmentosa, a retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP85 is an autosomal recessive form manifesting as early-onset progressive difficulty to adapt in dim light and gradually decreasing visual acuity in both eyes. Note=The disease is caused by variants affecting the gene represented in this entry. nuclear chromatin RNA polymerase II transcription factor activity, sequence-specific DNA binding TFIID-class transcription factor binding transcription coactivator binding blood vessel development DNA binding transcription factor activity, sequence-specific DNA binding RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding protein binding nucleus nucleoplasm transcription factor complex cytoplasm cytosol regulation of transcription, DNA-templated regulation of transcription from RNA polymerase II promoter transcription from RNA polymerase II promoter xenobiotic metabolic process apoptotic process cell cycle transcription factor binding response to xenobiotic stimulus response to toxic substance regulation of gene expression TBP-class protein binding cAMP-mediated signaling intracellular receptor signaling pathway regulation of B cell proliferation circadian regulation of gene expression macromolecular complex aryl hydrocarbon receptor complex cytosolic aryl hydrocarbon receptor complex enhancer binding protein homodimerization activity transcription regulatory region DNA binding negative regulation of transcription, DNA-templated positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter protein heterodimerization activity protein dimerization activity rhythmic process Hsp90 protein binding E-box binding cellular response to cAMP cellular response to forskolin cellular response to 2,3,7,8-tetrachlorodibenzodioxine sequence-specific double-stranded DNA binding uc011jxz.1 uc011jxz.2 uc011jxz.3 
ENST00000242059.10 SCRN1 ENST00000242059.10 secernin 1, transcript variant 2 (from RefSeq NM_014766.5) A8K0E9 B4DHM0 B4DIP5 C9JPG0 ENST00000242059.1 ENST00000242059.2 ENST00000242059.3 ENST00000242059.4 ENST00000242059.5 ENST00000242059.6 ENST00000242059.7 ENST00000242059.8 ENST00000242059.9 KIAA0193 NM_014766 Q12765 Q25QX7 Q8IWD1 SCRN1_HUMAN uc003tak.1 uc003tak.2 uc003tak.3 uc003tak.4 uc003tak.5 This gene likely encodes a member of the secernin family of proteins. A similar protein in rat functions in regulation of exocytosis in mast cells. Alternatively spliced transcript variants have been described. [provided by RefSeq, Mar 2009]. Regulates exocytosis in mast cells. Increases both the extent of secretion and the sensitivity of mast cells to stimulation with calcium (By similarity). Q12765; Q9BQQ3: GORASP1; NbExp=3; IntAct=EBI-2690712, EBI-2561458; Q12765; P10636-8: MAPT; NbExp=5; IntAct=EBI-2690712, EBI-366233; Q12765-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12027936, EBI-742054; Q12765-2; Q9BQQ3: GORASP1; NbExp=3; IntAct=EBI-12027936, EBI-2561458; Q12765-2; P42858: HTT; NbExp=3; IntAct=EBI-12027936, EBI-466029; Q12765-2; P17030: ZNF25; NbExp=3; IntAct=EBI-12027936, EBI-7934204; Cytoplasm Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q12765-1; Sequence=Displayed; Name=2; IsoId=Q12765-2; Sequence=VSP_044454; Name=3; IsoId=Q12765-3; Sequence=VSP_044453; 'Secern' is an archaic English term meaning 'secrete'. Belongs to the peptidase C69 family. Secernin subfamily. Sequence=BAA12106.2; Type=Erroneous initiation; Evidence=; molecular_function protein binding nucleus cytoplasm proteolysis exocytosis dipeptidase activity nuclear membrane uc003tak.1 uc003tak.2 uc003tak.3 uc003tak.4 uc003tak.5 
ENST00000242067.11 BBS9 ENST00000242067.11 Bardet-Biedl syndrome 9, transcript variant 2 (from RefSeq NM_198428.3) E9PDC9 ENST00000242067.1 ENST00000242067.10 ENST00000242067.2 ENST00000242067.3 ENST00000242067.4 ENST00000242067.5 ENST00000242067.6 ENST00000242067.7 ENST00000242067.8 ENST00000242067.9 NM_198428 P78514 PTHB1 PTHB1_HUMAN Q3SYG4 Q7KYS6 Q7KYS7 Q8N570 Q99844 Q99854 Q9Y699 Q9Y6A0 uc003tdn.1 uc003tdn.2 uc003tdn.3 This gene is downregulated by parathyroid hormone in osteoblastic cells, and therefore is thought to be involved in parathyroid hormone action in bones. The exact function of this gene has not yet been determined. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jan 2017]. The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for proper BBSome complex assembly and its ciliary localization. Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with LZTL1; the interaction mediates the association of LZTL1 with the BBsome complex and regulates BBSome ciliary trafficking. Q3SYG4; Q8NFJ9: BBS1; NbExp=12; IntAct=EBI-2826852, EBI-1805484; Q3SYG4; Q8TAM1: BBS10; NbExp=2; IntAct=EBI-2826852, EBI-6128013; Q3SYG4; Q6ZW61: BBS12; NbExp=2; IntAct=EBI-2826852, EBI-6128352; Q3SYG4; Q9BXC9: BBS2; NbExp=14; IntAct=EBI-2826852, EBI-748297; Q3SYG4; Q96RK4: BBS4; NbExp=6; IntAct=EBI-2826852, EBI-1805814; Q3SYG4; Q8N3I7: BBS5; NbExp=7; IntAct=EBI-2826852, EBI-2892592; Q3SYG4; Q15051: IQCB1; NbExp=5; IntAct=EBI-2826852, EBI-2805823; Q3SYG4; Q9NQ48: LZTFL1; NbExp=8; IntAct=EBI-2826852, EBI-2824799; Q3SYG4; A0A0C4DGX9: TTC8; NbExp=3; IntAct=EBI-2826852, EBI-20959097; Q3SYG4; Q8TAM2: TTC8; NbExp=2; IntAct=EBI-2826852, EBI-2892638; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Event=Alternative splicing; Named isoforms=7; Name=1; IsoId=Q3SYG4-1; Sequence=Displayed; Name=2; IsoId=Q3SYG4-2; Sequence=VSP_018426; Name=3; IsoId=Q3SYG4-3; Sequence=VSP_018428; Name=4; IsoId=Q3SYG4-4; Sequence=VSP_018427; Name=5; IsoId=Q3SYG4-5; Sequence=VSP_018421, VSP_018422, VSP_018423; Name=6; IsoId=Q3SYG4-6; Sequence=VSP_018424, VSP_018425; Name=7; IsoId=Q3SYG4-7; Sequence=VSP_054063; Widely expressed. Expressed in adult heart, skeletal muscle, lung, liver, kidney, placenta and brain, and in fetal kidney, lung, liver and brain. Down-regulated by parathyroid hormone. Note=A chromosomal aberration involving PTHB1 has been found in Wilms tumor. Translocation t(1;7)(q42;p15) with OBSCN. Bardet-Biedl syndrome 9 (BBS9) [MIM:615986]: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and intellectual disability. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. Note=The disease is caused by variants affecting the gene represented in this entry. Sequence=AAD25980.1; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence=; Sequence=AAD25981.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence=; pericentriolar material molecular_function protein binding cytoplasm microtubule organizing center cytosol cytoskeleton plasma membrane cilium visual perception protein transport membrane cell projection organization centriolar satellite BBSome ciliary transition zone cell projection fat cell differentiation response to stimulus ciliary membrane cilium assembly protein localization to cilium uc003tdn.1 uc003tdn.2 uc003tdn.3 
ENST00000242104.6 OCM ENST00000242104.6 oncomodulin, transcript variant 3 (from RefSeq NM_001391991.1) B9EJH7 ENST00000242104.1 ENST00000242104.2 ENST00000242104.3 ENST00000242104.4 ENST00000242104.5 NM_001391991 OCM1 OCMN ONCO_HUMAN P0CE72 P32930 Q6ISI5 Q75MW0 uc003spe.1 uc003spe.2 uc003spe.3 uc003spe.4 uc003spe.5 uc003spe.6 Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions. P0CE72; P12532: CKMT1B; NbExp=6; IntAct=EBI-11955379, EBI-1050662; P0CE72; O00560: SDCBP; NbExp=3; IntAct=EBI-11955379, EBI-727004; Belongs to the parvalbumin family. calcium ion binding nucleus cytoplasm metal ion binding uc003spe.1 uc003spe.2 uc003spe.3 uc003spe.4 uc003spe.5 uc003spe.6 
ENST00000242108.9 EEPD1 ENST00000242108.9 endonuclease/exonuclease/phosphatase family domain containing 1 (from RefSeq NM_030636.3) EEPD1_HUMAN ENST00000242108.1 ENST00000242108.2 ENST00000242108.3 ENST00000242108.4 ENST00000242108.5 ENST00000242108.6 ENST00000242108.7 ENST00000242108.8 KIAA1706 NM_030636 Q7L9B9 Q96K64 Q9C0F7 uc003tfa.1 uc003tfa.2 uc003tfa.3 uc003tfa.4 uc003tfa.5 Q7L9B9; Q9Y3R0-3: GRIP1; NbExp=3; IntAct=EBI-12262046, EBI-12193965; Sequence=BAB21797.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence=; DNA binding DNA repair uc003tfa.1 uc003tfa.2 uc003tfa.3 uc003tfa.4 uc003tfa.5 
ENST00000242109.6 KIAA0087 ENST00000242109.6 KIAA0087 lncRNA (from RefSeq NR_022006.1) ENST00000242109.1 ENST00000242109.2 ENST00000242109.3 ENST00000242109.4 ENST00000242109.5 NR_022006 uc003sya.1 uc003sya.2 uc003sya.3 uc003sya.4 uc003sya.1 uc003sya.2 uc003sya.3 uc003sya.4 
ENST00000242140.10 WIPF3 ENST00000242140.10 WAS/WASL interacting protein family member 3, transcript variant 1 (from RefSeq NM_001080529.3) A6NGB9 B8ZZV2 CR16 ENST00000242140.1 ENST00000242140.2 ENST00000242140.3 ENST00000242140.4 ENST00000242140.5 ENST00000242140.6 ENST00000242140.7 ENST00000242140.8 ENST00000242140.9 NM_001080529 WIPF3_HUMAN uc022aaz.1 uc022aaz.2 May be a regulator of cytoskeletal organization. May have a role in spermatogenesis (By similarity). Interacts with WASL, and monomeric and filamentous actin. Cytoplasm. Note=In hippocampal neurons colocalizes with WASL in the cell body, axons and the growth cone. The WH2 domain is found in a number of putative actin-binding proteins. The profilin-binding motif has been implicated in the interaction with profilin and SH3 domains. The KLKR motif is essential for G-actin binding and for actin polymerization. Belongs to the verprolin family. actin cortical patch assembly actin binding cytoplasm cytosol actin filament endocytosis multicellular organism development spermatogenesis SH3 domain binding actin filament-based movement cell differentiation actin cortical patch Fc-gamma receptor signaling pathway involved in phagocytosis actin filament binding actin cortical patch localization uc022aaz.1 uc022aaz.2 
ENST00000242152.7 NPY ENST00000242152.7 neuropeptide Y (from RefSeq NM_000905.4) ENST00000242152.1 ENST00000242152.2 ENST00000242152.3 ENST00000242152.4 ENST00000242152.5 ENST00000242152.6 NM_000905 NPY_HUMAN P01303 uc003sww.1 uc003sww.2 uc003sww.3 uc003sww.4 This gene encodes a neuropeptide that is widely expressed in the central nervous system and influences many physiological processes, including cortical excitability, stress response, food intake, circadian rhythms, and cardiovascular function. The neuropeptide functions through G protein-coupled receptors to inhibit adenylyl cyclase, activate mitogen-activated protein kinase (MAPK), regulate intracellular calcium levels, and activate potassium channels. A polymorphism in this gene resulting in a change of leucine 7 to proline in the signal peptide is associated with elevated cholesterol levels, higher alcohol consumption, and may be a risk factor for various metabolic and cardiovascular diseases. The protein also exhibits antimicrobial activity against bacteria and fungi. [provided by RefSeq, Oct 2014]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: DA330523.1, BC029497.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1966682, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000242152.7/ ENSP00000242152.2 Protein has antimicrobial activity :: PMID: 9756788 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. P01303; F1D8P7: NR1H2; NbExp=3; IntAct=EBI-3905877, EBI-10177172; P01303; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-3905877, EBI-947187; Secreted. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle One of the most abundant peptides in the nervous system. Also found in some chromaffin cells of the adrenal medulla. The neuropeptide Y form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro). Belongs to the NPY family. Name=Wikipedia; Note=Neuropeptide Y entry; URL="https://en.wikipedia.org/wiki/Neuropeptide_Y"; Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="https://atlasgeneticsoncology.org/gene/44438/NPY"; G-protein coupled receptor binding response to yeast G-protein coupled receptor activity receptor binding hormone activity neuropeptide hormone activity calcium channel regulator activity extracellular region extracellular space cell cytoplasm Golgi apparatus G-protein coupled receptor signaling pathway G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger neuropeptide signaling pathway chemical synaptic transmission feeding behavior regulation of blood pressure adult feeding behavior antibacterial humoral response antifungal humoral response central nervous system neuron development cerebral cortex development neuron projection development neuropeptide Y receptor binding positive regulation of appetite innate immune response defense response to Gram-negative bacterium defense response to Gram-positive bacterium intestinal epithelial cell differentiation uc003sww.1 uc003sww.2 uc003sww.3 uc003sww.4 
ENST00000242159.5 HOXA7 ENST00000242159.5 homeobox A7 (from RefSeq NM_006896.4) A4D191 ENST00000242159.1 ENST00000242159.2 ENST00000242159.3 ENST00000242159.4 HOX1A HXA7_HUMAN NM_006896 O43368 O43486 O95655 P31268 Q9NSC8 Q9UDM1 uc003sys.1 uc003sys.2 uc003sys.3 uc003sys.4 uc003sys.5 In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. For example, the encoded protein represses the transcription of differentiation-specific genes during keratinocyte proliferation, but this repression is then overcome by differentiation signals. This gene is highly similar to the antennapedia (Antp) gene of Drosophila. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.1100454.1, SRR1803614.291174.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000242159.5/ ENSP00000242159.3 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. P31268; O00560: SDCBP; NbExp=3; IntAct=EBI-3910421, EBI-727004; Nucleus. Belongs to the Antp homeobox family. negative regulation of transcription from RNA polymerase II promoter nuclear chromatin RNA polymerase II core promoter proximal region sequence-specific DNA binding RNA polymerase II distal enhancer sequence-specific DNA binding RNA polymerase II transcription factor activity, sequence-specific DNA binding transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding angiogenesis negative regulation of cell-matrix adhesion negative regulation of leukocyte migration DNA binding transcription factor activity, sequence-specific DNA binding nucleus nucleoplasm regulation of transcription, DNA-templated multicellular organism development transcription factor binding anterior/posterior pattern specification nuclear membrane sequence-specific DNA binding negative regulation of keratinocyte differentiation negative regulation of monocyte differentiation negative regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter embryonic skeletal system morphogenesis stem cell differentiation uc003sys.1 uc003sys.2 uc003sys.3 uc003sys.4 uc003sys.5 
ENST00000242208.5 INHBA ENST00000242208.5 inhibin subunit beta A (from RefSeq NM_002192.4) ENST00000242208.1 ENST00000242208.2 ENST00000242208.3 ENST00000242208.4 INHBA_HUMAN NM_002192 P08476 Q14599 uc003thr.1 uc003thr.2 uc003thr.3 uc003thr.4 uc003thr.5 This gene encodes a member of the TGF-beta (transforming growth factor-beta) superfamily of proteins. The encoded preproprotein is proteolytically processed to generate a subunit of the dimeric activin and inhibin protein complexes. These complexes activate and inhibit, respectively, follicle stimulating hormone secretion from the pituitary gland. The encoded protein also plays a role in eye, tooth and testis development. Elevated expression of this gene may be associated with cancer cachexia in human patients. [provided by RefSeq, Aug 2016]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.577620.1, BC007858.2 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA2149398 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000242208.5/ ENSP00000242208.4 RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3. P08476; P21674: Fst; Xeno; NbExp=2; IntAct=EBI-8077140, EBI-5746973; Secreted. Belongs to the TGF-beta family. Name=Wikipedia; Note=Activin entry; URL="https://en.wikipedia.org/wiki/Activin"; G1/S transition of mitotic cell cycle ovarian follicle development mesoderm formation hair follicle development hematopoietic progenitor cell differentiation receptor binding cytokine activity transforming growth factor beta receptor binding hormone activity protein binding extracellular region extracellular space regulation of transcription from RNA polymerase II promoter defense response cell cycle arrest cell surface receptor signaling pathway cell-cell signaling nervous system development growth factor activity negative regulation of cell proliferation male gonad development positive regulation of gene expression positive regulation of pathway-restricted SMAD protein phosphorylation peptide hormone binding striatal medium spiny neuron differentiation cell differentiation erythrocyte differentiation negative regulation of cell growth positive regulation of cellular protein metabolic process activin receptor signaling pathway inhibin binding endodermal cell differentiation negative regulation of phosphorylation odontogenesis response to drug hemoglobin biosynthetic process progesterone secretion identical protein binding regulation of apoptotic process regulation of MAPK cascade activin A complex inhibin A complex negative regulation of interferon-gamma biosynthetic process negative regulation of B cell differentiation positive regulation of erythrocyte differentiation negative regulation of macrophage differentiation negative regulation of cell cycle positive regulation of transcription, DNA-templated positive regulation of transcription from RNA polymerase II promoter regulation of follicle-stimulating hormone secretion positive regulation of follicle-stimulating hormone secretion negative regulation of follicle-stimulating hormone secretion protein heterodimerization activity mesodermal cell differentiation cell development perinuclear region of cytoplasm palate development positive regulation of ovulation SMAD protein signal transduction eyelid development in camera-type eye type II activin receptor binding cellular response to follicle-stimulating hormone stimulus cellular response to cholesterol GABAergic neuron differentiation extrinsic apoptotic signaling pathway positive regulation of extrinsic apoptotic signaling pathway in absence of ligand response to wounding uc003thr.1 uc003thr.2 uc003thr.3 uc003thr.4 uc003thr.5 
ENST00000242209.9 FKBP9 ENST00000242209.9 FKBP prolyl isomerase 9, transcript variant 1 (from RefSeq NM_007270.5) B3KY35 B7Z1G9 B7Z6H3 ENST00000242209.1 ENST00000242209.2 ENST00000242209.3 ENST00000242209.4 ENST00000242209.5 ENST00000242209.6 ENST00000242209.7 ENST00000242209.8 FKBP60 FKBP63 FKBP9_HUMAN NM_007270 O95302 Q2M2A1 Q3MIR7 Q6IN76 Q6P2N1 Q96EX5 Q96IJ9 uc003tdh.1 uc003tdh.2 uc003tdh.3 uc003tdh.4 uc003tdh.5 uc003tdh.6 PPIases accelerate the folding of proteins during protein synthesis. Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Inhibited by FK506. Endoplasmic reticulum Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O95302-1; Sequence=Displayed; Name=2; IsoId=O95302-2; Sequence=VSP_054825; Name=3; IsoId=O95302-3; Sequence=VSP_054826; Phosphorylated. protein peptidyl-prolyl isomerization peptidyl-prolyl cis-trans isomerase activity calcium ion binding endoplasmic reticulum protein folding isomerase activity metal ion binding uc003tdh.1 uc003tdh.2 uc003tdh.3 uc003tdh.4 uc003tdh.5 uc003tdh.6 
ENST00000242248.10 POLM ENST00000242248.10 DNA polymerase mu, transcript variant 6 (from RefSeq NR_156112.2) D3DVK4 DPOLM_HUMAN ENST00000242248.1 ENST00000242248.2 ENST00000242248.3 ENST00000242248.4 ENST00000242248.5 ENST00000242248.6 ENST00000242248.7 ENST00000242248.8 ENST00000242248.9 NR_156112 Q6P5X8 Q86WQ9 Q9NP87 polmu uc003tjt.1 uc003tjt.2 uc003tjt.3 uc003tjt.4 uc003tjt.5 uc003tjt.6 Gap-filling polymerase involved in repair of DNA double- strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence=; Q9NP87; P14079: tax; Xeno; NbExp=3; IntAct=EBI-9675790, EBI-9675698; Nucleus Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9NP87-1; Sequence=Displayed; Name=2; IsoId=Q9NP87-2; Sequence=VSP_055290; Name=3; IsoId=Q9NP87-3; Sequence=VSP_055288, VSP_055289, VSP_055291; Expressed in a number of tissues. Abundant in thymus. DPOLM has a reduced ability to distinguish dNTP and rNTP as substrates, and elongates them on DNA primer strand with a similar efficiency. It is able to polymerize nucleotides on RNA primer strands. Belongs to the DNA polymerase type-X family. Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/polm/"; DNA binding DNA-directed DNA polymerase activity protein binding nucleus nucleoplasm DNA repair base-excision repair double-strand break repair via nonhomologous end joining DNA recombination cellular response to DNA damage stimulus somatic hypermutation of immunoglobulin genes transferase activity nucleotidyltransferase activity B cell differentiation DNA polymerase activity metal ion binding DNA biosynthetic process uc003tjt.1 uc003tjt.2 uc003tjt.3 uc003tjt.4 uc003tjt.5 uc003tjt.6 
ENST00000242249.8 RAMP3 ENST00000242249.8 receptor activity modifying protein 3 (from RefSeq NM_005856.3) ENST00000242249.1 ENST00000242249.2 ENST00000242249.3 ENST00000242249.4 ENST00000242249.5 ENST00000242249.6 ENST00000242249.7 NM_005856 O60896 Q7Z2Y1 RAMP3_HUMAN uc003tnb.1 uc003tnb.2 uc003tnb.3 uc003tnb.4 The protein encoded by this gene is a member of the RAMP family of single-transmembrane-domain proteins, called receptor (calcitonin) activity modifying proteins (RAMPs). RAMPs are type I transmembrane proteins with an extracellular N terminus and a cytoplasmic C terminus. RAMPs are required to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR, a receptor with seven transmembrane domains, can function as either a calcitonin-gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In the presence of this (RAMP3) protein, CRLR functions as an adrenomedullin receptor. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.309688.1, SRR5189667.82182.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##R